UNC-52/perlecan isoform diversity and function in Caenorhabditis elegans. (May 2001)

• Record Type: Journal Article
• Authors: Rogalski, T. M.; Mullen, G. P.; Bush, J. A.; Gilchrist, E. J.; Moerman, D. G.
• Is Part Of: Biochemical Society transactions. Volume 29:Number 2(2001)
• Page Start: 171
• Page End: 176
• Publication Date: 2001-05
• Subjects: adhesion complex -- alternative splicing -- integrin -- proteoglycan; LDL, low-density lipoprotein -- NCAM, neural cell-adhesion molecule -- ECM, extracellular matrix -- Pat, paralysed, arrested elongation at two-fold -- S, short -- M, medium -- L, long; Biochemistry -- Congresses; 572
• DOI: 10.1042/bst0290171
• Languages: English
• ISSNs: 0300-5127

Abstract

Abstract : The unc-52 gene encodes the nematode homologue of mammalian perlecan, the major heparan sulphate proteoglycan of the extracellular matrix. This is a large complex protein with regions similar to low-density lipoprotein receptors, laminin and neural cell-adhesion molecules. Three major classes of UNC-52/perlecan isoforms are produced through alternative splicing, and these distinct proteins exhibit complex spatial and temporal expression patterns throughout development. The unc-52 gene plays an essential role in myofilament assembly in body-wall muscle during embryonic development.