The Npc1 mutation causes an altered expression of caveolin-1, annexin II and protein kinases and phosphorylation of caveolin-1 and annexin II in murine livers.

[1]  M. Bomsel,et al.  In adrenocortical tissue, annexins II and VI are attached to clathrin coated vesicles in a calcium-independent manner. , 1998, Biochimica et biophysica acta.

[2]  J. Kawabe,et al.  Caveolin Interaction with Protein Kinase C , 1997, The Journal of Biological Chemistry.

[3]  M. Lisanti,et al.  Interaction of a Receptor Tyrosine Kinase, EGF-R, with Caveolins , 1997, The Journal of Biological Chemistry.

[4]  R. Erickson,et al.  Altered expression of caveolin-1 and increased cholesterol in detergent insoluble membrane fractions from liver in mice with Niemann-Pick disease type C. , 1997, Biochimica et biophysica acta.

[5]  C. Fielding,et al.  Intracellular cholesterol transport. , 1997, Journal of lipid research.

[6]  R. Rousson,et al.  Modulation of protein kinase C by endogenous sphingosine: inhibition of phorbol dibutyrate binding in Niemann-Pick C fibroblasts. , 1997, The Biochemical journal.

[7]  W. Pavan,et al.  Murine model of Niemann-Pick C disease: mutation in a cholesterol homeostasis gene. , 1997, Science.

[8]  K. G. Coleman,et al.  Niemann-Pick C1 disease gene: homology to mediators of cholesterol homeostasis. , 1997, Science.

[9]  R. Huber,et al.  Three-dimensional structure of annexins , 1997, Cellular and Molecular Life Sciences CMLS.

[10]  B. Rothhut Participation of annexins in protein phosphorylation , 1997, Cellular and Molecular Life Sciences CMLS.

[11]  A. Bist,et al.  Caveolin mRNA levels are up-regulated by free cholesterol and down-regulated by oxysterols in fibroblast monolayers. , 1997, Proceedings of the National Academy of Sciences of the United States of America.

[12]  R. Kellner,et al.  Specific release of membrane-bound annexin II and cortical cytoskeletal elements by sequestration of membrane cholesterol. , 1997, Molecular biology of the cell.

[13]  C. Fielding,et al.  Intracellular transport of low density lipoprotein derived free cholesterol begins at clathrin-coated pits and terminates at cell surface caveolae. , 1996, Biochemistry.

[14]  T. Kadowaki,et al.  Annexin II Is a Novel Player in Insulin Signal Transduction , 1996, The Journal of Biological Chemistry.

[15]  M. Lisanti,et al.  Src tyrosine kinases, Galpha subunits, and H-Ras share a common membrane-anchored scaffolding protein, caveolin. Caveolin binding negatively regulates the auto-activation of Src tyrosine kinases. , 1996, The Journal of biological chemistry.

[16]  A. Boneh,et al.  Protein kinase C activation and phosphate uptake are altered in intact mucolipidosis type-4 skin fibroblasts. , 1996, Biochemical and molecular medicine.

[17]  N. Hooper,et al.  A role for calcium and annexins in the formation of caveolae. , 1996, Biochemical Society transactions.

[18]  M. Lisanti,et al.  Phosphorylation of Caveolin by Src Tyrosine Kinases , 1996, The Journal of Biological Chemistry.

[19]  H. Lodish,et al.  Identification, sequence, and expression of caveolin-2 defines a caveolin gene family. , 1996, Proceedings of the National Academy of Sciences of the United States of America.

[20]  G. Bloom,et al.  Caveolin cycles between plasma membrane caveolae and the Golgi complex by microtubule-dependent and microtubule-independent steps , 1995, The Journal of cell biology.

[21]  C. Fielding,et al.  Plasma membrane caveolae mediate the efflux of cellular free cholesterol. , 1995, Biochemistry.

[22]  R. G. Anderson,et al.  Hormonal regulation of caveolae internalization , 1995, The Journal of cell biology.

[23]  P. Oh,et al.  Endothelial Caveolae Have the Molecular Transport Machinery for Vesicle Budding, Docking, and Fusion Including VAMP, NSF, SNAP, Annexins, and GTPases (*) , 1995, The Journal of Biological Chemistry.

[24]  P. Conrad,et al.  Caveolin moves from caveolae to the Golgi apparatus in response to cholesterol oxidation , 1994, The Journal of cell biology.

[25]  M. Lisanti,et al.  The primary sequence of murine caveolin reveals a conserved consensus site for phosphorylation by protein kinase C. , 1994, Gene.

[26]  M. Lisanti,et al.  In vitro phosphorylation of caveolin-rich membrane domains: identification of an associated serine kinase activity as a casein kinase II-like enzyme. , 1994, Oncogene.

[27]  M. Ohnishi,et al.  Involvement of annexin I and annexin II in hepatocyte proliferation: Can annexins I and II be markers for proliferative hepatocytes? , 1994, Hepatology.

[28]  N. Hooper,et al.  Purification and characterization of smooth muscle cell caveolae , 1994, The Journal of cell biology.

[29]  S. Walkley,et al.  Feline Niemann-Pick disease type C. , 1994, The American journal of pathology.

[30]  R. Rousson,et al.  Free sphingoid bases in tissues from patients with type C Niemann-Pick disease and other lysosomal storage disorders. , 1994, Biochimica et biophysica acta.

[31]  H. Pollard,et al.  Annexins: the problem of assessing the biological role for a gene family of multifunctional calcium- and phospholipid-binding proteins. , 1994, Biochimica et biophysica acta.

[32]  R. G. Anderson,et al.  Protein kinase C activators inhibit receptor-mediated potocytosis by preventing internalization of caveolae , 1994, The Journal of cell biology.

[33]  M. Lisanti,et al.  Signal transducing molecules and glycosyl-phosphatidylinositol-linked proteins form a caveolin-rich insoluble complex in MDCK cells , 1993, The Journal of cell biology.

[34]  P. Pentchev,et al.  Differential accumulation of cholesterol in Golgi compartments of normal and Niemann-Pick type C fibroblasts incubated with LDL: a cytochemical freeze-fracture study. , 1993, Journal of lipid research.

[35]  D. Waisman,et al.  Phosphorylation of annexin II tetramer by protein kinase C inhibits aggregation of lipid vesicles by the protein. , 1992, The Journal of biological chemistry.

[36]  R. Brady,et al.  Type C Niemann-Pick disease: a murine model of the lysosomal cholesterol lipidosis accumulates sphingosine and sphinganine in liver. , 1992, Biochimica et biophysica acta.

[37]  J. Slotte Enzyme-catalyzed oxidation of cholesterol in mixed phospholipid monolayers reveals the stoichiometry at which free cholesterol clusters disappear. , 1992, Biochemistry.

[38]  S. Pelech,et al.  Purification and characterization of echinoderm casein kinase II. Regulation by protein kinase C. , 1992, The Biochemical journal.

[39]  Richard G. W. Anderson,et al.  Caveolin, a protein component of caveolae membrane coats , 1992, Cell.

[40]  R. Brady,et al.  Niemann-Pick type-C disease: deficient intracellular transport of exogenously derived cholesterol. , 1992, American journal of medical genetics.

[41]  Y. Hannun,et al.  Activation of casein kinase II by sphingosine. , 1991, The Journal of biological chemistry.

[42]  C. Creutz,et al.  Ca(2+)-dependent annexin self-association on membrane surfaces. , 1991, Biochemistry.

[43]  L. Alberghina,et al.  Characterization of the tyrosine phosphorylation of calpactin I (annexin II) induced by platelet-derived growth factor. , 1991, The Biochemical journal.

[44]  J. Ernst,et al.  Characterization of Ca2(+)-dependent phospholipid binding, vesicle aggregation and membrane fusion by annexins. , 1990, The Biochemical journal.

[45]  J. Glenney Tyrosine phosphorylation of a 22-kDa protein is correlated with transformation by Rous sarcoma virus. , 1989, The Journal of biological chemistry.

[46]  L. Liscum,et al.  The intracellular transport of low density lipoprotein-derived cholesterol is defective in Niemann-Pick type C fibroblasts , 1989, The Journal of cell biology.

[47]  H. Hanafusa,et al.  p60c-src is complexed with a cellular protein in subcellular compartments involved in exocytosis , 1988, The Journal of cell biology.

[48]  R. Brady,et al.  Type-C Niemann-Pick disease: low density lipoprotein uptake is associated with premature cholesterol accumulation in the Golgi complex and excessive cholesterol storage in lysosomes. , 1988, Proceedings of the National Academy of Sciences of the United States of America.

[49]  C. Kahn,et al.  Lipocortins 1 and 2 as substrates for the insulin receptor kinase in rat liver. , 1988, The Journal of biological chemistry.

[50]  J. Glenney,et al.  Regulation of calpactin I phospholipid binding by calpactin I light-chain binding and phosphorylation by p60v-src. , 1987, The Biochemical journal.

[51]  S. Courtneidge,et al.  An 81 kd protein complexed with middle T antigen and pp60c-src : A possible phosphatidylinositol kinase , 1987, Cell.

[52]  K. Gould,et al.  The protein-tyrosine kinase substrate p36 is also a substrate for protein kinase C in vitro and in vivo , 1986, Molecular and cellular biology.

[53]  J. Glenney Two related but distinct forms of the Mr 36,000 tyrosine kinase substrate (calpactin) that interact with phospholipid and actin in a Ca2+-dependent manner. , 1986, Proceedings of the National Academy of Sciences of the United States of America.

[54]  N. Simionescu,et al.  Specific binding sites for albumin restricted to plasmalemmal vesicles of continuous capillary endothelium: receptor-mediated transcytosis , 1986, The Journal of cell biology.

[55]  R. Brady,et al.  A defect in cholesterol esterification in Niemann-Pick disease (type C) patients. , 1985, Proceedings of the National Academy of Sciences of the United States of America.

[56]  A. M. Cook,et al.  [15] Total phosphorus determination by spectrophotometry , 1981 .

[57]  J. Heider,et al.  The picomole determination of free and total cholesterol in cells in culture. , 1978, Journal of lipid research.