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 - Funding Information:
The authors thank Dan Pietryla for his excellent technical assistance with the HPLC analyses. The research was supported by NIH Grants AR39239 and HD 23681 and an Arthritis Foundation Illinois chapter grant (M.W.O).
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
SN - 0006-291X
VL - 219
SP - 301
EP - 305
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 2
ER -