Title

Compensation for Col11a1 Deficiency by Other Minor Collagens

Document Type

Presentation

Publication Date

April 2010

Faculty Sponsor

Dr. Julia Oxford

Abstract

Collagens are triple helical proteins found in the extracellular matrix and are of broad biomedical importance. Understanding collagens are essential in elucidating the mechanisms that take place during embryogenesis, in the development of diseases such as arthritis, cardiovascular disease, during tumor invasion, and in the applications of tissue repair and regenerative medicine. The most abundant collagens are type I and type II. In contrast, collagen XI and collagen V are minor constituents of the extracellular matrix and are essential in regulation of fibril assembly and diameter of collagen fibrils. Collagen II-containing fibrils cannot form in the absence of collagen XI. Likewise, collagen I fibrils do not form correctly in the absence of collagen V. Collagen XI shares structural homology with collagen V and may share functions. We investigated mRNA expression in a mouse model with a deficiency in Col11a1 to detect evidence for compensation by Col5a1 and Col5a3. Our studies allowed us to answer the questions, “do minor fibrillar collagens share functions during development and cell differentiation or, alternatively, do they perform unique functions?” To answer this research question, we extracted RNA from mouse tissues and generated cDNA by reverse transcription. The cDNA was then amplified by PCR and the products were detected using agarose gel electrophoresis. We show that the mouse model, UAB Col11a1deltaVR, differentially expressed Col11a1 mRNA when compared to the wild type. To address the possibility of compensation for the deficiency in Col11a1 by other minor collagens, we will carry out RT-PCR using primers specific for mRNA encoding the other minor collagen chains. Identifying differential expression of mRNA for other minor collagens may provide diagnostic medical tools and could improve early detection of diseases and disorders associated with minor collagens such as Ehlers-Danlos and Stickler syndromes.

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