Proteoglycan complex

Fig. 4.—Structural Model of Bovine Nasal-Cartilage, Proteoglycan Complex. [-------,...

Dermatan sulfate is found in the skin, arterial walls, and tendon where it is a part of another proteoglycan complex. It is about the same size as chondroitin sulfate and is also able to form helical conformations. 

Hygroscopic Substance. Perhaps the most distinctive and vitally important surface property of SC is its capacity to absorb up to six times its own weight in water (16, 89, 90). Attempts have been made to associate this property with protein surfaces (20, 91), protein-lipid interfaces (38, 63, 66), or with lipids alone (66, 92). Recently, investigators have emphasized the joint importance of lipids and proteins, or proteoglycan complexes, in hygroscopic properties (16, 66, 92). 

Goldstein, S.M., Leong, J., Schwartz, L.B. and Cooke, D. (1992). Protease composition of exocytosed human skin mast cell protease-proteoglycan complexes tryptase resides in a complex distinct from chymase and carboxypeptidase. J. Immunol. 148, 2475-2482. 

Bronner-Fraser, M. and Laller, T. (1988) A monoclonal antibody against a laminin-heparan sulfate proteoglycan complex perturbs cranial neural crest migration in vivo. J. Cell Biol. 106 1321-1329. 

Figure 6.6 Chemical composition of the dermatan sulfate and structure of aggregan complexes, (a) Chemical structure of repeated disaccharide of the GAG dermatan sulfate (protons are not indicated in this schematic diagram), (b) Schematic diagram of the aggregan proteoglycan complex showing the relationship between the core and linker proteins, GAGs, and hyaluronic acid).

Affinity chromatographic purification of components of the hyaluronate-proteoglycan complex of cartilage... 

Regions of blood vessels that accumulate proteoglycans have a high propensity to accumulate lipid, particularly in areas associated with endothelial regrowth (72). LDL-proteoglycan complexes have been isolated from different regions of ECM within atherosclerotic vessels. 

FIGURE 1 A schematic view of the proteoglycan complex in cartilage used to bind to collagen in a strong network. 

Chondroitin 4-sulphate and cartilagenous proteoglycans form ionic complexes with lysozyme. The complexes are solubilized by either salts or alkali, although a higher salt concentration is needed to solubilize the proteoglycan complexes. The distribution of charges on the complexes and the implications of the formation of ionic complexes in tissues were discussed. 

Kleine, T.O. Hyaluronate proteoglycan complex evidence for separate biosynthesis mechanisms of the macromolecules. Connective Tiss. Res. 1978, 5, 195-199. 

Vijayagopal P. Regulation of the metabolism oflipoprotein-proteoglycan complexes in human monocyte-derived macrophages. Biochem J 301 675-81, 1994. 

Ismail NA, Alavi MZ and Moore S. Lipoprotein-proteoglycan complexes from injured rabbit aortas accelerate lipoprotein uptake by arterial smooth muscle cells. Atherosclerosis 105 79-87, 1994. 

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