A Col2a1 Mutation Leads to Increased Degradation of Type II Collagen in Articular Cartilage: A Murine Model for Osteoarthritis

Authors

Peter Crane, Brigham Young University
Dr. Robert Seegmiller, Brigham Young University

Keywords

Col2a1 mutation, type II collagen, articular cartilage, osteoarthritis

College

Life Sciences

Department

Physiology and Developmental Biology

Abstract

Normal articular cartilage is characterized by a resilient collagen and proteoglycan matrix interdispersed with chondrocytes. Collagen type II is the most abundant collagen found in the matrix and is responsible for providing tensile strength to the tissue. The highly conserved Col2a1 gene is responsible for coding all type II collagen á-helix chains.1 The process of enzymatic MMP cleavage is a natural part of collagen recycling, but has been observed to be upregulated in articular cartilage of osteoarthritis (OA) patients. It is hypothesized that further denaturation (unwinding) of enzymatically cleaved collagen takes place following enzymatic cleavage by MMP. Because increased degraded type II collagen has been observed in human OA patients through use of immunohistchemistry, there is a need for an animal model to study and use to develop treatments.2, 3 C3H mice with disproportionate micromelia (Dmm) carry a radiation-induced mutation in the region of the Col2a1 gene that codes the C-propeptide of type II collagen.

Recommended Citation

Crane, Peter and Seegmiller, Dr. Robert (2013) "A Col2a1 Mutation Leads to Increased Degradation of Type II Collagen in Articular Cartilage: A Murine Model for Osteoarthritis," Journal of Undergraduate Research: Vol. 2013: Iss. 1, Article 1396.
Available at: https://scholarsarchive.byu.edu/jur/vol2013/iss1/1396