Immunofluorescent localization of type-V collagen as a fibrillar component of the interstitial connective tissue of human oral mucosa, artery and liver

1986 ◽  
Vol 243 (3) ◽  
Author(s):  
D. Schuppan ◽  
J. Becker ◽  
H. Boehm ◽  
E.G. Hahn
Keyword(s):  
Connective Tissue ◽  
Oral Mucosa ◽  
Immunofluorescent Localization ◽  
Type V Collagen ◽  
Interstitial Connective Tissue ◽  
Fibrillar Component ◽  
Type V

scholarly journals Characterization of muscle epimysium, perimysium and endomysium collagens

1984 ◽  
Vol 219 (3) ◽  
pp. 1017-1026 ◽  
Author(s):  
N Light ◽  
A E Champion
Keyword(s):  
Connective Tissue ◽  
Sodium Dodecyl Sulphate ◽  
Type Iv Collagen ◽  
Sodium Dodecyl ◽  
Basement Membranes ◽  
Type Iii Collagen ◽  
Type I ◽  
Type V Collagen ◽  
Type Iv ◽  
Type V

In the past it has been proven difficult to separate and characterize collagen from muscle because of its relative paucity in this tissue. The present report presents a comprehensive methodology, combining methods previously described by McCollester [(1962) Biochim. Biophys. Acta 57, 427-437] and Laurent, Cockerill, McAnulty & Hastings [(1981) Anal. Biochem. 113, 301-312], in which the three major tracts of muscle connective tissue, the epimysium, perimysium and endomysium, may be prepared and separated from the bulk of muscle protein. Connective tissue thus prepared may be washed with salt and treated with pepsin to liberate soluble native collagen, or can be washed with sodium dodecyl sulphate to produce a very clean insoluble collagenous product. This latter type of preparation may be used for quantification of the ratio of the major genetic forms of collagen or for measurement of reducible cross-link content to give reproducible results. It was shown that both the epimysium and perimysium contain type I collagen as the major component and type III collagen as a minor component; perimysium also contained traces of type V collagen. The endomysium, the sheaths of individual muscle fibres, was shown to contain both type I and type III collagen as major components. Type V collagen was also present in small amounts, and type IV collagen, the collagenous component of basement membranes, was purified from endomysial preparations. This is the first biochemical demonstration of the presence of type IV collagen in muscle endomysium. The preparation was shown to be very similar to other type IV collagens from other basement membranes on sodium dodecyl sulphate/polyacrylamide-gel electrophoresis and was indistinguishable from EHS sarcoma collagen and placenta type IV collagen in the electron microscope after rotary shadowing.

Immunological detection of the type V collagen propeptide fragment, PVCP-1230, in connective tissue remodeling associated with liver fibrosis

Biomarkers ◽  
2011 ◽  
Vol 16 (5) ◽  
pp. 426-433 ◽  
Author(s):  
Efstathios Vassiliadis ◽  
Sanne S. Veidal ◽  
Henrik Simonsen ◽  
Dorthe V. Larsen ◽  
Ben Vainer ◽  
...  
Keyword(s):  
Liver Fibrosis ◽  
Connective Tissue ◽  
Tissue Remodeling ◽  
Type V Collagen ◽  
Immunological Detection ◽  
Type V ◽  
Connective Tissue Remodeling

Architectural remodelling in lungs of rabbits induced by type V collagen immunization: a preliminary morphologic model to study diffuse connective tissue diseases

2004 ◽  
Vol 200 (10) ◽  
pp. 681-691 ◽  
Author(s):  
Walcy R. Teodoro ◽  
Ana P. Velosa ◽  
Samira S. Witzel ◽  
Ana L. Garippo ◽  
Cecília Farhat ◽  
...  
Keyword(s):  
Connective Tissue ◽  
Connective Tissue Diseases ◽  
Type V Collagen ◽  
Type V

ISOLATION OF INTACT TYPE V COLLAGEN FROM FISH INTRAMUSCULAR CONNECTIVE TISSUE

1998 ◽  
Vol 22 (3) ◽  
pp. 213-225 ◽  
Author(s):  
KENJI SATO ◽  
CHIHO OHASHI ◽  
MITSUMI MURAKI ◽  
HUKIKO ITSUDA ◽  
YOSHIHIRO YOKOYAMA ◽  
...  
Keyword(s):  
Connective Tissue ◽  
Type V Collagen ◽  
Type V

Induction and Differentiation of Dental Epithelium in Vivo and in Vitro

1982 ◽  
Vol 40 ◽  
pp. 142-145
Author(s):  
E. J. Kollar
Keyword(s):  
Connective Tissue ◽  
Oral Mucosa ◽  
Basal Lamina ◽  
Functional Derivatives ◽  
Specific Source ◽  
Dental Epithelium ◽  
Connective Tissue Stroma

The differentiation and maintenance of many specialized epithelial structures are dependent on the underlying connective tissue stroma and on an intact basal lamina. These requirements are especially stringent in the development and maintenance of the skin and oral mucosa. The keratinization patterns of thin or thick cornified layers as well as the appearance of specialized functional derivatives such as hair and teeth can be correlated with the specific source of stroma which supports these differentiated expressions.

Collagen fibrillogenesis in vitro: interaction of types I and V collagen

1986 ◽  
Vol 44 ◽  
pp. 210-211
Author(s):  
Arthur J. Wasserman ◽  
Kathy C. Kloos ◽  
David E. Birk
Keyword(s):  
Type I Collagen ◽  
Corneal Stroma ◽  
Minor Component ◽  
Homogeneous Distribution ◽  
Type I ◽  
Type V Collagen ◽  
Fibril Morphology ◽  
Type V ◽  
In Vitro Interaction

Type I collagen is the predominant collagen in the cornea with type V collagen being a quantitatively minor component. However, the content of type V collagen (10-20%) in the cornea is high when compared to other tissues containing predominantly type I collagen. The corneal stroma has a homogeneous distribution of these two collagens, however, immunochemical localization of type V collagen requires the disruption of type I collagen structure. This indicates that these collagens may be arranged as heterpolymeric fibrils. This arrangement may be responsible for the control of fibril diameter necessary for corneal transparency. The purpose of this work is to study the in vitro assembly of collagen type V and to determine whether the interactions of these collagens influence fibril morphology.

scholarly journals Binding of heparan sulfate to type V collagen

1989 ◽  
Vol 264 (14) ◽  
pp. 7950-7956 ◽  
Author(s):  
R G LeBaron ◽  
A Höök ◽  
J D Esko ◽  
S Gay ◽  
M Höök
Keyword(s):  
Heparan Sulfate ◽  
Type V Collagen ◽  
Type V
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