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• W2158832664 startingPage "245" @default.
• W2158832664 abstract "To investigate the functional significance of putative integrin divalent cation binding sites, several mutated alpha 4 subunit cDNAs were constructed. Mutants contained the conservative substitution of Glu for Asp or Asn at the third position in each of three putative divalent cation sites. Transfection of wild-type or mutated alpha 4 into K562 cells yielded comparable expression levels and immunoprecipitation profiles. However, for all three alpha 4 mutants, adhesion to CS1/fibronectin was greatly diminished in either the presence or absence of the stimulatory anti-beta 1 mAb TS2/16. Constitutive adhesion to vascular cell adhesion molecule (VCAM) 1 was also diminished but, unlike CS1 adhesion, was restored upon TS2/16 stimulation. In contrast, adhesion to the bacterial protein invasin was minimally affected by any of the three mutations. For each of the mutants, the order of preference for divalent cations was unchanged compared to wild-type alpha 4, on CS1/fibronectin (Mn2+ &gt; Mg2+ &gt; Ca2+), on VCAM-1 (Mn2+ &gt; Mg2+ = Ca2+) and on invasin (Mg2+ = Ca2+). However for the three mutants, the efficiency of divalent cation utilization was decreased. On VCAM-1, 68-108 microM Mn2+ was required to support half-maximal adhesion for the mutants compared with 14-18 microM for wild-type alpha 4. These results indicate (a) that three different ligands for VLA-4 show widely differing sensitivities to mutations within putative divalent cation sites, and (b) each of the three putative divalent cation sites in alpha 4 have comparable functional importance with respect to both divalent cation usage and cell adhesion." @default.
• W2158832664 created "2016-06-24" @default.
• W2158832664 creator A5018714380 @default.
• W2158832664 creator A5044165924 @default.
• W2158832664 date "1993-10-01" @default.
• W2158832664 modified "2023-10-11" @default.
• W2158832664 title "Mutation of putative divalent cation sites in the alpha 4 subunit of the integrin VLA-4: distinct effects on adhesion to CS1/fibronectin, VCAM-1, and invasin." @default.
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• W2158832664 doi "https://doi.org/10.1083/jcb.123.1.245" @default.
• W2158832664 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2119803" @default.
• W2158832664 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/7691827" @default.
• W2158832664 hasPublicationYear "1993" @default.
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