Integrin alpha 7 as substrate for a glycosylphosphatidylinositol-anchored ADP-ribosyltransferase on the surface of skeletal muscle cells.
作者： A Zolkiewska , J Moss
DOI: 10.1016/S0021-9258(19)74388-9
关键词:
摘要: An arginine-specific mono-ADP-ribosyltransferase is expressed on the surface of differentiated mouse skeletal muscle cells and anchored in membrane via a glycosylphosphatidylinositol tail. Following incubation intact with [adenylate-32P]NAD analysis by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), 97-kDa [32P]ADP-ribosylated protein was observed under reducing conditions 140-kDa complex nonreducing conditions. The ADP-ribosylated purified laminin affinity column. Based its N-terminal sequence (FNLDVM-GAIRKEGEPGSLFGF) partial internal (GLMRSEELSFVAGAP), modified identified as integrin alpha 7. trypsin digestion, 39-kDa/79-kDa radiolabeled fragment produced (reduced/nonreduced SDS-PAGE), narrowing ADP-ribosylation site to 39-kDa segment extracellular domain Labeling optimal at least 0.4 mol ADP-ribose/mol Selective expression both ADP-ribosyltransferase 7 cardiac muscle, similar developmental appearance, apparently specific ADP-ribosylation, are consistent regulatory association between these proteins. may modulate receptor signaling could play significant role regulation cell function matrix.
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