TY - JOUR
T1 - Identification and immunolocalization of type X collagen at the ligament-bone interface
AU - Niyibizi, Christopher
AU - Sagarriga Visconti, Camilla
AU - Gibson, Gary
AU - Kavalkovich, Karl
N1 - Funding Information:
We thank Dr. Simon Watkins for help with confocal microscopy. This work was supported in part by NIH Grant R29AR42720.
PY - 1996/5/15
Y1 - 1996/5/15
N2 - In some ligaments, ligamentous collagen fibrils attach to bone by first passing through non-mineralized and mineralized fibrocartilage present at the ligament-bone interface. To understand better the function of these fibrocartilages, collagens present at the femoral insertion of the bovine medial collateral ligament were isolated and characterized. Types II and IX collagens were identified in pepsin digests of the tissue in addition to type X collagen originally thought to be associated with the cartilages undergoing endochondral bone formation. Presence of type X collagen was confirmed by immunoblotting and by immunofluorescence localization using laser confocal microscopy. Type X collagen was localized predominantly in the mineralized zone of the ligament insertion. These data indicate that type X collagen may play a role in ligament attachment to bone.
AB - In some ligaments, ligamentous collagen fibrils attach to bone by first passing through non-mineralized and mineralized fibrocartilage present at the ligament-bone interface. To understand better the function of these fibrocartilages, collagens present at the femoral insertion of the bovine medial collateral ligament were isolated and characterized. Types II and IX collagens were identified in pepsin digests of the tissue in addition to type X collagen originally thought to be associated with the cartilages undergoing endochondral bone formation. Presence of type X collagen was confirmed by immunoblotting and by immunofluorescence localization using laser confocal microscopy. Type X collagen was localized predominantly in the mineralized zone of the ligament insertion. These data indicate that type X collagen may play a role in ligament attachment to bone.
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U2 - 10.1006/bbrc.1996.0787
DO - 10.1006/bbrc.1996.0787
M3 - Article
C2 - 8670248
AN - SCOPUS:0030585343
SN - 0006-291X
VL - 222
SP - 584
EP - 589
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 2
ER -