Abstract Title

Regulation of Type II Collagen Fibrillogenesis In Vitro by Accessory and Chaperone Proteins

Disciplines

Biology | Cell and Developmental Biology | Chemistry

Abstract

Studies have shown that both Type I and Type II Collagen undergo fibrillogenesis under similar conditions, namely at near normal body temperature and pH. It is understood that accessory proteins or chaperone proteins can either speed up or slow down fibrillogenesis in Type I Collagen. However, there is a lack of research on how these same proteins can regulate the kinetics of fibril formation in Type II Collagen.

If certain proteins are found to speed up Type II fibril formation, they could greatly decrease the time required for healing in cartilage injuries or diseases, especially those due to the inherent lack of vascularity in cartilage. On the other hand, some proteins may slow down Type II fibril formation and have applications in diseases that are caused by excessive fibril formation such as fibrosis or scar formation. To test the effects of specific accessory proteins, recombinant forms of these proteins were added with Collagen Type II in a buffered solution at 7.4 pH, and a temperature of 25⁰ C. The resulting effects on the kinetics of fibrillogenesis of Type II Collagen were observed using Ultraviolet Visible Spectroscopy, and are presented here.

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Regulation of Type II Collagen Fibrillogenesis In Vitro by Accessory and Chaperone Proteins

Studies have shown that both Type I and Type II Collagen undergo fibrillogenesis under similar conditions, namely at near normal body temperature and pH. It is understood that accessory proteins or chaperone proteins can either speed up or slow down fibrillogenesis in Type I Collagen. However, there is a lack of research on how these same proteins can regulate the kinetics of fibril formation in Type II Collagen.

If certain proteins are found to speed up Type II fibril formation, they could greatly decrease the time required for healing in cartilage injuries or diseases, especially those due to the inherent lack of vascularity in cartilage. On the other hand, some proteins may slow down Type II fibril formation and have applications in diseases that are caused by excessive fibril formation such as fibrosis or scar formation. To test the effects of specific accessory proteins, recombinant forms of these proteins were added with Collagen Type II in a buffered solution at 7.4 pH, and a temperature of 25⁰ C. The resulting effects on the kinetics of fibrillogenesis of Type II Collagen were observed using Ultraviolet Visible Spectroscopy, and are presented here.