Medical College of Wisconsin
CTSIResearch InformaticsREDCap

Type II collagen levels correlate with mineralization by articular cartilage vesicles. Arthritis Rheum 2009 Sep;60(9):2741-6

Date

08/29/2009

Pubmed ID

19714645

Pubmed Central ID

PMC2749926

DOI

10.1002/art.24773

Scopus ID

2-s2.0-69449107152 (requires institutional sign-in at Scopus site)   16 Citations

Abstract

OBJECTIVE: Pathologic mineralization is common in osteoarthritic (OA) cartilage and may be mediated by extracellular organelles known as articular cartilage vesicles (ACVs). Paradoxically, ACVs isolated from OA human cartilage mineralize poorly in vitro compared with those isolated from normal porcine cartilage. We recently showed that collagens regulate ACV mineralization. We sought to determine differences between collagens and collagen receptors on human and porcine ACVs as a potential explanation of their different mineralization behaviors.

METHODS: ACVs were enzymatically released from old and young human and porcine hyaline articular cartilage. Western blotting was used to determine the presence of types I, II, VI, and X collagen and various collagen receptors on ACVs. Type II collagen was quantified by enzyme-linked immunosorbent assay. Biomineralization was assessed by measuring the uptake of (45)Ca by isolated ACVs in agarose gels and by ACVs in situ in freeze-thawed cartilage.

RESULTS: As previously shown, isolated human ACVs mineralized poorly in response to ATP compared with porcine ACVs, but human and porcine ACVs mineralized similarly in situ in freeze-thawed cartilage. Type II collagen levels were 100-fold higher in isolated human ACVs than in porcine ACVs. Type II collagen in human ACVs was of high molecular weight. Transglutaminase-crosslinked type II collagen showed increased resistance to collagenase, suggesting a possible explanation for residual collagen on human ACVs. Expression of other collagens and collagen receptors was similar on human and porcine ACVs.

CONCLUSION: Higher levels of type II collagen in human ACV preparations, perhaps mediated by increased transglutaminase crosslinking, may contribute to the decreased mineralization observed in isolated human ACVs in vitro.

Author List

Jubeck B, Muth E, Gohr CM, Rosenthal AK

Author

Ann K. Rosenthal MD Associate Dean, Professor in the Medicine department at Medical College of Wisconsin




MESH terms used to index this publication - Major topics in bold

Adolescent
Adult
Aged
Aged, 80 and over
Animals
Calcium Phosphates
Calcium Pyrophosphate
Cartilage, Articular
Collagen Type II
Humans
Organelles
Osteoarthritis
Receptors, Collagen
Swine
Transglutaminases
Young Adult