Positive regulation of mu-calpain action by polyphosphoinositides.

[1]  J. Meienhofer,et al.  Solid-phase peptide synthesis using mild base cleavage of N alpha-fluorenylmethyloxycarbonylamino acids, exemplified by a synthesis of dihydrosomatostatin. , 2009, International journal of peptide and protein research.

[2]  E. Nishida,et al.  Mutational analysis of an actin-binding site of cofilin and characterization of chimeric proteins between cofilin and destrin. , 1992, The Journal of biological chemistry.

[3]  K. Suzuki,et al.  Purification and characterization of protein kinase C epsilon from rabbit brain. , 1992, Biochemistry.

[4]  E. Nishida,et al.  A short sequence responsible for both phosphoinositide binding and actin binding activities of cofilin. , 1991, The Journal of biological chemistry.

[5]  F. Shibasaki,et al.  Two types of phosphatidylinositol 3-kinase from bovine thymus. Monomer and heterodimer form. , 1991, The Journal of biological chemistry.

[6]  J. Card,et al.  Proteolytic processing of beta-amyloid precursor by calpain I , 1990, The Journal of neuroscience : the official journal of the Society for Neuroscience.

[7]  H. Yoshiyama,et al.  The phorbol ester TPA strongly inhibits HIV-1-induced syncytia formation but enhances virus production: possible involvement of protein kinase C pathway. , 1990, Virology.

[8]  G. Kucera,et al.  Human platelets form 3-phosphorylated phosphoinositides in response to alpha-thrombin, U46619, or GTP gamma S. , 1990, The Journal of biological chemistry.

[9]  T. Kadowaki,et al.  Substrates for Insulin-Receptor Kinase , 1990, Diabetes Care.

[10]  R. Roth,et al.  Phosphatidylinositol kinase or an associated protein is a substrate for the insulin receptor tyrosine kinase. , 1990, The Journal of biological chemistry.

[11]  P. Gordon-Weeks,et al.  GAP-43 in growth cones is associated with areas of membrane that are tightly bound to substrate and is a component of a membrane skeleton subcellular fraction , 1990, The Journal of neuroscience : the official journal of the Society for Neuroscience.

[12]  J. Morrow,et al.  Calmodulin regulates fodrin susceptibility to cleavage by calcium-dependent protease I. , 1989, The Journal of biological chemistry.

[13]  M. Weber,et al.  Fibroblasts transformed with v-src show enhanced formation of an inositol tetrakisphosphate. , 1989, Science.

[14]  K. Wang,et al.  Calmodulin-binding proteins as calpain substrates. , 1989, The Biochemical journal.

[15]  G. Lynch,et al.  Ischemia triggers NMDA receptor-linked cytoskeletal proteolysis in hippocampus , 1989, Brain Research.

[16]  P. Libby,et al.  PDGF-dependent tyrosine phosphorylation stimulates production of novel polyphosphoinositides in intact cells , 1989, Cell.

[17]  E. Becker,et al.  Inhibition of calpain in intact platelets by the thiol protease inhibitor E-64d. , 1989, Biochemical and biophysical research communications.

[18]  R. Steinhardt,et al.  Increased protein degradation results from elevated free calcium levels found in muscle from mdx mice , 1988, Nature.

[19]  P. Insel,et al.  Phorbol ester and neomycin dissociate bradykinin receptor-mediated arachidonic acid release and polyphosphoinositide hydrolysis in Madin-Darby canine kidney cells. Evidence that bradykinin mediates noninterdependent activation of phospholipases A2 and C. , 1988, The Journal of biological chemistry.

[20]  V. Steen,et al.  Neomycin inhibits platelet functions and inositol phospholipid metabolism upon stimulation with thrombin, but not with ionomycin or 12-O-tetradecanoyl-phorbol 13-acetate. , 1988, European journal of biochemistry.

[21]  A. Jesaitis,et al.  Lateral segregation of neutrophil chemotactic receptors into actin- and fodrin-rich plasma membrane microdomains depleted in guanyl nucleotide regulatory proteins , 1988, The Journal of cell biology.

[22]  G. Gawdi,et al.  Biochemical and functional responses stimulated by platelet-activating factor in murine peritoneal macrophages [published erratum appears in J Cell Biol 1988 Sep;107(3):following 1260] , 1988, The Journal of cell biology.

[23]  J. Imaki,et al.  Isolation and characterization of two different forms of inositol phospholipid-specific phospholipase C from rat brain. , 1988, The Journal of biological chemistry.

[24]  J. H. Wang,et al.  Characterization of fodrin phosphorylation by spleen protein tyrosine kinase. , 1988, Biochemistry.

[25]  T. Takenawa,et al.  Mitogenesis in response to PDGF and bombesin abolished by microinjection of antibody to PIP2. , 1988, Science.

[26]  J. H. Wang,et al.  Effect of phosphorylation by cyclic AMP-dependent protein kinase on the smooth muscle actomyosin Mg2+-ATPase stimulatory activity of fodrin. , 1987, Journal of Biological Chemistry.

[27]  H. Kawasaki,et al.  Calcium‐activated neutral protease and its endogenous inhibitor Activation at the cell membrane and biological function , 1987, FEBS letters.

[28]  H. Ishii,et al.  Procalpain is activated on the plasma membrane and the calpain acts on the membrane. , 1987, Biochimica et biophysica acta.

[29]  R. Burgoyne,et al.  Role of fodrin in secretion , 1987, Nature.

[30]  C. C. Reynolds,et al.  Spectrin is associated with membrane-bound actin filaments in platelets and is hydrolyzed by the Ca2+-dependent protease during platelet activation. , 1987, Blood.

[31]  K. Suzuki,et al.  Complete amino acid sequence of the large subunit of the low‐Ca2+‐requiring form of human Ca2+‐activated neutral protease (μCANP) deduced from its cDNA sequence , 1986, FEBS letters.

[32]  D. Hathaway,et al.  The role of subunit autolysis in activation of smooth muscle Ca2+-dependent proteases. , 1986, The Journal of biological chemistry.

[33]  M. Prentki,et al.  Neomycin: a specific drug to study the inositol‐phospholipid signalling system? , 1986, FEBS letters.

[34]  B. Horecker,et al.  Binding to erythrocyte membrane is the physiological mechanism for activation of Ca2+-dependent neutral proteinase. , 1985, Biochemical and biophysical research communications.

[35]  R. Tsien,et al.  A new generation of Ca2+ indicators with greatly improved fluorescence properties. , 1985, The Journal of biological chemistry.

[36]  R. Tsien,et al.  Cytosolic Ca2+ homeostasis in Ehrlich and Yoshida carcinomas. A new, membrane-permeant chelator of heavy metals reveals that these ascites tumor cell lines have normal cytosolic free Ca2+. , 1985, The Journal of biological chemistry.

[37]  N. R. Burns Neuroscience: Skeleton key to memory? , 1985, Nature.

[38]  J. McCord,et al.  Oxygen-derived free radicals in postischemic tissue injury. , 1985, The New England journal of medicine.

[39]  G. Lynch,et al.  Regulation of glutamate receptor binding by the cytoskeletal protein fodrin , 1985, Nature.

[40]  D. Hathaway,et al.  Effect of L-alpha-phosphatidylinositol on a vascular smooth muscle Ca2+-dependent protease. Reduction of the Ca2+ requirement for autolysis. , 1984, The Journal of biological chemistry.

[41]  R. Goldman,et al.  A rapid procedure for preparing fluorescein-labeled specific antibodies from whole antiserum: its use in analyzing cytoskeletal architecture , 1983, The Journal of cell biology.

[42]  P. Siekevitz,et al.  Identification of fodrin as a major calmodulin-binding protein in postsynaptic density preparations , 1983, The Journal of cell biology.

[43]  Klaus Weber,et al.  An F-actin- and calmodulin-binding protein from isolated intestinal brush borders has a morphology related to spectrin , 1982, Cell.

[44]  F. Palmer Chromatography of acidic phospholipids on immobilized neomycin. , 1981, Journal of lipid research.

[45]  J. Levine,et al.  Fodrin: axonally transported polypeptides associated with the internal periphery of many cells , 1981, The Journal of cell biology.

[46]  H. Hendrickson,et al.  Phosphoinositide interconversion: a model for control of Na + and K + permeability in the nerve axon membrane. , 1971, Biochemical and biophysical research communications.

[47]  A. Derksen,et al.  Quantification of human platelet inositides and the influence of ionic environment on their incorporation of orthophosphate-32P. , 1971, The Journal of clinical investigation.

[48]  U. K. Laemmli,et al.  Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 , 1970, Nature.

[49]  S. Mehdi,et al.  Cell-penetrating inhibitors of calpain. , 1991, Trends in biochemical sciences.