The function and distinctive regulation of the integrin VLA-3 in cell adhesion, spreading, and homotypic cell aggregation - PubMed (original) (raw)
. 1993 Apr 25;268(12):8651-7.
Affiliations
- PMID: 8473308
Free article
The function and distinctive regulation of the integrin VLA-3 in cell adhesion, spreading, and homotypic cell aggregation
J B Weitzman et al. J Biol Chem. 1993.
Free article
Abstract
To assess directly the functional role of the integrin VLA-3 (alpha 3 beta 1), we transfected human alpha 3 cDNA into erythroleukemia (K562) cells and rhabdomyosarcoma (RD) cells. The resulting transfectants (KA3 and RA3) expressed alpha 3 beta 1 on the cell surface as confirmed using a panel of nine anti-alpha 3 monoclonal antibodies. Neither of the transfected cells exhibited increased adhesion to the extracellular matrix proteins fibronectin, laminin, and collagen. However, the KA3 transfectants did bind strongly to the extracellular matrix deposited by epidermal and carcinoma cell lines, allowing the cells to attach and spread. Binding to this cell-deposited ligand, probably containing epiligrin/kalinin, was specific to VLA-3 and could be inhibited by anti-alpha 3 antibodies and by EDTA, but not by RGD peptides. In marked contrast to other integrins (VLA-2 and VLA-4), VLA-3 showed high constitutive activity in K562 cells, but was minimally active in RD cells. Also contrasting with other beta 1 integrins, VLA-3 was minimally stimulated by the anti-beta 1 monoclonal antibody TS/216 under normal conditions. VLA-3-mediated adhesive function was well supported by either Mg2+ or Mn2+, but was almost completely abolished by the presence of 1 mM Ca2+. Surprisingly, this negative Ca2+ effect was completely overcome by the addition of the stimulatory anti-beta 1 monoclonal antibody TS2/16. Together, these results point to markedly distinct regulation for VLA-3 function compared to other beta 1 integrins. Also, all anti-VLA-3 antibodies were able to induce temperature-dependent homotypic cell aggregation of KA3 cells, but not K562 cells. However, this aggregation did not appear to be directly mediated by VLA-3 since it was not inhibited by EDTA. In addition, no enhancement of heterotypic cell-cell adhesion was observed in alpha 3-transfected cells.
Similar articles
- Investigation of the role of beta 1 integrins in cell-cell adhesion.
Weitzman JB, Chen A, Hemler ME. Weitzman JB, et al. J Cell Sci. 1995 Nov;108 ( Pt 11):3635-44. doi: 10.1242/jcs.108.11.3635. J Cell Sci. 1995. PMID: 8586674 - A region of the integrin VLA alpha 4 subunit involved in homotypic cell aggregation and in fibronectin but not vascular cell adhesion molecule-1 binding.
Muñoz M, Serrador J, Sánchez-Madrid F, Teixidó J. Muñoz M, et al. J Biol Chem. 1996 Feb 2;271(5):2696-702. doi: 10.1074/jbc.271.5.2696. J Biol Chem. 1996. PMID: 8576243 - Adhesion of T and B lymphocytes to extracellular matrix and endothelial cells can be regulated through the beta subunit of VLA.
van de Wiel-van Kemenade E, van Kooyk Y, de Boer AJ, Huijbens RJ, Weder P, van de Kasteele W, Melief CJ, Figdor CG. van de Wiel-van Kemenade E, et al. J Cell Biol. 1992 Apr;117(2):461-70. doi: 10.1083/jcb.117.2.461. J Cell Biol. 1992. PMID: 1560035 Free PMC article. - Multiple ligand binding functions for VLA-2 (alpha 2 beta 1) and VLA-3 (alpha 3 beta 1) in the integrin family.
Hemler ME, Elices MJ, Chan BM, Zetter B, Matsuura N, Takada Y. Hemler ME, et al. Cell Differ Dev. 1990 Dec 2;32(3):229-38. doi: 10.1016/0922-3371(90)90035-u. Cell Differ Dev. 1990. PMID: 1965952 Review.
Cited by
- Visualization of integrin molecules by fluorescence imaging and techniques.
Cai C, Sun H, Hu L, Fan Z. Cai C, et al. Biocell. 2021;45(2):229-257. doi: 10.32604/biocell.2021.014338. Epub 2021 Feb 19. Biocell. 2021. PMID: 34219865 Free PMC article. - Absence of integrin α3β1 promotes the progression of HER2-driven breast cancer in vivo.
Ramovs V, Secades P, Song JY, Thijssen B, Kreft M, Sonnenberg A. Ramovs V, et al. Breast Cancer Res. 2019 May 17;21(1):63. doi: 10.1186/s13058-019-1146-8. Breast Cancer Res. 2019. PMID: 31101121 Free PMC article. - Integrins as Therapeutic Targets for Respiratory Diseases.
Teoh CM, Tan SS, Tran T. Teoh CM, et al. Curr Mol Med. 2015;15(8):714-34. doi: 10.2174/1566524015666150921105339. Curr Mol Med. 2015. PMID: 26391549 Free PMC article. Review. - Hypoxia-induced changes to integrin α 3 glycosylation facilitate invasion in epidermoid carcinoma cell line A431.
Ren Y, Hao P, Law SK, Sze SK. Ren Y, et al. Mol Cell Proteomics. 2014 Nov;13(11):3126-37. doi: 10.1074/mcp.M114.038505. Epub 2014 Jul 30. Mol Cell Proteomics. 2014. PMID: 25078904 Free PMC article. - CRF2 signaling is a novel regulator of cellular adhesion and migration in colorectal cancer cells.
Ducarouge B, Pelissier-Rota M, Lainé M, Cristina N, Vachez Y, Scoazec JY, Bonaz B, Jacquier-Sarlin M. Ducarouge B, et al. PLoS One. 2013 Nov 18;8(11):e79335. doi: 10.1371/journal.pone.0079335. eCollection 2013. PLoS One. 2013. PMID: 24260200 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Miscellaneous