scholarly journals Laminin-binding integrins are essential for the maintenance of functional mammary secretory epithelium in lactation

Development ◽  
2020 ◽  
Vol 147 (4) ◽  
pp. dev181552 ◽  
Author(s):  
Mathilde Romagnoli ◽  
Laura Bresson ◽  
Amandine Di-Cicco ◽  
María Pérez-Lanzón ◽  
Patricia Legoix ◽  
...  
Keyword(s):  
Secretory Epithelium ◽  
Laminin Binding

scholarly journals Receptor functions for the integrin VLA-3: fibronectin, collagen, and laminin binding are differentially influenced by Arg-Gly-Asp peptide and by divalent cations.

1991 ◽  
Vol 112 (1) ◽  
pp. 169-181 ◽  
Author(s):  
M J Elices ◽  
L A Urry ◽  
M E Hemler
Keyword(s):  
Cell Adhesion ◽  
Divalent Cations ◽  
Small Cell Lung Carcinoma ◽  
Rgd Peptide ◽  
Dependent Manner ◽  
Cell Lung Carcinoma ◽  
Ligand Affinity ◽  
Rgd Site ◽  
Inhibition Studies ◽  
Laminin Binding

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.

Abstract LB256: Dynamic kindlin-2 complexes containing a laminin-binding integrin are responsive to hypoxia

2021 ◽  
Author(s):  
Daniel Hernandez-Cortes ◽  
Beatrice S. Knudsen ◽  
Noel A. Warfel ◽  
Anne E. Cress
Keyword(s):  
Laminin Binding
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