+ Site Statistics
+ Search Articles
+ Subscribe to Site Feeds
EurekaMag Most Shared ContentMost Shared
EurekaMag PDF Full Text ContentPDF Full Text
+ PDF Full Text
Request PDF Full TextRequest PDF Full Text
+ Follow Us
Follow on FacebookFollow on Facebook
Follow on TwitterFollow on Twitter
Follow on Google+Follow on Google+
Follow on LinkedInFollow on LinkedIn

+ Translate

Extended and globular protein domains in cartilage proteoglycans

Biochemical Journal 245(3): 763-772
Extended and globular protein domains in cartilage proteoglycans
Electron microscopy after rotary shadowing and negative staining of the large chondroitin sulphate proteoglycan from rat chondrosarcoma, bovine nasal cartilage and pig laryngeal cartilage demonstrated a unique multidomain structure for the protein core. A main characteristic is a pair of globular domains (diameter 6-8 nm), one of which forms the N-terminal hyaluronate-binding region. They are connected by a 25 nm-long rod-like domain of limited flexibility. This segment is continued by a 280 nm-long polypeptide strand containing most chondroitin sulphate chains (average length 40 nm) in a brush-like array and is terminated by a small C-terminal globular domain. The core protein showed a variable extent of degradation, including the loss of the C-terminal globular domain and sections of variable length of the chondroitin sulphate-bearing strand. The high abundance (30-50%) of the C-terminal domain in some extracted proteoglycan preparations indicated that this structure is present in the cartilage matrix rather than being a precursor-specific segment. It may contain the hepatolectin-like segment deduced from cDNA sequences corresponding to the 3'-end of protein core mRNA [Doege, Fernandez, Hassell, Sasaki & Yamada (1986) J. Biol. Chem. 261, 8108-8111; Sai, Tanaka, Kosher & Tanzer (1986) Proc. Natl. Acad. Sci. 83, 5081-5085; Oldberg, Antonsson & Heinegård (1987) Biochem. J. 243, 255-259].

Accession: 005432541

PMID: 3663190

DOI: 10.1042/bj2450763

Related references

Isolation of the N-terminal globular protein domains from cartilage proteoglycans. Identification of G2 domain and its lack of interaction with hyaluronate and link protein. Biochemical Journal 261(3): 801-809, 1989

Isolation of the amino terminal globular protein domains from cartilage proteoglycans identification of g2 domain and its lack of interaction with hyaluronate and link protein. Biochemical Journal 261(3): 801-810, 1989

The globular domains of type VI collagen are related to the collagen-binding domains of cartilage matrix protein and von Willebrand factor. Embo Journal 8(4): 1073-1077, 1989

Differences between the proteoglycans of fetal cartilage and those of the cartilage of a growing animal (a study of proteoglycans of joint cartilage and of growth cartilage in the baboon, using polyacrylamide gel-agarose electrophoresis). Comptes Rendus Hebdomadaires des Seances de L'academie des Sciences. Serie D: Sciences Naturelles 276(12): 1871-1873, 1973

Cartilage proteoglycan aggregates. The link protein and proteoglycan amino-terminal globular domains have similar structures. Journal of Biological Chemistry 262(36): 17768-17778, 1987

Antigenicity of cartilage proteoglycans: the effect of cartilage and on cartilage proteoglycans of "crude alpha-amylase" from Bacillus subtilis. Calcified Tissue Research: Suppl:76-7, 1970

Link protein interactions with hyaluronate and proteoglycans. Characterization of two distinct domains in bovine cartilage link proteins. Journal of Biological Chemistry 262(27): 13269-13272, 1987

Differences entre les proteoglycans du cartiage du foetus et du cartilage de I'animal en croissance (etude des proteoglycans du cartilage articulaire et du cartilage de croissance de babouin par electrophorese sur gel de polyacrylamide-agarose). Compte r Hebd Seanc Acad Sci Paris (Ser D): 27612: 1871-1873, 1973

Domains in cartilage proteoglycans: do they define function?. Biochemical Society Transactions 18(2): 202-204, 1990

Proteoglycans in human laryngeal cartilage. Identification of proteoglycan types in successive cartilage extracts with particular reference to aggregating proteoglycans. Biochimie 86(3): 221-229, 2004