Imbalance in the Synthesis of Collagen Type I and Collagen Type III in Smooth Muscle Cells Derived from Human Varicose Veins

2001 ◽  
Vol 38 (6) ◽  
pp. 560-568 ◽  
Author(s):  
Patricia Sansilvestri-Morel ◽  
Alain Rupin ◽  
Cécile Badier-Commander ◽  
Patrick Kern ◽  
Jean-Noël Fabiani ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Smooth Muscle Cells ◽  
Collagen Type ◽  
Varicose Veins ◽  
Muscle Cells ◽  
Collagen Type I ◽  
Type I ◽  
Collagen Type Iii ◽  
Type Iii

scholarly journals Collagen degradation and platelet-derived growth factor stimulate the migration of vascular smooth muscle cells

2000 ◽  
Vol 113 (11) ◽  
pp. 2055-2064
Author(s):  
E. Stringa ◽  
V. Knauper ◽  
G. Murphy ◽  
J. Gavrilovic
Keyword(s):  
Smooth Muscle ◽  
Vascular Smooth Muscle ◽  
Smooth Muscle Cells ◽  
Smooth Muscle Cell ◽  
Vascular Smooth Muscle Cells ◽  
Muscle Cell ◽  
Collagen Type ◽  
Muscle Cells ◽  
Collagen Type I ◽  
Type I

Cell migration is a key event in many biological processes and depends on signals from both extracellular matrix and soluble motogenic factors. During atherosclerotic plaque development, vascular smooth muscle cells migrate from the tunica media to the intima through a basement membrane and interstitial collagenous matrix and proliferate to form a neointima. Matrix metalloproteinases have previously been implicated in neointimal formation and in this study smooth muscle cell adhesion and migration on degraded collagen have been evaluated. Vascular smooth muscle cells adhered to native intact collagen type I and to its first degradation by-product, 3/4 fragment (generated by collagenase-3 cleavage), unwound at 35 degrees C to mimic physiological conditions. PDGF-BB pre-treatment induced a fourfold stimulation of smooth muscle cell motility on the collagen 3/4 fragment whereas no increase in smooth muscle cell motility on collagen type I was observed. Cell migration on collagen type I was mediated by alpha2 integrin, whereas PDGF-BB-stimulated migration on the 3/4 collagen fragment was dependent on alphavbeta3 integrin. alphavbeta3 integrin was organised in clusters concentrated at the leading and trailing edges of the cells and was only expressed when cells were exposed to the 3/4 collagen fragment. Tyrphostin A9, an inhibitor of PDGF receptor-beta tyrosine kinase activity, resulted in complete abolition of migration of PDGF-BB treated cells on collagen type I and 3/4 fragment. These results strongly support the hypothesis that the cellular migratory response to soluble motogens can be regulated by proteolytic modification of the extracellular matrix.

In Vitro Growth of Human Urinary Tract Smooth Muscle Cells on Laminin and Collagen Type I-Coated Membranes under Static and Dynamic Conditions

2005 ◽  
Vol 11 (1-2) ◽  
pp. 161-171 ◽  
Author(s):  
Ulrich Hubschmid ◽  
Phaik-Mooi Leong-Morgenthaler ◽  
Aurelia Basset-Dardare ◽  
Sylvie Ruault ◽  
Peter Frey
Keyword(s):  
Smooth Muscle ◽  
Urinary Tract ◽  
Smooth Muscle Cells ◽  
Collagen Type ◽  
Muscle Cells ◽  
Collagen Type I ◽  
Type I ◽  
In Vitro Growth ◽  
Coated Membranes

SIRT1 deacetylates RFX5 and antagonizes repression of collagen type I (COL1A2) transcription in smooth muscle cells

2012 ◽  
Vol 428 (2) ◽  
pp. 264-270 ◽  
Author(s):  
Jun Xia ◽  
Xiaoyan Wu ◽  
Yuyu Yang ◽  
Yuhao Zhao ◽  
Mingming Fang ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Smooth Muscle Cells ◽  
Collagen Type ◽  
Muscle Cells ◽  
Collagen Type I ◽  
Type I

scholarly journals An In situ Collagen-HA Hydrogel System Promotes Survival and Preserves the Proangiogenic Secretion of hiPSC-derived Vascular Smooth Muscle Cells

2020 ◽  
Author(s):  
Biraja C. Dash ◽  
Kaiti Duan ◽  
Hao Xing ◽  
Themis R. Kyriakides ◽  
Henry C. Hsia
Keyword(s):  
Smooth Muscle ◽  
Vascular Smooth Muscle ◽  
Smooth Muscle Cells ◽  
Vascular Smooth Muscle Cells ◽  
Collagen Type ◽  
Muscle Cells ◽  
Collagen Type I ◽  
Type I ◽  
Hydrogel System

AbstractHuman induced pluripotent stem cell-derived vascular smooth muscle cells (hiPSC-VSMCs) with proangiogenic properties have huge therapeutic potential. While hiPSC-VSMCs have already been utilized for wound healing using a biomimetic collagen scaffold, an in situ forming hydrogel mimicking the native environment of skin offers the promise of hiPSC-VSMC mediated repair and regeneration. Herein, the impact of a collagen type-I-hyaluronic acid (HA) in situ hydrogel cross-linked using a PEG-based cross-linker on hiPSC-VSMCs viability and proangiogenic paracrine secretion was investigated. Our study demonstrated increases in cell viability, maintenance of phenotype and proangiogenic growth factor secretion, and proangiogenic activity in response to the conditioned medium. The optimally cross-linked and functionalized collagen type-I/HA hydrogel system developed in this study shows promise as an in situ hiPSC-VSMC carrier system for wound regeneration.

Decreased Production of Collagen Type III in Cultured Smooth Muscle Cells from Varicose Vein Patients Is due to a Degradation by MMPs: Possible Implication of MMP-3

2005 ◽  
Vol 42 (5) ◽  
pp. 388-398 ◽  
Author(s):  
Patricia Sansilvestri-Morel ◽  
Alain Rupin ◽  
Nicolas D. Jullien ◽  
Nathalie Lembrez ◽  
Patricia Mestries-Dubois ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Smooth Muscle Cells ◽  
Varicose Vein ◽  
Collagen Type ◽  
Muscle Cells ◽  
Collagen Type Iii ◽  
Type Iii ◽  
Cultured Smooth Muscle Cells

scholarly journals Effect of acute resistance exercise and sex on human patellar tendon structural and regulatory mRNA expression

2009 ◽  
Vol 106 (2) ◽  
pp. 468-475 ◽  
Author(s):  
Bridget E. Sullivan ◽  
Chad C. Carroll ◽  
Bozena Jemiolo ◽  
Scott W. Trappe ◽  
S. Peter Magnusson ◽  
...  
Keyword(s):  
Resistance Exercise ◽  
Mrna Expression ◽  
Patellar Tendon ◽  
Type I Collagen ◽  
Collagen Type ◽  
Collagen Type I ◽  
Tissue Inhibitors Of Metalloproteinases ◽  
Type I ◽  
Collagen Type Iii ◽  
Type Iii

Tendon is mainly composed of collagen and an aqueous matrix of proteoglycans that are regulated by enzymes called matrix metalloproteinases (MMPs) and tissue inhibitors of metalloproteinases (TIMPs). Although it is known that resistance exercise (RE) and sex influence tendon metabolism and mechanical properties, it is uncertain what structural and regulatory components contribute to these responses. We measured the mRNA expression of tendon's main fibrillar collagens (type I and type III) and the main proteoglycans (decorin, biglycan, fibromodulin, and versican) and the regulatory enzymes MMP-2, MMP-9, MMP-3, and TIMP-1 at rest and after RE. Patellar tendon biopsy samples were taken from six individuals (3 men and 3 women) before and 4 h after a bout of RE and from a another six individuals (3 men and 3 women) before and 24 h after RE. Resting mRNA expression was used for sex comparisons (6 men and 6 women). Collagen type I, collagen type III, and MMP-2 were downregulated ( P < 0.05) 4 h after RE but were unchanged ( P > 0.05) 24 h after RE. All other genes remained unchanged ( P > 0.05) after RE. Women had higher resting mRNA expression ( P < 0.05) of collagen type III and a trend ( P = 0.08) toward lower resting expression of MMP-3 than men. All other genes were not influenced ( P > 0.05) by sex. Acute RE appears to stimulate a change in collagen type I, collagen type III, and MMP-2 gene regulation in the human patellar tendon. Sex influences the structural and regulatory mRNA expression of tendon.

scholarly journals Connective tissue, glial and neuronal expressions in testis of the African giant rat (Cricetomys gambianus)

2017 ◽  
Vol 34 (03) ◽  
pp. 186-193
Author(s):  
T. Falade ◽  
M. Olude ◽  
O. Mustapha ◽  
E. Mbajiorgu ◽  
A. Ihunwo ◽  
...  
Keyword(s):  
Connective Tissue ◽  
Type I Collagen ◽  
Collagen Type ◽  
Neuronal Cells ◽  
Collagen Type I ◽  
Type I ◽  
Collagen Type Iii ◽  
Neuronal Markers ◽  
Type Iii ◽  
African Giant Rat

Abstract Introduction: This study was carried out to investigate the expression of connective tissue (Collagens I and III), glia and neuronal markers in the testis of the African giant rat using histology and immunohistochemistry techniques. Materials and Methods: Eight (8) apparently healthy wild male African giant rats were used for this experiment, divided into 2 groups (juvenile and adult) of 4 animals each. The testes were harvested following intracardial perfusion of the rats and histology was performed using Haematoxylin-Eosin stain and Mallory-Heideinhain rapid one- step staining for connective tissue. Immunohistochemical identification was achieved using the following antibodies: anti-collagen type I, anti-collagen type III, anti-glial fibrillary acidic protein and anti-p75 nerve growth factor for the expression of collagen type I, collagen type III, astrocyte-like cell and neuronal cells respectively. Photomicrography was achieved using Axioskop® microscope and quantitative data were analyzed using student t-test. Results: The cyto-architecture of the testis was typical in the African giant rat. The connective tissue expressed in the juvenile and adult group, signaling of glial-like cells were seen in the perivascular region across the experimental groups. Immuno-localization of neuronal cells were seen in the interstitial spaces across all the groups, but with more expressions in the juvenile. Conclusion: This work has provided a clear description of the expression of connective tissue, neuronal and glial cells in the testis of the African giant rat and their possible relationships across juvenile and adult groups.

Enhancement by Heparin of Affinity between Cold-Insoluble Globulin and Native Collagen Type III

1979 ◽  
Author(s):  
H. Hörmann ◽  
F. Jilek
Keyword(s):  
Collagen Type ◽  
Weight Ratio ◽  
Collagen Type I ◽  
Type I ◽  
Collagen Type Iii ◽  
Type Iii ◽  
Soluble Collagen ◽  
Native Collagen ◽  
Collagen Molecules ◽  
Cold Insoluble Globulin

Affinity between collagen and cold-insoluble globulin was measured by complexing soluble 125-J labelled collagen preparations with the globulin. Precipitates containing considerable activity were formed at 4°C and 22°C by denatured soluble collagen, type I and type III, but only little by native soluble collagen. The precipitation of native collagen, type III, by cold-insoluble globulin was enhanced by heparin. Under optimal conditions at a weight ratio or heparin and cold-insoluble globulin of about 1:1 up to 60% of the collagen applied was insolubilized. Native collagen, type I, was complexed far less effectively even in presence of heparin. Electronmicroscopic and precipitation experiments using 125-J labelled cold-insoluble globulin indicated that heparin might induce a partial conversion of cold-insoluble globulin to a fibrillar derivative which exhibited improved binding properties for the rod-like native collagen molecules. – Supported by Deutsche Forschungsgemeinschaft, Project Ho 740/1.

A Novel In-Vitro System for the Simultaneous Exposure of Bladder Smooth Muscle Cells to Mechanical Strain and Sustained Hydrostatic Pressure

2002 ◽  
Vol 124 (2) ◽  
pp. 208-213 ◽  
Author(s):  
Karen M. Haberstroh ◽  
Martin Kaefer ◽  
Natacha DePaola ◽  
Sarah A. Frommer ◽  
Rena Bizios
Keyword(s):  
Smooth Muscle ◽  
Hydrostatic Pressure ◽  
Smooth Muscle Cells ◽  
Collagen Type ◽  
Mechanical Strain ◽  
Muscle Cells ◽  
Collagen Type Iii ◽  
Bladder Smooth Muscle ◽  
Simultaneous Exposure

The novel hydrostrain system was designed in an effort to establish and maintain conditions that simulate the in-vivo mechanical environment of the bladder. In this laboratory system, ovine bladder smooth muscle cells on flexible, 10-cm-dia silastic membranes were exposed simultaneously to hydrostatic pressure (40 cm H2O, a pressure level currently associated with bladder pathologies) and mechanical strains (up to 25 percent) under standard cell culture conditions for 7 h. Under these conditions, Heparin Binding-Epidermal Growth Factor and Collagen Type III mRNA expression were significantly increased (p<0.01 and 0.1, respectively); however, no changes were observed in Collagen Type I mRNA expression. Decreases in the Collagen Type I:Type III ratio following simultaneous exposure of bladder smooth muscle cells to pathological levels of hydrostatic pressure and mechanical strain in vitro are in agreement with clinically observed increases in Collagen Type III with concomitant decreased human bladder compliance. The results of the present study, therefore, provide cellular/molecular level information relevant to bladder pathology that could have significant implications in the field of clinical urology.

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