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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/312705
- author
- Adams, JC
; Monk, R
; Taylor, AL
; Ozbek, S
; Fascetti, Nora
LU
; Baumgartner, Stefan
LU
and Engel, J
- organization
- publishing date
- 2003
- 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
- 2016-04-01 17:02:40
- date last changed
- 2022-01-28 23:55:39
@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}},
keywords = {{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}},
doi = {{10.1016/S0022-2836(03)00248-1}},
volume = {{328}},
year = {{2003}},
}