Aggrecan, large aggregating proteoglycan or chondroitin sulfate proteoglycan 1 is a proteoglycan, or a protein modified with carbohydrates; the human form of the protein is 2316 amino acids long and can be expressed in multiple isoforms due to alternative splicing. Along with Type-II collagen, aggrecan forms a major structural component of cartilage, particularly articular cartilage. Aggrecan consists of two globular structural domains at the N-terminal end and one globular domain at the C-terminal end, separated by a large domain heavily modified with glycosaminoglycans. The two main modifier moieties are themselves arranged into distinct regions, a chondroitin sulfate and a keratan sulfate region.
The linker domain between the N-terminal globular domains, called the interglobular domain, is highly sensitive to proteolysis. Such degradation has been associated with the development of arthritis. Proteases capable of degrading aggrecans are called aggrecanases, and they are members of the ADAM (A Disintegrin And Metalloprotease) protein family.
Aggrecan has been shown to interact with versican.
- ↑ Doege KJ, Sasaki M, Kimura T, Yamada Y (1991). "Complete coding sequence and deduced primary structure of the human cartilage large aggregating proteoglycan, aggrecan. Human-specific repeats, and additional alternatively spliced forms". J. Biol. Chem. 266 (2): 894–902. PMID 1985970. http://www.jbc.org/cgi/content/abstract/266/2/894.
- ↑ East CJ, Stanton H, Golub SB, Rogerson FM, Fosang AJ (2007). "ADAMTS-5 deficiency does not block aggrecanolysis at preferred cleavage sites in the chondroitin sulfate-rich region of aggrecan". J. Biol. Chem. 282 (12): 8632–40. doi:10.1074/jbc.M605750200. PMID 17255106.
- ↑ Matsumoto, Kazu; Shionyu Masafumi, Go Mitiko, Shimizu Katsuji, Shinomura Tamayuki, Kimata Koji, Watanabe Hideto (Oct. 2003). "Distinct interaction of versican/PG-M with hyaluronan and link protein". J. Biol. Chem. (United States) 278 (42): 41205–12. doi:10.1074/jbc.M305060200. ISSN 0021-9258. PMID 12888576.
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