Abstract:
The present invention describes a direct interaction between myosin and the cytoplasmic domain of membrane proteins, particularly the phosphorylated cytoplasmic domains of the β-subunit of integrins. The invention provides methods of identifying agents which block integrin binding to myosin, methods of using agents which block integrin binding to myosin to modulate biological and pathological processes, and provides agents that block integrin mediated binding to myosin and thereby modulate related cellular or cellular component movement.
Abstract:
The present invention describes a direct interaction between phosphorylated GPIIIa cytoplasmic domains with 1) src/ non- src family kinases and 2) phosphatases. The invention provides methods for identifying agents that block GPIIIa interactions with src/ non- scr family kinases and phosphatases, methods of using agents that block GPIIIa interactions with src/ non- src family kinases and PIP-1C phosphatases to modulate biological and pathological processes and agents that block GPIIIa mediated binding to src/ non- scr family kinases and PIP-1C phosphatases, thereby modulating related GPIIIa mediated signaling.
Abstract:
This invention relates to the glycoprotein v gene. Specifically, this invention discloses the sequence and structure of the glycoprotein v gene and the amino acid sequence of the glycoprotein v polypeptide. In addition, the evolutionary relationship of the glycoprotein v gene with other glycoproteins is described and several uses of the isolated glycoprotein v gene are shown.
Abstract:
The present invention relates to nonhuman transgenic animals in which the GP V gene has been modified. The invention is also useful for identifying agents that modulate the biological functions of GP V, including the screening and identification of potential therapeutic agents.
Abstract:
A method for identifying an agent, which modulates the interaction of an integrin with myosin, comprises the steps of: a) incubating a peptide comprising the phosphorylated cytoplasmic domain of the b-subunit of the integrin with myosin and with the agent, and b) determining whether the agent modulates the binding of myosin to the peptide. An agent that modulates the interaction of myosin and integrin is used in the manufacture of a medicament for modulating the direct interaction of an integrin with myosin in a cell. An agent that blocks the bonding of integrin to myosin is used in the manufacture of a medicament to block the direct interaction of an integrin with myosin such as reducing the severity of a pathological state mediated by direct integrin attachment to myosin. The agent can be a peptide sequence derived from the cytoplasmic domain of an integrin wherein the tyrosine residues are phosphorylated such as a diphosphorylated peptide corresponding to residues 740-762 of b3-subunit having the following sequence: Biotin-D-T-A-N-N-P-L-Y(PO3)-K-E-A-T-S-T-F-T-N-I-T-Y(PO3)-R-G-T-COOH (peptide 1).
Abstract:
The present invention provides the amino acid and nucleotide sequence of a protein that binds to beta 3 integrins, alpha IIb and Src kinase and is involved in integrin mediated signaling. Based on this disclosure, the present invention provides methods for identifying agents that block integrin mediated signaling, methods of using agents that block integrin mediated signaling to modulate biological and pathological processes, and agents that block integrin mediated signaling.
Abstract:
The present invention provides the amino acid and nucleotide sequence of a protein that binds to .beta.3 integrins, .alpha.IIb and Src kinase and is involved in integrin mediated signaling. Based on this disclosure, the present invention provides methods for identifying agents that block integrin mediated signaling, methods of using agents that block integrin mediated signaling to modulate biological and pathological processes, and agents that block integrin mediated signaling.
Abstract:
The present invention relates to nonhuman transgenic animals in which the GP V gene has been modified. The invention is also useful for identifying agents that modulate the biological functions of GP V, including the screening and identification of potential therapeutic agents.