Characterisation of Drosophila thrombospondin defines an early origin of pentameric thrombospondins

被引:50
作者
Adams, JC
Monk, R
Taylor, AL
Ozbek, S
Fascetti, N
Baumgartner, S
Engel, J
机构
[1] UCL, MRC, Mol Cell Biol Lab, London WC1E 6BT, England
[2] UCL, Dept Biochem & Mol Biol, London WC1E 6BT, England
[3] Cleveland Clin Fdn, Dept Cell Biol, Lerner Res Inst, Cleveland, OH 44195 USA
[4] Univ Basel, Dept Biophys Chem, Biozentrum, CH-4056 Basel, Switzerland
[5] Lund Univ, Dept Cell & Mol Biol, Sect Dev Biol, S-22184 Lund, Sweden
基金
英国惠康基金;
关键词
extracellular matrix; cell interactions; heparin-binding; RGD-motif; molecular phylogeny;
D O I
10.1016/S0022-2836(03)00248-1
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Thrombospondins (TSPs) are multidomain oligomers that have complex roles in cell interactions and tissue organisation. The five vertebrate TSPs comprise two subgroups, A and B, that are assembled as trimers or pentamers, respectively. An invertebrate TSP was recently discovered in Drosophila melanogaster, but there is no knowledge of the oligomerisation status or properties of this molecule. We developed by bioinformatics a new dataset containing the single TSP of Drosophila melanogaster and four other newly identified invertebrate TSPs to examine the phylogenetic relationships of TSPs. These analyses clearly indicate pentamerisation as an early attribute of TSPs. We demonstrate experimentally that D. melanogaster TSP is assembled as a pentamer, has heparin-binding activity and is a component of extracellular matrix (ECM). During embryogenesis, the TSP transcript is concentrated at muscle attachment sites and is expressed by a subset of myoblasts and in imaginal discs. These novel results establish TSPs as highly conserved ECM components in both invertebrates and vertebrates and open fresh perspectives on the conservation of structure and biological function within this family (C) 2003 Elsevier Science Ltd. All rights reserved.
引用
收藏
页码:479 / 494
页数:16
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