Integrin alpha 3 beta 1, a Novel Receptor for alpha 3(IV) noncollagenous domain and a trans-dominant inhibitor for integrin alpha v beta 3
Borza, Corina M. ; Pozzi, Ambra ; Borza, Dorin-Bogdan ; Pedchenko, Vadim ; Hellmark, Thomas LU
; Hudson, Billy G.
and Zent, Roy
(2006)
In Journal of Biological Chemistry
281(30).
p.20932-20939
- Abstract
- Exogenous soluble human alpha 3 noncollagenous (NC1) domain of collagen IV inhibits angiogenesis and tumor growth. These biological functions are attributed to the binding of alpha 3NC1 to integrin alpha v beta 3. However, in some tumor cells that express integrin alpha v beta 3, the alpha 3NC1 domain does not inhibit proliferation, suggesting that integrin alpha v beta 3 expression is not sufficient to mediate the anti-tumorigenic activity of this domain. Therefore, in the present study, we searched for novel binding receptors for the soluble alpha 3NC1 domain in cells lacking alpha v beta 3 integrin. In these cells, soluble alpha 3NC1 bound integrin alpha 3 beta 1; however, unlike alpha v beta 3, alpha 3 beta 1 integrin did not mediate... (More)
- Exogenous soluble human alpha 3 noncollagenous (NC1) domain of collagen IV inhibits angiogenesis and tumor growth. These biological functions are attributed to the binding of alpha 3NC1 to integrin alpha v beta 3. However, in some tumor cells that express integrin alpha v beta 3, the alpha 3NC1 domain does not inhibit proliferation, suggesting that integrin alpha v beta 3 expression is not sufficient to mediate the anti-tumorigenic activity of this domain. Therefore, in the present study, we searched for novel binding receptors for the soluble alpha 3NC1 domain in cells lacking alpha v beta 3 integrin. In these cells, soluble alpha 3NC1 bound integrin alpha 3 beta 1; however, unlike alpha v beta 3, alpha 3 beta 1 integrin did not mediate cell adhesion to immobilized alpha 3NC1 domain. Interestingly, in cells lacking integrin alpha 3 beta 1, adhesion to the alpha 3NC1 domain was enhanced due to activation of integrin alpha v beta 3. These findings indicate that integrin alpha 3 beta 1 is a receptor for the alpha 3NC1 domain and transdominantly inhibits integrin alpha v beta 3 activation. Thus integrin alpha 3 beta 1, in conjunction with integrin alpha v beta 3, modulates cellular responses to the alpha 3NC1 domain, which may be pivotal in the mechanism underpinning its anti-angiogenic and anti-tumorigenic activities. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/401338
- author
- Borza, Corina M.
; Pozzi, Ambra
; Borza, Dorin-Bogdan
; Pedchenko, Vadim
; Hellmark, Thomas
LU
; Hudson, Billy G.
and Zent, Roy
- organization
- publishing date
- 2006
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Biological Chemistry
- volume
- 281
- issue
- 30
- pages
- 20932 - 20939
- publisher
- American Society for Biochemistry and Molecular Biology
- external identifiers
-
- wos:000239187300030
- scopus:33746325825
- ISSN
- 1083-351X
- DOI
- 10.1074/jbc.M601147200
- language
- English
- LU publication?
- yes
- id
- d0450e74-f498-4c38-8730-d804698c7534 (old id 401338)
- date added to LUP
- 2016-04-01 12:28:13
- date last changed
- 2022-04-21 07:54:11
@article{d0450e74-f498-4c38-8730-d804698c7534,
abstract = {{Exogenous soluble human alpha 3 noncollagenous (NC1) domain of collagen IV inhibits angiogenesis and tumor growth. These biological functions are attributed to the binding of alpha 3NC1 to integrin alpha v beta 3. However, in some tumor cells that express integrin alpha v beta 3, the alpha 3NC1 domain does not inhibit proliferation, suggesting that integrin alpha v beta 3 expression is not sufficient to mediate the anti-tumorigenic activity of this domain. Therefore, in the present study, we searched for novel binding receptors for the soluble alpha 3NC1 domain in cells lacking alpha v beta 3 integrin. In these cells, soluble alpha 3NC1 bound integrin alpha 3 beta 1; however, unlike alpha v beta 3, alpha 3 beta 1 integrin did not mediate cell adhesion to immobilized alpha 3NC1 domain. Interestingly, in cells lacking integrin alpha 3 beta 1, adhesion to the alpha 3NC1 domain was enhanced due to activation of integrin alpha v beta 3. These findings indicate that integrin alpha 3 beta 1 is a receptor for the alpha 3NC1 domain and transdominantly inhibits integrin alpha v beta 3 activation. Thus integrin alpha 3 beta 1, in conjunction with integrin alpha v beta 3, modulates cellular responses to the alpha 3NC1 domain, which may be pivotal in the mechanism underpinning its anti-angiogenic and anti-tumorigenic activities.}},
author = {{Borza, Corina M. and Pozzi, Ambra and Borza, Dorin-Bogdan and Pedchenko, Vadim and Hellmark, Thomas and Hudson, Billy G. and Zent, Roy}},
issn = {{1083-351X}},
language = {{eng}},
number = {{30}},
pages = {{20932--20939}},
publisher = {{American Society for Biochemistry and Molecular Biology}},
series = {{Journal of Biological Chemistry}},
title = {{Integrin alpha 3 beta 1, a Novel Receptor for alpha 3(IV) noncollagenous domain and a trans-dominant inhibitor for integrin alpha v beta 3}},
url = {{http://dx.doi.org/10.1074/jbc.M601147200}},
doi = {{10.1074/jbc.M601147200}},
volume = {{281}},
year = {{2006}},
}