proteoglycan
Sign in to saveAlso known as proteoglycans
thumb|right|250px|Aggrecan, the major proteoglycan in [[cartilage, has 2316 amino acids ]]
Research
60,382 papers- Proteoglycan form and function: A comprehensive nomenclature of proteoglycans.Matrix biology : journal of the International Society for Matrix Biology · 2015
- Chondroitin sulfate proteoglycan 4: An attractive target for antibody-based immunotherapy.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2024
- The microRNA-cell surface proteoglycan axis in cancer progression.American journal of physiology. Cell physiology · 2022
- Structural deciphering of the NG2/CSPG4 proteoglycan multifunctionality.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019
- Chemical editing of proteoglycan architecture.Nature chemical biology · 2022
via PubMed
Wikidata facts
Show 1 more fact
- Commons category
- Proteoglycans
Sources (2)
via Wikidata · CC0
~4 min read
Article
7 sectionsContents
- Types
- Function
- Synthesis
- Clinical significance
- Distinction between proteoglycans and glycoproteins
- References
- External links
thumb|right|250px|Aggrecan, the major proteoglycan in [[cartilage, has 2316 amino acids ]]
Proteoglycans are proteins that are heavily glycosylated. The basic proteoglycan unit consists of a "core protein" with one or more covalently attached glycosaminoglycan (GAG) chain(s). The point of attachment is a serine (Ser) residue to which the glycosaminoglycan is joined through a tetrasaccharide bridge (e.g. chondroitin sulfate-GlcA-Gal-Gal-Xyl-PROTEIN). The Ser residue is generally in the sequence -Ser-Gly-X-Gly- (where X can be any amino acid residue but proline), although not every protein with this sequence has an attached glycosaminoglycan. The chains are long, linear carbohydrate polymers that are negatively charged under physiological conditions due to the occurrence of sulfate and uronic acid groups. Proteoglycans occur in connective tissue.