N-telopeptide of type II collagen interacts with annexin V on human chondrocytes.
Type II collagen binds to chondrocytes through integrins and annexin V. While the potential integrin binding sites have been identified, it is unclear which domains bind to annexin V. Proteolytic fragments of collagen are known to modulate cell signaling pathways resulting in degradation of articular cartilage; it is unknown whether annexin V binds to the fragments. The focus of our study was to determine the binding of type II collagen and its fragments to chondrocytes using flow cytometry and fluorescence microscopy. The N-telopeptide binds to annexin V, whereas the C-telopeptide and triple helical peptides do not. These data suggest that the binding of the N-telopeptide of type II collagen is through annexin V, whereas binding of the C-telopeptide and the triple helical peptide to the surface of chondrocytes are potentially facilitated through other collagen receptors, such as integrins or cell-associated matrix proteins.
Lucic
Danijela
D
Department of Biochemistry, Rush University at Rush-Presbyterian-St Luke's Medical Center, Chicago, Illinois 60612, USA.
Mollenhauer
Juergen
J
Kilpatrick
Katherine E
KE
Cole
Ada A
AA
D000368:Aged; D000369:Aged, 80 and over; D000595:Amino Acid Sequence; D000818:Animals; D000843:Ankle Joint; D017304:Annexin A5 / Q000378:metabolism*; D001665:Binding Sites; D002358:Cartilage, Articular / Q000166:cytology; D002417:Cattle; D002478:Cells, Cultured; D019902:Chondrocytes / Q000166:cytology / Q000378:metabolism*; D024043:Collagen Type II / Q000378:metabolism*; D006801:Humans; D008875:Middle Aged; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000378:metabolism*
D017304:Annexin A5; D024043:Collagen Type II; D010446:Peptide Fragments