Susceptibility of type V collagen to neutral proteases: evidence that the major molecular species is a thrombin-sensitive heteropolymer, [.alpha.1(V)]2.alpha.2(V)

Biochemistry ◽  
1981 ◽  
Vol 20 (13) ◽  
pp. 3778-3784 ◽  
Author(s):  
Helene Sage ◽  
Pam Pritzl ◽  
Paul Bornstein
1988 ◽  
Vol 91 (3) ◽  
pp. 238-242 ◽  
Author(s):  
Yoko Hashimoto ◽  
Kunihiko Kobayashi ◽  
Takeshi Hoshino ◽  
Hisashi Aoyama ◽  
Taro Hayakawa

Author(s):  
Arthur J. Wasserman ◽  
Kathy C. Kloos ◽  
David E. Birk

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.


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

1993 ◽  
Vol 268 (21) ◽  
pp. 15544-15549
Author(s):  
J. Takagi ◽  
T. Fujisawa ◽  
T. Usui ◽  
T. Aoyama ◽  
Y. Saito
Keyword(s):  

1986 ◽  
Vol 6 (1) ◽  
pp. 1-13 ◽  
Author(s):  
Antonius L.J.J. Bronckers ◽  
Steffen Gay ◽  
Donacian M. Lyaruu ◽  
Renate E. Gay ◽  
Edward J. Miller

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