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N-telopeptide of type II collagen interacts with annexin V on human chondrocytes

Danijela Lucic1, Juergen Mollenhauer, Katherine E Kilpatrick

  • 1Department of Biochemistry, Rush University at Rush-Presbyterian-St Luke's Medical Center, Chicago, Illinois 60612, USA.

Connective Tissue Research
|December 9, 2003
PubMed

Insights

The N-telopeptide of type II collagen binds to chondrocytes via annexin V. Other collagen fragments likely use different receptors, suggesting complex cell-collagen interactions in cartilage.

Area of Science:

  • Biochemistry
  • Cell Biology
  • Biomaterials Science

Background:

  • Type II collagen is crucial for articular cartilage structure and function.
  • Chondrocytes interact with collagen via cell surface receptors like integrins and annexin V.
  • The specific binding domains of collagen fragments to annexin V remain largely uncharacterized.

Purpose of the Study:

  • To investigate the binding interactions between type II collagen fragments and chondrocytes.
  • To identify the specific domains of type II collagen that bind to annexin V.
  • To elucidate the binding mechanisms of collagen fragments to chondrocytes.

Main Methods:

  • Utilized flow cytometry to quantify binding.
  • Employed fluorescence microscopy for visualizing binding sites.
  • Analyzed binding of full-length type II collagen and its proteolytic fragments (N-telopeptide, C-telopeptide, triple helical peptide) to chondrocytes.

Main Results:

  • The N-telopeptide of type II collagen demonstrated binding to annexin V on chondrocytes.
  • The C-telopeptide and triple helical peptides did not bind to annexin V.
  • These findings indicate distinct binding pathways for different collagen fragments.

Conclusions:

  • Annexin V mediates the binding of the N-telopeptide of type II collagen to chondrocytes.
  • Binding of C-telopeptide and triple helical peptides likely involves alternative receptors, such as integrins or cell-associated matrix proteins.
  • Understanding these specific interactions is vital for comprehending cartilage degradation and developing therapeutic strategies.

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