ArticleMolecular biology of the cell1997
The laminin-binding activity of the alpha 7 integrin receptor is defined by developmentally regulated splicing in the extracellular domain.
Article in Molecular biology of the cell, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Laminin Receptors in Peripheral Tissues: Functions Revealed by Analysis of Knockout Mice.The American journal of pathology · 2025Review
- Spatial proteomics reveals recombinant human laminin-111 restores adhesion signaling to laminin-α2-deficient muscle.JCI insight · 2025Article
- Integrin α7 Mutations Are Associated With Adult-Onset Cardiac Dysfunction in Humans and Mice.Journal of the American Heart Association · 2022Article
- Integrins and extracellular matrix proteins modulate adipocyte thermogenic capacity.Scientific reports · 2021Article
- Short form of α9 promotes α9β1 integrin-dependent cell adhesion by modulating the function of the full-length α9 subunit.Experimental cell research · 2011Article
- Genetically determined proteolytic cleavage modulates alpha7beta1 integrin function.The Journal of biological chemistry · 2008Article
- Exercise promotes alpha7 integrin gene transcription and protection of skeletal muscle.American journal of physiology. Regulatory, integrative and comparative physiology · 2008Article
- The beta1 cytoplasmic domain regulates the laminin-binding specificity of the alpha7X1 integrin.Molecular biology of the cell · 2003Article
- Sensory neuron subtypes have unique substratum preference and receptor expression before target innervation.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2003Article
- Expression of alpha7beta1 integrin splicing variants during skeletal muscle regeneration.The American journal of pathology · 2002Article
- Integrin alpha 7 beta 1 in muscular dystrophy/myopathy of unknown etiology.The American journal of pathology · 2002Article
- Evidence that distinct states of the integrin alpha6beta1 interact with laminin and an ADAM.The Journal of cell biology · 1999Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
The expression pattern of the laminin-binding alpha 7 beta 1 integrin is developmentally regulated in skeletal, cardiac, and smooth muscle. The X1/X2 alternative splicing in the extracellular domain of alpha 7 is found in the variable region between conserved alpha-chain homology repeat domains III and IV, a site implicated in ligand binding. To assess differences in X1/X2 isoform activity, we generated MCF-7 cell lines transfected with alpha 7-X1/X2 cDNAs. Transfectants expressing the alpha 7-X2 variant adhered rapidly to laminin 1, whereas those expressing alpha 7-X1 failed to attach. That alpha 7-X1 exists in an inactive state was established in assays using an activating beta 1 antibody that induced X1-dependent cell adhesion and spreading. Furthermore, the activation of alpha 7-X1 was cell type specific, and when expressed in HT1080 cells, the integrin was converted into a fully functional receptor capable of promoting adhesion. Thus, the expression of the alpha 7-X1/X2 integrin is a novel mechanism that regulates receptor affinity states in a cell-specific context and may modulate integrin-dependent events during muscle development and repair.
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