TY - JOUR
T1 - Type X collagen isolated from the hypertrophic cartilage of embryonic chick tibiae contains both hydroxylysyl- and lysylpyridinoline cross-links
AU - Orth, M. W.
AU - Luchene, L. J.
AU - Schmid, T. M.
N1 - Copyright:
Copyright 2017 Elsevier B.V., All rights reserved.
PY - 1996/2/15
Y1 - 1996/2/15
N2 - Hypertrophic cartilage from the tibiotarsus of Day 20 chick embryonic tibiae was found to contain an unusually high concentration of lysylpyridinoline (LP), a nonreducible collagen cross-link normally found only in bone and dentin but not in cartilage. Since type X collagen is abundant in this cartilage, research was conducted to see if type X was the primary source of LP. The 45-kDa pepsin-resistant form of type X was purified by immunoaffinity chromatography. It contained a high concentration of the LP cross-link while type II contained primarily hydroxylysylpyridinoline (HP), the predominant cross-link in cartilage. This, to our knowledge is the first time that type X has been shown directly to form nonreducible cross-links and that a collagen other than type I has a high level of LP. Also, it is interesting that the HP and LP cross-links are found in a collagen that is degraded so rapidly. Possible explanations for these findings are discussed.
AB - Hypertrophic cartilage from the tibiotarsus of Day 20 chick embryonic tibiae was found to contain an unusually high concentration of lysylpyridinoline (LP), a nonreducible collagen cross-link normally found only in bone and dentin but not in cartilage. Since type X collagen is abundant in this cartilage, research was conducted to see if type X was the primary source of LP. The 45-kDa pepsin-resistant form of type X was purified by immunoaffinity chromatography. It contained a high concentration of the LP cross-link while type II contained primarily hydroxylysylpyridinoline (HP), the predominant cross-link in cartilage. This, to our knowledge is the first time that type X has been shown directly to form nonreducible cross-links and that a collagen other than type I has a high level of LP. Also, it is interesting that the HP and LP cross-links are found in a collagen that is degraded so rapidly. Possible explanations for these findings are discussed.
UR - http://www.scopus.com/inward/record.url?scp=0030005878&partnerID=8YFLogxK
U2 - 10.1006/bbrc.1996.0227
DO - 10.1006/bbrc.1996.0227
M3 - Article
C2 - 8604981
AN - SCOPUS:0030005878
VL - 219
SP - 301
EP - 305
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 2
ER -