Log in

Relevant bibliographies by topics / Connexin 37 / Journal articles

To see the other types of publications on this topic, follow the link: Connexin 37.

Journal articles on the topic 'Connexin 37'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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 'Connexin 37.'

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

Yeh, Hung-I., Emmanuel Dupont, Steven Coppen, Stephen Rothery, and Nicholas J. Severs. "Gap Junction Localization and Connexin Expression in Cytochemically Identified Endothelial Cells of Arterial Tissue." Journal of Histochemistry & Cytochemistry 45, no. 4 (April 1997): 539–50. http://dx.doi.org/10.1177/002215549704500406.

Full text

Abstract:

Vascular endothelial cells interact with one another via gap junctions, but information on the precise connexin make-up of endothelial gap junctions in intact arterial tissue is limited. One factor contributing to this lack of information is that standard immunocytochemical methodologies applied to arterial sections do not readily permit unequivocal localization of connexin immunolabeling to endothelium. Here we introduce a method for multiple labeling with specific endothelial cell markers and one or more connexin-specific antibodies which overcomes this limitation. Applying this method to localize connexins 43, 40, and 37 by confocal microscopy, we show that the three connexin types have quite distinctive labeling patterns in different vessels. Whereas endothelial cells of rat aorta and coronary artery characteristically show extensive, prominent connexin40, and heterogeneous scattered connexin37, the former, unlike the latter, also has abundant connexin43. The relative lack of connexin43 in coronary artery endothelium was confirmed in both rat and human using three alternative antibodies. In the aorta, connexins43 and 40 commonly co-localize to the same junctional plaque. Even within a given type of endothelium, zonal variation in connexin expression was apparent. In rat endocardium, a zone just below the mitral valve region is marked by expression of greater quantities of connexin43 than surrounding areas. These results are consistent with the idea that differential expression of connexins may contribute to modulation of endothelial gap junction function in different segments and subzones of the arterial system.

APA, Harvard, Vancouver, ISO, and other styles

2

Łukowicz, Krzysztof, Karolina Fijał, Aleksandra Nowak, and Anna M. Osyczka. "Connexin 43 in osteogenesis." Postępy Higieny i Medycyny Doświadczalnej 74 (September 25, 2020): 406–15. http://dx.doi.org/10.5604/01.3001.0014.4153.

Full text

Abstract:

Skeleton formation and its proper functioning is possible thanks to specialized bone tissue cells: bone forming osteoblasts, bone resorbing osteoclasts and osteocytes located in bone cavities. Gap junctions are transmembrane channels connecting neighboring cell. Thanks to gap junctions it is possible for signals to be directly transmitted by cells. Gap junction type channels, and more specifically the connexin proteins that build them, have a key impacton the bone turnover process, and thus on both bone building and remodeling. A particularly important connexin in bone tissue is connexin43 (Cx43), which is necessary in the proper course of the bone formation process and in maintaining bone homeostasis. The importance of the presence of Cx43 in bones is showed by skeletal defects in diseases such as ODD syndrome and craniometaphyseal dysplasia caused by mutations in GJA1, the gene encoding Cx43. The role of Cx43 in the differentiation of stem cells into bone cells, anti-apoptotic action of bisphosphonates and bone responses to hormonal and mechanical stimuli have also been demonstrated. In addition to connexin43, the presence of other connexins such as connexin45, 46 and 37 was also noted in bone tissue.

APA, Harvard, Vancouver, ISO, and other styles

3

Carter, T. D., X. Y. Chen, G. Carlile, E. Kalapothakis, D. Ogden, and W. H. Evans. "Porcine aortic endothelial gap junctions: identification and permeation by caged InsP3." Journal of Cell Science 109, no. 7 (July 1, 1996): 1765–73. http://dx.doi.org/10.1242/jcs.109.7.1765.

Full text

Abstract:

Gap junction channels permit the direct intercellular transfer of ions and small molecules and allow electrotonic coupling within tissues. Porcine aortic endothelial cells were extensively coupled, as assessed by gap junctional transfer of Lucifer yellow and the fluorescent calcium indicators fluo-3 and furaptra, but were not permeable to rhodamine B isothiocyanate-dextran 10S. The subunit composition of gap junction channels of porcine aortic endothelial cells was characterised using both northern blot analysis and RT-PCR techniques. Messenger RNA encoding connexins 37 and 43, but not 26, 32 or 40, were found in freshly isolated and cultured porcine aortic endothelial cells. Western blots using antipeptide antibodies raised to unique sequences of connexins 37, 40 and 43 showed the presence of connexins 37 and 43, but no connexin 40 was detected. Immunostaining with anticonnexin 43 antibodies showed extensive punctate fluorescent decoration of contacting membranes, whilst antibodies to connexin 37 showed predominantly intracellular staining. Caged InsP3 was found to readily permeate endothelial gap junctions. These results show that primary cultures of porcine aortic endothelial cells express connexin 37 and 43, and provide strong evidence that the second messenger molecule InsP3 can permeate porcine endothelial gap junctions.

APA, Harvard, Vancouver, ISO, and other styles

4

Li, Zhenyu, and Susan S. Smyth. "Connexin 37 Counteracts Clotting." Circulation 124, no. 8 (August 23, 2011): 873–75. http://dx.doi.org/10.1161/circulationaha.111.045104.

Full text

APA, Harvard, Vancouver, ISO, and other styles

5

Sorensen, Charlotte Mehlin, Max Salomonsson, Thomas Hartig Braunstein, Morten Schak Nielsen, and Niels-Henrik Holstein-Rathlou. "Connexin mimetic peptides fail to inhibit vascular conducted calcium responses in renal arterioles." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 295, no. 3 (September 2008): R840—R847. http://dx.doi.org/10.1152/ajpregu.00491.2007.

Full text

Abstract:

Vascular conducted responses are believed to play a central role in controlling the microcirculatory blood flow. The responses most likely spread through gap junctions in the vascular wall. At present, four different connexins (Cx) have been detected in the renal vasculature, but their role in transmission of conducted vasoconstrictor signals in the preglomerular arterioles is unknown. Connexin mimetic peptides were previously reported to target and inhibit specific connexins. We, therefore, investigated whether conducted vasoconstriction in isolated renal arterioles could be blocked by the use of mimetic peptides directed against one or more connexins. Preglomerular resistance vessels were microdissected from kidneys of Sprague-Dawley rats and loaded with fura 2. The vessels were stimulated locally by applying electrical current through a micropipette, and the conducted calcium response was measured 500 μm from the site of stimulation. Application of connexin mimetic peptides directed against Cx40, 37/43, 45, or a cocktail with equimolar amounts of each, did not inhibit the propagated response, whereas the nonselective gap junction uncoupler carbenoxolone completely abolished the propagated response. However, the connexin mimetic peptides were able to reduce dye coupling between rat aorta endothelial cells shown to express primarily Cx40. In conclusion, we did not observe any attenuating effects on conducted calcium responses in isolated rat interlobular arteries when exposed to connexin mimetic peptides directed against Cx40, 37/43, or 45. Further studies are needed to determine whether conducted vasoconstriction is mediated via previously undescribed pathways.

APA, Harvard, Vancouver, ISO, and other styles

6

Burt, Janis M., Tasha K. Nelson, Alexander M. Simon, and Jennifer S. Fang. "Connexin 37 profoundly slows cell cycle progression in rat insulinoma cells." American Journal of Physiology-Cell Physiology 295, no. 5 (November 2008): C1103—C1112. http://dx.doi.org/10.1152/ajpcell.299.2008.

Full text

Abstract:

In addition to providing a pathway for intercellular communication, the gap junction-forming proteins, connexins, can serve a growth-suppressive function that is both connexin and cell-type specific. To assess its potential growth-suppressive function, we stably introduced connexin 37 (Cx37) into connexin-deficient, tumorigenic rat insulinoma (Rin) cells under the control of an inducible promoter. Proliferation of these iRin37 cells, when induced to express Cx37, was profoundly slowed: cell cycle time increased from 2 to 9 days. Proliferation and cell cycle time of Rin cells expressing Cx40 or Cx43 did not differ from Cx-deficient Rin cells. Cx37 suppressed Rin cell proliferation irrespective of cell density at the time of induced expression and without causing apoptosis. All phases of the cell cycle were prolonged by Cx37 expression, and progression through the G1/S checkpoint was delayed, resulting in accumulation of cells at this point. Serum deprivation augmented the effect of Cx37 to accumulate cells in late G1. Cx43 expression also affected cell cycle progression of Rin cells, but its effects were opposite to Cx37, with decreases in G1 and increases in S-phase cells. These effects of Cx43 were also augmented by serum deprivation. Cx-deficient Rin cells were unaffected by serum deprivation. Our results indicate that Cx37 expression suppresses cell proliferation by significantly increasing cell cycle time by extending all phases of the cell cycle and accumulating cells at the G1/S checkpoint.

APA, Harvard, Vancouver, ISO, and other styles

7

Jose, Pedro A., Shiyou Chen, and Ines Armando. "Connections in chronic kidney disease: connexin 43 and connexin 37 interaction." American Journal of Physiology-Renal Physiology 301, no. 1 (July 2011): F21—F23. http://dx.doi.org/10.1152/ajprenal.00204.2011.

Full text

APA, Harvard, Vancouver, ISO, and other styles

8

Johnson, Tiffany L., and Robert M. Nerem. "Endothelial Connexin 37, Connexin 40, and Connexin 43 Respond Uniquely to Substrate and Shear Stress." Endothelium 14, no. 4-5 (January 2007): 215–26. http://dx.doi.org/10.1080/10623320701617233.

Full text

APA, Harvard, Vancouver, ISO, and other styles

9

Simon, Alexander M., Daniel A. Goodenough, En Li, and David L. Paul. "Female infertility in mice lacking connexin 37." Nature 385, no. 6616 (February 1997): 525–29. http://dx.doi.org/10.1038/385525a0.

Full text

APA, Harvard, Vancouver, ISO, and other styles

10

De los Reyes, M., J. Palomino, R. Espinoza, and C. Gallego. "116 Differential expression of connexin 43 and 37 mRNA transcripts during the estrous cycle in canines." Reproduction, Fertility and Development 31, no. 1 (2019): 184. http://dx.doi.org/10.1071/rdv31n1ab116.

Full text

Abstract:

Gap junctions are intercellular channels that mediate cell-to-cell communication, allowing the passage of small signalling molecules. In the ovary, connexin 43 (Cx43) and connexin 37 (Cx37) are important gap junctional proteins expressed in the granulosa and cumulus cells or oocytes of several species. Gap junctions and connexins are required for the regulation of the oocytes meiotic resumption in preovulatory follicles after the surge of LH. However, unlike other species, canine oocytes do not resume meiosis before ovulation, which could be related to expression patterns of Cx43 and Cx37 during oocyte development and ovulation. Therefore, this study aimed to address the canine Cx37 and Cx43 gene expressions throughout the oestrous cycle, including the preovulatory period. The ovaries were obtained from bitches 1-6 years old (n=72) following ovariohysterectomy. The stage of the oestrous cycle was assessed according the ovarian structures and by measurements of serum progesterone (P4) levels obtained from blood samples on the day of surgery. Anestrus was <0.1 ng/mL P4 and absence of follicles or corpus luteum in the ovarian surface; proestrus was 0.2-2 ng/mL P4 and growing small to medium follicles on the surface of the ovaries; oestrus was 2-19 mg/mL P4 and large follicles on the surface of the ovaries; and diestrus was >20 ng/mL P4 and mainly predominant corpus luteum on the ovaries. For Cx43 analysis, follicular cells (granulosa and theca) were mechanically recovered from follicles (n=620) distributed into 4 types: prenatal (1 layer of granulosa cells up to the onset of antrum formation), small antral (~0.2-0.39mm), medium antral (~0.4-5.9mm), and large antral (~6-10mm). For Cx37 study, the cumulus-oocytes complexes (COC) from the same follicles were used. Total RNA extraction was performed, and the evaluation of gene expression levels was achieved by relative quantification quantitative PCR analysis in follicular cells and COC. The data from at least 3 independent experiments for each gene were evaluated by ANOVA. The gene expression of both Connexins were observed in all stages of follicular development; however, the mRNA levels varied over the oestrous cycle. Both Cx43 and Cx37 transcripts showed the highest (P<0.05) levels at anestrus when compared to other phases. The mRNA levels of both genes remained without changes in large follicles at oestrus stage, suggesting that, in contrast to other mammals where LH down-regulates connexins expression leading to the subsequent loss of intercellular coupling, the communication between the oocyte and follicular cells was maintained in canines. In conclusion, these 2 connexin genes were differentially expressed in canine follicular cells and COC during the follicular development. The maintenance of the gene expression of these connexins at the final follicular growth may be involved in the prolonged meiotic arrest in this species. Supported by Ga grant from FONDECYT (1171670).

APA, Harvard, Vancouver, ISO, and other styles

11

Foote, Cynthia I., Lan Zhou, Xing Zhu, and Bruce J. Nicholson. "The Pattern of Disulfide Linkages in the Extracellular Loop Regions of Connexin 32 Suggests a Model for the Docking Interface of Gap Junctions." Journal of Cell Biology 140, no. 5 (March 9, 1998): 1187–97. http://dx.doi.org/10.1083/jcb.140.5.1187.

Full text

Abstract:

Connexins, like true cell adhesion molecules, have extracellular domains that provide strong and specific homophilic, and in some cases, heterophilic interactions between cells. Though the structure of the binding domains of adhesion proteins have been determined, the extracellular domains of connexins, consisting of two loops of ∼34–37 amino acids each, are not easily studied in isolation from the rest of the molecule. As an alternative, we used a novel application of site-directed mutagenesis in which four of the six conserved cysteines in the extracellular loops of connexin 32 were moved individually and in all possible pairwise and some quadruple combinations. This mapping allowed us to deduce that all disulfides form between the two loops of a single connexin, with the first cysteine in one loop connected to the third of the other. Furthermore, the periodicity of movements that produced functional channels indicated that these loops are likely to form antiparallel β sheets. A possible model that could explain how these domains from apposed connexins interact to form a complete channel is discussed.

APA, Harvard, Vancouver, ISO, and other styles

12

Afanasyeva, Marina H., Vyacheslav M. Bolotskih, and Victoria O. Polyakova. "Signal molecules as biomarkers of prediction of the premature rupture of membranes (clinicodiagnostic aspects)." Journal of obstetrics and women's diseases 65, no. 6 (December 15, 2016): 19–27. http://dx.doi.org/10.17816/jowd65619-27.

Full text

Abstract:

One of the most commonly encountered pregnancy complications is the premature rupture of membranes. This pathology results in the increase of frequency of operative delivery, birth traumatism and neonatal complications. The purpose of the research described was verification of key signal molecules, providing integrity of fetal membranes, with subsequent development of possible biomarkers of non-invasive prediction of the premature rupture of membranes. This work presents the comparison studies of expression of VEGF, MMP-9, connexin 37, connexin 40, endorphins, enkephalins, actin, miosin in a buccal epithelium and fetal membranes for 70 patients of the basic group (with premature rupture of membranes) and for 70 patients of the control group (with timely rupture of membranes). Research of fetal membranes and buccal epithelium was carried out by means of primary monoclonal mouse antibodies to the investigated markers. The universal basis set was used as the secondary antibodies, containing of biotinylated anti-mouse immunoproteins. The study of the preparations was carried out in the confocal microscope OLYMPUS FLUOVIEW FV 1000 at the image enlargement of ×400 and ×1000 with use of the system MRC-1024, with the software suite for computer processing OLYMPUS FLUOVIEW 5.0. Statistical processing of the material was carried out with the application of the standard statistical software suite Statistica 10.0. Obtained in a group with the premature rupture of membranes and in a control group were the reliable differences of expression of MMP-9, VEGF, connexin 37 and connexin 40 were. The multifactorial analysis of the indices of expression of signal molecules allowed to discover the high information significance for premature rupture of membranes prediction, matrix metalloproteinase ММP-9, connexin 37 and connexin 40, as well as VEGF. Matrix metalloproteinase ММP-9, connexin 37 and connexin 40, VEGF can be considered as non-invasive markers of premature rupture of membranes prediction.

APA, Harvard, Vancouver, ISO, and other styles

13

Nuttinck, Fabienne, Nathalie Peynot, Patrice Humblot, Alban Massip, Franz Dessy, and Jacques E. Fl�chon. "Comparative immunohistochemical distribution of connexin 37 and connexin 43 throughout folliculogenesis in the bovine ovary." Molecular Reproduction and Development 57, no. 1 (2000): 60–66. http://dx.doi.org/10.1002/1098-2795(200009)57:1<60::aid-mrd9>3.0.co;2-6.

Full text

APA, Harvard, Vancouver, ISO, and other styles

14

Park, Seoung Ju, Kyung Sun Lee, So Ri Kim, Kyung Hoon Min, Ka Young Lee, Yeong Hun Choe, Seung Yong Park, Sang Hyun Hong, and Yong Chul Lee. "Change of connexin 37 in allergen-induced airway inflammation." Experimental & Molecular Medicine 39, no. 5 (October 2007): 629–40. http://dx.doi.org/10.1038/emm.2007.69.

Full text

APA, Harvard, Vancouver, ISO, and other styles

15

Angelillo-Scherrer, Anne, Pierre Fontana, Laurent Burnier, Isabelle Roth, Rocco Sugamele, Anne Brisset, Sandrine Morel, et al. "Connexin 37 Limits Thrombus Propensity by Downregulating Platelet Reactivity." Circulation 124, no. 8 (August 23, 2011): 930–39. http://dx.doi.org/10.1161/circulationaha.110.015479.

Full text

APA, Harvard, Vancouver, ISO, and other styles

16

Borowczyk, Ewa, Mary Lynn Johnson, Jerzy J. Bilski, Pawel Borowicz, Dale A. Redmer, Lawrence P. Reynolds, and Anna T. Grazul-Bilska. "Gap Junctional Connexin 37 Is Expressed in Sheep Ovaries." Endocrine 30, no. 2 (2006): 223–30. http://dx.doi.org/10.1385/endo:30:2:223.

Full text

APA, Harvard, Vancouver, ISO, and other styles

17

Xue, Jianxiang, Linto Thomas, Jessica A. Dominguez Rieg, Robert A. Fenton, and Timo Rieg. "Genetic deletion of connexin 37 causes polyuria and polydipsia." PLOS ONE 15, no. 12 (December 17, 2020): e0244251. http://dx.doi.org/10.1371/journal.pone.0244251.

Full text

Abstract:

The connexin 37 (Cx37) channel is clustered at gap junctions between cells in the renal vasculature or the renal tubule where it is abundant in basolateral cell interdigitations and infoldings of epithelial cells in the proximal tubule, thick ascending limb, distal convoluted tubule and collecting duct; however, physiological data regarding its role are limited. In this study, we investigated the role of Cx37 in fluid homeostasis using mice with a global deletion of Cx37 (Cx37-/- mice). Under baseline conditions, Cx37-/- had ~40% higher fluid intake associated with ~40% lower urine osmolality compared to wild-type (WT) mice. No differences were observed between genotypes in urinary adenosine triphosphate or prostaglandin E2, paracrine factors that alter renal water handling. After 18-hours of water deprivation, plasma aldosterone and urine osmolality increased significantly in Cx37-/- and WT mice; however, the latter remained ~375 mmol/kg lower in Cx37-/- mice, an effect associated with a more pronounced body weight loss despite higher urinary AVP/creatinine ratios compared to WT mice. Consistent with this, fluid intake in the first 3 hours after water deprivation was 37% greater in Cx37-/- vs WT mice. Cx37-/- mice showed significantly lower renal AQP2 abundance and AQP2 phosphorylation at serine 256 than WT mice in response to vehicle or dDAVP, suggesting a partial contribution of the kidney to the lower urine osmolality. The abundance and responses of the vasopressin V2 receptor, AQP3, NHE3, NKCC2, NCC, H+-ATPase, αENaC, γENaC or Na+/K+-ATPase were not significantly different between genotypes. In summary, these results demonstrate that Cx37 is important for body water handling.

APA, Harvard, Vancouver, ISO, and other styles

18

Koval, M., S. T. Geist, E. M. Westphale, A. E. Kemendy, R. Civitelli, E. C. Beyer, and T. H. Steinberg. "Transfected connexin45 alters gap junction permeability in cells expressing endogenous connexin43." Journal of Cell Biology 130, no. 4 (August 15, 1995): 987–95. http://dx.doi.org/10.1083/jcb.130.4.987.

Full text

Abstract:

Many cells express multiple connexins, the gap junction proteins that interconnect the cytosol of adjacent cells. Connexin43 (Cx43) channels allow intercellular transfer of Lucifer Yellow (LY, MW = 443 D), while connexin45 (Cx45) channels do not. We transfected full-length or truncated chicken Cx45 into a rat osteosarcoma cell line ROS-17/2.8, which expresses endogenous Cx43. Both forms of Cx45 were expressed at high levels and colocalized with Cx43 at plasma membrane junctions. Cells transfected with full-length Cx45 (ROS/Cx45) and cells transfected with Cx45 missing the 37 carboxyl-terminal amino acids (ROS/Cx45tr) showed 30-60% of the gap junctional conductance exhibited by ROS cells. Intercellular transfer of three negatively charged fluorescent reporter molecules was examined. In ROS cells, microinjected LY was transferred to an average of 11.2 cells/injected cell, while dye transfer between ROS/Cx45 cells was reduced to 3.9 transfer between ROS/Cx45 cells was reduced to 3.9 cells. In contrast, ROS/Cx45tr cells transferred LY to > 20 cells. Transfer of calcein (MW = 623 D) was also reduced by approximately 50% in ROS/Cx45 cells, but passage of hydroxycoumarin carboxylic acid (HCCA; MW = 206 D) was only reduced by 35% as compared to ROS cells. Thus, introduction of Cx45 altered intercellular coupling between cells expressing Cx43, most likely the result of direct interaction between Cx43 and Cx45. Transfection of Cx45tr and Cx45 had different effects in ROS cells, consistent with a role of the carboxyl-terminal domain of Cx45 in determining gap junction permeability or interactions between connexins. These data suggest that coexpression of multiple connexins may enable cells to achieve forms of intercellular communication that cannot be attained by expression of a single connexin.

APA, Harvard, Vancouver, ISO, and other styles

19

Lee, Robert Kuo-Kuang, Sheng-Hsiang Li, Chung-Hao Lu, Hsin-Yi Ho, Ying-Jie Chen, and Hung-I. Yeh. "Abnormally low expression of connexin 37 and connexin 43 in subcutaneously transplanted cryopreserved mouse ovarian tissue." Journal of Assisted Reproduction and Genetics 25, no. 9-10 (September 2008): 489–97. http://dx.doi.org/10.1007/s10815-008-9264-8.

Full text

APA, Harvard, Vancouver, ISO, and other styles

20

Sabry, Reem, Charlotte Apps, Jaqueline A. Reiter-Saunders, Angela C. Saleh, Sumetha Balachandran, Elizabeth J. St. John, and Laura A. Favetta. "BPA and BPS Affect Connexin 37 in Bovine Cumulus Cells." Genes 12, no. 2 (February 23, 2021): 321. http://dx.doi.org/10.3390/genes12020321.

Full text

Abstract:

Bisphenol S (BPS) is used as an alternative plasticizer to Bisphenol A (BPA), despite limited knowledge of potential adverse effects. BPA exhibits endocrine disrupting effects during development. This article focuses on the impact of bisphenols during oocyte maturation. Connexins (Cx) are gap junctional proteins that may be affected by bisphenols, providing insight into their mechanism during development. Cxs 37 and 43 are crucial in facilitating cell communication between cumulus cells and oocytes. Cumulus-oocyte complexes (COCs), denuded oocytes, and cumulus cells were exposed to 0.05 mg/mL BPA or BPS for 24 h. Both compounds had no effect on Cx43. Cumulus cells exhibited a significant increase in Cx37 expression following BPA (p = 0.001) and BPS (p = 0.017) exposure. COCs treated with BPA had increased Cx37 protein expression, whilst BPS showed no effects, suggesting BPA and BPS act through different mechanisms. Experiments conducted in in vitro cultured cumulus cells, obtained by stripping germinal vesicle oocytes, showed significantly increased expression of Cx37 in BPA, but not the BPS, treated group. BPA significantly increased Cx37 protein expression, while BPS did not. Disrupted Cx37 following BPA exposure provides an indication of possible effects of bisphenols on connexins during the early stages of development.

APA, Harvard, Vancouver, ISO, and other styles

21

Horan, P. G. "The connexin 37 gene polymorphism and coronary artery disease in Ireland." Heart 92, no. 3 (October 10, 2005): 395–96. http://dx.doi.org/10.1136/hrt.2004.055665.

Full text

APA, Harvard, Vancouver, ISO, and other styles

22

Cai, Wei-jun, Sophie Koltai, Dimitri Scholz, Wolfgang Schaper, and Jutta Schaper. "Connexin 37 and desmin, early markers for arteriogenesis in canine heart." Journal of Molecular and Cellular Cardiology 33, no. 6 (June 2001): A17. http://dx.doi.org/10.1016/s0022-2828(01)90067-7.

Full text

APA, Harvard, Vancouver, ISO, and other styles

23

Ludwig, M., O. Eickmeier, C. Smaczny, F. Schreiner, W. Dubois, D. NGampolo, R. Schubert, S. Zielen, R. Ganschow, and S. Schmitt-Grohé. "Connexin 37 and Connexin 43 genotypes in correlation to cytokines in induced sputum and blood in cystic fibrosis (CF)." Molecular and Cellular Pediatrics 1, Suppl 1 (2014): A11. http://dx.doi.org/10.1186/2194-7791-1-s1-a11.

Full text

APA, Harvard, Vancouver, ISO, and other styles

24

Stoessel, Adelina, Nina Himmerkus, Markus Bleich, Sebastian Bachmann, and Franziska Theilig. "Connexin 37 is localized in renal epithelia and responds to changes in dietary salt intake." American Journal of Physiology-Renal Physiology 298, no. 1 (January 2010): F216—F223. http://dx.doi.org/10.1152/ajprenal.00295.2009.

Full text

Abstract:

Connexins are the main components of gap junction channels, which are important for intercellular communication. In the kidney, several members of the connexin (Cx) family have been identified. Renal vascular expression and hemodynamic impacts have so far been shown for Cx37, Cx40, and Cx43. Additionally, Cx30, Cx30.3, and Cx43 have been identified to be part of tubular epithelial gap junctions and/or hemichannels. However, the localization and role of other Cx family members in renal epithelial structures remain undetermined. We aimed to localize Cx37 in the kidney to obtain information on its epithelial expression and potential functions. Immunohistochemistry in rodent kidney showed characteristic punctate patterns in the vasculature and along the nephron. Strong basolateral expression was found in the thick ascending limb and distal convoluted tubule. Weaker abundances were found in the proximal tubule and the collecting duct also at the basolateral side. In situ hybridization and real-time PCR of isolated nephron segments confirmed this distribution at the mRNA level. Ultrastructurally, Cx37 immunostaining was confined to basolateral cell interdigitations and infoldings. As a functional approach, rats were fed low- or high-salt diets. Compared with control and high-salt diets, rats treated with low-salt diet showed significantly increased Cx37 mRNA and protein levels. This may be indicative of an adaptive tubular response to changes in sodium reabsorption. In summary, renal epithelia express Cx37 in their basolateral membranes. Here, the formation of Cx37 gap junctions may be involved in cellular communication and adjustments of vectorial epithelial transport.

APA, Harvard, Vancouver, ISO, and other styles

25

GUO, SUXIA, JIHONG ZHU, ZHENYU YANG, JIAN FENG, KULIN LI, RUXING WANG, and XIANGJUN YANG. "Reduction of connexin 37 expression by RNA interference decreases atherosclerotic plaque formation." Molecular Medicine Reports 11, no. 4 (December 4, 2014): 2664–70. http://dx.doi.org/10.3892/mmr.2014.3053.

Full text

APA, Harvard, Vancouver, ISO, and other styles

26

Lin, S. H., C. Y. Lu, R. Muhammad, W. Y. Chou, F. C. Lin, P. C. Wu, C. R. Lin, and L. C. Yang. "Induction of connexin 37 expression in a rat model of neuropathic pain." Molecular Brain Research 99, no. 2 (March 2002): 134–40. http://dx.doi.org/10.1016/s0169-328x(02)00112-2.

Full text

APA, Harvard, Vancouver, ISO, and other styles

27

Culler, C. E., P. S. Gargalovic, T. G. Kirchgessner, and A. J. Lusis. "Tu-P7: 156 Regulation of connexin 37 by oxidized phospholipids in atherosclerosis." Atherosclerosis Supplements 7, no. 3 (January 2006): 219. http://dx.doi.org/10.1016/s1567-5688(06)80862-7.

Full text

APA, Harvard, Vancouver, ISO, and other styles

28

Berke, Gideon, Vladimir Krutovskikh, and Hiroshi Yamasaki. "Connexin 37 gene is not mutated in lung carcinomas 3LL and CMT." Cancer Letters 195, no. 1 (May 2003): 67–72. http://dx.doi.org/10.1016/s0304-3835(03)00128-9.

Full text

APA, Harvard, Vancouver, ISO, and other styles

29

Krutovskikh, V., N. Mironov, and H. Yamasaki. "SHORT COMMUNICATION: Human connexin 37 is polymorphic but not mutated in tumours." Carcinogenesis 17, no. 8 (1996): 1761–63. http://dx.doi.org/10.1093/carcin/17.8.1761.

Full text

APA, Harvard, Vancouver, ISO, and other styles

30

Ludwig, M., O. Eickmeier, C. Smaczny, F. Schreiner, W. Dubois, D. N. Gampolo, R. Schubert, S. Zielen, R. Ganschow, and S. Schmitt-Grohé. "3 Connexin 37 and connexin 43 genotypes in correlation to cytokines in induced sputum and blood in cystic fibrosis (CF)." Journal of Cystic Fibrosis 14 (June 2015): S56. http://dx.doi.org/10.1016/s1569-1993(15)30180-6.

Full text

APA, Harvard, Vancouver, ISO, and other styles

31

Pan, Xiu-Di, Li-Ying Liang, Yi-Peng Du, Hong Ouyang, and Zhao-Hua Zeng. "Age-related changed expressions of connexin 37 and connexin 40 in ApoE-/-mice Fed with hyperlipidemic diet: atherosclerosis exacerbates the alteration." Journal of the American Society of Hypertension 10, no. 4 (April 2016): e50. http://dx.doi.org/10.1016/j.jash.2016.03.121.

Full text

APA, Harvard, Vancouver, ISO, and other styles

32

Good, Miranda E., José F. Ek-Vitorín, and Janis M. Burt. "Structural Determinants and Proliferative Consequences of Connexin 37 Hemichannel Function in Insulinoma Cells." Journal of Biological Chemistry 289, no. 44 (September 12, 2014): 30379–86. http://dx.doi.org/10.1074/jbc.m114.583054.

Full text

Abstract:

Connexin (Cx) 37 suppresses vascular and cancer cell proliferation. The C terminus and a channel able to function are necessary, and neither by itself is sufficient, for Cx37 to mediate growth suppression. Cx37 supports transmembrane and intercellular signaling by forming functional hemichannels (HCs) and gap junction channels (GJCs), respectively. Here we determined whether Cx37 with HC, but not GJC, functionality would suppress proliferation of rat insulinoma (Rin) cells comparably to wild-type Cx37 (Cx37-WT). We mutated extracellular loop residues hypothesized to compromise HC docking but not HC function (six cysteines mutated to alanine, C54A,C61A,C65A, C187A,C192A,C198A (designated as C6A); N55I; and Q58L). All three mutants trafficked to the plasma membrane and formed protein plaques comparably to Cx37-WT. None of the mutants formed functional GJCs, and Cx37-C6A did not form functional HCs. Cx37-N55I and -Q58L formed HCs with behavior and permeation properties similar to Cx37-WT (especially Q58L), but none of the mutants suppressed Rin cell proliferation. The data indicate that determinants of Cx37 HC function differ from other Cxs and that HC functions with associated HC-supported protein-protein interactions are not sufficient for Cx37 to suppress Rin cell proliferation. Together with previously published data, these results suggest that Cx37 suppresses Rin cell proliferation only when in a specific conformation achieved by interaction of the C terminus with a Cx37 pore-forming domain able to open as a GJC.

APA, Harvard, Vancouver, ISO, and other styles

33

Grapes, L., Y. Zhang, and M. F. Rothschild. "Rapid communication: physical and linkage mapping of the porcine connexin 37 (CX37) gene." Journal of Animal Science 80, no. 5 (May 1, 2002): 1375–76. http://dx.doi.org/10.2527/2002.8051375x.

Full text

APA, Harvard, Vancouver, ISO, and other styles

34

Dominguez Rieg, J. A., J. M. Burt, P. Ruth, and T. Rieg. "P2Y2receptor activation decreases blood pressure via intermediate conductance potassium channels and connexin 37." Acta Physiologica 213, no. 3 (January 8, 2015): 628–41. http://dx.doi.org/10.1111/apha.12446.

Full text

APA, Harvard, Vancouver, ISO, and other styles

35

Guo, Suxia, Weixiang Chen, Ying Yang, Zhenyu Yang, and Minghua Cao. "Association Between 1019C/T Polymorphism in the Connexin 37 Gene and Essential Hypertension." Heart, Lung and Circulation 23, no. 10 (October 2014): 924–29. http://dx.doi.org/10.1016/j.hlc.2014.02.016.

Full text

APA, Harvard, Vancouver, ISO, and other styles

36

Teilmann, Stefan Cuoni. "Differential expression and localisation of connexin-37 and connexin-43 in follicles of different stages in the 4-week-old mouse ovary." Molecular and Cellular Endocrinology 234, no. 1-2 (April 2005): 27–35. http://dx.doi.org/10.1016/j.mce.2004.10.014.

Full text

APA, Harvard, Vancouver, ISO, and other styles

37

Hadizadeh, Mahrooyeh, Seiied Mohaddes Ardebili, Mansoor Salehi, Chris Young, Fariborz Mokarian, James McClellan, Qin Xu, et al. "GJA4/Connexin 37 Mutations Correlate with Secondary Lymphedema Following Surgery in Breast Cancer Patients." Biomedicines 6, no. 1 (February 22, 2018): 23. http://dx.doi.org/10.3390/biomedicines6010023.

Full text

APA, Harvard, Vancouver, ISO, and other styles

38

Pitha, J., P. Pithova, and J. A. Hubacek. "The role of connexin 37 gene polymorphism (1019C > T; Pro319Ser) in cardiovascular disease." Biopolymers and Cell 27, no. 2 (March 20, 2011): 118–23. http://dx.doi.org/10.7124/bc.00008a.

Full text

APA, Harvard, Vancouver, ISO, and other styles

39

Arensbak, Birgitte, Hanne B. Mikkelsen, Finn Gustafsson, Thorkil Christensen, and Niels-Henrik Holstein-Rathlou. "Expression of connexin 37, 40, and 43 mRNA and protein in renal preglomerular arterioles." Histochemistry and Cell Biology 115, no. 6 (June 2001): 479–87. http://dx.doi.org/10.1007/s004180100275.

Full text

APA, Harvard, Vancouver, ISO, and other styles

40

Boerma, M., L. Forsberg, L. Van Zeijl, R. Morgenstern, U. De Faire, C. Lemne, D. Erlinge, T. Thulin, Y. Hong, and I. A. Cotgreave. "A genetic polymorphism in connexin 37 as a prognostic marker for atherosclerotic plaque development." Journal of Internal Medicine 246, no. 2 (August 1999): 211–18. http://dx.doi.org/10.1046/j.1365-2796.1999.00564.x.

Full text

APA, Harvard, Vancouver, ISO, and other styles

41

Gustafsson, Finn, Hanne B. Mikkelsen, Birgitte Arensbak, Lars Thuneberg, Søren Neve, Lars J. Jensen, and Niels-Henrik Holstein-Rathlou. "Expression of connexin 37, 40 and 43 in rat mesenteric arterioles and resistance arteries." Histochemistry and Cell Biology 119, no. 2 (February 2003): 139–48. http://dx.doi.org/10.1007/s00418-002-0493-0.

Full text

APA, Harvard, Vancouver, ISO, and other styles

42

Inai, Tetsuichiro, and Yosaburo Shibata. "Heterogeneous expression of endothelial connexin (Cx) 37, Cx40, and Cx43 in rat large veins." Anatomical Science International 84, no. 3 (March 26, 2009): 237–45. http://dx.doi.org/10.1007/s12565-009-0029-y.

Full text

APA, Harvard, Vancouver, ISO, and other styles

43

Takenaka, Tsuneo, Tsutomu Inoue, Yoshihiko Kanno, Hirokazu Okada, Caryl E. Hill, and Hiromichi Suzuki. "Connexins 37 and 40 transduce purinergic signals mediating renal autoregulation." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 294, no. 1 (January 2008): R1—R11. http://dx.doi.org/10.1152/ajpregu.00269.2007.

Full text

Abstract:

Our previous data indicated that various subtypes of connexin (Cx) were expressed in the juxtaglomerular apparatus. Experiments were performed to characterize the effects on renal autoregulation of specific mimetic peptides that inhibit these Cx subtypes in Wistar-Kyoto rats. Intrarenal infusion of Cx37,43GAP27 increased autoregulatory index of renal plasma flow (0.06 ± 0.05 to 0.47 ± 0.06, n = 6, P < 0.05) and glomerular filtration rate (GFR; 0.01 ± 0.07 to 0.49 ± 0.07, P < 0.05). The additional administration of 8-cyclopentyl- 1,3-dipropylxanthine (CPX) produced a further elevation of autoregulatory index of RPF (0.86 ± 0.07, P < 0.05) and GFR (0.88 ± 0.09, P < 0.05), compared with Cx37,43GAP27 alone. However, the addition of pyridoxal-phosphate-6-azophenyl-2,4-disulfonic acid (PPADS) to Cx37,43GAP27 did not. Combined treatment with CPX and PPADS markedly worsened autoregulatory index of RPF (0.04 ± 0.10 to 0.81 ± 0.06, n = 6 P < 0.01) and GFR (0.05 ± 0.08 to 0.79 ± 0.05, P < 0.01). Cx40GAP27 induced similar changes to Cx37,43GAP27. Renal autoregulation was preserved in the presence of Cx43GAP26. Our results indicate that the inhibition of gap junction impaired renal autoregulation. Furthermore, the present data provide evidence that both adenosine and purinergic receptors contribute to glomerular autoregulation. Finally, our findings suggest that gap junctions, at least in part, transduce purinergic signals mediating renal autoregulation.

APA, Harvard, Vancouver, ISO, and other styles

44

JING, YUANMING, SUXIA GUO, XIAOPING ZHANG, AIJING SUN, FENG TAO, HAIXING JU, and HAIXIN QIAN. "Effects of small interfering RNA interference of connexin 37 on subcutaneous gastric tumours in mice." Molecular Medicine Reports 10, no. 6 (October 8, 2014): 2955–60. http://dx.doi.org/10.3892/mmr.2014.2609.

Full text

APA, Harvard, Vancouver, ISO, and other styles

45

Pitha, J., P. Pithova, P. Stavek, J. A. Hubacek, O. Auzky, R. Houdkova, S. Eisenreichova, T. Neskudla, T. Pelikanova, and M. Kvapil. "Connexin 37 gene polymorphism and atherosclerotic changes in women with diabetes type 1 and 2." Atherosclerosis 275 (August 2018): e184-e185. http://dx.doi.org/10.1016/j.atherosclerosis.2018.06.563.

Full text

APA, Harvard, Vancouver, ISO, and other styles

46

Han, Yaling, Suya Xi, Xiaolin Zhang, Chenghui Yan, Yong Yang, and Jian Kang. "Association of Connexin 37 Gene Polymorphisms with Risk of Coronary Artery Disease in Northern Han Chinese." Cardiology 110, no. 4 (December 12, 2007): 260–65. http://dx.doi.org/10.1159/000112410.

Full text

APA, Harvard, Vancouver, ISO, and other styles

47

Koutsoumpas, Andreas, Dimitrios Polymeros, Zacharias Tsiamoulos, Daniel Smyk, George Karamanolis, Konstantinos Triantafyllou, E. I. Rigopoulou, et al. "Peculiar antibody reactivity to human connexin 37 and its microbial mimics in patients with Crohn's disease." Journal of Crohn's and Colitis 5, no. 2 (April 2011): 101–9. http://dx.doi.org/10.1016/j.crohns.2010.10.009.

Full text

APA, Harvard, Vancouver, ISO, and other styles

48

Pit′ha, J., P. Pithova, P. Stavek, J. A. Hubacek, O. Auzky, T. Neskudla, T. Pelikanova, and M. Kvapil. "Gene for connexin 37 is associated with athersclerotic changes in women with diabetes mellitus type 2." Atherosclerosis 252 (September 2016): e144-e145. http://dx.doi.org/10.1016/j.atherosclerosis.2016.07.715.

Full text

APA, Harvard, Vancouver, ISO, and other styles

49

BEHR, B. "The gap junction gene Connexin 37 is upregulated by low level GM-CSF in mouse preimplantation embryos." Fertility and Sterility 77 (April 2002): S9. http://dx.doi.org/10.1016/s0015-0282(02)03018-2.

Full text

APA, Harvard, Vancouver, ISO, and other styles

50

Zhang, Lixia, Ruohong Ding, Peng Kuang, Leiping Wang, Huixin Deng, Qingqing Xiong, and Hong Jiang. "Interaction between CONNEXIN37 and PDE4D gene polymorphisms with susceptibility to ischemic stroke in Chinese population." Experimental Biology and Medicine 244, no. 18 (October 25, 2019): 1642–47. http://dx.doi.org/10.1177/1535370219885079.

Full text

Abstract:

The objective of this study was to test the relationship of several single nucleotide polymorphisms (SNPs) within phosphodiesterase 4D ( PDE4D) and connexin 37 ( CONNEXIN37) gene additional interactions with ischemic stroke (IS) risk. The online software SNPstats was used for Hardy–Weinberg equilibrium testing. Generalized multifactor dimensionality reduction (GMDR) was employed to detect the potential interactions among CONNEXIN37 gene, PDE4D gene, and smoking. The results indicated that the rs1764391-T and rs966221-G were correlated with higher IS risk, the corresponding ORs (95% CI) were 1.66 (1.21–2.03) and 1.48 (1.11–1.92), respectively. We also found that the first two loci including rs1764391 and rs918592, and the other two-loci including rs1764391 and smoking were significant in the GMDR model. Participants with rs1764391-CT/TT and rs918592-CT/TT genotype have the highest IS risk, compared to subjects with rs1764391-CC and rs918592-CC genotype, OR (95%CI) = 3.16 (1.83–4.45); smokers with rs1764391-CT/TT genotype also have the highest IS risk, compared to never smokers with rs1764391-CC genotype, OR (95%CI) = 2.82 (1.53–4.15), but no significant interaction combinations were found between gene and alcohol drinking. So in this study, the rs1764391-T and rs966221-G, rs1764391–rs918592 interaction, rs1764391–smoking interaction were all associated with higher IS susceptibility. Impact statement Till now, no study investigated the interaction between CONNEXIN37 and PDE4D gene, and the gene–environment interaction. Therefore, in the current study, we aimed to evaluate the impact of interactions between CONNEXIN37 and PDE4D gene, and its interaction with environmental risk factors on susceptibility to ischemic stroke (IS).

APA, Harvard, Vancouver, ISO, and other styles

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!