Receptor functions for the integrin VLA-3: fibronectin, collagen, and laminin binding are differentially influenced by Arg-Gly-Asp peptide and by divalent cations - PubMed (original) (raw)
Receptor functions for the integrin VLA-3: fibronectin, collagen, and laminin binding are differentially influenced by Arg-Gly-Asp peptide and by divalent cations
M J Elices et al. J Cell Biol. 1991 Jan.
Abstract
The capability of the integrin VLA-3 to function as a receptor for collagen (Coll), laminin (Lm), and fibronectin (Fn) was addressed using both whole cell adhesion assays and ligand affinity columns. Analysis of VLA-3-mediated cell adhesion was facilitated by the use of a small cell lung carcinoma line (NCI-H69), which expresses VLA-3 but few other integrins. While VLA-3 interaction with Fn was often low or undetectable in cells having both VLA-3 and VLA-5, NCI-H69 cells readily attached to Fn in a VLA-3-dependent manner. Both Arg-Gly-Asp (RGD) peptide inhibition studies, and Fn fragment affinity columns suggested that VLA-3, like VLA-5, may bind to the RGD site in human Fn. However, unlike Fn, both Coll and Lm supported VLA-3-mediated adhesion that was not inhibited by RGD peptide, and was totally unaffected by the presence of VLA-5. In addition, VLA-3-mediated binding to Fn was low in the presence of Ca++, but was increased 6.6-fold with Mg++, and 30-fold in the presence of Mn++. In contrast, binding to Coll was increased only 1.2-fold with Mg++, and 1.7-fold in Mn++, as compared to the level seen with Ca++. Together, these experiments indicate that VLA-3 can bind Coll, Lm, and Fn, and also show that (a) VLA-3 can recognize both RGD-dependent and RGD-independent ligands, and (b) different VLA-3 ligands have distinctly dissimilar divalent cation sensitivities.
Similar articles
- 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. - Adhesion of precursor-B acute lymphoblastic leukaemia cells to bone marrow stromal proteins.
Makrynikola V, Bradstock KF. Makrynikola V, et al. Leukemia. 1993 Jan;7(1):86-92. Leukemia. 1993. PMID: 8418384 - Fibronectin and integrins in invasion and metastasis.
Akiyama SK, Olden K, Yamada KM. Akiyama SK, et al. Cancer Metastasis Rev. 1995 Sep;14(3):173-89. doi: 10.1007/BF00690290. Cancer Metastasis Rev. 1995. PMID: 8548867 Review.
Cited by
- FGF1 Suppresses Allosteric Activation of β3 Integrins by FGF2: A Potential Mechanism of Anti-Inflammatory and Anti-Thrombotic Action of FGF1.
Takada YK, Wu X, Wei D, Hwang S, Takada Y. Takada YK, et al. Biomolecules. 2024 Jul 23;14(8):888. doi: 10.3390/biom14080888. Biomolecules. 2024. PMID: 39199276 Free PMC article. - Integrin α3 promotes TH17 cell polarization and extravasation during autoimmune neuroinflammation.
Park E, Barclay WE, Barrera A, Liao TC, Salzler HR, Reddy TE, Shinohara ML, Ciofani M. Park E, et al. Sci Immunol. 2023 Oct 20;8(88):eadg7597. doi: 10.1126/sciimmunol.adg7597. Epub 2023 Oct 13. Sci Immunol. 2023. PMID: 37831759 Free PMC article. - Irisin acts through its integrin receptor in a two-step process involving extracellular Hsp90α.
A M, Wales TE, Zhou H, Draga-Coletă SV, Gorgulla C, Blackmore KA, Mittenbühler MJ, Kim CR, Bogoslavski D, Zhang Q, Wang ZF, Jedrychowski MP, Seo HS, Song K, Xu AZ, Sebastian L, Gygi SP, Arthanari H, Dhe-Paganon S, Griffin PR, Engen JR, Spiegelman BM. A M, et al. Mol Cell. 2023 Jun 1;83(11):1903-1920.e12. doi: 10.1016/j.molcel.2023.05.008. Mol Cell. 2023. PMID: 37267907 Free PMC article. - Pro-Inflammatory Chemokines CCL5, CXCL12, and CX3CL1 Bind to and Activate Platelet Integrin αIIbβ3 in an Allosteric Manner.
Takada YK, Fujita M, Takada Y. Takada YK, et al. Cells. 2022 Sep 29;11(19):3059. doi: 10.3390/cells11193059. Cells. 2022. PMID: 36231020 Free PMC article. - Recurrence of Papillary Thyroid Cancer: A Systematic Appraisal of Risk Factors.
Nieto HR, Thornton CEM, Brookes K, Nobre de Menezes A, Fletcher A, Alshahrani M, Kocbiyik M, Sharma N, Boelaert K, Cazier JB, Mehanna H, Smith VE, Read ML, McCabe CJ. Nieto HR, et al. J Clin Endocrinol Metab. 2022 Apr 19;107(5):1392-1406. doi: 10.1210/clinem/dgab836. J Clin Endocrinol Metab. 2022. PMID: 34791326 Free PMC article.
References
- J Cell Biol. 1989 Oct;109(4 Pt 1):1817-26 - PubMed
- J Biol Chem. 1990 Apr 15;265(11):6346-52 - PubMed
- J Biol Chem. 1989 Nov 15;264(32):19034-8 - PubMed
- J Cell Biol. 1989 Nov;109(5):2455-62 - PubMed
- EMBO J. 1989 Oct;8(10):2955-65 - PubMed
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Miscellaneous