Defining the Roles of Collagen and Collagen‐Like Proteins Within the Proteome

Abstract

The collagen family is a diverse group of proteins distinguished by a native triple‐helical structure. The collagen triple‐helix is important for the integrity and workings of multiple connective tissues, including skin, bone, cartilage, tendon, and dentin. Most collagens assist in anchoring cells to the extracellular matrix and some function in cellular regulation. Multiple hereditary connective tissue diseases have been linked to collagen mutations. These mutations most often disrupt collagen folding. The very nature of the collagen family, one that is extensive, ubiquitous, abundant, well characterized, and responsible for various disease states, makes it a model protein family for intense proteomic studies. Proteomic analyses for triple‐helical proteins may involve several different multidimensional approaches, such as two‐dimensional liquid chromatography (2DLC), coupled liquid chromatography/capillary electrophoresis, and multidimensional protein identification technique (MudPIT) that couples 2DLC with mass spectrometry (MS). Following analysis, collagen and collagen‐like proteins may be further characterized by expression of collagen and/or synthesis of triple‐helical peptides (THPs) incorporating collagen sequences of interest. Collagen structure–function relationships have been well established by combined proteomic approaches.

Keywords:

• Collagen
• Triple‐helical peptides
• Reversed‐phase HPLC
• Osteogenesis imperfecta
• Proteome

Acknowledgments

Work in our laboratory on collagen structure–function relationships has been supported by grants from the National Institutes of Health (HL62427/EB00289, KD44494/CA77402, AR01929, and CA98799 to G.B.F.).