TY - JOUR
T1 - Type III collagen can be present on banded collagen fibrils regardless of fibril diameter
AU - Keene, D. R.
AU - Sakai, L. Y.
AU - Bachinger, H. P.
AU - Burgerson, R. E.
PY - 1987
Y1 - 1987
N2 - Monoclonal antibodies that recognize an epitope within the triple helix of type III collagen have been used to examine the distribution of that collagen type in human skin, cornea, amnion, aorta, and tendon. Ultrastructural examination of those tissues indicates antibody binding to collagen fibrils in skin, amnion, aorta, and tendon regardless of the diameter of the fibril. The antibody distribution is unchanged with donor age, site of biopsy, or region of tissue examined. In contrast, antibody applied to adult human cornea localizes to isolated fibrils, which appear randomly throughout the matrix. These studies indicate that type III collagen remains associated with collagen fibrils after removal of the amino and carboxyl propeptides, and suggests that fibrils of skin, tendon, and amnion (and presumably many other tissues that contain both types I and III collagens) are copolymers of at least types I and III collagens.
AB - Monoclonal antibodies that recognize an epitope within the triple helix of type III collagen have been used to examine the distribution of that collagen type in human skin, cornea, amnion, aorta, and tendon. Ultrastructural examination of those tissues indicates antibody binding to collagen fibrils in skin, amnion, aorta, and tendon regardless of the diameter of the fibril. The antibody distribution is unchanged with donor age, site of biopsy, or region of tissue examined. In contrast, antibody applied to adult human cornea localizes to isolated fibrils, which appear randomly throughout the matrix. These studies indicate that type III collagen remains associated with collagen fibrils after removal of the amino and carboxyl propeptides, and suggests that fibrils of skin, tendon, and amnion (and presumably many other tissues that contain both types I and III collagens) are copolymers of at least types I and III collagens.
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U2 - 10.1083/jcb.105.5.2393
DO - 10.1083/jcb.105.5.2393
M3 - Article
C2 - 2445760
AN - SCOPUS:0023576831
SN - 0021-9525
VL - 105
SP - 2393
EP - 2402
JO - Journal of Cell Biology
JF - Journal of Cell Biology
IS - 5
ER -