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Characterisation of Drosophila thrombospondin defines an early origin of pentameric thrombospondins

Adams, JC; Monk, R; Taylor, AL; Ozbek, S; Fascetti, Nora LU ; Baumgartner, Stefan LU and Engel, J (2003) In Journal of Molecular Biology 328(2). p.479-494
Abstract
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... (More)
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 (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
molecular phylogeny, RGD-motif, heparin-binding, extracellular matrix, cell interactions
in
Journal of Molecular Biology
volume
328
issue
2
pages
479 - 494
publisher
Elsevier
external identifiers
  • wos:000182431200014
  • pmid:12691755
  • scopus:0037466330
ISSN
1089-8638
DOI
10.1016/S0022-2836(03)00248-1
language
English
LU publication?
yes
id
832c1a06-5b6e-453b-8fd9-6bc567d67c53 (old id 312705)
date added to LUP
2007-08-21 11:46:49
date last changed
2017-10-01 04:52:06
@article{832c1a06-5b6e-453b-8fd9-6bc567d67c53,
  abstract     = {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},
  author       = {Adams, JC and Monk, R and Taylor, AL and Ozbek, S and Fascetti, Nora and Baumgartner, Stefan and Engel, J},
  issn         = {1089-8638},
  keyword      = {molecular phylogeny,RGD-motif,heparin-binding,extracellular matrix,cell interactions},
  language     = {eng},
  number       = {2},
  pages        = {479--494},
  publisher    = {Elsevier},
  series       = {Journal of Molecular Biology},
  title        = {Characterisation of Drosophila thrombospondin defines an early origin of pentameric thrombospondins},
  url          = {http://dx.doi.org/10.1016/S0022-2836(03)00248-1},
  volume       = {328},
  year         = {2003},
}