Splice variants of the Drosophila PS2 integrins differentially interact with RGD-containing fragments of the extracellular proteins tiggrin, Ten-m, and D-laminin α2
Graner, Michael W. ; Bunch, Thomas A. ; Baumgartner, Stefan LU
; Kerschen, Arthur
and Brower, Danny L.
(1998)
In Journal of Biological Chemistry
273(29).
p.18235-18241
- Abstract
Two new potential ligands of the Drosophila PS2 integrins have been characterized by functional interaction in cell culture. These potential ligands are a new Drosophila laminin α2 chain encoded by the wing blister locus and Ten-m, an extracellular protein known to be involved in embryonic pattern formation. As with previously identified PS2 ligands, both contain RGD sequences, and RGD-containing fragments of these two proteins (DLAM-RGD and TENM-RGD) can support PS2 integrin-mediated cell spreading. In all cases, this spreading is inhibited specifically by short RGD-containing peptides. As previously found for the PS2 ligand tiggrin (and the tiggrin fragment TIG- RGD), TENM-RGD induces maximal spreading of cells expressing integrin... (More)
Two new potential ligands of the Drosophila PS2 integrins have been characterized by functional interaction in cell culture. These potential ligands are a new Drosophila laminin α2 chain encoded by the wing blister locus and Ten-m, an extracellular protein known to be involved in embryonic pattern formation. As with previously identified PS2 ligands, both contain RGD sequences, and RGD-containing fragments of these two proteins (DLAM-RGD and TENM-RGD) can support PS2 integrin-mediated cell spreading. In all cases, this spreading is inhibited specifically by short RGD-containing peptides. As previously found for the PS2 ligand tiggrin (and the tiggrin fragment TIG- RGD), TENM-RGD induces maximal spreading of cells expressing integrin containing the α(PS2C) splice variant. This is in contrast to DLAM-RGD, which is the first Drosophila polypeptide shown to interact preferentially with cells expressing the α(PS2) (M8) splice variant. The β(PS) integrin subunit also varies in the presumed ligand binding region as a result of alternative splicing. For TIG-RGD and TENM-RGD, the β splice variant has little effect, but for DLAM-RGD, maximal cell spreading is supported only by the β(PS4A) form of the protein. Thus, the diversity in PS2 integrins due to splicing variations, in combination with diversity of matrix ligands, can greatly enhance the functional complexity of PS2-ligand interactions in the developing animal. The data also suggest that the Splice variants may alter regions of the subunits that are directly involved in ligand interactions, and this is discussed with respect to models of integrin structure.
(Less)
- author
- Graner, Michael W.
; Bunch, Thomas A.
; Baumgartner, Stefan
LU
; Kerschen, Arthur
and Brower, Danny L.
- organization
- publishing date
- 1998-07-17
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Biological Chemistry
- volume
- 273
- issue
- 29
- pages
- 18235 - 18241
- publisher
- American Society for Biochemistry and Molecular Biology
- external identifiers
-
- pmid:9660786
- scopus:0032541043
- ISSN
- 0021-9258
- DOI
- 10.1074/jbc.273.29.18235
- language
- English
- LU publication?
- yes
- id
- 1de50c22-66fd-4599-a15f-78faad308be5
- date added to LUP
- 2019-05-21 14:05:58
- date last changed
- 2024-01-01 05:54:21
@article{1de50c22-66fd-4599-a15f-78faad308be5,
abstract = {{<p>Two new potential ligands of the Drosophila PS2 integrins have been characterized by functional interaction in cell culture. These potential ligands are a new Drosophila laminin α2 chain encoded by the wing blister locus and Ten-m, an extracellular protein known to be involved in embryonic pattern formation. As with previously identified PS2 ligands, both contain RGD sequences, and RGD-containing fragments of these two proteins (DLAM-RGD and TENM-RGD) can support PS2 integrin-mediated cell spreading. In all cases, this spreading is inhibited specifically by short RGD-containing peptides. As previously found for the PS2 ligand tiggrin (and the tiggrin fragment TIG- RGD), TENM-RGD induces maximal spreading of cells expressing integrin containing the α(PS2C) splice variant. This is in contrast to DLAM-RGD, which is the first Drosophila polypeptide shown to interact preferentially with cells expressing the α(PS2) (M8) splice variant. The β(PS) integrin subunit also varies in the presumed ligand binding region as a result of alternative splicing. For TIG-RGD and TENM-RGD, the β splice variant has little effect, but for DLAM-RGD, maximal cell spreading is supported only by the β(PS4A) form of the protein. Thus, the diversity in PS2 integrins due to splicing variations, in combination with diversity of matrix ligands, can greatly enhance the functional complexity of PS2-ligand interactions in the developing animal. The data also suggest that the Splice variants may alter regions of the subunits that are directly involved in ligand interactions, and this is discussed with respect to models of integrin structure.</p>}},
author = {{Graner, Michael W. and Bunch, Thomas A. and Baumgartner, Stefan and Kerschen, Arthur and Brower, Danny L.}},
issn = {{0021-9258}},
language = {{eng}},
month = {{07}},
number = {{29}},
pages = {{18235--18241}},
publisher = {{American Society for Biochemistry and Molecular Biology}},
series = {{Journal of Biological Chemistry}},
title = {{Splice variants of the Drosophila PS2 integrins differentially interact with RGD-containing fragments of the extracellular proteins tiggrin, Ten-m, and D-laminin α2}},
url = {{http://dx.doi.org/10.1074/jbc.273.29.18235}},
doi = {{10.1074/jbc.273.29.18235}},
volume = {{273}},
year = {{1998}},
}