Physarum vitronectin-like protein: an Arg-Gly-Asp-dependent cell-spreading protein with a distinct NH2-terminal sequence.
A 70-kDa protein cross-reacted with anti-bovine vitronectin was isolated from slime mold Physarum polycephalum. The NH2-terminal amino acid sequence of the protein, referred to as Physarum vitronectin-like protein, did not share any homology with those of animal vitronectins. It had cell-spreading activity, which was specifically inhibited by an Arg-Gly-Asp (RGD)-containing peptide.
Miyazaki
K
K
Department of Biology, Ochanomizu University, Tokyo, Japan.
Hamano
T
T
Hayashi
M
M
D000595:Amino Acid Sequence; D000818:Animals; D002460:Cell Line; D002465:Cell Movement / Q000187:drug effects / Q000502:physiology; D004305:Dose-Response Relationship, Drug; D005656:Fungal Proteins / Q000737:chemistry* / Q000302:isolation & purification; D006023:Glycoproteins / Q000737:chemistry* / Q000302:isolation & purification / Q000502:physiology*; D007700:Kinetics; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000494:pharmacology*; D010804:Physarum / Q000737:chemistry*; D015800:Protozoan Proteins; D019096:Vitronectin
D005656:Fungal Proteins; D006023:Glycoproteins; D009842:Oligopeptides; D015800:Protozoan Proteins; D019096:Vitronectin; C072699:vitronectin-like protein, Physarum polycephalum; C047981:arginyl-glycyl-aspartic acid