Relevant bibliographies by topics / Pax3 and Pax7 / Journal articles
To see the other types of publications on this topic, follow the link: Pax3 and Pax7.

Journal articles on the topic 'Pax3 and Pax7'

Author: Grafiati
Published: 4 June 2021
Last updated: 25 May 2024

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Consult the top 50 journal articles for your research on the topic 'Pax3 and Pax7.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Browse journal articles on a wide variety of disciplines and organise your bibliography correctly.

1

Matsunaga, Eiji, Isato Araki, and Harukazu Nakamura. "Role of Pax3/7 in the tectum regionalization." Development 128, no. 20 (October 15, 2001): 4069–77. http://dx.doi.org/10.1242/dev.128.20.4069.

Full text
Abstract:
Pax3/7 is expressed in the alar plate of the mesencephalon. The optic tectum differentiates from the alar plate of the mesencephalon, and expression of Pax3/7 is well correlated to the tectum development. To explore the function of Pax3 and Pax7 in the tectum development, we misexpressed Pax3 and Pax7 in the diencephalon and ventral mesencephalon. Morphological and molecular marker gene analysis indicated that Pax3 and Pax7 misexpression caused fate change of the alar plate of the presumptive diencephalon to that of the mesencephalon, that is, a tectum and a torus semicircularis were formed ectopically. Ectopic tectum in the diencephalon appeared to be generated through sequential induction of Fgf8, En2 and Pax3/7. In ventral mesencephalon, which expresses En but does not differentiate to the tectum in normal development, Pax3 and Pax7 misexpression induced ectopic tectum. In normal development, Pax3 and Pax7 expression in the mesencephalon commences after Otx2, En and Pax2/5 expression. In addition, expression domain of Pax3 and Pax7 is well consistent with presumptive tectum region in a dorsoventral axis. Taken together with normal expression pattern of Pax3 and Pax7, results of misexpression experiments suggest that Pax3 and Pax7 define the tectum region subsequent to the function of Otx2 and En.
APA, Harvard, Vancouver, ISO, and other styles
2

Zhou, Hong-Ming, and Simon J. Conway. "Pax3 Hypomorphs Reveal Hidden Pax7 Functional Genetic Compensation in Utero." Journal of Developmental Biology 10, no. 2 (May 17, 2022): 19. http://dx.doi.org/10.3390/jdb10020019.

Full text
Abstract:
Pax3 and Pax7 transcription factors are paralogs within the Pax gene family that that are expressed in early embryos in partially overlapping expression domains and have distinct functions. Significantly, mammalian development is largely unaffected by Pax7 systemic deletion but systemic Pax3 deletion results in defects in neural tube closure, neural crest emigration, cardiac outflow tract septation, muscle hypoplasia and in utero lethality by E14. However, we previously demonstrated that Pax3 hypomorphs expressing only 20% functional Pax3 protein levels exhibit normal neural tube and heart development, but myogenesis is selectively impaired. To determine why only some Pax3-expressing cell lineages are affected and to further titrate Pax3 threshold levels required for neural tube and heart development, we generated hypomorphs containing both a hypomorphic and a null Pax3 allele. This resulted in mutants only expressing 10% functional Pax3 protein with exacerbated neural tube, neural crest and muscle defects, but still a normal heart. To examine why the cardiac neural crest appears resistant to very low Pax3 levels, we examined its paralog Pax7. Significantly, Pax7 expression is both ectopically expressed in Pax3-expressing dorsal neural tube cells and is also upregulated in the Pax3-expressing lineages. To test whether this compensatory Pax7 expression is functional, we deleted Pax7 both systemically and lineage-specifically in hypomorphs expressing only 10% Pax3. Removal of one Pax7 allele resulted in partial outflow tract defects, and complete loss of Pax7 resulted in full penetrance outflow tract defects and in utero lethality. Moreover, combinatorial loss of Pax3 and Pax7 resulted in severe craniofacial defects and a total block of neural crest cell emigration from the neural tube. Pax7Cre lineage mapping revealed ectopic labeling of Pax3-derived neural crest tissues and within the outflow tract of the heart, experimentally confirming the observation of ectopic activation of Pax7 in 10% Pax3 hypomorphs. Finally, genetic cell ablation of Pax7Cre-marked cells is sufficient to cause outflow tract defects in hypomorphs expressing only 10% Pax3, confirming that ectopic and induced Pax7 can play an overlapping functional genetic compensational role in both cardiac neural crest lineage and during craniofacial development, which is normally masked by the dominant role of Pax3.
APA, Harvard, Vancouver, ISO, and other styles
3

Kumar, Deepak, Jennifer L. Shadrach, Amy J. Wagers, and Andrew B. Lassar. "Id3 Is a Direct Transcriptional Target of Pax7 in Quiescent Satellite Cells." Molecular Biology of the Cell 20, no. 14 (July 15, 2009): 3170–77. http://dx.doi.org/10.1091/mbc.e08-12-1185.

Full text
Abstract:
Pax7 is a key regulator of skeletal muscle stem cells and is required along with Pax3 to generate skeletal muscle precursors. We have identified a collection of genes induced by either Pax3 or Pax7 in C2C12 muscle cells. Two notable Pax3/7 targets are the inhibitory helix-loop-helix (HLH) proteins inhibitor of DNA binding (Id) 2 and Id3, both of which are coordinately expressed with Pax7 in quiescent satellite cells and are induced in quiescent C2C12 myogenic cells after ectopic expression of either Pax3 or Pax7. Ectopic Pax7 activates expression of a luciferase reporter driven by the Id3 promoter, and maximal induction of this reporter requires a conserved Pax7 binding site located upstream of the Id3 gene. Chromatin immunoprecipitation indicated that Pax7 is bound upstream of the Id3 promoter in quiescent satellite cells. In addition, short hairpin RNA-mediated knockdown of Pax7 expression in cultured satellite cells coordinately decreased both Id2 and Id3 expression. Together, these findings indicate that Id3 is a direct transcriptional target for Pax7 in quiescent satellite cells, and they suggest that Pax7 acts to block premature differentiation of quiescent satellite cells by inducing the expression of Id2 and Id3, which in turn may act to block either the precocious induction of myogenic basic (b)HLH proteins, the activity of myogenic bHLH proteins, or both.
APA, Harvard, Vancouver, ISO, and other styles
4

Kelly, K. M., R. B. Womer, P. H. Sorensen, Q. B. Xiong, and F. G. Barr. "Common and variant gene fusions predict distinct clinical phenotypes in rhabdomyosarcoma." Journal of Clinical Oncology 15, no. 5 (May 1997): 1831–36. http://dx.doi.org/10.1200/jco.1997.15.5.1831.

Full text
Abstract:
PURPOSE We evaluated the clinical features of the common PAX3-FKHR and variant PAX7-FKHR gene fusions observed in rhabdomyosarcoma. PATIENTS AND METHODS Reverse-transcriptase polymerase chain reaction (RT-PCR) assays were used to detect the gene fusions in 34 cases of rhabdomyosarcoma. Clinical data were obtained retrospectively and compared with the molecular results. RESULTS The PAX3-FKHR and PAX7-FKHR gene fusions were present in tumors from 18 and 16 patients, respectively. The group with a PAX7-FKHR fusion was younger (P = .01) and presented more often with an extremity lesion (82% v 22%; P = .001). PAX7-FKHR tumors were more often localized than PAX3-FKHR tumors (P = .03). In patients with metastatic disease at diagnosis, the patterns were different: PAX7-FKHR patients had metastatic disease that involved only bone (n = 2) and distant nodes (n = 2), while the PAX3-FKHR group had multiple sites involved, including bone (n = 7), marrow (n = 7), lungs (n = 3), distant nodes (n = 2), skin (n = 1), and brain (n = 1). No significant difference in relapse rate was observed. A trend toward improved overall survival in the PAX7-FKHR group was noted (P = .09). Event-free survival for this PAX7-FKHR group was significantly longer (P = .04). CONCLUSION Our results suggest that the common PAX3-FKHR and the variant PAX7-FKHR fusions are associated with distinct clinical phenotypes. Identification of fusion gene status may be a useful diagnostic tool in rhabdomyosarcoma.
APA, Harvard, Vancouver, ISO, and other styles
5

Kirkpatrick, Lisa J., Zipora Yablonka-Reuveni, and Benjamin W. C. Rosser. "Retention of Pax3 Expression in Satellite Cells of Muscle Spindles." Journal of Histochemistry & Cytochemistry 58, no. 4 (December 21, 2009): 317–27. http://dx.doi.org/10.1369/jhc.2009.954792.

Full text
Abstract:
Intrafusal fibers within muscle spindles retain features characteristic of immaturity, unlike the larger and more numerous extrafusal fibers constituting the bulk of skeletal muscle. Satellite cells (SCs), myogenic progenitors, are detected on the surfaces of both intrafusal and extrafusal fibers, but little is known of spindle SCs. We have recently demonstrated that, like their extrafusal counterparts, SCs in muscle spindles of posthatch chickens express paired box transcription factor 7 (Pax7) protein. During vertebrate embryogenesis, myogenic progenitors express both Pax7 and Pax3 proteins. In postnatal mice, Pax3 appears in rare SC subsets, whereas Pax7 is expressed by all SCs within extrafusal fibers. Here we test the hypothesis that Pax3 protein maintains localized expression within SCs of muscle spindles. Immunohistochemical techniques were used to identify SCs by their Pax7 expression within anterior latissimus dorsi muscle excised from posthatch chickens of various ages. A greater percentage of SCs express Pax3 within intrafusal than extrafusal fibers at each age, and the proportion of SCs expressing Pax3 declines with aging. This is the first study to localize Pax3 expression in posthatch avian muscle and within SCs of muscle spindles. We suggest that Pax3-positive SCs are involved in fiber maintenance.
APA, Harvard, Vancouver, ISO, and other styles
6

Relaix, Frédéric, Didier Montarras, Stéphane Zaffran, Barbara Gayraud-Morel, Didier Rocancourt, Shahragim Tajbakhsh, Ahmed Mansouri, Ana Cumano, and Margaret Buckingham. "Pax3 and Pax7 have distinct and overlapping functions in adult muscle progenitor cells." Journal of Cell Biology 172, no. 1 (December 27, 2005): 91–102. http://dx.doi.org/10.1083/jcb.200508044.

Full text
Abstract:
The growth and repair of skeletal muscle after birth depends on satellite cells that are characterized by the expression of Pax7. We show that Pax3, the paralogue of Pax7, is also present in both quiescent and activated satellite cells in many skeletal muscles. Dominant-negative forms of both Pax3 and -7 repress MyoD, but do not interfere with the expression of the other myogenic determination factor, Myf5, which, together with Pax3/7, regulates the myogenic differentiation of these cells. In Pax7 mutants, satellite cells are progressively lost in both Pax3-expressing and -nonexpressing muscles. We show that this is caused by satellite cell death, with effects on the cell cycle. Manipulation of the dominant-negative forms of these factors in satellite cell cultures demonstrates that Pax3 cannot replace the antiapoptotic function of Pax7. These findings underline the importance of cell survival in controlling the stem cell populations of adult tissues and demonstrate a role for upstream factors in this context.
APA, Harvard, Vancouver, ISO, and other styles
7

Sorensen, Poul H. B., James C. Lynch, Stephen J. Qualman, Roberto Tirabosco, Jerian F. Lim, Harold M. Maurer, Julia A. Bridge, William M. Crist, Timothy J. Triche, and Frederic G. Barr. "PAX3-FKHR and PAX7-FKHR Gene Fusions Are Prognostic Indicators in Alveolar Rhabdomyosarcoma: A Report From the Children’s Oncology Group." Journal of Clinical Oncology 20, no. 11 (June 1, 2002): 2672–79. http://dx.doi.org/10.1200/jco.2002.03.137.

Full text
Abstract:
PURPOSE: Alveolar rhabdomyosarcoma (ARMS) is an aggressive soft tissue malignancy of children and adolescents. Most ARMS patients express PAX3-FKHR or PAX7-FKHR gene fusions resulting from t(2;13) or t(1;13) translocations, respectively. We wished to confirm the diagnostic specificity of gene fusion detection in a large cohort of RMS patients and to evaluate whether these alterations influence clinical outcome in ARMS. PATIENTS AND METHODS: We determined PAX3-FKHR or PAX7-FKHR fusion status in 171 childhood rhabdomyosarcoma (RMS) patients entered onto the Intergroup Rhabdomyosarcoma Study IV, including 78 ARMS patients, using established reverse transcriptase polymerase chain reaction assays. All patients received central pathologic review and were treated using uniform protocols, allowing for meaningful outcome analysis. We examined the relationship between gene fusion status and clinical outcome in the ARMS cohort. RESULTS: PAX3-FKHR and PAX7-FKHR fusion transcripts were detected in 55% and 22% of ARMS patients, respectively; 23% were fusion-negative. All other RMS patients lacked transcripts, confirming the specificity of these alterations for ARMS. Fusion status was not associated with outcome differences in patients with locoregional ARMS. However, in patients presenting with metastatic disease, there was a striking difference in outcome between PAX7-FKHR and PAX3-FKHR patient groups (estimated 4-year overall survival rate of 75% for PAX7-FKHR v 8% for PAX3-FKHR; P = .0015). Multivariate analysis demonstrated a significantly increased risk of failure (P = .025) and death (P = .019) in patients with metastatic disease if their tumors expressed PAX3-FKHR. Among metastatic ARMS, bone marrow involvement was significantly higher in PAX3-FKHR–positive patients. CONCLUSION: Not only are PAX-FKHR fusion transcripts specific for ARMS, but expression of PAX3-FKHR and PAX7-FKHR identifies a very high-risk subgroup and a favorable outcome subgroup, respectively, among patients presenting with metastatic ARMS.
APA, Harvard, Vancouver, ISO, and other styles
8

Kuang, Shihuan, Sophie B. Chargé, Patrick Seale, Michael Huh, and Michael A. Rudnicki. "Distinct roles for Pax7 and Pax3 in adult regenerative myogenesis." Journal of Cell Biology 172, no. 1 (January 2, 2006): 103–13. http://dx.doi.org/10.1083/jcb.200508001.

Full text
Abstract:
We assessed viable Pax7−/− mice in 129Sv/J background and observed reduced growth and marked muscle wasting together with a complete absence of functional satellite cells. Acute injury resulted in an extreme deficit in muscle regeneration. However, a small number of regenerated myofibers were detected, suggesting the presence of residual myogenic cells in Pax7-deficient muscle. Rare Pax3+/MyoD+ myoblasts were recovered from Pax7−/− muscle homogenates and cultures of myofiber bundles but not from single myofibers free of interstitial tissues. Finally, we identified Pax3+ cells in the muscle interstitial environment and demonstrated that they coexpressed MyoD during regeneration. Sublaminar satellite cells in hind limb muscle did not express detectable levels of Pax3 protein or messenger RNA. Therefore, we conclude that interstitial Pax3+ cells represent a novel myogenic population that is distinct from the sublaminar satellite cell lineage and that Pax7 is essential for the formation of functional myogenic progenitors from sublaminar satellite cells.
APA, Harvard, Vancouver, ISO, and other styles
9

Hangul, Ceren, Esin Guvenir Celik, Hacer Kaya, Onur Eroglu, Hilmi Uysal, and Sibel Berker Karauzum. "Estradiol differentially regulates DUX4, β-catenin and PAX3/PAX7 in primary myoblasts of facioscapulohumeral muscular dystrophy patients." Turkish Journal of Biochemistry 46, no. 4 (January 5, 2021): 435–44. http://dx.doi.org/10.1515/tjb-2020-0351.

Full text
Abstract:
Abstract Objectives There is a clinical variability and heterogeneity among Facioscapulohumeral Muscular Dystrophy (FSHD) patients. Escalation after menopause in women, early onset in men suggests that estrogen might be a protective factor on the course of FSHD. In spite of few molecular studies supporting the protective role of estrogen in FSHD in vitro, there is no study revealing the effect of estradiol on the protein levels of DUX4, β-catenin and PAX3/PAX7. In present study, we investigated the effect of estradiol treatment on the expressions of DUX4, β-catenin and PAX3/PAX7 protein levels. Materials and Methods Primary myoblasts of 63 and 71 years old (63yM/71yM) males; 47 years old (47yF) female FSHD patients were used. Cells were processed under these conditions; (i) untreated, (ii) 10 nM-30 min estradiol and (iii) 10 nM-4 h estradiol treated. The expression of DUX4, PAX3/PAX7 and β-catenin were examined by western-blotting. Results Expression of DUX4 significantly downregulated after 4 h treatment of estradiol while PAX3/PAX7 56 kDa variant expression upregulated in 71yM cells. β-catenin and PAX3 expression was variable among the samples. Conclusion Our results suggest that estrogen might be a palliative treatment option via downregulation of DUX4 protein in DUX4 expressing FSHD patients.
APA, Harvard, Vancouver, ISO, and other styles
10

Kelly, Kara M., Richard B. Womer, and Frederic G. Barr. "PAX3-FKHR and PAX7-FKHR." Journal of Pediatric Hematology/Oncology 20, no. 5 (September 1998): 517. http://dx.doi.org/10.1097/00043426-199809000-00027.

Full text
APA, Harvard, Vancouver, ISO, and other styles
11

Manceau, Line, Julien Richard Albert, Pier-Luigi Lollini, Maxim V. C. Greenberg, Pascale Gilardi-Hebenstreit, and Vanessa Ribes. "Divergent transcriptional and transforming properties of PAX3-FOXO1 and PAX7-FOXO1 paralogs." PLOS Genetics 18, no. 5 (May 23, 2022): e1009782. http://dx.doi.org/10.1371/journal.pgen.1009782.

Full text
Abstract:
The hallmarks of the alveolar subclass of rhabdomyosarcoma are chromosomal translocations that generate chimeric PAX3-FOXO1 or PAX7-FOXO1 transcription factors. Overexpression of either PAX-FOXO1s results in related cell transformation in animal models. Yet, in patients the two structural genetic aberrations they derived from are associated with distinct pathological manifestations. To assess the mechanisms underlying these differences, we generated isogenic fibroblast lines expressing either PAX-FOXO1 paralog. Mapping of their genomic recruitment using CUT&Tag revealed that the two chimeric proteins have distinct DNA binding preferences. In addition, PAX7-FOXO1 binding results in greater recruitment of the H3K27ac activation mark than PAX3-FOXO1 binding and is accompanied by greater transcriptional activation of neighbouring genes. These effects are associated with a PAX-FOXO1-specific alteration in the expression of genes regulating cell shape and the cell cycle. Consistently, PAX3-FOXO1 accentuates fibroblast cellular traits associated with contractility and surface adhesion and limits entry into S phase. In contrast, PAX7-FOXO1 drives cells to adopt an amoeboid shape, reduces entry into M phase, and causes increased DNA damage. Altogether, our results argue that the diversity of rhabdomyosarcoma manifestation arises, in part, from the divergence between the genomic occupancy and transcriptional activity of PAX3-FOXO1 and PAX7-FOXO1.
APA, Harvard, Vancouver, ISO, and other styles
12

Borycki, A. G., J. Li, F. Jin, C. P. Emerson, and J. A. Epstein. "Pax3 functions in cell survival and in pax7 regulation." Development 126, no. 8 (April 15, 1999): 1665–74. http://dx.doi.org/10.1242/dev.126.8.1665.

Full text
Abstract:
In developing vertebrate embryos, Pax3 is expressed in the neural tube and in the paraxial mesoderm that gives rise to skeletal muscles. Pax3 mutants develop muscular and neural tube defects; furthermore, Pax3 is essential for the proper activation of the myogenic determination factor gene, MyoD, during early muscle development and PAX3 chromosomal translocations result in muscle tumors, providing evidence that Pax3 has diverse functions in myogenesis. To investigate the specific functions of Pax3 in development, we have examined cell survival and gene expression in presomitic mesoderm, somites and neural tube of developing wild-type and Pax3 mutant (Splotch) mouse embryos. Disruption of Pax3 expression by antisense oligonucleotides significantly impairs MyoD activation by signals from neural tube/notochord and surface ectoderm in cultured presomitic mesoderm (PSM), and is accompanied by a marked increase in programmed cell death. In Pax3 mutant (Splotch) embryos, MyoD is activated normally in the hypaxial somite, but MyoD-expressing cells are disorganized and apoptosis is prevalent in newly formed somites, but not in the neural tube or mature somites. In neural tube and somite regions where cell survival is maintained, the closely related Pax7 gene is upregulated, and its expression becomes expanded into the dorsal neural tube and somites, where Pax3 would normally be expressed. These results establish that Pax3 has complementary functions in MyoD activation and inhibition of apoptosis in the somitic mesoderm and in repression of Pax7 during neural tube and somite development.
APA, Harvard, Vancouver, ISO, and other styles
13

Incitti, Tania, Alessandro Magli, Radbod Darabi, Ce Yuan, Karena Lin, Robert W. Arpke, Karim Azzag, et al. "Pluripotent stem cell-derived myogenic progenitors remodel their molecular signature upon in vivo engraftment." Proceedings of the National Academy of Sciences 116, no. 10 (February 13, 2019): 4346–51. http://dx.doi.org/10.1073/pnas.1808303116.

Full text
Abstract:
Optimal cell-based therapies for the treatment of muscle degenerative disorders should not only regenerate fibers but provide a quiescent satellite cell pool ensuring long-term maintenance and regeneration. Conditional expression of Pax3/Pax7 in differentiating pluripotent stem cells (PSCs) allows the generation of myogenic progenitors endowed with enhanced regenerative capacity. To identify the molecular determinants underlying their regenerative potential, we performed transcriptome analyses of these cells along with primary myogenic cells from several developmental stages. Here we show that in vitro-generated PSC-derived myogenic progenitors possess a molecular signature similar to embryonic/fetal myoblasts. However, compared with fetal myoblasts, following transplantation they show superior myofiber engraftment and ability to seed the satellite cell niche, respond to multiple reinjuries, and contribute to long-term regeneration. Upon engraftment, the transcriptome of reisolated Pax3/Pax7–induced PSC-derived myogenic progenitors changes toward a postnatal molecular signature, particularly in genes involved in extracellular matrix remodeling. These findings demonstrate that Pax3/Pax7–induced myogenic progenitors remodel their molecular signature and functionally mature upon in vivo exposure to the adult muscle environment.
APA, Harvard, Vancouver, ISO, and other styles
14

Matsunaga, E., I. Araki, and H. Nakamura. "Pax6 defines the di-mesencephalic boundary by repressing En1 and Pax2." Development 127, no. 11 (June 1, 2000): 2357–65. http://dx.doi.org/10.1242/dev.127.11.2357.

Full text
Abstract:
Transcriptional factors and signaling molecules are responsible for regionalization of the central nervous system. In the early stage of neural development, Pax6 is expressed in the prosencephalon, while En1 and Pax2 are expressed in the mesencephalon. Here, we misexpressed Pax6 in the mesencephalon to elucidate the mechanism of the di-mesencephalic boundary formation. Histological analysis, expression patterns of diencephalic marker genes, and fiber trajectory of the posterior commissure indicated that Pax6 misexpression caused a caudal shift of the di-mesencephalic boundary. Pax6 repressed En1, Pax2 and other tectum (mesencephalon)-related genes such as En2, Pax5, Pax7, but induced Tcf4, a diencephalon marker gene. To know how Pax6 represses En1 and Pax2, we ectopically expressed a dominant-active or negative form of Pax6. The dominant-active form of Pax6 showed a similar but more severe phenotype than Pax6, while the dominant-negative form showed an opposite phenotype, suggesting that Pax6 acts as a transcriptional activator. Thus Pax6 may repress tectum-related genes by activating an intervening repressor. The results of misexpression experiments, together with normal expression patterns of Pax6, En1 and Pax2, suggest that repressive interaction between Pax6 and En1/Pax2 defines the di-mesencephalic boundary.
APA, Harvard, Vancouver, ISO, and other styles
15

Nowoshilow, Sergej, Siegfried Schloissnig, Ji-Feng Fei, Andreas Dahl, Andy W. C. Pang, Martin Pippel, Sylke Winkler, et al. "The axolotl genome and the evolution of key tissue formation regulators." Nature 554, no. 7690 (January 24, 2018): 50–55. http://dx.doi.org/10.1038/nature25458.

Full text
Abstract:
Abstract Salamanders serve as important tetrapod models for developmental, regeneration and evolutionary studies. An extensive molecular toolkit makes the Mexican axolotl (Ambystoma mexicanum) a key representative salamander for molecular investigations. Here we report the sequencing and assembly of the 32-gigabase-pair axolotl genome using an approach that combined long-read sequencing, optical mapping and development of a new genome assembler (MARVEL). We observed a size expansion of introns and intergenic regions, largely attributable to multiplication of long terminal repeat retroelements. We provide evidence that intron size in developmental genes is under constraint and that species-restricted genes may contribute to limb regeneration. The axolotl genome assembly does not contain the essential developmental gene Pax3. However, mutation of the axolotl Pax3 paralogue Pax7 resulted in an axolotl phenotype that was similar to those seen in Pax3 −/− and Pax7 −/− mutant mice. The axolotl genome provides a rich biological resource for developmental and evolutionary studies.
APA, Harvard, Vancouver, ISO, and other styles
16

Zalc, Antoine, and Frédéric Relaix. "Pax3 et Pax7 : gardiens du développement craniofacial." médecine/sciences 31, no. 8-9 (August 2015): 723–25. http://dx.doi.org/10.1051/medsci/20153108007.

Full text
APA, Harvard, Vancouver, ISO, and other styles
17

Helm, Bryan R., Xiaohui Zhan, Pankita H. Pandya, Mary E. Murray, Karen E. Pollok, Jamie L. Renbarger, Michael J. Ferguson, et al. "Gene Co-Expression Networks Restructured Gene Fusion in Rhabdomyosarcoma Cancers." Genes 10, no. 9 (August 30, 2019): 665. http://dx.doi.org/10.3390/genes10090665.

Full text
Abstract:
Rhabdomyosarcoma is subclassified by the presence or absence of a recurrent chromosome translocation that fuses the FOXO1 and PAX3 or PAX7 genes. The fusion protein (FOXO1-PAX3/7) retains both binding domains and becomes a novel and potent transcriptional regulator in rhabdomyosarcoma subtypes. Many studies have characterized and integrated genomic, transcriptomic, and epigenomic differences among rhabdomyosarcoma subtypes that contain the FOXO1-PAX3/7 gene fusion and those that do not; however, few investigations have investigated how gene co-expression networks are altered by FOXO1-PAX3/7. Although transcriptional data offer insight into one level of functional regulation, gene co-expression networks have the potential to identify biological interactions and pathways that underpin oncogenesis and tumorigenicity. Thus, we examined gene co-expression networks for rhabdomyosarcoma that were FOXO1-PAX3 positive, FOXO1-PAX7 positive, or fusion negative. Gene co-expression networks were mined using local maximum Quasi-Clique Merger (lmQCM) and analyzed for co-expression differences among rhabdomyosarcoma subtypes. This analysis observed 41 co-expression modules that were shared between fusion negative and positive samples, of which 17/41 showed significant up- or down-regulation in respect to fusion status. Fusion positive and negative rhabdomyosarcoma showed differing modularity of co-expression networks with fusion negative (n = 109) having significantly more individual modules than fusion positive (n = 53). Subsequent analysis of gene co-expression networks for PAX3 and PAX7 type fusions observed 17/53 were differentially expressed between the two subtypes. Gene list enrichment analysis found that gene ontology terms were poorly matched with biological processes and molecular function for most co-expression modules identified in this study; however, co-expressed modules were frequently localized to cytobands on chromosomes 8 and 11. Overall, we observed substantial restructuring of co-expression networks relative to fusion status and fusion type in rhabdomyosarcoma and identified previously overlooked genes and pathways that may be targeted in this pernicious disease.
APA, Harvard, Vancouver, ISO, and other styles
18

Mansouri, A., A. Stoykova, M. Torres, and P. Gruss. "Dysgenesis of cephalic neural crest derivatives in Pax7−/− mutant mice." Development 122, no. 3 (March 1, 1996): 831–38. http://dx.doi.org/10.1242/dev.122.3.831.

Full text
Abstract:
Pax7 is a member of the paired box containing gene family. Its expression pattern suggests a function in cephalic neural crest derivatives, skeletal muscle and central nervous system development. To understand the role of Pax7 during mouse embryogenesis, we used the homologous recombination technique in embryonic stem cells and generated Pax7−/− mice. Homozygous animals are born but die shortly afer weaning. They exhibit malformations in facial structures involving the maxilla and nose. Our analysis suggests that the observed phenotype is due to a cephalic neural crest defect. No obvious phenotype could be detected in the central nervous system and skeletal muscle. Functional redundancy between Pax7 and Pax3 is discussed.
APA, Harvard, Vancouver, ISO, and other styles
19

Buckingham, Margaret, and Frédéric Relaix. "PAX3 and PAX7 as upstream regulators of myogenesis." Seminars in Cell & Developmental Biology 44 (August 2015): 115–25. http://dx.doi.org/10.1016/j.semcdb.2015.09.017.

Full text
APA, Harvard, Vancouver, ISO, and other styles
20

Lagha, Mounia, Didier Rocancourt, and Frédéric Relaix. "Origine du muscle squelettique : rôles de Pax3/Pax7." médecine/sciences 21, no. 10 (October 2005): 801–3. http://dx.doi.org/10.1051/medsci/20052110801.

Full text
APA, Harvard, Vancouver, ISO, and other styles
21

Shaw, Taryn, Kay Nakazawa, Purushottam Tiwari, Eryn Nelson, Jeffrey Formen, Christian Wolf, Jeffrey Toretsky, and Aykut Üren. "Abstract 1093: Small molecule inhibitors of the PAX3::FOXO1 fusion protein in rhabdomyosarcoma." Cancer Research 84, no. 6_Supplement (March 22, 2024): 1093. http://dx.doi.org/10.1158/1538-7445.am2024-1093.

Full text
Abstract:
Abstract Rhabdomyosarcoma (RMS) is the most common pediatric soft tissue sarcoma. It is commonly divided into subtypes based on histopathological appearance. The oncogenic fusion proteins PAX3::FOXO1 or PAX7::FOXO1 are present in the alveolar subtype of RMS (ARMS). These chimeric proteins are formed by reciprocal chromosomal translocations and consist of an N-terminal portion of the PAX3 or PAX7 transcription factor fused to a C-terminal portion of the FOXO1 transcription factor. These fusion proteins have been shown to drive malignant transformation in ARMS, and patients with fusion-positive ARMS have a worse prognosis than patients with fusion-negative ARMS and embryonal RMS. We recently reported that piperacetazine, a phenothiazine derivative and first-generation antipsychotic, is capable of binding to and inhibiting the transcriptional activity of PAX3::FOXO1, reducing the expression of PAX3::FOXO1 target genes, and inhibiting the ability of fusion-positive RMS cells to grow in soft agar. We hypothesize that other phenothiazine derivatives may have stronger binding affinity for PAX3::FOXO1 and greater ability to reduce tumor growth in vivo. We employed a structure-activity relationship campaign to develop new phenothiazine derivatives that may be more potent inhibitors of PAX3::FOXO1 than piperacetazine. We synthesized and tested 10 new compounds, in addition to 9 existing FDA-approved phenothiazine derivatives, for their ability to bind to PAX3::FOXO1 and inhibit its transcriptional activity and target gene expression as well as inhibiting the growth of fusion-positive RMS cells in 3D culture. Seven derivatives inhibited PAX3::FOXO1 reporter activity better than piperacetazine, nine of them performed worse, and three of them showed comparable activity to piperacetazine. We demonstrated that piperacetazine does not alter PAX3::FOXO1 levels, subcellular localization, binding to a PAX3::FOXO1 target DNA sequence, or phosphorylation at Ser256 in the FOXO1 portion of the fusion protein. We therefore hypothesize that piperacetazine may be disrupting interactions between PAX3::FOXO1 and its partner proteins. We are employing a proximity-based biotinylation method to identify proteins that are competed away from PAX3::FOXO1 by piperacetazine. Our data suggest that it is possible to target PAX3::FOXO1 protein using small molecules that can directly bind to it and inhibit its activity in fusion-positive RMS cells. Citation Format: Taryn Shaw, Kay Nakazawa, Purushottam Tiwari, Eryn Nelson, Jeffrey Formen, Christian Wolf, Jeffrey Toretsky, Aykut Üren. Small molecule inhibitors of the PAX3::FOXO1 fusion protein in rhabdomyosarcoma [abstract]. In: Proceedings of the American Association for Cancer Research Annual Meeting 2024; Part 1 (Regular Abstracts); 2024 Apr 5-10; San Diego, CA. Philadelphia (PA): AACR; Cancer Res 2024;84(6_Suppl):Abstract nr 1093.
APA, Harvard, Vancouver, ISO, and other styles
22

Gonzalez Curto, Gloria, Audrey Der Vartanian, Youcef El-Mokhtar Frarma, Line Manceau, Lorenzo Baldi, Selene Prisco, Nabila Elarouci, et al. "The PAX-FOXO1s trigger fast trans-differentiation of chick embryonic neural cells into alveolar rhabdomyosarcoma with tissue invasive properties limited by S phase entry inhibition." PLOS Genetics 16, no. 11 (November 11, 2020): e1009164. http://dx.doi.org/10.1371/journal.pgen.1009164.

Full text
Abstract:
The chromosome translocations generating PAX3-FOXO1 and PAX7-FOXO1 chimeric proteins are the primary hallmarks of the paediatric fusion-positive alveolar subtype of Rhabdomyosarcoma (FP-RMS). Despite the ability of these transcription factors to remodel chromatin landscapes and promote the expression of tumour driver genes, they only inefficiently promote malignant transformation in vivo. The reason for this is unclear. To address this, we developed an in ovo model to follow the response of spinal cord progenitors to PAX-FOXO1s. Our data demonstrate that PAX-FOXO1s, but not wild-type PAX3 or PAX7, trigger the trans-differentiation of neural cells into FP-RMS-like cells with myogenic characteristics. In parallel, PAX-FOXO1s remodel the neural pseudo-stratified epithelium into a cohesive mesenchyme capable of tissue invasion. Surprisingly, expression of PAX-FOXO1s, similar to wild-type PAX3/7, reduce the levels of CDK-CYCLIN activity and increase the fraction of cells in G1. Introduction of CYCLIN D1 or MYCN overcomes this PAX-FOXO1-mediated cell cycle inhibition and promotes tumour growth. Together, our findings reveal a mechanism that can explain the apparent limited oncogenicity of PAX-FOXO1 fusion transcription factors. They are also consistent with certain clinical reports indicative of a neural origin of FP-RMS.
APA, Harvard, Vancouver, ISO, and other styles
23

Lagutina, Irina, Simon J. Conway, Jack Sublett, and Gerard C. Grosveld. "Pax3-FKHR Knock-In Mice Show Developmental Aberrations but Do Not Develop Tumors." Molecular and Cellular Biology 22, no. 20 (October 15, 2002): 7204–16. http://dx.doi.org/10.1128/mcb.22.20.7204-7216.2002.

Full text
Abstract:
ABSTRACT Alveolar rhabdomyosarcoma is a pediatric disease specified by the recurrent chromosome translocations t(2;13) and t(1;13). These translocations result in the formation of the PAX3-FKHR and PAX7-FKHR fusion genes, which are thought to play a causal role in the genesis of this disease. Although PAX3-FKHR exhibits transforming activity in immortalized fibroblast cell lines, a direct role of this fusion protein in tumorigenesis in vivo has not been shown. We determined whether expression of Pax3-FKHR in the mouse germ line would render these animals prone to the development of rhabdomyosarcomas. By targeting FKHR cDNA sequences into the Pax3 locus of embryonic stem cells, we used these cells to generate mice carrying a Pax3-FKHR knock-in allele. Despite low expression of the knock-in allele, heterozygous offspring of Pax3-FKHR chimeric mice showed developmental abnormalities. These included intraventricular septum defects, tricuspid valve insufficiency, and diaphragm defects, which caused congestive heart failure leading to perinatal death. In addition, Pax3-FKHR heterozygous offspring displayed malformations of some but not all hypaxial muscles. However, neither newborn heterozygous pups nor their chimeric parents showed any signs of malignancy. We conclude that the Pax3-FKHR allele causes lethal developmental defects in knock-in mice but might be insufficient to cause muscle tumors.
APA, Harvard, Vancouver, ISO, and other styles
24

Kadzik, Rachel S., Tiffany L. Barnes, Lisa M. Galli, Katie Sanders, and Laura W. Burrus. "Divergent proliferative roles for Pax3 and Pax7 in chick." Developmental Biology 295, no. 1 (July 2006): 362. http://dx.doi.org/10.1016/j.ydbio.2006.04.114.

Full text
APA, Harvard, Vancouver, ISO, and other styles
25

Missiaglia, Edoardo, Dan Williamson, Julia Chisholm, Pratyaksha Wirapati, Gaëlle Pierron, Fabien Petel, Jean-Paul Concordet, et al. "PAX3/FOXO1 Fusion Gene Status Is the Key Prognostic Molecular Marker in Rhabdomyosarcoma and Significantly Improves Current Risk Stratification." Journal of Clinical Oncology 30, no. 14 (May 10, 2012): 1670–77. http://dx.doi.org/10.1200/jco.2011.38.5591.

Full text
Abstract:
Purpose To improve the risk stratification of patients with rhabdomyosarcoma (RMS) through the use of clinical and molecular biologic data. Patients and Methods Two independent data sets of gene-expression profiling for 124 and 101 patients with RMS were used to derive prognostic gene signatures by using a meta-analysis. These and a previously published metagene signature were evaluated by using cross validation analyses. A combined clinical and molecular risk-stratification scheme that incorporated the PAX3/FOXO1 fusion gene status was derived from 287 patients with RMS and evaluated. Results We showed that our prognostic gene-expression signature and the one previously published performed well with reproducible and significant effects. However, their effect was reduced when cross validated or tested in independent data and did not add new prognostic information over the fusion gene status, which is simpler to assay. Among nonmetastatic patients, patients who were PAX3/FOXO1 positive had a significantly poorer outcome compared with both alveolar-negative and PAX7/FOXO1-positive patients. Furthermore, a new clinicomolecular risk score that incorporated fusion gene status (negative and PAX3/FOXO1 and PAX7/FOXO1 positive), Intergroup Rhabdomyosarcoma Study TNM stage, and age showed a significant increase in performance over the current risk-stratification scheme. Conclusion Gene signatures can improve current stratification of patients with RMS but will require complex assays to be developed and extensive validation before clinical application. A significant majority of their prognostic value was encapsulated by the fusion gene status. A continuous risk score derived from the combination of clinical parameters with the presence or absence of PAX3/FOXO1 represents a robust approach to improving current risk-adapted therapy for RMS.
APA, Harvard, Vancouver, ISO, and other styles
26

Du, Shouying, Eric J. Lawrence, Donna Strzelecki, Prerna Rajput, Shujuan J. Xia, Dina M. Gottesman, and Frederic G. Barr. "Co-expression of alternatively spliced forms of PAX3, PAX7, PAX3-FKHR and PAX7-FKHR with distinct DNA binding and transactivation properties in rhabdomyosarcoma." International Journal of Cancer 115, no. 1 (2005): 85–92. http://dx.doi.org/10.1002/ijc.20844.

Full text
APA, Harvard, Vancouver, ISO, and other styles
27

Bois, Philippe R. J., Kamel Izeradjene, Peter J. Houghton, John L. Cleveland, Janet A. Houghton, and Gerard C. Grosveld. "FOXO1a acts as a selective tumor suppressor in alveolar rhabdomyosarcoma." Journal of Cell Biology 170, no. 6 (September 12, 2005): 903–12. http://dx.doi.org/10.1083/jcb.200501040.

Full text
Abstract:
Rhabdomyosarcoma (RMS), the most common pediatric soft-tissue sarcoma, has two major histological subtypes: embryonal RMS (ERMS), which has a favorable prognosis, and alveolar RMS (ARMS), which has a poor outcome. Although both forms of RMS express muscle cell–specific markers, only ARMS cells express PAX3-FOXO1a or PAX7-FOXO1a chimeric proteins. In mice, Pax3 and Pax7 play key roles in muscle cell development and differentiation, and FoxO1a regulates myoblast differentiation and fusion; thus, the aberrant regulation of these proteins may contribute to the development of ARMS. In this paper, we report that FOXO1a is not expressed in primary ARMS tumors or ARMS-derived tumor cell lines and that restoration of FOXO1a expression in ARMS cells is sufficient to induce cell cycle arrest and apoptosis. Strikingly, the effects of FOXO1a are selective, as enforced expression of FOXO1a in ERMS-derived tumor cell lines had no effect. Furthermore, FOXO1a induced apoptosis in ARMS by directly activating the transcription of caspase-3. We conclude that FOXO1a is a potent and specific tumor suppressor in ARMS, suggesting that agents that restore or augment FOXO1a activity may be effective as ARMS therapeutics.
APA, Harvard, Vancouver, ISO, and other styles
28

Pelletier, Audrey, Alexandre Mayran, Arthur Gouhier, James G. Omichinski, Aurelio Balsalobre, and Jacques Drouin. "Pax7 pioneer factor action requires both paired and homeo DNA binding domains." Nucleic Acids Research 49, no. 13 (July 1, 2021): 7424–36. http://dx.doi.org/10.1093/nar/gkab561.

Full text
Abstract:
Abstract The pioneer transcription factor Pax7 contains two DNA binding domains (DBD), a paired and a homeo domain. Previous work on Pax7 and the related Pax3 showed that each DBD binds a cognate DNA sequence, thus defining two targets of binding and possibly modalities of action. Genomic targets of Pax7 pioneer action leading to chromatin opening are enriched for composite DNA target sites containing juxtaposed sites for both paired and homeo domains. The present work investigated the implication of the DBDs in pioneer action. We show that the composite sequence is a higher affinity binding site and that efficient binding to this site involves both DBDs of the same Pax7 molecule. This binding is not sensitive to cytosine methylation of the DNA sites consistent with pioneer action within nucleosomal heterochromatin. Introduction of single amino acid mutations in either paired or homeo domain that impair binding to cognate DNA sequences showed that both DBDs must be intact for pioneer action. In contrast, only the paired domain is required for low affinity binding of heterochromatin sites. Thus, Pax7 pioneer action on heterochromatin requires unique protein:DNA interactions that are more complex compared to its simpler DNA binding modalities at accessible enhancer target sites.
APA, Harvard, Vancouver, ISO, and other styles
29

Mansouri, Ahmed. "The Role of Pax3 and Pax7 in Development and Cancer." Critical Reviews™ in Oncogenesis 9, no. 2 (1998): 141–50. http://dx.doi.org/10.1615/critrevoncog.v9.i2.40.

Full text
APA, Harvard, Vancouver, ISO, and other styles
30

Horst, David, Svetlana Ustanina, Consolato Sergi, Gregor Mikuz, Herbert Juergens, Thomas Braun, and Eugene Vorobyov. "Comparative expression analysis of Pax3 and Pax7 during mouse myogenesis." International Journal of Developmental Biology 50, no. 1 (2006): 47–54. http://dx.doi.org/10.1387/ijdb.052111dh.

Full text
APA, Harvard, Vancouver, ISO, and other styles
31

Relaix, Frédéric, Didier Rocancourt, Ahmed Mansouri, and Margaret Buckingham. "A Pax3/Pax7-dependent population of skeletal muscle progenitor cells." Nature 435, no. 7044 (April 20, 2005): 948–53. http://dx.doi.org/10.1038/nature03594.

Full text
APA, Harvard, Vancouver, ISO, and other styles
32

Otto, Anthony, Corina Schmidt, and Ketan Patel. "Pax3 and Pax7 expression and regulation in the avian embryo." Anatomy and Embryology 211, no. 4 (February 28, 2006): 293–310. http://dx.doi.org/10.1007/s00429-006-0083-3.

Full text
APA, Harvard, Vancouver, ISO, and other styles
33

Keller, C. "Pax3:Fkhr interferes with embryonic Pax3 and Pax7 function: implications for alveolar rhabdomyosarcoma cell of origin." Genes & Development 18, no. 21 (November 1, 2004): 2608–13. http://dx.doi.org/10.1101/gad.1243904.

Full text
APA, Harvard, Vancouver, ISO, and other styles
34

Lozano-Velasco, Estefanía, Alejandra Contreras, Colin Crist, Francisco Hernández-Torres, Diego Franco, and Amelia E. Aránega. "Pitx2c modulates Pax3+/Pax7+ cell populations and regulates Pax3 expression by repressing miR27 expression during myogenesis." Developmental Biology 357, no. 1 (September 2011): 165–78. http://dx.doi.org/10.1016/j.ydbio.2011.06.039.

Full text
APA, Harvard, Vancouver, ISO, and other styles
35

Horwitz, Marshall S., and Matthew R. Hart. "Co-Opting the Genetic Redundancy of the Pax Family to Treat PAX5 Mutated Pre-B ALL." Blood 126, no. 23 (December 3, 2015): 2445. http://dx.doi.org/10.1182/blood.v126.23.2445.2445.

Full text
Abstract:
Abstract Pre-B cell ALL is the most common pediatric malignancy. More than a third of cases acquire loss-of-function mutations of PAX5, a regulatory transcription factor which is required for the differentiation of B lymphocytes. Additionally, germline loss of function PAX5 mutation is a cause of familial pre-B cell ALL. These observations indicate that loss of PAX5 activity drives leukemogenesis. We have seen that PAX5 re-expression in PAX5 -mutated pre-B cell ALL restores differentiation capacity and promotes apoptosis. However, because the gene is deleted or otherwise mutated it may not be possible to easily repair or restore PAX5 expression in leukemic cells. Nevertheless, PAX5 possesses two closely related paralogs, PAX2 and PAX8, which are structurally and functionally similar to PAX5, yet are neither expressed in lymphocytes nor mutated in ALL. Toward the goal of exploiting PAX family genomic redundancy for therapeutic purposes, we have tested the ability of PAX2 and PAX8 to replace PAX5 in pre-B ALL cell lines. Preliminary results indicate that both PAX2 and PAX8 rescue B cell differentiation and function similarly to PAX5 in this context. These results include modulation of B cell developmental markers, CD10, CD19 and CD22, as well as induction of PAX5 target genes, CD79a and BACH2. Cells also display a reduction in size which may be indicative of the large to small B cell transition and importantly show increased levels of cell death following PAX2 and PAX8 expression. We have further investigated the epigenetic status of PAX2 and PAX8 promoters in B cells and find that both loci are hypermethylated, suggesting that demethylation with agents such as methotrexate, may represent a therapeutic entry point for activating expression of PAX5 paralogs. Finally, based on observations that electrical polarization during early embryogenesis regulates developmental transcription factor expression, including for PAX genes, we have tested the ability of approved drugs targeting ion channels for their ability to induce PAX factor expression and thereby complement for loss of PAX5 in pre-B cell ALL. The anti-parasitic drug ivermectin, which activates chloride channels, is one of several compounds that appear promising in early studies. Disclosures No relevant conflicts of interest to declare.
APA, Harvard, Vancouver, ISO, and other styles
36

Guram, Sheena, Julia Dirks, Shivali Barot, Anthony Griffin, Ilan Weinreb, Elizabeth Demicco, David Benjamin Shultz, Albiruni Ryan Abdul Razak, Rebecca Anne Gladdy, and Abha A. Gupta. "Is PAX3-FOXO1 associated with worse outcome in adults with rhabdomyosarcoma (RMS)?" Journal of Clinical Oncology 37, no. 15_suppl (May 20, 2019): e22525-e22525. http://dx.doi.org/10.1200/jco.2019.37.15_suppl.e22525.

Full text
Abstract:
e22525 Background: Rhabdomyosarcoma (RMS) is a rare soft tissue sarcoma in adults. The PAX3-FOXO1 fusion gene is associated with alveolar rhabdomyosarcoma. PAX3-FOXO1 results from a stable reciprocal translocation of chromosomes 2 and 13, which fuses in-frame the DNA binding domain of PAX3 with the transactivation domain of FOXO1. Occasionally, PAX7-FOXO1 is expressed. In children, the PAX3-FOXO1 fusion gene is associated with worse outcome. We evaluated the prognostic role of FOXO1 fusion status in adults with RMS treated in a single, large volume sarcoma centre. Methods: A retrospective review of adult RMS patients (pts) diagnosed from 1984 to 2018 was done. Information on demographics, treatment, fusion status and survival was collected. Primary favourable site was defined as tumour arising in orbit, non-bladder/prostate genitourinary system and non-parameningeal head and neck. Factors were compared using Fisher’s Exact test. Event-free survival (EFS) was estimated by the Kaplan-Meier method and compared with log rank test. FOXO1 fusion status was coded as FP (fusion positive) or FN (fusion negative). Results: Of 134 pts identified in our database, fusion testing was performed in 55 (41%). Of these, PAX3 fusion was detected in 22 (40%). PAX7 was not detected. The median age of FP and FN pts was 25 yrs (range 18, 90) and 27 yrs (range 18, 65), respectively. Gender distribution was similar between FP and FN. Favourable site was seen in 13 (60%) FP and 21 (64%) FN. Nodal disease was present in 21 (95%) FP and 21 (64%) FN (p = 0.02). Distant metastases were present in 10 (45%) FP and 9 (27%) FN (n.s.). Treatment received was as follows for FP and FN, respectively: chemotherapy (21(95%), 33(100%)), radiation (14(64%), 22(67%)) and surgery (4(18%), 17(52%)). 5-yr EFS for pts without distant metastases was 27% (CI 22.6-76.6) and 46% (CI 21.5 – 70.5) for FP and FN respectively (n.s.). Conclusions: FP and FN RMS occurs in adults of all ages. Similar to children, adults with FP are more likely to present with nodal disease. Our study did not show that fusion status was associated with poorer EFS in adult RMS, however, larger series are needed to confirm this preliminary data.
APA, Harvard, Vancouver, ISO, and other styles
37

Wang, Mengya, Weihao Song, Chaofan Jin, Kejia Huang, Qianwen Yu, Jie Qi, Quanqi Zhang, and Yan He. "Pax3 and Pax7 Exhibit Distinct and Overlapping Functions in Marking Muscle Satellite Cells and Muscle Repair in a Marine Teleost, Sebastes schlegelii." International Journal of Molecular Sciences 22, no. 7 (April 5, 2021): 3769. http://dx.doi.org/10.3390/ijms22073769.

Full text
Abstract:
Pax3 and Pax7 are members of the Pax gene family which are essential for embryo and organ development. Both genes have been proved to be markers of muscle satellite cells and play key roles in the process of muscle growth and repair. Here, we identified two Pax3 genes (SsPax3a and SsPax3b) and two Pax7 genes (SsPax7a and SsPax7b) in a marine teleost, black rockfish (Sebastes schlegelii). Our results showed SsPax3 and SsPax7 marked distinct populations of muscle satellite cells, which originated from the multi-cell stage and somite stage, respectively. In addition, we constructed a muscle injury model to explore the function of these four genes during muscle repair. Hematoxylin–eosin (H–E) of injured muscle sections showed new-formed myofibers occurred at 16 days post-injury (dpi). ISH (in situ hybridization) analysis demonstrated that the expression level of SsPax3a and two SsPax7 genes increased gradually during 0–16 dpi and peaked at 16 dpi. Interestingly, SsPax3b showed no significant differences during the injury repair process, indicating that the satellite cells labeled by SsPax3b were not involved in muscle repair. These results imply that the muscle stem cell populations in teleosts are more complicated than in mammals. This lays the foundation for future studies on the molecular mechanism of indeterminant growth and muscle repair of large fish species.
APA, Harvard, Vancouver, ISO, and other styles
38

Tarnowski, Maciek, Radoslaw Maksym, Ryan Reca, Mariusz Z. Ratajczak, and Magdalena Kucia. "Expression of CXCR4 and CXCR7 Receptors for Stromal Derived Factor-1 (SDF- 1) Is Differently Regulated in Human Rhabdomyosarcomas (RMS): The Biological Consequences." Blood 112, no. 11 (November 16, 2008): 4764. http://dx.doi.org/10.1182/blood.v112.11.4764.4764.

Full text
Abstract:
Abstract Rhabdomyosarcoma (RMS) is the most common soft-tissue sarcoma of adolescents and children that frequently infiltrates bone marrow (BM). RMS is divided in two sub-types, alveolar-RMS (ARMS) and embryonal-RMS (ERMS). The ARMS subtype is often associated with a more aggressive phenotype, poorer clinical prognosis, and expression of Pax3-FKHR and Pax7-FKHR fusion proteins that function as potent transcriptional activators with enhanced activity as compared to normal Pax3 or Pax7 transcription factors. We reported that the stromal derived factor-1 (SDF-1)-CXCR4 receptor axis plays a crucial role in RMS metastasis to BM (Blood2002;100:2597, Cancer Res2003;63:7926, Cancer Res.2007;67:213). After the recent identification of CXCR7, a new receptor for SDF-1, we became interested in its potential role in metastases of RMS cells. We found that CXCR7 was expressed and functional on all 10 human RMS cell lines investigated in this study. Furthermore, we noticed that while CXCR4 was more involved in regulating RMS chemotaxis, CXCR7 primarily regulated adhesion of RMS cells. Based on this observation, we assessed the mechanisms that regulate expression of these receptors. We noticed that CXCR4 is highly expressed on the more metastatic ARMS while CXCR7 is expressed at higher levels on the less metastatic ERMS cell lines. However, both receptors express several hypoxia-inducible factor (HIF)-1a binding sites, expression of CXCR4 was not affected by exposure to hypoxia, and expression of CXCR7 was even paradoxically downregulated in hypoxic conditions. We also observed that ERMS cells transduced with Pax3-FKHR, a gene typical for ARMS fusion that enhances RMS metastatic behavior, highly upregulated expression of CXCR4. In contrast, expression of CXCR7 was again down-regulated. To learn more on the role of Pax-3-FKHR in the expression of CXCR4, we performed a functional analysis of promoter fragments subcloned into luciferase vector. To our surprise, expression of CXCR4 did not depend on direct binding of Pax3-FKHR to classical Pax3 binding sites in promoter sequences but on direct protein-to-protein interaction with nuclear respiratory factor (NRF)-1 transcription factor. These results suggest that the Pax3-FKHR-NRF-1 complex binds to the NRF-1 binding site and aberrantly activates transcription. In conclusion, both of the SDF-1 binding receptors (CXCR4 and CXCR7) are differently regulated in RMS cells. Since CXCR7 is more important in adhesion and becomes downregulated during hypoxia, this may give an advantage for SDF-1 to signal through CXCR4 receptor to activate pathways critical for chemotactic responses. As a biological consequence, this may increase the metastatic potential of RMS by “mobilizing” RMS cells from the primary tumor to migrate and metastasize. In addition, the novel transcriptional mechanism for the Pax3-FKHR-NRF-1 complex in regulating CXCR4 receptors in RMS cells has been identified.
APA, Harvard, Vancouver, ISO, and other styles
39

Lagha, M., T. Sato, L. Bajard, P. Daubas, M. Esner, D. Montarras, F. Relaix, and M. Buckingham. "Regulation of Skeletal Muscle Stem Cell Behavior by Pax3 and Pax7." Cold Spring Harbor Symposia on Quantitative Biology 73 (January 1, 2008): 307–15. http://dx.doi.org/10.1101/sqb.2008.73.006.

Full text
APA, Harvard, Vancouver, ISO, and other styles
40

Kadzik, Rachel S., Tiffany L. Barnes, Lisa M. Galli, and Laura W. Burrus. "A proliferative role for Pax3 and Pax7 in the chick somite." Developmental Biology 306, no. 1 (June 2007): 367. http://dx.doi.org/10.1016/j.ydbio.2007.03.268.

Full text
APA, Harvard, Vancouver, ISO, and other styles
41

Relaix, F. "Divergent functions of murine Pax3 and Pax7 in limb muscle development." Genes & Development 18, no. 9 (April 22, 2004): 1088–105. http://dx.doi.org/10.1101/gad.301004.

Full text
APA, Harvard, Vancouver, ISO, and other styles
42

Rattenbach, Revital, Andrew Ho, Anne Rochat, and Frederic Relaix. "03-P130 Pax3 and Pax7 play key functions in craniofacial development." Mechanisms of Development 126 (August 2009): S105. http://dx.doi.org/10.1016/j.mod.2009.06.182.

Full text
APA, Harvard, Vancouver, ISO, and other styles
43

Reca, Ryan, Kacper Jankowski, Grzegorz Przybylski, Anna Janowska-Wieczorek, and Mariusz Z. Ratajczak. "CXCR4 Is a PAX Family Transcription Factor Regulated Gene." Blood 104, no. 11 (November 16, 2004): 4205. http://dx.doi.org/10.1182/blood.v104.11.4205.4205.

Full text
Abstract:
Abstract CXCR4 is a G protein-coupled receptor expressed on versatile tissue/organ specific stem cells that binds the α-chemokine SDF-1, and the PAX gene family (PAX1 – 9) encodes transcription factors that have been implicated in organogenesis and stem cell development. It has been demonstrated that the SDF-1-CXCR4 axis regulates trafficking of several types of normal early stem/progenitor cells and malignant tumor cells that derive from them. Recently our group focused on the role of CXCR4 in regulating the motility of skeletal muscle stem/progenitors and reported that it is expressed on normal skeletal muscle satellite stem cells (Stem Cells2003; 21: 363.), and is highly up-regulated on rhabdomyosarcomas (RMS) (Blood2002; 100: 2597) originating from transformed muscle satellite cells. We observed that the expression of CXCR4 correlated with the presence of PAX3 and PAX7 transcription factors (muscle satellite stem cells) and was up-regulated in RMS cells that express the more active version of PAX genes, PAX3-FKHR and PAX7-FKHR fusion proteins. Based on this we hypothesized that PAX genes regulate CXCR4 expression in normal muscle satellite stem cells and their more active fusion-gene counterparts are responsible for up-regulation of CXCR4 in RMS. To better address this issue, we first compared CXCR4 expression by real-time RT-PCR and FACS in several human RMS cells lines and found that expression of CXCR4 correlated with the more metastatic, alveolar subtype of RMS and a better responsiveness to SDF-1. Second, sequence analysis of the CXCR4 promoter revealed several putative PAX gene binding sites (ATTA and GTNNN motifs) at −658–672, −696–709, −737–758, −809–821, −1580–1610, −1693–1697, −1853–1857, −1865–1879, −1937–1946, −2195–2199 and −2297–2302 bp of the reported CXCR4 promoter sequence. Third, to evaluate whether PAX regulates the expression of CXCR4, a 2335 bp upstream fragment of the human CXCR4 promoter gene or its shorter fragments (1819 bp, 1547 bp, 850 bp, 528 bp and 106 bp) were subcloned into a CAT basic reporter gene plasmid and assayed in cells expressing or not expressing the PAX3-FKHR fusion gene. We observed that the CAT activity of all promoter fragments except the 1547 bp fragment was significantly enhanced in cells transduced with the PAX3-FKHR expression vector, what suggests the presence of a negative regulatory element in addition to several positive regulatory PAX binding domains. No promoter activity was observed with the smallest 106 bp fragment. Finally, chromatin immunoprecipitation (ChIP) assay revealed that the PAX3-FKHR protein binds to the CXCR4 promoter. Thus, we provide evidence that expression of CXCR4 is regulated by PAX transcription regulatory factors. Furthermore, we postulate that various PAX proteins that bind to similar DNA consensus sequences may regulate CXCR4 expression in various early normal stem/progenitor cells in a tissue-specific manner (e.g., PAX 1 in osteoblastic progenitors, PAX 3 in neural-crest and skeletal muscle progenitors, PAX 5 in B lymphocytes, PAX 6 in endocrine pancreatic progenitors, PAX 7 in skeletal muscle satellite cells, etc.), what is crucial for proper trafficking of these cells during organogenesis. Furthermore, the potential deregulation of PAX genes in tumor cells leads to overexpression of CXCR4, enhanced responsiveness to SDF-1 and metastasis.
APA, Harvard, Vancouver, ISO, and other styles
44

Boldrin, L., C. Collins, V. Gnocchi, P. Zammit, and J. E. Morgan. "P37 Pax3/Pax7 transcriptional activity is in vivo required for muscle differentiation." Neuromuscular Disorders 20 (March 2010): S15. http://dx.doi.org/10.1016/s0960-8966(10)70052-3.

Full text
APA, Harvard, Vancouver, ISO, and other styles
45

Kassar-Duchossoy, L. "Pax3/Pax7 mark a novel population of primitive myogenic cells during development." Genes & Development 19, no. 12 (June 15, 2005): 1426–31. http://dx.doi.org/10.1101/gad.345505.

Full text
APA, Harvard, Vancouver, ISO, and other styles
46

Möller, Emely, Margareth Isaksson, Nils Mandahl, Fredrik Mertens, and Ioannis Panagopoulos. "Comparison of the proximal promoter regions of the PAX3 and PAX7 genes." Cancer Genetics and Cytogenetics 178, no. 2 (October 2007): 114–19. http://dx.doi.org/10.1016/j.cancergencyto.2007.06.006.

Full text
APA, Harvard, Vancouver, ISO, and other styles
47

Charytonowicz, Elizabeth, Igor Matushansky, Mireia Castillo-Martin, Todd Hricik, Carlos Cordon-Cardo, and Mel Ziman. "Alternate PAX3 and PAX7 C-terminal isoforms in myogenic differentiation and sarcomagenesis." Clinical and Translational Oncology 13, no. 3 (March 2011): 194–203. http://dx.doi.org/10.1007/s12094-011-0640-y.

Full text
APA, Harvard, Vancouver, ISO, and other styles
48

Pfeffer, P. L., T. Gerster, K. Lun, M. Brand, and M. Busslinger. "Characterization of three novel members of the zebrafish Pax2/5/8 family: dependency of Pax5 and Pax8 expression on the Pax2.1 (noi) function." Development 125, no. 16 (August 15, 1998): 3063–74. http://dx.doi.org/10.1242/dev.125.16.3063.

Full text
Abstract:
The mammalian Pax2, Pax5 and Pax8 genes code for highly related transcription factors, which play important roles in embryonic development and organogenesis. Here we report the characterization of all members of the zebrafish Pax2/5/8 family. These genes have arisen by duplications before or at the onset of vertebrate evolution. Due to an additional genome amplification in the fish lineage, the zebrafish contains two Pax2 genes, the previously known Pax[b] gene (here renamed as Pax2.1) and a novel Pax2.2 gene. The zebrafish Pax2.1 gene most closely resembles the mammalian Pax2 gene in its expression pattern, as it is transcribed first in the midbrain-hindbrain boundary region, then in the optic stalk, otic system, pronephros and nephric ducts, and lastly in specific interneurons of the hindbrain and spinal cord. Pax2.2 differs from Pax2.1 by the absence of expression in the nephric system and by a delayed onset of transcription in other Pax2.1 expession domains. Pax8 is also expressed in the same domains as Pax2.1, but its transcription is already initiated during gastrulation in the primordia of the otic placode and pronephric anlage, thus identifying Pax8 as the earliest developmental marker of these structures. The zebrafish Pax5 gene, in contrast to its mouse orthologue, is transcribed in the otic system in addition to its prominent expression at the midbrain-hindbrain boundary. The no isthmus (noi) mutation is known to inactivate the Pax2.1 gene, thereby affecting the development of the midbrain-hindbrain boundary region, pronephric system, optic stalk and otic region. Although the different members of the Pax2/5/8 family may potentially compensate for the loss of Pax2.1 function, we demonstrate here that only the expression of the Pax2.2 gene remains unaffected in noi mutant embryos. The expression of Pax5 and Pax8 is either not initiated at the midbrain-hindbrain boundary or is later not maintained in other expression domains. Consequently, the noi mutation of zebrafish is equivalent to combined inactivation of the mouse Pax2 and Pax5 genes with regard to the loss of midbrain-hindbrain boundary development.
APA, Harvard, Vancouver, ISO, and other styles
49

Burrill, J. D., L. Moran, M. D. Goulding, and H. Saueressig. "PAX2 is expressed in multiple spinal cord interneurons, including a population of EN1+ interneurons that require PAX6 for their development." Development 124, no. 22 (November 15, 1997): 4493–503. http://dx.doi.org/10.1242/dev.124.22.4493.

Full text
Abstract:
Members of the PAX family of transcription factors are candidates for controlling cell identity in the spinal cord. We have morphologically analyzed cells that express one of these transcription factors, PAX2, demonstrating multiple interneuron cell types express PAX2. Two ventral populations of PAX2-expressing interneurons in the spinal cord are marked by coexpression of the transcription factors, EN1 and EVX1. Interestingly, the expression domains of PAX2, EN1 and EVX1 in postmitotic neurons correlate closely with those of Pax6 and Pax7 in the ventricular zone, implicating these patterning genes in the regulation of PAX2, EN1 and EVX1. We show that one of these patterning genes, Pax6, is required for the correct specification of ventral PAX2+ interneurons that coexpress EN1. These results demonstrate that the early activity of patterning genes in the ventricular zone determines interneuron identity in the spinal cord.
APA, Harvard, Vancouver, ISO, and other styles
50

Yin, H. D., D. Y. Li, L. Zhang, M. Y. Yang, X. L. Zhao, Y. Wang, Y. P. Liu, and Q. Zhu. "Housing system influences abundance of Pax3 and Pax7 in postnatal chicken skeletal muscles." Poultry Science 93, no. 6 (June 2014): 1337–43. http://dx.doi.org/10.3382/ps.2013-03555.

Full text
APA, Harvard, Vancouver, ISO, and other styles
You might also be interested in the bibliographies on the topic 'Pax3 and Pax7' for other source types:
Dissertations / Theses Books
We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!

To the bibliography