Common Structures of the Core Proteins of Interstitial Proteoglycans

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Abstract
Connective tissues, with few exceptions, contain easily distinguishable large and small proteoglycans with chondroitin sulphate or dermatan sulphate side-chains. One group consists of the large aggregating proteoglycans that have the capacity to interact specifically with hyaluronate, thereby forming very large aggregates. These proteoglycans can be divided into two families which can be separated by electrophoresis. Preliminary results indicate that one of these may be derived from the other by processing in the extracellular matrix. Although most prominent in cartilage, similar proteoglycans are present in many types of tissue, such as aorta, sclera and tendon. Another population are the large non-aggregating proteoglycans, identified in cartilage. These proteoglycans show structural features partially different from any of the others. They may represent a distinct population of molecules present in many connective tissues. Many tissues contain major populations of small, non-aggregating proteoglycans. These can be divided into two major groups, differing in the composition of their core proteins, while having similar types of side-chain constituents. One group is represented by proteoglycans from nasal cartilage and aorta, while the other is represented by proteoglycans from tendon, bone, sclera and cornea.