Actin binds to the cytoplasmic tail of alpha 1 subunit of integrin in hepatocytes.
alpha 1 beta 1-Integrin is a common receptor for laminin and collagen IV on hepatocytes. The interactions of intracellular domain of integrins with cytoplasmic elements are critical in the initiation and transduction of signals. In order to understand the nature of cytoplasmic components that can interact with cytoplasmic domain of alpha 1 integrin, cytoplasmic extracts of monolayers of rat hepatocytes were subjected to chromatography over an affinity column prepared by coupling a 60-mer synthetic cytoplasmic tail of alpha 1 subunit. SDS-PAGE analysis of the eluate showed the presence of a 47 kDa protein. Dot-Blot assay using radio-iodinated 47 kDa protein showed the binding of the protein to 60-mer C tail in a concentration dependent manner. Immunoblot analysis using specific antibodies showed that the 47 kDa protein is actin.
Menon
B
B
Department of Biochemistry, University of Kerala, Kariavattom, Trivandrum, India.
Sudhakaran
P R
PR
D000199:Actins / Q000378:metabolism*; D000595:Amino Acid Sequence; D000818:Animals; D015703:Antigens, CD / Q000737:chemistry / Q000378:metabolism*; D001665:Binding Sites; D003593:Cytoplasm / Q000378:metabolism; D066298:In Vitro Techniques; D039423:Integrin alpha1; D008099:Liver / Q000166:cytology / Q000378:metabolism*; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism; D051381:Rats
D000199:Actins; D015703:Antigens, CD; D039423:Integrin alpha1; D010446:Peptide Fragments