Collagen-Glycosaminoglycan Interactions

Proteo-glycosaminoglycans determine the structure of cartilage, the permeability of basement membranes to small molecules, the stability of collagen fibrils, and the response of tendons, cartilage and periodontal ligaments to injury. 

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Pihlajamaa, T., Lankinen, H., Ylostalo, J., Valmu, L., Jaalinoja, J., Zaucke, F. Characterization of recombinant amino-terminal NC4 domain of human collagen IX—Interaction with glycosaminoglycans and cartilage oligomeric matrix protein. J. Biol. Chem. 2004, 279 (23), 24265-24273. 

We have used the collagen-glycosaminoglycan (collagen-GAG) mesh scaffold to probe molecular level cell-biomaterials interactions [11]. We seeded lMR-90 human fibroblasts onto three-dimensional (3-D) collagen-GAG meshes and control surfaces of tissue culture polystyrene (TCPS). Nucleic acids (mRNA) from cells from each culture were isolated, amplified, and hybridized to human genome microarrays (U133A Gene Chip, Affymetrix, Santa Clara, CA). 

Grzesik, J.J., et al. Enhancement of cell interactions with collagen/glycosaminoglycan matrices by RGD derivatization. Biomaterials, 18 1625-1632,1997. 

Hematopoiesis, the process of generating mature blood cells, is mainly located in the red bone marrow, predominantly in the sternum, femur and pelvic bones [1]. In the marrow the hematopoietic cells are embedded in stromal tissue. This consists of different cell types (e.g., fibroblasts, endothehal cells, adipocytes, macrophages) that provide soluble and membrane-bound growth factors and produce an extracellular matrix consisting of collagen, laminin, fibronectin, and glycosaminoglycans [2, 3]. The interactions between hematopoietic cells, stromal cells and extracellular matrix are indicated in Fig. 1 [4,5]. 

Blackwell and his co-workers have used circular dichroism spectroscopy to study the interactions of glycosaminoglycans with collagen, and with synthetic cationic polypeptides. In the absence of glycosaminoglycans, poly-L-lysine and poly-L-arginine exist in an extended charged coil conformation. Glycosaminoglycans bind to these cationic polypeptides and cause them to assume an a-helical conformation. In a series of systematic studies (76-83). Blackwell and his co-workers... 

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