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Journal articles on the topic 'Versican'

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Published: 4 June 2021
Last updated: 31 January 2023

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1

Papadas, Athanasios, Garrett Arauz, Alexander Cicala, Joshua Wiesner, and Fotis Asimakopoulos. "Versican and Versican-matrikines in Cancer Progression, Inflammation, and Immunity." Journal of Histochemistry & Cytochemistry 68, no. 12 (July 6, 2020): 871–85. http://dx.doi.org/10.1369/0022155420937098.

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Versican is an extracellular matrix proteoglycan with key roles in multiple facets of cancer development, ranging from proliferative signaling, evasion of growth-suppressor pathways, regulation of cell death, promotion of neoangiogenesis, and tissue invasion and metastasis. Multiple lines of evidence implicate versican and its bioactive proteolytic fragments (matrikines) in the regulation of cancer inflammation and antitumor immune responses. The understanding of the dynamics of versican deposition/accumulation and its proteolytic turnover holds potential for the development of novel immune biomarkers as well as approaches to reset the immune thermostat of tumors, thus promoting efficacy of modern immunotherapies. This article summarizes work from several laboratories, including ours, on the role of this central matrix proteoglycan in tumor progression as well as tumor-immune cell cross-talk:
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2

Brune, Jourdan E., Mary Y. Chang, William A. Altemeier, and Charles W. Frevert. "Type I Interferon Signaling Increases Versican Expression and Synthesis in Lung Stromal Cells During Influenza Infection." Journal of Histochemistry & Cytochemistry 69, no. 11 (October 19, 2021): 691–709. http://dx.doi.org/10.1369/00221554211054447.

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Versican, a chondroitin sulfate proteoglycan, is an essential component of the extracellular matrix (ECM) in inflammatory lung disease. Versican’s potential as an immunomodulatory molecule makes it a promising therapeutic target for controlling host immune responses in the lungs. To establish changes to versican expression and accumulation during influenza A viral pneumonia, we document the temporal and spatial changes to versican mRNA and protein in concert with pulmonary inflammatory cell infiltration. These studies were performed in the lungs of wild-type C57BL6/J mice on days 3, 6, 9, and 12 post-infection with influenza A virus using immunohistochemistry, in situ hybridization, and quantitative digital pathology. Using duplex in situ hybridization, we demonstrate that type I interferon signaling contributes significantly to versican expression in lung stromal cells. Our findings show that versican is a type I interferon–stimulated gene in pulmonary fibroblasts and pericytes in the context of viral pneumonia. These data also provide a guide for future studies to determine the role of versican in the pulmonary immune response to influenza infection:
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3

Rahmani, Maziar, Brian W. Wong, Lisa Ang, Caroline C. Cheung, Jon M. Carthy, Hubert Walinski, and Bruce M. McManus. "Versican: signaling to transcriptional control pathwaysThis paper is one of a selection of papers published in this Special Issue, entitled Young Investigator's Forum." Canadian Journal of Physiology and Pharmacology 84, no. 1 (January 2006): 77–92. http://dx.doi.org/10.1139/y05-154.

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Versican, a chondroitin sulfate proteoglycan, is one of the main components of the extracellular matrix, which provides a loose and hydrated matrix during key events in development and disease. Versican participates in cell adhesion, proliferation, migration, and angiogenesis, and hence plays a central role in tissue morphogenesis and maintenance. In addition, versican contributes to the development of a number of pathologic processes including atherosclerotic vascular diseases, cancer, tendon remodeling, hair follicle cycling, central nervous system injury, and neurite outgrowth. Versican is a complex molecule consisting of modular core protein domains and glycosaminoglycan side chains, and there are various steps of synthesis and processes regulating them. Also, there is differential temporal and spatial expression of versican by multiple cell types and in different developmental and pathological time frames. To fully appreciate the functional roles of versican as it relates to changing patterns of expression in development and disease, an in depth knowledge of versican’s biosynthetic processing is necessary. The goal of this review is to evaluate the current status of our knowledge regarding the transcriptional control of versican gene regulation. We will be focusing on the signal transduction pathways, promoter regions, cis-acting elements, and trans-factors that have been characterized.
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4

Sheng, Wang, Guizhi Wang, David P. La Pierre, Jianping Wen, Zhaoqun Deng, Chung-Kwun Amy Wong, Daniel Y. Lee, and Burton B. Yang. "Versican Mediates Mesenchymal-Epithelial Transition." Molecular Biology of the Cell 17, no. 4 (April 2006): 2009–20. http://dx.doi.org/10.1091/mbc.e05-10-0951.

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Versican is a large extracellular chondroitin sulfate proteoglycan that belongs to the family of lecticans. Alternative splicing of versican generates at least four isoforms named V0, V1, V2, and V3. We show here that ectopic expression of versican V1 isoform induced mesenchymal-epithelial transition (MET) in NIH3T3 fibroblasts, and inhibition of endogenous versican expression abolished the MET in metanephric mesenchyme. MET in NIH3T3 cells was demonstrated by morphological changes and dramatic alterations in both membrane and cytoskeleton architecture. Molecular analysis showed that V1 promoted a “switch” in cadherin expression from N- to E-cadherin, resulting in epithelial specific adhesion junctions. V1 expression reduced vimentin levels and induced expression of occludin, an epithelial-specific marker, resulting in polarization of V1-transfected cells. Furthermore, an MSP (methylation-specific PCR) assay showed that N-cadherin expression was suppressed through methylation of its DNA promoter. Exogenous expression of N-cadherin in V1-transfected cells reversed V1's effect on cell aggregation. Reduction of E-cadherin expression by Snail transfection and siRNA targeting E-cadherin abolished V1-induced morphological alteration. Transfection of an siRNA construct targeting versican also reversed the changed morphology induced by V1 expression. Silencing of endogenous versican prevented MET of metanephric mesenchyme. Taken together, our results demonstrate the involvement of versican in MET: expression of versican is sufficient to induce MET in NIH3T3 fibroblasts and reduction of versican expression decreased MET in metanephric mesenchyme.
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5

Zimmermann, DR, MT Dours-Zimmermann, M. Schubert, and L. Bruckner-Tuderman. "Versican is expressed in the proliferating zone in the epidermis and in association with the elastic network of the dermis." Journal of Cell Biology 124, no. 5 (March 1, 1994): 817–25. http://dx.doi.org/10.1083/jcb.124.5.817.

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The expression of the large chondroitin sulfate proteoglycan versican was studied in human adult skin. For this purpose, bacterial fusion proteins containing unique portions of the versican core protein were prepared. Polyclonal antibodies against the fusion proteins specifically reacted with versican from a proteoglycan fraction of MG63 osteosarcoma cells. In immunohistochemical experiments, the affinity-purified antibodies localized versican in the stratum basale of the epidermis, as well as in the papillary and reticular layers of the dermis. An apparent codistribution of versican with the various fiber forms of the elastic network of the dermis suggested an association of versican with microfibrils. Both dermal fibroblasts and keratinocytes expressed versican in culture during active cell proliferation. In line with the observation that versican is absent in the suprabasal layers of the epidermis where keratinocytes terminally differentiate, culture conditions promoting keratinocyte differentiation induced a down-regulation of versican synthesis. In Northern blots versican mRNA could be detected in extracts from proliferating keratinocytes and dermal fibroblasts. Comparison of RNA preparations from semi-confluent and confluent fibroblast cultures demonstrated decreasing amounts of versican mRNA at higher cell densities. This inverse correlation of versican expression and cell density was confirmed by indirect immunofluorescence staining of cultured fibroblasts and keratinocytes. The localization of versican in the basal zone of the epidermis as well as the density dependence of versican in cell cultures suggest a general function of versican in cell proliferation processes that may not solely be confined to the skin.
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6

Landolt, R. M., L. Vaughan, K. H. Winterhalter, and D. R. Zimmermann. "Versican is selectively expressed in embryonic tissues that act as barriers to neural crest cell migration and axon outgrowth." Development 121, no. 8 (August 1, 1995): 2303–12. http://dx.doi.org/10.1242/dev.121.8.2303.

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Chondroitin sulfate proteoglycans have been implicated in the regulation of cell migration and pattern formation in the developing peripheral nervous system. To identify whether the large aggregating proteoglycan versican might be mediating these processes, we prepared monospecific antibodies against a recombinant core protein fragment of chick versican. The purified antibodies recognize the predominant versican splice-variants V0 and V1. Using these antibodies, we revealed a close correlation between the spacio-temporal expression of versican and the formation of molecular boundaries flanking or transiently blocking the migration pathways of neural crest cells or motor and sensory axons. Versican is present in the caudal sclerotome, the early dorsolateral tissue underneath the ectoderm, the pelvic girdle precursor and to a certain extent in the perinotochordal mesenchyme. Versican is completely absent from tissues invaded by neural crest cells and extending axons. Upon completion of neural crest cell migration and axon outgrowth, versican expression is shifted to pre-chondrogenic areas. Since versican inhibits cellular interactions with fibronectin, laminin and collagen I in vitro, the selective expression of versican within barrier tissues may be linked to a functional role of versican in the guidance of migratory neural crest cells and outgrowing axons.
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7

Mohamed, Mohamed. "Versican and coronary artery spasm." Medical Research Journal 11, no. 1 (June 2012): 1–6. http://dx.doi.org/10.1097/01.mjx.0000414711.94482.58.

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8

Theocharis, Achilleas D. "Versican in Health and Disease." Connective Tissue Research 49, no. 3-4 (January 2008): 230–34. http://dx.doi.org/10.1080/03008200802147571.

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9

Kenagy, Richard D., Anna H. Plaas, and Thomas N. Wight. "Versican Degradation and Vascular Disease." Trends in Cardiovascular Medicine 16, no. 6 (August 2006): 209–15. http://dx.doi.org/10.1016/j.tcm.2006.03.011.

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10

LeBaron, R. G., D. R. Zimmermann, and E. Ruoslahti. "Hyaluronate binding properties of versican." Journal of Biological Chemistry 267, no. 14 (May 1992): 10003–10. http://dx.doi.org/10.1016/s0021-9258(19)50191-0.

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11

Nakamura, Megumi, Shinya Sone, Ichiro Takahashi, Itaru Mizoguchi, Seishi Echigo, and Yasuyuki Sasano. "Expression of Versican and ADAMTS1, 4, and 5 During Bone Development in the Rat Mandible and Hind Limb." Journal of Histochemistry & Cytochemistry 53, no. 12 (June 27, 2005): 1553–62. http://dx.doi.org/10.1369/jhc.5a6669.2005.

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Extracellular matrix (ECM) remodeling is achieved by both production and degradation of ECM molecules during bone development. ADAMTS (a disintegrin and metalloprotease with thrombospondin type 1 motifs) constitutes a family of extracellular proteases which are implicated in cleaving the protein versican. The present study was designed to investigate the expression of versican and ADAMTS1, 4, and 5 mRNA during bone development in rat mandibles and hind limbs by RT-PCR and in situ hybridization. Versican was localized by immunohistochemistry. The process of bone development from day 14 postcoitum through week 6 postnatum was divided into the beginning of osteogenesis, woven bone, and lamellar bone stages. Versican protein was abundant in the woven bone matrix, but decreased in the lamellar bone matrix. Versican mRNA was prominent in some osteoblasts with corresponding localization of the cognate protein. The temporal and spatial mRNA expression pattern of ADAMTS1, 4, and 5 was comparable to that of versican. These results suggest that woven bone rich in versican alters into lamellar bone containing little versican during bone development in both mandibles and hind limbs, where some osteoblasts may be involved in production as well as degradation of versican by secreting ADAMTS1, 4, and 5.
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12

Xu, Fangfang, Wenping Cai, Weiting Chen, Lefeng Li, Xuyan Li, and Beizhan Jiang. "Expression of Different Isoforms of Versican During the Development of Mouse Mandibular First Molars." Journal of Histochemistry & Cytochemistry 67, no. 7 (April 29, 2019): 471–80. http://dx.doi.org/10.1369/0022155419846875.

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Versican is a large chondroitin sulfate proteoglycan enriched in the extracellular matrix, and it has at least four different isoforms, termed V0, V1, V2, and V3. Although several studies have demonstrated that versican is stably expressed in various developing organs, the expression of versican isoforms during tooth development has not been elucidated yet. Therefore, the present study was to investigate the expression of versican isoforms in the developing mouse molars. The mandibular first molars from embryonic day (E) 11.5 to postnatal day (PN) 21 were used to investigate the expression of versican isoforms by immunohistochemistry, and the gene expressions of versican ( Vcan) isoforms from E13.5 to PN7 were analyzed by quantitative real-time PCR. The results exhibited different expressing patterns of versican isoforms—the stellate reticulum (SR) and the dental mesenchymal cells adjacent to Hertwig’s Epithelial Root Sheath (HERS) only expressed V1 and the mature odontoblasts mainly expressed V2, while the dental papilla and the ameloblasts might both express V0/V1/V2. These results suggested that different versican isoforms may act different roles in the tooth development, and we speculated that V0/V1 might be intimately involved in the cell proliferation while V2 was associated in the cytodifferentiation.
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13

Islam, Shamima, and Hideto Watanabe. "Versican: A Dynamic Regulator of the Extracellular Matrix." Journal of Histochemistry & Cytochemistry 68, no. 11 (September 10, 2020): 763–75. http://dx.doi.org/10.1369/0022155420953922.

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Versican is a large chondroitin sulfate/dermatan sulfate proteoglycan belonging to the aggrecan/lectican family. In adults, this proteoglycan serves as a structural macromolecule of the extracellular matrix in the brain and large blood vessels. In contrast, versican is transiently expressed at high levels during development and under pathological conditions when the extracellular matrix dramatically changes, including in the inflammation and repair process. There are many reports showing the upregulation of versican in cancer, which correlates with cancer aggressiveness. Versican has four classical splice variants, and all the variants contain G1 and G3 domains at N- and C-termini, respectively. There are two glycosaminoglycan attachment domains CSα and CSβ. The largest V0 variant contains both CSα and CSβ, V1 contains CSβ, V2 contains CSα, and the shortest G3 variant has neither of them. Versican degradation is initiated by cleavage at a site in the CSβ domain by ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) proteinases. The N-terminal fragment containing the G1 domain has been reported to exert various biological functions, although its mechanisms of action have not yet been elucidated. In this review, we describe the role of versican in inflammation and cancer and also address the biological function of versikine.
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Chang, Mary Y., Inkyung Kang, Michael Gale, Anne M. Manicone, Michael G. Kinsella, Kathleen R. Braun, Tara Wigmosta, et al. "Versican is produced by Trif- and type I interferon-dependent signaling in macrophages and contributes to fine control of innate immunity in lungs." American Journal of Physiology-Lung Cellular and Molecular Physiology 313, no. 6 (December 1, 2017): L1069—L1086. http://dx.doi.org/10.1152/ajplung.00353.2017.

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Growing evidence suggests that versican is important in the innate immune response to lung infection. Our goal was to understand the regulation of macrophage-derived versican and the role it plays in innate immunity. We first defined the signaling events that regulate versican expression, using bone marrow-derived macrophages (BMDMs) from mice lacking specific Toll-like receptors (TLRs), TLR adaptor molecules, or the type I interferon receptor (IFNAR1). We show that LPS and polyinosinic-polycytidylic acid [poly(I:C)] trigger a signaling cascade involving TLR3 or TLR4, the Trif adaptor, type I interferons, and IFNAR1, leading to increased expression of versican by macrophages and implicating versican as an interferon-stimulated gene. The signaling events regulating versican are distinct from those for hyaluronan synthase 1 (HAS1) and syndecan-4 in macrophages. HAS1 expression requires TLR2 and MyD88. Syndecan-4 requires TLR2, TLR3, or TLR4 and both MyD88 and Trif. Neither HAS1 nor syndecan-4 is dependent on type I interferons. The importance of macrophage-derived versican in lungs was determined with LysM/ Vcan−/− mice. These studies show increased recovery of inflammatory cells in the bronchoalveolar lavage fluid of poly(I:C)-treated LysM/ Vcan−/− mice compared with control mice. IFN-β and IL-10, two important anti-inflammatory molecules, are significantly decreased in both poly(I:C)-treated BMDMs from LysM/ Vcan−/− mice and bronchoalveolar lavage fluid from poly(I:C)-treated LysM/ Vcan−/− mice compared with control mice. In short, type I interferon signaling regulates versican expression, and versican is necessary for type I interferon production. These findings suggest that macrophage-derived versican is an immunomodulatory molecule with anti-inflammatory properties in acute pulmonary inflammation.
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Bode-Lesniewska, B., M. T. Dours-Zimmermann, B. F. Odermatt, J. Briner, P. U. Heitz, and D. R. Zimmermann. "Distribution of the large aggregating proteoglycan versican in adult human tissues." Journal of Histochemistry & Cytochemistry 44, no. 4 (April 1996): 303–12. http://dx.doi.org/10.1177/44.4.8601689.

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We studied the distribution of the large hyaluronan-binding proteoglycan versican (also known as PG-M) in human adult tissues using affinity-purified polyclonal antibodies that recognize the core protein of the prominent versican splice variants VO and V1. Versican was present in the loose connective tissues of various organs and was often associated with the elastic fiber network. Furthermore, it was localized in most smooth muscle tissues and in fibrous and elastic cartilage. Versican staining was also noted in the central and peripheral nervous system, in the basal layer of the epidermis, and on the luminal surface of some glandular epithelia. In blood vessels, versican was present in all three wall layers of veins and elastic arteries. In muscular arteries the immunoreactivity was normally restricted to the tunica adventitia. However, it appeared in the media and the split elastica interna of atherosclerotically transformed vessel walls. Our survey of the distribution of versican in normal human tissues now forms the basis for extended studies of potentially aberrant versican expression during pathogenic processes.
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Wu, Yaojiong, Wang Sheng, Liwen Chen, Haiheng Dong, Vivian Lee, Fred Lu, C. Shun Wong, Wei-Yang Lu, and Burton B. Yang. "Versican V1 Isoform Induces Neuronal Differentiation and Promotes Neurite Outgrowth." Molecular Biology of the Cell 15, no. 5 (May 2004): 2093–104. http://dx.doi.org/10.1091/mbc.e03-09-0667.

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The chondroitin sulfate proteoglycan versican is one of the major extracellular components in the developing and adult brain. Here, we show that isoforms of versican play different roles in neuronal differentiation and neurite outgrowth. Expression of versican V1 isoform in PC12 cells induced complete differentiation, whereas expression of V2 induced an aborted differentiation accompanied by apoptosis. V1 promoted neurite outgrowth of hippocampal neurons, but V2 failed to do so. V1 transfection enhanced expression of epidermal growth factor receptor and integrins, and facilitated sustained extracellular signal-regulated kinase/MAPK phosphorylation. Blockade of the epidermal growth factor receptor, β1 integrin, or Src significantly inhibited neuronal differentiation. Finally, we demonstrated that versican V1 isoform also promoted differentiation of neural stem cells into neurons. Our results have implications for understanding how versican regulates neuronal development, function, and repair.
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17

Dunning, K. R., C. X. Yeo, and D. L. Russell. "230. Altered matrix composition of cumulus oocyte complexes following in vitro maturation." Reproduction, Fertility and Development 17, no. 9 (2005): 90. http://dx.doi.org/10.1071/srb05abs230.

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The luteinizing hormone (LH) surge initiates cumulus expansion, through synthesis of hyaluronan and cross-linking proteins including versican, which stabilise the cumulus oocyte complex (COC) matrix. Versican is a substrate for the protease ADAMTS-1 and mRNA for each are localised to granulosa cells (GCs) and greatly induced following the LH surge. In humans, the use of in vitro maturation (IVM) of oocytes is an appealing option, reducing costs and risk of side effects associated with in vitro fertilisation. IVM oocytes are of poorer quality, likely resulting from altered gene expression and environmental conditions during oocyte maturation. Real-time PCR showed that IVM and immature COCs from Balb/c mice have 12 and 13 fold-reduced levels of ADAMTS-1 and versican expression respectively compared to in vivo matured COCs (PMSG+hCG 12h). Ovulated COCs (PMSG+hCG 15h) had similar low levels of ADAMTS-1 and versican. Samples isolated from F1 C57Bl/6xCBA mice showed similar reduced versican and ADAMTS-1 mRNA. Western blot analysis revealed that full length and cleaved versican, from ADAMTS-1/4 activity, was not detected in immature COCs, was present in in vivo matured COCs isolated from follicles, but strongest in ovulated COCs. IVM COCs had no detectable versican protein, supporting the mRNA data. Full-length versican was also present in GCs after PMSG+hCG 12h or 15h. ADAMTS-1 protein was most abundant in in vivo matured COCs with reduced levels seen in ovulated COCs, but was absent from IVM and immature COCs. These results indicate that ADAMTS-1 and versican are secreted products of granulosa cells that bind and incorporate into the COC matrix. The presence of versican and ADAMTS-1 is not essential for cumulus matrix expansion in vitro, but may contribute to oocyte maturation, ovulation of the COC and/or interaction with sperm during fertilisation.
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de Souza Neto, Osvaldo Rodrigues, Hellen Thais Fuzii, Suély Vieira Da Silva, Vanessa Morais Freitas, and João de Jesus Viana Pinheiro. "Gene Expression and Immunochemistry Analysis of ADAMTS-1 and Versican in Ameloblastoma." International Journal of Dentistry 2022 (October 26, 2022): 1–11. http://dx.doi.org/10.1155/2022/5235376.

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Background. Ameloblastoma is a benign but locally invasive odontogenic epithelial tumor, associated with a high recurrence rate after treatment. The action of enzymes of the metalloproteinase family is important to the degraded extracellular matrix, contributing to invasion. Thus, this study aimed to investigate the gene and protein expression of ADAMTS-1 and versican in ameloblastoma. Materials and Methods. Twenty cases of ameloblastoma (n = 20) and ten dental follicles (DF) (n = 10) were used as a source for immunochemistry and quantitative RT-PCR for determining the protein and mRNA expressions of the concerned genes, respectively. Moreover, western blot and indirect immunofluorescence analysis were performed in AME cells. Results. ADAMTS-1 and versican were overexpressed in DF than ameloblastoma by RT-PCR. However, in the immunolocalization analysis, ADAMTS-1 was expressed in ameloblastoma more than in DF and versican immunostaining obtained a similar pattern between ameloblastoma and DF. Indirect immunofluorescence detected the ADAMTS-1 and versican expression in cell lines derived from ameloblastoma. Western blot from cell lysate and conditioned medium detected ADAMTS-1 bands representing full-length and different processed forms. Monensin treatment confined ADAMTS-1 in the cell cytoplasm. Versican fragments also were detected in different compartments, intracellular and conditioned medium, allowing the versican process by ADAMTS-1. Conclusion. This study showed a distinct expression of ADAMTS-1 and versican in ameloblastoma and DF, with ADAMTS-1 protein higher expression observed in ameloblastoma and possibly cleaved versican. These findings suggested that ADAMTS-1 may participate in tumor invasion, especially for the degradation of substrates (versican) in the ECM.
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Tani, Hirohiko, Yukiyasu Sato, Masashi Ueda, Yumiko Miyazaki, Koh Suginami, Akihito Horie, Ikuo Konishi, and Tamayuki Shinomura. "Role of Versican in the Pathogenesis of Peritoneal Endometriosis." Journal of Clinical Endocrinology & Metabolism 101, no. 11 (August 17, 2016): 4349–56. http://dx.doi.org/10.1210/jc.2016-2391.

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Context: Sampson’s theory cannot explain why only some cycling women develop peritoneal endometriosis. Few studies have focused on the pelvic peritoneum, which receives regurgitated endometrial tissues. We hypothesized that molecular alterations in the peritoneum are involved in the development of peritoneal endometriosis and conducted a microarray analysis to compare macroscopically normal peritoneum sampled from women with peritoneal endometriosis (endometriotic peritoneum) and those without (non-endometriotic peritoneum). Versican, a major proteoglycan component of the extracellular matrix, is one of the molecules up-regulated in endometriotic peritoneum. Objective: To investigate the role of versican in peritoneal endometriosis. Design, Patients, and Main Outcome Measure: Endometriotic peritoneum and non-endometriotic peritoneum were subjected to RT-PCR, immunostaining, and Western blotting. The versican V1 isoform was stably transfected into Chinese hamster ovary cells (CHO-V1), and the effects of CHO-V1-derived conditioned medium (V1-CM) on primary human endometrial stromal cells were investigated with attachment, invasion, and proliferation assays. The effects of peritoneal fluid collected from endometriotic women (endometriotic PF) or cytokines/growth factors, which were shown to be elevated in endometriotic PF, on versican expression in a human peritoneal cell line (HMrSV5) were also examined. Results: Versican V1 expression levels were significantly higher in endometriotic peritoneum. In vitro, V1-CM promoted attachment to the HMrSV5 cell monolayer as well as the Matrigel invasion of endometrial stromal cells. Although versican V1 expression was up-regulated by TGF-β1 in HMrSV5 cells, it remained unchanged in endometriotic PF. Conclusions: Our results suggest the involvement of peritoneal versican in the development of peritoneal endometriosis.
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Barallobre-Barreiro, Javier, Tamás Radovits, Marika Fava, Ursula Mayr, Wen-Yu Lin, Elizaveta Ermolaeva, Diego Martínez-López, et al. "Extracellular Matrix in Heart Failure: Role of ADAMTS5 in Proteoglycan Remodeling." Circulation 144, no. 25 (December 21, 2021): 2021–34. http://dx.doi.org/10.1161/circulationaha.121.055732.

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Background: Remodeling of the extracellular matrix (ECM) is a hallmark of heart failure (HF). Our previous analysis of the secretome of murine cardiac fibroblasts returned ADAMTS5 (a disintegrin and metalloproteinase with thrombospondin motifs 5) as one of the most abundant proteases. ADAMTS5 cleaves chondroitin sulfate proteoglycans such as versican. The contribution of ADAMTS5 and its substrate versican to HF is unknown. Methods: Versican remodeling was assessed in mice lacking the catalytic domain of ADAMTS5 (Adamts5 ΔCat ). Proteomics was applied to study ECM remodeling in left ventricular samples from patients with HF, with a particular focus on the effects of common medications used for the treatment of HF. Results: Versican and versikine, an ADAMTS-specific versican cleavage product, accumulated in patients with ischemic HF. Versikine was also elevated in a porcine model of cardiac ischemia/reperfusion injury and in murine hearts after angiotensin II infusion. In Adamts5 ΔCat mice, angiotensin II infusion resulted in an aggravated versican build-up and hyaluronic acid disarrangement, accompanied by reduced levels of integrin β1, filamin A, and connexin 43. Echocardiographic assessment of Adamts5 ΔCat mice revealed a reduced ejection fraction and an impaired global longitudinal strain on angiotensin II infusion. Cardiac hypertrophy and collagen deposition were similar to littermate controls. In a proteomics analysis of a larger cohort of cardiac explants from patients with ischemic HF (n=65), the use of β-blockers was associated with a reduction in ECM deposition, with versican being among the most pronounced changes. Subsequent experiments in cardiac fibroblasts confirmed that β1-adrenergic receptor stimulation increased versican expression. Despite similar clinical characteristics, patients with HF treated with β-blockers had a distinct cardiac ECM profile. Conclusions: Our results in animal models and patients suggest that ADAMTS proteases are critical for versican degradation in the heart and that versican accumulation is associated with impaired cardiac function. A comprehensive characterization of the cardiac ECM in patients with ischemic HF revealed that β-blockers may have a previously unrecognized beneficial effect on cardiac chondroitin sulfate proteoglycan content.
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Timms, Katherine Payne, and Sean Bertram Maurice. "Context-dependent bioactivity of versican fragments." Glycobiology 30, no. 6 (October 24, 2019): 365–73. http://dx.doi.org/10.1093/glycob/cwz090.

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Abstract Versican (VCAN) proteolysis and the accumulation of VCAN fragments occur in many developmental and disease processes, affecting extracellular matrix (ECM) structure and cell phenotype. Little is known about the significance of proteolysis and the roles of fragments, or how this ECM remodeling affects the microenvironment and phenotype of diseased cells. G1-DPEAAE fragments promote aspects of epithelial–mesenchymal transitioning in developing and diseased cells, resulting in cell migration. Enhanced proliferation and invasion of tumor and endothelial cells is directly associated with G1 domain deposition and G1-DPEAAE localization respectively. These tumorigenic and angiogenic roles could explain the disease exacerbating effect often associated with G1-containing fragments, however, the pathogenicity of G1 fragments depends entirely upon the context. Overall, VCAN fragments promote tumorigenesis and inflammation; however, the specific cleavage site, the extent of cleavage activity and the microenvironment in which cleavage occurs collectively determine how this pleiotropic molecule and its fragments influence cells.
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Wight, Thomas N., Inkyung Kang, and Mervyn J. Merrilees. "Versican and the control of inflammation." Matrix Biology 35 (April 2014): 152–61. http://dx.doi.org/10.1016/j.matbio.2014.01.015.

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23

Sorrell, J. M., David A. Carrino, Marilyn A. Baber, and Arnold I. Caplan. "Versican in human fetal skin development." Anatomy and Embryology 199, no. 1 (January 1, 1999): 45–56. http://dx.doi.org/10.1007/s004290050208.

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Kodama, J., Hasengaowa, T. Kusumoto, N. Seki, T. Matsuo, K. Nakamura, A. Hongo, and Y. Hiramatsu. "Versican expression in human cervical cancer." European Journal of Cancer 43, no. 9 (June 2007): 1460–66. http://dx.doi.org/10.1016/j.ejca.2007.02.007.

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Schmitt, Michael. "Versican vs versikine: tolerance vs attack." Blood 128, no. 5 (August 4, 2016): 612–13. http://dx.doi.org/10.1182/blood-2016-06-721092.

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Carthy, J. M., S. Boroomand, M. Rahmani, D. Knight, and B. M. McManus. "130: Versican Expression Induces Tissue Remodeling." Journal of Heart and Lung Transplantation 28, no. 2 (February 2009): S111. http://dx.doi.org/10.1016/j.healun.2008.11.808.

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Sheng, Wang, Haiheng Dong, Daniel Y. Lee, Wei-yang Lu, and Burton B. Yang. "Versican modulates gap junction intercellular communication." Journal of Cellular Physiology 211, no. 1 (2007): 213–19. http://dx.doi.org/10.1002/jcp.20921.

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Nagyova, Eva, Antonietta Salustri, Lucie Nemcova, Sona Scsukova, Jaroslav Kalous, and Antonella Camaioni. "Versican G1 Fragment Establishes a Strongly Stabilized Interaction with Hyaluronan-Rich Expanding Matrix during Oocyte Maturation." International Journal of Molecular Sciences 21, no. 7 (March 25, 2020): 2267. http://dx.doi.org/10.3390/ijms21072267.

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In the mammalian ovary, the hyaluronan (HA)-rich cumulus extracellular matrix (ECM) organized during the gonadotropin-induced process of oocyte maturation is essential for ovulation of the oocyte-cumulus complex (OCC) and fertilization. Versican is an HA-binding proteoglycan that regulates cell function and ECM assembly. Versican cleavage and function remain to be determined in ovarian follicle. We investigated versican expression in porcine ovarian follicles by real-time (RT)-PCR and western blotting. The aims of the present work were to determine whether 1) versican was produced and cleaved by porcine OCCs during gonadotropin stimulation; 2) these processes were autonomous or required the participation of mural granulosa cells (MGCs); and 3) versican cleavage was involved in the formation or degradation of expanded cumulus ECM. We demonstrate two cleavage products of G1 domain of versican (V1) accumulated in the HA-rich cumulus ECM. One of them, a G1-DPEAAE N-terminal fragment (VG1) of ~70 kDa, was generated from V1 during organization of HA in in vivo and in vitro expanded porcine OCCs. Second, the V1-cleaved DPEAAE-positive form of ~65 kDa was the only species detected in MGCs. No versican cleavage products were detected in OCCs cultured without follicular fluid. In summary, porcine OCCs are autonomous in producing and cleaving V1; the cleaved fragment of ~70 kDa VG1 is specific for formation of the expanded cumulus HA-rich ECM.
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Schmalfeldt, M., C. E. Bandtlow, M. T. Dours-Zimmermann, K. H. Winterhalter, and D. R. Zimmermann. "Brain derived versican V2 is a potent inhibitor of axonal growth." Journal of Cell Science 113, no. 5 (March 1, 2000): 807–16. http://dx.doi.org/10.1242/jcs.113.5.807.

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In this paper, we identify the chondroitin sulfate proteoglycan versican V2 as a major inhibitor of axonal growth in the extracellular matrix of the mature central nervous system. In immunohistochemical and in situ hybridization experiments we show that this tissue-specific splice variant of versican is predominantly present in myelinated fiber tracts of the brain and in the optic nerve, most likely being expressed by oligodendrocytes. We demonstrate that isolated versican V2 strongly inhibits neurite outgrowth of central and peripheral neurons in stripe-choice assays using laminin-1 as permissive substrate. The inhibitory character of versican V2 is maintained after removal of chondroitin sulfate and N- and O-linked oligosaccharide side chains, but it is abolished after core protein digestion with proteinase-K. Our data support the notion, that intact versican V2 prevents excessive axonal growth during late phases of development and hereby participates in the structural stabilization of the mature central nervous system.
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Perides, G., R. A. Asher, M. W. Lark, W. S. Lane, R. A. Robinson, and A. Bignami. "Glial hyaluronate-binding protein: a product of metalloproteinase digestion of versican?" Biochemical Journal 312, no. 2 (December 1, 1995): 377–84. http://dx.doi.org/10.1042/bj3120377.

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Glial hyaluronate-binding protein (GHAP) is a 60 kDa glycoprotein with an amino acid sequence identical to that of the hyaluronate-binding region of versican, a large fibroblast aggregating proteoglycan found in the brain. Both GHAP and versican were identified by immunoblot in bovine brain extracts prepared only minutes after death. Human recombinant collagenase, stromelysin, mouse gelatinase and gelatinases isolated from human brain by affinity chromatography digest versican and give rise to a polypeptide with electrophoretic mobility identical to GHAP. Immunoblot analysis, peptide mapping and C-terminal amino acid sequencing indicate that the polypeptide generated by digestion with human brain gelatinases is identical to GHAP. We suggest that GHAP is a naturally occurring versican degradation product.
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Shukla, Shreya, Rekha Nair, Marsha W. Rolle, Kathleen R. Braun, Christina K. Chan, Pamela Y. Johnson, Thomas N. Wight, and Todd C. McDevitt. "Synthesis and Organization of Hyaluronan and Versican by Embryonic Stem Cells Undergoing Embryoid Body Differentiation." Journal of Histochemistry & Cytochemistry 58, no. 4 (December 21, 2009): 345–58. http://dx.doi.org/10.1369/jhc.2009.954826.

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Embryonic stem cells (ESCs) provide a convenient model to probe the molecular and cellular dynamics of developmental cell morphogenesis. ESC differentiation in vitro via embryoid bodies (EBs) recapitulates many aspects of early stages of development, including the epithelial–mesenchymal transition (EMT) of pluripotent cells into more differentiated progeny. Hyaluronan and versican are important extracellular mediators of EMT processes, yet the temporal expression and spatial distribution of these extracellular matrix (ECM) molecules during EB differentiation remains undefined. Thus, the objective of this study was to evaluate the synthesis and organization of hyaluronan and versican by using murine ESCs during EB differentiation. Hyaluronan and versican (V0 and V1 isoforms), visualized by immunohistochemistry and evaluated biochemically, accumulated within EBs during the course of differentiation. Interestingly, increasing amounts of a 70-kDa proteolytic fragment of versican were also detected over time, along with ADAMTS-1 and −5 protein expression. ESCs expressed each of the hyaluronan synthases (HAS) −1, −2, and −3 and versican splice variants (V0, V1, V2, and V3) throughout EB differentiation, but HAS-2, V0, and V1 were expressed at significantly increased levels at each time point examined. Hyaluronan and versican exhibited overlapping expression patterns within EBs in regions of low cell density, and versican expression was excluded from clusters of epithelial (cytokeratin-positive) cells but was enriched within the vicinity of mesenchymal (N-cadherin-positive) cells. These results indicate that hyaluronan and versican synthesized by ESCs within EB microenviron-ments are associated with EMT processes and furthermore suggest that endogenously produced ECM molecules play a role in ESC differentiation. This manuscript contains online supplemental material at http://www.jhc.org . Please visit this article online to view these materials.
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Yamagata, M., and K. Kimata. "Repression of a malignant cell-substratum adhesion phenotype by inhibiting the production of the anti-adhesive proteoglycan, PG-M/versican." Journal of Cell Science 107, no. 9 (September 1, 1994): 2581–90. http://dx.doi.org/10.1242/jcs.107.9.2581.

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Malignantly transformed cells usually display a rosette-like morphology of substratum adhesions (called podosomes) and disorganized microfilaments, and are often associated with elevated production of chondroitin sulphate. We previously showed that many tissues and cells express alternatively spliced multiforms of the large chondroitin sulphate proteoglycan termed PG-M (versican is one of the short transcripts). Since PG-M/versican inhibits many types of cell-substratum adhesion and is found to be excluded from focal contacts of cultured fibroblasts, it is likely that this proteoglycan is generally involved in regulating cell-substratum adhesion. We report here that PG-M/versican is selectively excluded from podosomes of human osteosarcoma cells and that specific inhibition of its biosynthesis by an antisense method suppresses such a malignant cell-adhesive phenotype. The results support the idea that PG-M/versican acts as an anti-adhesive molecule and raise the possibility that PG-M/versican controls one type of cancer cell behaviour.
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Theocharis, Achilleas D., Ioannis Tsolakis, Anders Hjerpe, and Nikos K. Karamanos. "Human abdominal aortic aneurysm is characterized by decreased versican concentration and specific downregulation of versican isoform V0." Atherosclerosis 154, no. 2 (February 2001): 367–76. http://dx.doi.org/10.1016/s0021-9150(00)00504-9.

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Higuchi, Tomoko, Daisuke Suzuki, Takafumi Watanabe, Kanda Fanhchaksai, Keiko Ota, Kazuhisa Yokoo, Hiroshi Furukawa, and Hideto Watanabe. "Versican contributes to ligament formation of knee joints." PLOS ONE 16, no. 4 (April 22, 2021): e0250366. http://dx.doi.org/10.1371/journal.pone.0250366.

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Versican is a large proteoglycan in the extracellular matrix. During embryonic stages, it plays a crucial role in the development of cartilage, heart, and dermis. Previously, we reported thatPrx1-Vcanconditional knockout mice, lacking Vcan expression in mesenchymal condensation areas of the limb bud, show the impaired joint formation and delayed cartilage development. Here, we investigated their phenotype in adults and found that they develop swelling of the knee joint. Histologically, their newborn joint exhibited impaired formation of both anterior and posterior cruciate ligaments. Immunostaining revealed a decrease in scleraxis-positive cells in both articular cartilage and ligament ofPrx1-Vcanknee joint, spotty patterns of type I collagen, and the presence of type II collagen concomitant with the absence of versican expression. These results suggest that versican expression during the perinatal period is required for cruciate ligaments’ formation and that its depletion affects joint function in later ages.
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Zhang, Zhenwei, Lei Miao, and Lianghua Wang. "Inflammation Amplification by Versican: The First Mediator." International Journal of Molecular Sciences 13, no. 6 (June 6, 2012): 6873–82. http://dx.doi.org/10.3390/ijms13066873.

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36

Bukong, Terence N., Sean B. Maurice, Barinder Chahal, David F. Schaeffer, and Paul J. Winwood. "Versican: a novel modulator of hepatic fibrosis." Laboratory Investigation 96, no. 3 (January 11, 2016): 361–74. http://dx.doi.org/10.1038/labinvest.2015.152.

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37

Carthy, Jon, Maziar Rahmani, Seti Boroomand, Darryl Knight, and Bruce McManus. "Versican induces fibroblast contraction of collagen gels." Matrix Biology 27 (December 2008): 57–58. http://dx.doi.org/10.1016/j.matbio.2008.09.413.

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38

Souza, L. P. G., K. S. N. Pires, J. C. Santos, C. M. Gonçalves, E. M. P. Silva, R. M. Botelho, H. G. S. Oliveira, A. L. M. Silva, K. S. C. Borbely, and A. U. Borbely. "Versican regulates trophoblast motility and cytoskeleton organization." Placenta 51 (March 2017): 113–14. http://dx.doi.org/10.1016/j.placenta.2017.01.057.

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39

Oliveira, H. G. S., K. S. N. Pires, J. C. Santos, C. M. Gonçalves, E. M. P. Silva, R. M. Botelho, L. P. G. Souza, et al. "Versican expression and roles in hydatidiform moles." Placenta 51 (March 2017): 125. http://dx.doi.org/10.1016/j.placenta.2017.01.091.

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40

Wang, Xiaobo, Guoqing Hu, and Jiliang Zhou. "Repression of Versican Expression by MicroRNA-143." Journal of Biological Chemistry 285, no. 30 (May 18, 2010): 23241–50. http://dx.doi.org/10.1074/jbc.m109.084673.

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41

Domenzain-Reyna, Clelia, Daniel Hernández, Laia Miquel-Serra, María José Docampo, Celia Badenas, Angels Fabra, and Anna Bassols. "Structure and Regulation of the Versican Promoter." Journal of Biological Chemistry 284, no. 18 (March 6, 2009): 12306–17. http://dx.doi.org/10.1074/jbc.m807108200.

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42

Hattori, Noriko, David A. Carrino, Mark E. Lauer, Amit Vasanji, James D. Wylie, Courtney M. Nelson, and Suneel S. Apte. "Pericellular Versican Regulates the Fibroblast-Myofibroblast Transition." Journal of Biological Chemistry 286, no. 39 (August 2, 2011): 34298–310. http://dx.doi.org/10.1074/jbc.m111.254938.

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43

Ito, Satoko, Utako Yokoyama, Taichi Nakakoji, Marion A. Cooley, Takako Sasaki, Sonoko Hatano, Yuko Kato, et al. "Fibulin-1 Integrates Subendothelial Extracellular Matrices and Contributes to Anatomical Closure of the Ductus Arteriosus." Arteriosclerosis, Thrombosis, and Vascular Biology 40, no. 9 (September 2020): 2212–26. http://dx.doi.org/10.1161/atvbaha.120.314729.

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Objective: The ductus arteriosus (DA) is a fetal artery connecting the aorta and pulmonary arteries. Progressive matrix remodeling, that is, intimal thickening (IT), occurs in the subendothelial region of DA to bring anatomic DA closure. IT is comprised of multiple ECMs (extracellular matrices) and migrated smooth muscle cells (SMCs). Because glycoprotein fibulin-1 binds to multiple ECMs and regulates morphogenesis during development, we investigated the role of fibulin-1 in DA closure. Approach and Results: Fibulin-1–deficient ( Fbln1 −/− ) mice exhibited patent DA with hypoplastic IT. An unbiased transcriptome analysis revealed that EP4 (prostaglandin E receptor 4) stimulation markedly increased fibulin-1 in DA-SMCs via phospholipase C-NFκB (nuclear factor κB) signaling pathways. Fluorescence-activated cell sorting (FACS) analysis demonstrated that fibulin-1 binding protein versican was derived from DA-endothelial cells (ECs). We examined the effect of fibulin-1 on directional migration toward ECs in association with versican by using cocultured DA-SMCs and ECs. EP4 stimulation promoted directional DA-SMC migration toward ECs, which was attenuated by either silencing fibulin-1 or versican. Immunofluorescence demonstrated that fibulin-1 and versican V0/V1 were coexpressed at the IT of wild-type DA, whereas 30% of versican-deleted mice lacking a hyaluronan binding site displayed patent DA. Fibulin-1 expression was attenuated in the EP4-deficient mouse ( Ptger4 −/− ) DA, which exhibits patent DA with hypoplastic IT, and fibulin-1 protein administration restored IT formation. In human DA, fibulin-1 and versican were abundantly expressed in SMCs and ECs, respectively. Conclusions: Fibulin-1 contributes to DA closure by forming an environment favoring directional SMC migration toward the subendothelial region, at least, in part, in combination with EC-derived versican and its binding partner hyaluronan.
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Sheng, Wang, Guizhi Wang, Yelina Wang, Jiyong Liang, Jianping Wen, Peng-Sheng Zheng, Yaojiong Wu, et al. "The Roles of Versican V1 and V2 Isoforms in Cell Proliferation and Apoptosis." Molecular Biology of the Cell 16, no. 3 (March 2005): 1330–40. http://dx.doi.org/10.1091/mbc.e04-04-0295.

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Versican is a large chondroitin sulfate proteoglycan belonging to the lectican family. Alternative splicing of versican generates at least four isoforms named V0, V1, V2, and V3. We have shown that the versican V1 isoform not only enhanced cell proliferation, but also modulated cell cycle progression and protected the cells from apoptosis. Futhermore, the V1 isoform was able to not only activate proto-oncogene EGFR expression and modulate its downstream signaling pathway, but also induce p27 degradation and enhance CDK2 kinase activity. As well, the V1 isoform down-regulated the expression of the proapoptotic protein Bad. By contrast, the V2 isoform exhibited opposite biological activities by inhibiting cell proliferation and down-regulated the expression of EGFR and cyclin A. Furthermore, V2 did not contribute apoptotic resistance to the cells. In light of these results, we are reporting opposite functions for the two versican isoforms whose expression is differentially regulated. Our studies suggest that the roles of these two isoforms are associated with the subdomains CSβ and CSα, respectively. These results were confirmed by silencing the expression of versican V1 with small interfering RNA (siRNA), which abolished V1-enhanced cell proliferation and V1-induced reduction of apoptosis.
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Evanko, Stephen P., Michel D. Gooden, Inkyung Kang, Christina K. Chan, Robert B. Vernon, and Thomas N. Wight. "A Role for HAPLN1 During Phenotypic Modulation of Human Lung Fibroblasts In Vitro." Journal of Histochemistry & Cytochemistry 68, no. 11 (October 16, 2020): 797–811. http://dx.doi.org/10.1369/0022155420966663.

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Hyaluronan and proteoglycan link protein 1 (HAPLN1) stabilizes interactions between two important extracellular matrix (ECM) macromolecules, versican and hyaluronan, which facilitate proliferation of fibroblasts and their conversion to myofibroblasts. However, the role of HAPLN1 in these events has not been studied. Using immunocytochemistry, cellular and ECM locations of HAPLN1 were evaluated in cultured human lung fibroblasts during proliferation and conversion to myofibroblasts. HAPLN1 localized to pericellular matrices, associating with both versican and hyaluronan in the ECM and on the cell surface. Nuclear and total HAPLN1 immunostaining increased after myofibroblast induction. Confocal microscopy showed HAPLN1 predominant in the ECM under cells while versican predominated above cells. Versican and HAPLN1 were also juxtaposed in columnar inclusions in the cytoplasm and nucleus. Nuclear HAPLN1 staining in interphase cells redistributed to the cytosol during mitosis. In the absence of TGF-β1, addition of exogenous bovine HAPLN1 (together with aggrecan G1) facilitated myofibroblast formation, as seen by significant upregulation of α-smooth muscle actin (SMA) staining, while adding full-length bovine versican had no effect. Increased compaction of hyaluronan-rich ECM suggests that HAPLN1 plus G1 addition affects hyaluronan networks and myofibroblast formation. These observations demonstrate changes in both extracellular and intracellular localization of HAPLN1 during fibroblast proliferation and myofibroblast conversion suggesting a possible role in fibrotic remodeling:
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46

Johnson, Katherine Anne, Philip Emmerich, Kristina A. Matkowskyj, and Dustin A. Deming. "Predicting CD8+ T-cell infiltration in colorectal cancer using versican proteolysis across molecular profiles." Journal of Clinical Oncology 38, no. 4_suppl (February 1, 2020): 189. http://dx.doi.org/10.1200/jco.2020.38.4_suppl.189.

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189 Background: The clinical indications for immunotherapies continue to increase across cancer types. In colorectal cancer (CRC), there has been little progress in the use of these therapies outside of mismatch repair deficient cancers (dMMR). However, even in dMMR cancers only a minority actually respond to the FDA-approved anti-PD1 agents. The tumor microenvironment is increasingly implicated in the resistance of cancers to immune-based therapies. Our group has previously described that accumulation of a matrix proteoglycan, versican, correlates with a reduction in CD8+ T-cell infiltration in CRCs, while proteolysis of versican, releasing the bioactive fragment versikine, correlates with increased infiltration. Here we examine the impact of pathogenic mutations on the utility of MMR status and versican proteolysis to predict CD8+ T-cell infiltration. Methods: Matched normal colon and CRC tissues from 122 patients were stained for versican, versikine, MLH1, MSH2, MSH6, PMS2, CNNB1, and CD8. Each was reviewed by a blinded GI surgical pathologist and CD8 quantified as tumor infiltrating lymphocytes (TILs) per high power field (hpf). 107 of the CRC samples were available for sequencing using the Qiagen Comprehensive Cancer Panel examining 160 genes across cancer relevant hotspots. The molecular profile was correlated with the IHC staining. Results: As previously reported, dMMR tumors had higher CD8+ T-cell infiltration. This trend persisted across dMMR genotypes (dMMR vs proficient (p)MMR p = 0.0016). Versican proteolysis correlated with increased CD8+ T cell infiltration in dMMR and pMMR cancers and was present in cancers with/without APC, TP53, and KRAS mutations. Across common mutations, cancers with the versican proteolysis predominant phenotype had more CD8+ T-cell infiltration than those without (APC mutant (mt): 11.82 vs 1.97 CD8+ TILs/hpf, p < 0.001; KRAS mt: 9.39 vs 3.08, p = 0.15; BRAF mt: 25.00 vs 7.50, p = 0.13; TP53 mt: 8.61 vs 1.63, p < 0.001). Conclusions: Across common mutations, versican proteolysis predicts CD8+ T-cell infiltration in both dMMR and pMMR CRC. Further investigation into whether this increase in infiltration will lead to greater immunotherapy response is warranted.
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Müller-Deile, Janina, Finn Gellrich, Heiko Schenk, Patricia Schroder, Jenny Nyström, Johan Lorenzen, Hermann Haller, and Mario Schiffer. "Overexpression of TGF-β Inducible microRNA-143 in Zebrafish Leads to Impairment of the Glomerular Filtration Barrier by Targeting Proteoglycans." Cellular Physiology and Biochemistry 40, no. 5 (2016): 819–30. http://dx.doi.org/10.1159/000453142.

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Background: TGF-β is known as an important stress factor of podocytes in glomerular diseases. Apart from activation of direct pro-apoptotic pathways we wanted to analyze micro-RNA (miRs) driven regulation of components involved in the integrity of the glomerular filtration barrier induced by TGF-β. Since miR-143-3p (miR-143) is described as a TGF-β inducible miR in other cell types, we examined this specific miR and its ability to induce glomerular pathology. Methods: We analyzed miR-143 expression in cultured human podocytes after stimulation with TGF-β. We also microinjected zebrafish eggs with a miR-143 mimic or with morpholinos specific for its targets syndecan and versican and compared phenotype and proteinuria development. Results: We detected a time dependent, TGF-β inducible expression of miR-143 in human podocytes. Targets of miR-143 relevant in glomerular biology are syndecans and versican, which are known components of the glycocalyx. We found that syndecan 1 and 4 were predominantly expressed in podocytes while syndecan 3 was largely expressed in glomerular endothelial cells. Versican could be detected in both cell types. After injection of a miR-143 mimic in zebrafish larvae, syndecan 3, 4 and versican were significantly downregulated. Moreover, miR-143 overexpression or versican knockdown by morpholino caused loss of plasma proteins, edema, podocyte effacement and endothelial damage. In contrast, knockdown of syndecan 3 and syndecan 4 had no effects on glomerular filtration barrier. Conclusion: Expression of versican and syndecan isoforms is indispensable for proper barrier function. Podocyte-derived miR-143 is a mediator for paracrine and autocrine cross talk between podocytes and glomerular endothelial cells and can alter expression of glomerular glycocalyx proteins.
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ILIC, Mirna Z., Phillip CARTER, Alicia TYNDALL, Jayesh DUDHIA, and Christopher J. HANDLEY. "Proteoglycans and catabolic products of proteoglycans present in ligament." Biochemical Journal 385, no. 2 (January 7, 2005): 381–88. http://dx.doi.org/10.1042/bj20040844.

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The aim of the present study was to characterize the proteoglycans and catabolic products of proteoglycans present in the tensile region of ligament and explant cultures of this tissue, and to compare these with those observed in the tensile region of tendon. Approx. 90% of the total proteoglycans in fresh ligament was decorin, as estimated by N-terminal amino acid sequence analysis. Other species that were detected were biglycan and the large proteoglycans versican (splice variants V0 and/or V1 and/or V2) and aggrecan. Approx. 23% of decorin detected in the matrix was degraded. Intact decorin and decorin fragments similar to those observed in the matrix that retained the N-terminus were also observed in the medium of ligament cultures. Intact biglycan core protein was detected in the matrix and medium of ligament cultures, and two fragments originating from the N-terminal region of biglycan were observed in the matrix of cultured ligament. Versican and versican fragments that retained the N-terminus of versican core protein were detected in fresh matrix and medium of tendon cultures. Approx. 42% of versican present in the fresh ligament was degraded. Aggrecan catabolites appearing in the culture medium were derived from aggrecanase cleavage of the core protein. An intact link protein and a degradation product from the N-terminal region of type XII collagen were also detected in the medium of the ligament explant.
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Lee, D.-Y., J.-H. Lee, J.-M. Yang, E.-S. Lee, G.-H. Mun, and K.-T. Jang. "Versican is localized to nail mesenchyme containing onychofibroblasts." Journal of the European Academy of Dermatology and Venereology 23, no. 11 (November 2009): 1328–29. http://dx.doi.org/10.1111/j.1468-3083.2009.03155.x.

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Ayars, Andrew G., Leonard C. Altman, Sue Potter-Perigo, Katherine Radford, Thomas N. Wight, and Parameswaran Nair. "Sputum Hyaluronan and Versican in Severe Eosinophilic Asthma." International Archives of Allergy and Immunology 161, no. 1 (2013): 65–73. http://dx.doi.org/10.1159/000343031.

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