Molecular and Cellular Biochemistry

, Volume 149, Issue 1, pp 301–322

Annexin II tetramer: structure and function

  • David M. Waisman
Article

Abstract

The annexins are a family of proteins that bind acidic phospholipids in the presence of Ca2+. The interaction of these proteins with biological membranes has led to the suggestion that these proteins may play a role in membrane trafficking events such as exocytosis, endocytosis and cell-cell adhesion. One member of the annexin family, annexin II, has been shown to exist as a monomer, heterodimer or heterotetramer. The ability of annexin II tetramer to bridge secretory granules to plasma membrane has suggested that this protein may play a role in Ca2+-dependent exocytosis. Annexin II tetramer has also been demonstrated on the extracellular face of some metastatic cells where it mediates the binding of certain metastatic cells to normal cells. Annexin II tetramer is a major cellular substrate of protein kinase C and pp60src. Phosphorylation of annexin II tetramer is a negative modulator of protein function.

Key words

annexins phosphorylation calcium binding phospholipids membrane bridging cell-cell interaction DNA polymerase 

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    Geisow MJ, Ali SM, Boustead C, Burgoyne RD, Taylor WR, Walker JH: Structures and functions of a supergene family of calcium and phospholipid binding proteins. Prog Clin Biol Res 349: 111–121, 1990PubMedGoogle Scholar
  2. 2.
    Johnsson N, Gerke V, Weber K: P36, member of the Ca2+/lipid binding proteins (annexins, calpactins, lipocortins) and its complex with P11; molecular aspects. Prog Clin Biol Res 349: 123–133, 1990PubMedGoogle Scholar
  3. 3.
    Burgoyne RD, Geisow MJ: The annexin family of calcium-binding proteins. Cell Calcium 10: 1–10, 1989PubMedGoogle Scholar
  4. 4.
    Gerke V: Tyrosine protein kinase substrate p36: a member of the annexin family of Ca2+/phospholipid-binding proteins. Cell Motil Cytoskeleton 14: 449–454, 1989PubMedGoogle Scholar
  5. 5.
    Crompton MR, Moss SE, Crumpton MJ: Diversity in the lipocortin/ calpactin family. Cell 55: 1–3, 1988PubMedGoogle Scholar
  6. 6.
    Klee CB: Ca2+-dependent phospholipid- (and membrane-) binding proteins. Biochemistry 27: 6645–6653, 1988PubMedGoogle Scholar
  7. 7.
    Tokuda M, Waisman DM, Hatase O: [Lipocortin-a Ca2+-binding proproteins. which has anti-phospholipase A2 activity]. Seikagaku 60: 26–31, 1988PubMedGoogle Scholar
  8. 8.
    Smith, V. L. and Dedman, J. R. The Role of Intracellular Calciumbinding Proteins in Stimulus-response Coupling. Smith, V. L. and Dedman, J. R. eds) Stimulus Response coupling; The Role of Intracellular Calcium-binding Proteins. CRC Press, Boca Raton, 1990, pp 1–19.Google Scholar
  9. 9.
    Raynal P, Pollard HB: Annexins: the problem of assessing the biological role for a gene family of multifunctional calcium- and phospholipid-binding proteins. Biochim Biophys Acta 1197: 63–93, 1994.PubMedGoogle Scholar
  10. 10.
    Bandorowicz J, Pikula S: Annexins-multifunctional, calcium-dependent, phospholipid-binding proteins. Acta Biochim Pol 40: 281–293, 1993PubMedGoogle Scholar
  11. 11.
    Swairjo MA, Seaton BA: Annexin Structure and Membrane Interactions: A Molecular Perspective. Ann Rev Biophys Biomol Struct 23: 193–213, 1994Google Scholar
  12. 12.
    Geisow MJ: Common domain structure of Ca2+ and lipid-binding proteins. FEBS Lett 203: 99–103, 1986PubMedGoogle Scholar
  13. 13.
    Geisow MJ, Fritsche U, Hexham JM, Dash B, Johnson T: A consensus animo-acid sequence repeat in Torpedo and mammalian Ca2+-dependent membrane-binding proteins. Nature 320: 636–638, 1986PubMedGoogle Scholar
  14. 14.
    Crumpton MJ, Dedman JR: Protein terminology tangle [letter] [see comments]. Nature 345: 212-1990PubMedGoogle Scholar
  15. 15.
    Creutz CE, Dowling LG, Sando JJ, Villar-Palasi C, Whipple JH, Zaks WJ: Characterization of the chromobindins. Soluble proteins that bind to the chromaffin granule membrane in the presence of Ca2+. J Biol Chem 258: 14664–14674, 1983PubMedGoogle Scholar
  16. 16.
    Emans N, Gorvel JP, Walter C, Gerke V, Kellner R, Griffiths G, Gruenberg J: Annexin II is a major component of fusogenic endosomal vesicles. J Cell Biol 120: 1357–1369, 1993PubMedGoogle Scholar
  17. 17.
    Burgoyne RD, Morgan A, Roth D: Characterization of proteins that regulate calcium-dependent exocytosis in adrenal chromaffin cells. Ann NY Acad Sci 710: 333–346, 1994PubMedGoogle Scholar
  18. 18.
    Morgan A, Roth D, Martin H, Aitken A, Burgoyne RD: Identification of cytosolic protein regulators of exocytosis. Biochem Soc Trans 21: 401–405, 1993PubMedGoogle Scholar
  19. 19.
    Saraffan T, Pradel LA, Henry JP, Aunis D, Bader MF: The participation of annexin II (calpactin I) in calcium-evoked exocytosis requires protein kinase C. J Cell Biol 114: 1135–1147, 1991PubMedGoogle Scholar
  20. 20.
    Wu YN, Wagner PD: Calpactin-depleted cytosolic proteins restore Ca(2+)-dependent secretion to digitonin-permeabilized bovine chromaffin cells. FEBS Lett 282: 197–199, 1991PubMedGoogle Scholar
  21. 21.
    Ali SM, Burgoyne RD: The stimulatory effect of calpactin (annexin II) on calcium-dependent exocytosis in chromaffin cells: requirement for both the N-terminal and core domains of p36 and ATP. Cell Signal 2: 265–276, 1990PubMedGoogle Scholar
  22. 22.
    All SM, Geisow MJ, Burgoyne RD: A role for calpactin in calciumdependent exocytosis in adrenal chromaffin cells. Nature 340: 313–315, 1989PubMedGoogle Scholar
  23. 23.
    Creutz CE: The annexins and exocytosis. Science 258: 924–931, 1992PubMedGoogle Scholar
  24. 24.
    Burgoyne RD, Morgan A, Robinson I, Pender N, Cheek TR: Exocytosis in adrenal chromaffin cells. J Anat 183: 309–314, 1993PubMedGoogle Scholar
  25. 25.
    Berendes R, Burger A, Voges D, Demange P, Huber R: Calcium influx through annexin V ion channels into large unilamellar vesicles measured with fura-2. FEBS Lett 317: 131–134, 1993PubMedGoogle Scholar
  26. 26.
    Burger A, Voges D, Demange P, Perez CR, Huber R, Berendes R: Structural and electrophysiological analysis of annexin V mutants. Mutagenesis of human annexin V, anin vitro voltage-gated calcium channel, provides inforamtion about the structural features of the ion pathway, the voltage sensor and the ion selectivity filter. J Mol Biol 237: 479–499, 1994PubMedGoogle Scholar
  27. 27.
    Rojas E, Arispe N, Haigler HT, Burns AL, Pollard HB: Identification of annexins as calcium channels in biological membranes. Bone Miner 17: 214–218, 1992PubMedGoogle Scholar
  28. 28.
    Pollard HB, Guy HR, Arispe N, de-la-Fuente M, Lee G, Rojas EM, Pollard JR, Srivastava M, Zhang-Keck ZY, Merezhinskaya N, et al.: Calcium channel and membrane fusion activity of synexin and other members of the Annexin gene family. Biophys J: 62: 15–18, 1992PubMedGoogle Scholar
  29. 29.
    Jones PG, Fitzpatrick S, Waisman DM: Chromaffin Granules Release Calcium on Contact With Annexin VI: Implications for Exocytosis. Biochemistry 33: 8180–8187, 1994PubMedGoogle Scholar
  30. 30.
    Khanna NC, Hee-Chong M, Severson DL, Tokuda M, Chong SM, Waisman DM: Inhibition of phospholipase A2 by protein I. Biochem Biophys Res Commun 139: 455–460, 1986PubMedGoogle Scholar
  31. 31.
    Khanna NC, Tokuda M, Waisman DM: Purification of three forms of lipocortin from bovine lung. Cell Calcium 8: 217–228, 1987PubMedGoogle Scholar
  32. 32.
    Huang KS, McGray P, Mattaliano RJ, Burne C, Chow EP, Sinclair LK, Pepinsky RB: Purification and characterization of proteolytic fragments of lipocortin I that inhibit phospholipase A2. J Biol Chem 262: 7639–7645, 1987PubMedGoogle Scholar
  33. 33.
    Bastian BC, Sellert C, Seekamp A, Romisch J, Paques EP, Brocker EB: In'nibition of human skin phospholipase A2 by ‘lipocortins’ is an indirect effect of substrate/lipocortin interaction. J Invest Dermatol 101: 359–363, 1993PubMedGoogle Scholar
  34. 34.
    Cirino G, Cicala C, Sorrentino L, Ciliberto G, Arpaia G, Perretti M, Flower RJ: Anti-inflammatory actions of an N-terminal peptide from human lipocortin 1. Br J Pharmacol 108: 573–574, 1993PubMedGoogle Scholar
  35. 35.
    Hayashi J, Liu P, Ferguson SE, Wen M, Sakata T, Teraoka H, Riley HD: Arachidonic acid metabolism in cells transfected with sense and anti-sense cDNA to annexin I. Biochem Mol Biol Int31: 143–151, 1993PubMedGoogle Scholar
  36. 36.
    Bohn E, Gerke V, Kresse H, Loffler BM, Kunze H: Annexin II inhibits calcium-dependent phospholipase A1 and lysophospholipase but not triacyl glycerol lipase activities of rat liver hepatic lipase. FEBS Lett 296: 237–240, 1992PubMedGoogle Scholar
  37. 37.
    Buhl WJ: Annexins and phospholipase A2 inhibition. Eicosanoids 5 Suppl: S26-S28, 1992PubMedGoogle Scholar
  38. 38.
    Sun J, Bird P, Salem HH: Interaction of annexin V and platelets: effects on platelet function and protein S binding. Thromb Res 69: 289–296, 1993PubMedGoogle Scholar
  39. 39.
    Chollet P, Malecaze F, Hullin F, Raynal P, Arne JL, Pagot V, Ragab-Thomas J, Chap H: Inhibition of intraocular fibrin formation with annexin V. Br J Ophthalmol 76: 450–452, 1992PubMedGoogle Scholar
  40. 40.
    Kondo S, Noguchi M, Funakoshi T, Fujikawa K, Kisiel W: Inhibition of human factor VIIa-tissue factor activity by placental anticoagulant protein. Thromb Res 48: 449–459, 1987PubMedGoogle Scholar
  41. 41.
    Cirino G, Cicala C: Human recombinant lipocortin 1 (annexin 1) has anticoagulant activity on human plasmain vitro. J Lipid Mediat 8: 81–86, 1993PubMedGoogle Scholar
  42. 42.
    Sun J, Bird P, Salem HH: Effects of annexin V on the activity of the anticoagulant proteins C and S. Thromb Res 69: 279–287, 1993PubMedGoogle Scholar
  43. 43.
    Andree HA, Stuart MC, Hermens WT, Reutelingsperger CP, Hemker HC, Frederik PM, Willems GM: Clustering of lipid-bound annexin V may explain its anticoagulant effect. J Biol Chem 267: 17907–17912, 1992PubMedGoogle Scholar
  44. 44.
    Ohyama N: [Effect of coagulation inhibitor proteins (Calphobindins) on tissue factor expression of endothelial cells]. Nippon Sanka Fujinka Gakkai Zasshi 44: 1119–1126, 1992PubMedGoogle Scholar
  45. 45.
    Sammaritano LR, Gharavi AE, Soberano C, Levy RA, Lockshin MD: Phospholipid binding of antiphospholipid antibodies and placental anticoagulant protein. J Clin Immunol 12: 27–35, 1992PubMedGoogle Scholar
  46. 46.
    Yoshizaki H, Arai K, Mizoguchi T, Shiratsuchi M, Hattori Y, Nagoya T, Shidara Y, Maki M: Isolation and characterization of an anticoagulant protein from human placenta. J Biochem Tokyo 105: 178–183, 1989PubMedGoogle Scholar
  47. 47.
    Rothhut B, Comera C, Cortial S, Haumont PY, Diep-Le KH, Cavadore JC, Conard J, Russo-Marie F, Lederer F: A 32 kDa lipocortin from human mononuclear cells appears to be identical with the placental inhibitor of blood coagulation. Biochem J 263: 929–935, 1989PubMedGoogle Scholar
  48. 48.
    Thiagarajan P, Tait JF: Binding of anexin V/placental anticoagulant protein I to platelets. Evidence for phosphatidylserine exposure in the procoagulant response of activated platelets. J Biol Chem 265: 17420–17423, 1990PubMedGoogle Scholar
  49. 49.
    Romisch J, Seiffge D, Reiner G, Paques EP, Heimburger N:In vivo antithrombotic potency of placenta protein 4 (annexin V). Thromb Res 61: 93–104, 1991PubMedGoogle Scholar
  50. 50.
    Romisch J, Schorlemmer U, Fickenscher K, Paques EP, Heimburger N: Anticoagulant properties of placenta protein 4 (annexin V). Thromb Res 60: 355–366, 1990PubMedGoogle Scholar
  51. 51.
    Vishwanatha JK, Jindal HK, Davis RG: The role of primer recognition proteins in DNA replication: association with nuclear matrix in HeLa cells. J Cell Sci 101: 25–34, 1992PubMedGoogle Scholar
  52. 52.
    Braslau DL, Ringo DL, Rocha V: Synthesis of novel calcium-dependent proteins associated with mammary epithelial cell migration and differentiation. Exp Cell Res 155: 213–221, 1984PubMedGoogle Scholar
  53. 53.
    Keutzer JC, Hirschhorn RR: The growth-regulated gene 1B6 is identified as the heavy chain of calpactin I. Exp Cell Res 188: 153–159, 1990PubMedGoogle Scholar
  54. 54.
    Croxtall JD, Pollard JW, Carey F, Forder RA, White JO: Colony stimulating factor-1 stimulates Ishikawa cell proliferation and lipocortin II synthesis. J Steroid Biochem Mol Biol 42: 121–129, 1992PubMedGoogle Scholar
  55. 55.
    Masiakowski P, Shooter EM: Nerve growth factor induces the genes for two proteins related to a family of calcium-binding proteins in PC12 cells. Proc Natl Acad Sci U S A 85: 1277–1281, 1988PubMedGoogle Scholar
  56. 56.
    Lozano JJ, Silberstein GB, Hwang S, Haindl AH, Rocha V: Developmental regulation of calcium-binding proteins (calelectrins and calpactin I) in mammary glands. J Cell Physiol 138: 503–510, 1989PubMedGoogle Scholar
  57. 57.
    William F, Mcroczkowski B, Cohen S, Kraft AS: Differentiation of HL-60 cells is associated with an increase in the 35-kDa protein lipocortin I. J Cell Physiol 137: 402–410, 1988PubMedGoogle Scholar
  58. 58.
    Fox MT, Prentice DA, Hughes JP: Increases in pll and annexin II proteins correlate with differentiation in the PC12 pheochromocytoma. Biochem Biophys Res Commun 177: 1188–1193, 1991PubMedGoogle Scholar
  59. 59.
    Hofmann C, Gropp R, von-der-Mark K: Expression of anchorin CII, a collagen-binding protein of the annexin family, in the developing chick embryo. Dev Biol 151: 391–400, 1992PubMedGoogle Scholar
  60. 60.
    Harder T, Thiel C, Gerke V: Formationof the annexin II2pll2 complex upon differentiation of F9 teratocarcinoma cells. J Cell Sci 104: 1109–1117, 1993PubMedGoogle Scholar
  61. 61.
    Leung MF, Lin TS, Sartorelli AC: Changes in actin and actin-binding proteins during the differentiation of HL-60 leukemia cells. Cancer Res 52: 3063–3066, 1992PubMedGoogle Scholar
  62. 62.
    Croxtall JD, Pollard JW, Carey F, Forder RA, White JO: Colony stimulating factor-1 stimulates Ishikawa cell proliferation and lipocortin II synthesis. J Steroid Biochem Mol Biol 42: 121–129, 1992PubMedGoogle Scholar
  63. 63.
    Pfaffle M, Ruggiero F, Hofmann H, Fernandez MP, Selmin O, Yamada Y, Garrone R, von-der-Mark K: Biosynthesis, secretion and extracellular localization of anchorin CII, a collagen-binding protein of the calpactin family. EMBO J 7: 2335–2342, 1988PubMedGoogle Scholar
  64. 64.
    Wuthier RE: Involvement of cellular metabolism of calcium and phosphate in calciffication of avian growth plate cartilage. J Nutr 123: 301–309, 1993PubMedGoogle Scholar
  65. 65.
    Genge BR, Cao X, Wu LN, Buzzi WR, Showman RW, Arsenault AL, Ishikawa Y, Wuthier RE: Establishment of the primary structure of the major lipid-dependent Ca2+ binding proteins of chicken growth plate cartilage matrix vesicles: identity with anchorin CII (annexin V) and annexin II. J Bone Miner Res 7: 807–819, 1992PubMedGoogle Scholar
  66. 66.
    Kirsch T, Pfaffle M: Selective binding of anchorin CII (annexin V) to type II and X collagen and to chondrocalcin (C-propeptide of type II collagen). Implications for anchoring function between matrix vesicles and matrix proteins. FEBS Lett 310: 143–147, 1992PubMedGoogle Scholar
  67. 67.
    Wu LN, Genge BR, Lloyd GC, Wuthier RE: Collagen-binding protein in collagenase-released matrix vesicles from cartilage. Interaction between matrix vesicle proteins and different types of collagen. J Biol Chem 266: 1195–1203, 1991PubMedGoogle Scholar
  68. 68.
    Pfaffle M, Borchert M, Deutzmann R, von-der-Mark K, Fernandez MP, Selmin O, Yamada Y, Martin G, Ruggiero F, Garrone R: Anchorin CII, a collagen-binding chondrocyte surface protein of the calpactin family. Prog Clin Biol Res 349: 147–157, 1990PubMedGoogle Scholar
  69. 69.
    Wirl G, Schwartz-Albiez R: Collagen-binding proteins of mammary epithelial cells are related to Ca2(+)-and phospholipid-binding annexins. J Cell Physiol 144: 511–522, 1990PubMedGoogle Scholar
  70. 70.
    Yeatman TJ, Updyke TV, Kaetzel MA, Dedman JR, Nicolson GL: Expression of annexins on the surfaces of non-metastatic and metastatic human and rodent tumor cells. Clin Exp Metastasis 11: 37–44, 1993PubMedGoogle Scholar
  71. 71.
    Tressler RJ, Updyke TV, Yeatman T, Nicolson GL: Extracellular annexin II is associated with divalent cation-dependent tumor cell-endothelial cell adhesion of metastatic RAW 117 large-cell lymphoma cells. J Cell Biochem 53: 265–276, 1993PubMedGoogle Scholar
  72. 72.
    Tressler RJ, Nicolson GL: Butanol-extractable and detergent-solubilized cell surface components from murine large cell lymphoma cells associated with adhesion to organ microvessel endothelial cells. J Cell Biochem 48: 162–171, 1992PubMedGoogle Scholar
  73. 73.
    Jindal HK, Chaney WG, Anderson CW, Davis RG, Vishwanatha JK: The protein-tyrosine kinase substrate, calpactin I heavy chain (p36), is part of the primer recognition protein complex that interacts with DNA polymerase α. J Biol Chem 266: 5169–5176, 1991PubMedGoogle Scholar
  74. 74.
    Gerke V, Weber K: Identity of p36K phosphorylated upon Rous sarcoma virus transformation with a protein purified from brush borders; calcium-dependent binding to non-erythroid spectrin and F-actin. EMBO J 3: 227–233, 1984PubMedGoogle Scholar
  75. 75.
    Erikson E, Tomasiewicz HG, Erikson RL: Biochemical characterization of a 34-kilodalton normal cellular substrate of pp60v-src and an associated 6-kilodalton protein. Mol Cell Biol 4: 77–85, 1984PubMedGoogle Scholar
  76. 76.
    Glenney J: 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. Proc Natl Acad Sci U S A 83: 4258–4262, 1986PubMedGoogle Scholar
  77. 77.
    Vishwanatha JK, Kumble S: Involvement of annexin II in DNA replication: Evidence from cell-free extracts ofXenopus eggs. J Cell Sci 105: 533–540, 1993PubMedGoogle Scholar
  78. 78.
    Kumble KD, Iversen PL, Vishwanatha JK: The role of primer recognition proteins in DNA replication: inhibition of cellular proliferation by antisense oligodeoxyribonucleotides. J Cell Sci 101: 35–41, 1992PubMedGoogle Scholar
  79. 79.
    Thiel C, Osborn M, Gerke V: The tight association of the tyrosine kinase substrate annexin II with the submembranous cytoskeleton depends on intact p 11-and Ca(2+)-binding sites. J Cell Sci 103: 733–742, 1992PubMedGoogle Scholar
  80. 80.
    Chiang Y, Schneiderman MH, Vishwanatha JK: Annexin II expression is regulated during mammalian cell cycle. Cancer Res 53: 6017–6021, 1993PubMedGoogle Scholar
  81. 81.
    Roth D, Morgan A, Burgoyne RD: Identification of a key domain in annexin and 14-3-3 proteins that stimulate calcium-dependent exocytosis in permeabilized adrenal chromaffin cells. FEBS Lett 320: 207–210, 1993PubMedGoogle Scholar
  82. 82.
    Burgoyne RD: Calpactin in exocytosis [news]. Nature 331: 20, 1988PubMedGoogle Scholar
  83. 83.
    Gruenberg J, Emans N: Annexins in membrane traffic. Trends Cell Biol 3: 224–227, 1993PubMedGoogle Scholar
  84. 84.
    Robitzki A, Schroder HC, Ugarkovic D, Gramzow M, Fritsche U, Batel R, Muller WE: cDNA structure and expression of calpactin, a peptide involved in Ca2(+)-dependent cell aggregation in sponges. Biochem J 271: 415–420, 1990PubMedGoogle Scholar
  85. 85.
    Nakata T, Sobue K, Hirokawa N: Conformational change and localization of calpactin I complex involved in exocytosis as revealed by quick-freeze, deep-etch electron microscopy and immunocytochemistry. J Cell Biol 110: 13–25, 1990PubMedGoogle Scholar
  86. 86.
    Senda T, Okabe T, Matsuda M, Fujita H: Quick-freeze, deep-etch visualization of exocytosis in anterior pituitary secretory cells: localization and possible roles of actin and annexin II. Cell Tissue Res 277: 51–60, 1964Google Scholar
  87. 87.
    Hubaishy I, Jones PG, Bjorge J, Bellagamba C, Fitzpatrick S, Fujita DJ, Waisman DM: Modulation of Annexin II Tetramer By Tyrosine Phosphorylation. J Biol Chem submitted, 1995Google Scholar
  88. 88.
    Ikebuchi NW, Waisman DM: Calcium-dependent regulation of actin filament bundling by lipocortin-85. J Biol Chem 265: 3392–3400, 1990PubMedGoogle Scholar
  89. 89.
    Glenney JR, Jr., Glenney P: Comparison of Ca++-regulated events in the intestinal brush border. J Cell Biol 100: 754–763, 1985PubMedGoogle Scholar
  90. 90.
    Regnouf F, Rendon A, Pradel LA: Biochemical characterization of annexins I and II isolated from pig nervous tissue. J Neurochem 56: 1985–1996, 1991PubMedGoogle Scholar
  91. 91.
    Jones PG, Moore GJ, Waisman DM: A nonapeptide to the putative F-actin binding site of annexin-II tetramer inhibits its calcium-dependent activation of actin filament bundling. J Biol Chem 267: 13993–13997, 1992PubMedGoogle Scholar
  92. 92.
    Glenney JR, Jr. Phosphorylation of p36in vitro with pp60src. Regulation by Ca2+ and phospholipid. FEBS Lett 192: 79–82, 1985PubMedGoogle Scholar
  93. 93.
    Glenney J: Phospholipid-dependent Ca2+ binding by the 36-kDa tyrosine kinase substrate (calpactin) and its 33-kDa core. J Biol Chem 261: 7247–7252, 1986PubMedGoogle Scholar
  94. 94.
    Johnstone SA, Hubaishy I, Waisman DM: Phosphorylation of annexin II tetramer by protein kinase C inhibits aggregation of lipid vesicles by the protein. J Biol Chem 267: 25976–25981, 1992PubMedGoogle Scholar
  95. 95.
    Jones PG, Fitzpatrick S, Waisman DM: Salt-dependency of chromaffin granule aggregation by annexin II Tetramer. Biochemistry 33: 13751–13760, 1994PubMedGoogle Scholar
  96. 96.
    Weber K, Johnsson N, Plessmann U, Van PN, Soling HD, Ampe C, Vandekerckhove J: The amino acid sequence of protein II and its phosphorylation site for protein kinase C; the domain structure Ca2+-modulated lipid binding proteins. EMBO J 6: 1599–1604, 1987PubMedGoogle Scholar
  97. 97.
    Johnsson N, Nguyen-Van P, Soling HD, Weber K: Functionally distinct serine phosphorylation sites of p36, the cellular substrate of retroviral protein kinase; differential inhibition of reassociation with pll. EMBO J 5: 3455–3460, 1986PubMedGoogle Scholar
  98. 98.
    Glenney JR, Jr., Tack BF: Amino-terminal sequence of p36 and associated p 10: identification of the site of tyrosine phosphorylation and homology with S-100. Proc Natl Acad Sci U S A 82: 7884–7888, 1985PubMedGoogle Scholar
  99. 99.
    Gould KL, Woodgett JR, Isacke CM, Hunter T: The protein-tyrosine kinase substrate p36 is also a substrate for protein kinase Cin vitro andin vivo. Mol Cell Biol 6: 2738–2744, 1986PubMedGoogle Scholar
  100. 100.
    Schlaepfer DD, Haigler HT:In vitro protein kinase C phosphorylation sites of placental lipocortin. Biochemistry 27: 4253–4258, 1988PubMedGoogle Scholar
  101. 101.
    Glenney JR, Jr., Boudreau M, Galyean R, Hunter T, Tack B: Association of the S-100-related calpactin I light chain with the NH2-terminal tail of the 36 kDa heavy chain. J Biol Chem 261: 10485–10488, 1986PubMedGoogle Scholar
  102. 102.
    Johnsson N, Marriott G, Weber K: p36, the major cytoplasmic substrate of src tyrosine protein kinase, binds to its p11 regulatory subunit via a short amino-terminal amphiphatic helix. EMBO J 7: 2435–2442, 1988PubMedGoogle Scholar
  103. 103.
    Johnsson N, Vandekerckhove J, Van-Damme J, Weber K: Binding sites for calcium, lipid and pll on p36, the substrate of retroviral tyrosine-specific protein kinases. FEBS Lett 198: 361–364, 1986PubMedGoogle Scholar
  104. 104.
    Glenney JR, Jr., Tack B, Powell MA: Calpactins: two distinct Ca++-regulated phospholipid-and actin-binding proteins isolated from lung and placenta. J Cell Biol 104: 503–511, 1987PubMedGoogle Scholar
  105. 105.
    Drust DS, Creutz CE: Aggregation of chromaffin granules by calpactin at micromolar levels of calcium. Nature 331: 88–91, 1988PubMedGoogle Scholar
  106. 106.
    Powell MA, Glenney JR: Regulation of calpactin I phospholipid binding by calpactin I light-chain binding and phosphorylation by p60v-src. Biochem J 247: 321–328, 1987PubMedGoogle Scholar
  107. 107.
    Ikebuchi, N. W. and Waisman, D. M. Lipocortin-II Tetramer: A calcium-dependent regulator of actin filament bundling. In: V.L. Smith, J.R. Dedman (eds) Stimulus Response Coupling: The Role of Intracellular Calcium-Binding Proteins. CRC Press, Roca Raton, 1990, pp 357–381Google Scholar
  108. 108.
    Gerke V, Weber K: Calcium-dependent conformational changes in the 36-kDa subunit of intestinal protein I related to the cellular 36 kDa target of Rous sarcoma virus tyrosine kinase. J Biol Chem 260: 1688–1695, 1985PubMedGoogle Scholar
  109. 109.
    Pigault C, Follenius-Wund A, Lux B, Gerard D: A fluorescence spectroscopy study of the calpactin I complex and its subunits p11 and p36: calcium-dependent conformation changes. Biochim Biophys Acta 1037: 106–114, 1990PubMedGoogle Scholar
  110. 110.
    Blackwood RA, Ernst JD: Characterization of Ca2(+)-dependent phospholipid binding, vesicle aggregation and membrane fusion by annexins. Biochem J 266: 195–200, 1990PubMedGoogle Scholar
  111. 111.
    Evans TC, Nelsestuen GL: Calcium and membrane-binding properties of monomeric and multimeric annexin II. Biochemistry 33: 13231–13238, 1994PubMedGoogle Scholar
  112. 112.
    Osborn M, Johnsson N, Wehland J, Weber K: The submembranous location of p11 and its interaction with the p36 substrate of pp60 src kinase in situ. Exp Cell Res 175: 81–96, 1988PubMedGoogle Scholar
  113. 113.
    Zokas L, Glenney JR, Jr., The calpactin light chain is tightly linked to the cytoskeletal form of calpactin I: studies using monoclonal antibodies to calpactin subunits. J Cell Biol 105: 2111–2121, 1987PubMedGoogle Scholar
  114. 114.
    Drust DS, Creutz CE: Differential subcellular distribution of p36 (the heavy chain of calpactin I) and other annexins in the adrenal medulla. J Neurochem 56: 469–478, 1991PubMedGoogle Scholar
  115. 115.
    Gould KL, Cooper JA, Hunter T: The 46,000-dalton tyrosine protein kinase substrate is widespread, whereas the 36,000-dalton substrate is only expressed at high levels in certain rodent tissues. J Cell Biol 98: 487–497, 1984PubMedGoogle Scholar
  116. 116.
    Amini S, Kaji A: Association of pp36, a phosphorylated form of the presumed target protein for the src protein of Rous sarcoma virus, with the membrane of chicken cells transformed by Rous sarcoma virus. Proc Natl Acad Sci USA 80: 960–964, 1983PubMedGoogle Scholar
  117. 117.
    Courtneidge S, Ralston R, Alitalo K, Bishop JM: Subcellular location of an abundant substrate (p36) for tyrosine-specific protein kinases. Mol Cell Biol 3: 340–350, 1983PubMedGoogle Scholar
  118. 118.
    Greenberg ME, Edelman GM: The 34 kd pp60src substrate is located at the inner face of the plasma membrane. Cell 33: 767–779, 1983PubMedGoogle Scholar
  119. 119.
    Nigg EA, Cooper JA, Hunter T: Immunofluorescent localization of a 39,000-dalton substrate of tyrosine protein kinsases to the cytoplasmic surface of the plasma membrane. J Cell Biol 96: 1601–1609, 1983PubMedGoogle Scholar
  120. 120.
    Cooper JA, Hunter T: Discrete primary locations of a tyrosine protein kinase and of three proteins that contain phosphoryrosine in virally transformed chick fibroblasts. J Cell Biol 94: 287–296, 1982PubMedGoogle Scholar
  121. 121.
    Cheng Y-SE, Chen LB: Detection of phosphotyrosine containing 34,000 dalton protein in the framework of cells transformed with Rous sarcoma virus. Proc Natl Acad Sci U S A 78: 2388–2392, 1981PubMedGoogle Scholar
  122. 122.
    Concha NO, Head JF, Kaetzel MA, Dedman JR, Seaton BA: Rat annexin V crystal structure: Ca(2+)-induced conformational changes. Science 261: 1321–1324, 1993PubMedGoogle Scholar
  123. 123.
    Sopkova J, Renouard M, Lewit Bentley A: The crystal structure of a new high-calcium form of annexin V. J Mol Biol 234: 816–825, 1993PubMedGoogle Scholar
  124. 124.
    Weng X, Luecke H, Song IS, Kang DS, Kim SH, Huber R: Crystal structure of human annexin I at 2.5 A resolution. Protein Sci 2: 448–458, 1993PubMedGoogle Scholar
  125. 125.
    Huber R, Berendes R, Burger A, Schneider M, Karshikov A, Luecke H, Romisch J, Paques E: Crystal and molecular structure of human annexin V after refinement. Implications for structure, membrane binding and ion channel formation of the annexin family of proteins. J Mol Biol 223: 683–704, 1992PubMedGoogle Scholar
  126. 126.
    Huber R, Berendes R, Burger A, Luecke H, Karshikov A: Annexin V-crystal structure and its implications on function. Behring Inst Mitt 107–125, 1992Google Scholar
  127. 127.
    Lewit Bentley A, Morera S, Huber R, Bodo G: The effect of metal binding on the structure of annexin V and implications for membrane binding. Eur J Biochem 210: 73–77, 1992PubMedGoogle Scholar
  128. 128.
    Brisson A, Mosser G, Huber R: Structure of soluble and membrane-bound human annexin V. J Mol Biol 220: 199–203, 1991PubMedGoogle Scholar
  129. 129.
    Huber R, Romisch J, Paques EP: The crystal and molecular structure of human annexin V, an anticoagulant protein that binds to calcium and membranes. EMBO J 9: 3867–3874, 1990PubMedGoogle Scholar
  130. 130.
    Huber R, Schneider M, Mayr I, Romisch J, Paques EP: The calcium binding sites in human annexin V by crystal structure analysis at 2.0 A resolution. Implications for membrane binding and calcium channel activity. FEBS Lett 275: 15–21, 1990PubMedGoogle Scholar
  131. 131.
    Jost M, Weber K, Gerke V: Annexin II contains two types of Ca(2+)-binding sites. Biochem J 298 Pt 3: 553–559, 1994PubMedGoogle Scholar
  132. 132.
    Jost M, Thiel C, Weber K, Gerke V: Mapping of three unique Ca(2+)-binding sites in human annexin II. Eur J Biochem 207: 923–930, 1992PubMedGoogle Scholar
  133. 133.
    Greenberg ME, Brackenbury R, Edelman GM: Changes in the distribution of the 34-kdalton tyrosine kinase substrate during differentiation and maturation of chicken tissues. J Cell Biol 98: 473–486 1984PubMedGoogle Scholar
  134. 134.
    Pepinsky RB, Tizard R, Mattaliano RJ, Sinclair LK, Miller GT, Browning JL Chow EP, Burne C, Huang KS, Pratt D et al.: Five distinct calcium and phospholipid binding proteins share homology with lipocortin I. J Biol Chem 263: 10799–10811, 1988PubMedGoogle Scholar
  135. 135.
    Geisow M, Childs J, Dash B, Harris A, Panayotou G, Sudhof T, Walker JH: Cellular distribution of three mammalian Ca2+-binding proteins related to Torpedo calelectrin. EMBO J 3: 2969–2974, 1984PubMedGoogle Scholar
  136. 136.
    Eberhard DA, Brown MD, VandenBerg SR: Alterations of annexin expression in pathological neuronal and glial reactions. Immunohistochemical localization of annexins I, II (p36 and p11 subunits), IV, and VI in the human hippocampus. Am J Path 145: 640–649, 1994PubMedGoogle Scholar
  137. 137.
    Reeves SA, Chavez Kappel C, Davis R, Rosenblum M, Israel MA: Developmental regulation of annexin II (Lipocortin 2) in human brain and expression in high grade glioma. Cancer Res 52: 6871–6876, 1992PubMedGoogle Scholar
  138. 138.
    Burgoyne RD, Cambray Deakin MA, Norman KM: Developmental regulation of tyrosine kinase substrate p 36 (calpactin heavy chain) in rat cerebellum. J Mol Neurosci 1: 47–54, 1989PubMedGoogle Scholar
  139. 139.
    Carter C, Howlett AR, Martin GS, Bissell MJ: The tyrosine phosphorylation substrate p36 is developmentally regulated in embryonic avian limb and is induced in cell culture. J Cell Biol 103: 2017–2024, 1986PubMedGoogle Scholar
  140. 140.
    Ohnishi M, Tokuda M, Masaki T, Fujimura T, Tai Y, Matsui H, Itano T, Ishida T, Takahara J, Konishi R, Hatase O: Changes in annexin I and II levels during the postnatal development of rat pancreatic islets. J Cell Sci 107: 2117–2125, 1994PubMedGoogle Scholar
  141. 141.
    Masaki T, Tokuda M, Fujimura T, Ohnishi M, Tai Y, Miyamoto K, Itano T, Matsui H, Watanabe S, Sogawa K, Yamada T, Konishi R, Nishioka M, Hatase O: Involvement of annexin I and annexin II in hepatocyte proliferation: can annexins I and II be markers for proliferative hepatocytes? Hepatology 20: 425–435, 1994PubMedGoogle Scholar
  142. 142.
    Saris CJ, Kristensen T, D'Eustachio P, Hicks LJ, Noonan DJ, Hunter T, Tack BF: cDNA sequence and tissue distribution of the mRNA for bovine and murine p 11, the S100-related light chain of the protein-tyrosine kinase substrate p36 (calpactin I). J Biol Chem 262: 10663–10671, 1987PubMedGoogle Scholar
  143. 143.
    Ernst JD, Mall A, Chew G: Annexins possess functionally distinguishable Ca2+ and phospholipid binding domains. Biochem Biophys Res Commun 200: 867–876, 1994PubMedGoogle Scholar
  144. 144.
    Trave G, Quignard JF, Lionne C, Sri Widada J, Liautard JP: Interdependence of phospholipid specificity and calcium binding in annexin I as shown by site-directed mutagenesis. Biochim Biophys Acta 1205: 215–222, 1994PubMedGoogle Scholar
  145. 145.
    Meers P, Daleke D, Hong K, Papahadjopoulos D: Interactions of annexins with membrane phospholipids. Biochemistry 30: 2903–2908, 1991PubMedGoogle Scholar
  146. 146.
    Genge BR, Wu LN, Wuthier RE: Differential fractionation of matrix vesicle proteins. Further characterization of the acidic phospholipid-dependent Ca2(+)-binding proteins. J Biol Chem 265: 4703–4710 1990PubMedGoogle Scholar
  147. 147.
    Walker JH: Isolation from cholinergic synapses of a protein that binds to membranes in a Ca21-dependent manner. J Neurochem 39: 815–823, 1982PubMedGoogle Scholar
  148. 148.
    Pollard HB, Rojas E: Ca2+-activated synexin forms highly selective, voltage-gated Ca2+ channels in phosphatidylserine bilayer membranes. Proc Natl Acad Sci U S A 85: 2974–2978, 1988PubMedGoogle Scholar
  149. 149.
    Pollard HB, Burns AL, Rojas E: Synexin, a new member of the annexin gene family, is a calcium channel and membrane fusion protein. Prog Clin Biol Res 349: 159–172, 1990PubMedGoogle Scholar
  150. 150.
    Rojas E, Pollard HB, Haigler HT, Parra C, Burns AL: Calcium-activated endonexin I1 forms calcium channels across acidic phospholipid bilayer membranes. J Biol Chem 265: 21207–21215, 1990PubMedGoogle Scholar
  151. 151.
    Zaks WJ, Creutz CE: Annexin-chromaffin granule membrane interactions: a comparative study of synexin, p32 and p67. Biochim Biophys Acta 1029: 149–160, 1990PubMedGoogle Scholar
  152. 152.
    Andree HA, Willems GM, Hauptmann R, Maurer Fogy I, Stuart MC, Hermens WT, Frederik PM, Reutelingsperger CP: Aggregation of phospholipid vesicles by a chimeric protein with the N-terminus of annexin I and the core of annexin V. Biochemistry 32: 4634–4640, 1993PubMedGoogle Scholar
  153. 153.
    Sargiacomo M, Sudol M, Tang Z, Lisanti MP: Signal transducing molecules and glycosyl-phosphatidylinositol-linked proteins form a caveolin-rich insoluble complex in MDCK cells. J Cell Biol 122: 789–807, 1993PubMedGoogle Scholar
  154. 154.
    Martin F, Derancourt J, Capony JP, Watrin A, Cavadore JC: A 36 kDA monomeric protein and its complex with a 10 kDa protein both isolated from bovine aorta are calpactin-like proteins that differ in their Ca2+-dependent calmodulin-binding and actin-severing properties. Biochem J 251: 777–785, 1988PubMedGoogle Scholar
  155. 155.
    Ma AS, Bystol ME, Tranvan A:In vitro modulation of filament bundling in F-actin and keratins by annexin II and calcium.In vitro Cell Develop Biol Animal: 329–335, 1994Google Scholar
  156. 156.
    Suzuki R, Morita F, Nishi N, Tokura S: Inhibition of actomyosin subfragment 1 ATPase activity by analog peptides of the actin-binding site around the Cys(SH1) of myosin heavy chain. J Biol Chem 256: 4939–4943, 1990Google Scholar
  157. 157.
    Khanna NC, Helwig ED, Ikebuchi NW, Fitzpatrick S, Bajwa R, Waisman DW: Purification and characterization of annexin proteins from bovine lung. Biochem 29: 4852–4862, 1990Google Scholar
  158. 158.
    Kojima K, Ogawa HK, Seno N, Yamamoto K, Irimura T, Osawa T, Matsumoto I: Carbohydrate-binding proteins in bovine kidney have consensus amino acid sequences of annexin family proteins. J Biol Chem 267: 20536–20539, 1992PubMedGoogle Scholar
  159. 159.
    Khanna NC, Tokuda M, Waisman DM: Phosphorylation of lipocortinsin vitro by protein kinase C. Biochem Biophys Res Commun 141: 547–554, 1986PubMedGoogle Scholar
  160. 160.
    Radke K, Martin GS: Transformation by Rous sarcoma virus: effects of src gene expression on the synthesis and phosphorylation of cellular polypeptides. Proc Natl Acad Sci U S A 76: 5212–5216, 1979PubMedGoogle Scholar
  161. 161.
    Erikson E, Erikson RL: Identification of a cellular protein substrate phosphorylated by the avian sarcoma virus-transforming gene product. Cell 21: 829–836, 1980PubMedGoogle Scholar
  162. 162.
    Martinez R, Nakamura KD, Weber MJ: Identification of phosphotyrosine containing proteins in untransformed and Rous sarcoma transformed chicken embryo fibroblasts. Mol Cell Biochem 2: 653–665, 1982Google Scholar
  163. 163.
    Cooper JA, Hunter T: Identification and characterization of cellular targets for tyrosine protein kinases. J Biol Chem 258: 1108–1115, 1983PubMedGoogle Scholar
  164. 164.
    Greenberg ME, Edelman GM: Comparison of the 34,000-Da pp60src substrate and a 38,000-Da phosphoprotein identified by monoclonal antibodies. J Biol Chem 258: 8497–8502, 1983PubMedGoogle Scholar
  165. 165.
    Grima DT, Kandel RA, Pepinsky B, Cruz TF: Lipocortin 2 (annexin 2) is a major substrate for constitutive tyrosine kinase activity in chondrocytes. Biochemistry 33: 2921–2926, 1994PubMedGoogle Scholar
  166. 166.
    Isacke CM, Trowbridge IS, Hunter I: Modulation of p36 phosphorylation in human cells: studies using anti-p36 monoclonal antibodies. Mol Cell Biol 6: 2745–2751, 1986PubMedGoogle Scholar
  167. 167.
    Brambilla R, Zippel R, Sturani E, Morello L, Peres A, Alberghina L: Characterization of the tyrosine phosphorylation of calpactin I (annexin II) induced by platelet-derived growth factor. Biochem J 278: 447–452, 1991PubMedGoogle Scholar
  168. 168.
    Zippel R, Morello L, Brambilla R, Comoglio PM, Alberghina L, Sturani E: Inhibition of phosphotyrosine phosphatases reveals candidate substrates of the PDGF receptor kinase. Eur J Cell Biol 50: 428–434, 1989PubMedGoogle Scholar
  169. 169.
    Gutierrez LM, Ballesta JJ, Hidalgo MJ, Gandia L, Garcia AG, Reig JA: A two-dimensional electrophoresis study of phosphorylation and dephosphorylation of chromaffin cell proteins in response to a secretory stimulus. J Neurochem 51: 1023–1030, 1988PubMedGoogle Scholar
  170. 170.
    Cote A, Doucet JP, Trifaro JM: Phosphorylation and dephosphorylation of chromaffin cell proteins in response to stimulation. Neuroscience 19: 629–645, 1986PubMedGoogle Scholar
  171. 171.
    Wu YN, Wagner PD: Effects of phosphatase inhibitors and a protein phosphatase on norepinephrine secretion by permeabilized bovine chromaffin cells. Biochem Biophys Acta 1092: 384–390, 1991PubMedGoogle Scholar
  172. 172.
    Creutz CE, Zaks WJ, Hamman HC, Crane S, Martin WH, Gould KL, Oddie KM, Parsons SJ: Identification of chromaffin granule-binding proteins. Relationship of the chromobindins to calelectrin, synhibin, and the tyrosine kinase substrates p35 and p36. J Biol Chem 262: 1860–1868, 1987PubMedGoogle Scholar
  173. 173.
    Bittner MA, Holz RW: Protein kinase C and clostridial neurotoxins affect discrete and related steps in the secretory pathway. Cell Mol Neurobiol 13: 649–664, 1993PubMedGoogle Scholar
  174. 174.
    Vitale ML, Rodriguez Del Castillo A, Trifaro JM: Protein kinase C activation by phorbol esters induces chromaffin cell cortical filamentous actin disassembly and increases the initial rate of exocytosis in response to nicotinic receptor stimulation. Neuroscience 51: 463–474, 1992PubMedGoogle Scholar
  175. 175.
    Rojas E, Cena V, Stutzin A, Forberg E, Pollard HB: Characteristics of receptor-operated and membrane potential-dependent ATP secretion from adrenal medullary chromaffin cells. [Review]. Annals NY Acad Sci 603: 311–322, 1990Google Scholar
  176. 176.
    Oddie KM, Litz JS, Balserak JC, Payne DM, Creutz CE, Parsons SJ: Modulation of pp60c-src tyrosine kinase activity during secretion in stimulated bovine adrenal chromaffin cells. J Neurosci Res 24:38–48, 1989PubMedGoogle Scholar
  177. 177.
    TerBush DR, Holz RW: Activation of protein kinase C is not required for exocytosis from bovine adrenal chromaffin cells. The effects of protein kinase C(19–31), Ca/CaM kinase II(291–317), and staurosporine. J Biol Chem 265: 21179–21184, 1990PubMedGoogle Scholar
  178. 178.
    Pritchard CG, Weaver DT, Baril EF, DePamphilis ML: DNA polymerase alpha cofactors C1C2 function as primer recognition proteins. J Biol Chem 258: 9810–9819, 1983PubMedGoogle Scholar
  179. 179.
    Pritchard CG, DePamphilis ML: Preparation of DNA polymerase alpha X C1C2 by reconstituting DNA polymerase alpha with its specific stimulatory cofactors, C1C2. J Biol Chem 258: 9801–9809, 1983PubMedGoogle Scholar
  180. 180.
    Jindal HK, Vishwanatha JK: Purification and characterization of primer recognition proteins from HeLa cells. Biochemistry 29: 4767–4773, 1990PubMedGoogle Scholar
  181. 181.
    Vishwanatha JK, Coughlin SA, Wesolowski-Owen M, Baril EF: A multiprotein form of DNA polymerase alpha from HeLa cells. Resolution of its associated catalytic activities. J Biol Chem 261: 6619–6628, 1986PubMedGoogle Scholar
  182. 182.
    Jindal HK, Vishwanatha JK: Functional identity of a primer recognition protein as phosphoglycerate kinase. J Biol Chem 26: 6540–6543, 1990Google Scholar
  183. 183.
    Kumble KD, Vishwanatha JK: Immunoelectron microscopic analysis of the intracellular distribution of primer recognition proteins, annexin 2 and phosphoglycerate kinase, in normal and transformed cells. J Cell Sci 99: 751–758, 1991PubMedGoogle Scholar
  184. 184.
    Johnstone SA, Waisman DM, Rattner JB: Enolase is present at the centrosome of HeLa cells. Experimental Cell Res 202: 458–463, 1992Google Scholar
  185. 185.
    Rattner JB, Martin L, Waisman DM, Johnstone SA, Frizler MJ: Autoantibodies to the centrosome (centriole) react with determinants present in the glycolytic enzyme enolase. J Immunol 146: 2341–2344, 1991PubMedGoogle Scholar
  186. 186.
    Goldberg M, Feinberg J, Rainteau D, Lecolle S, Kaetzel MA, Dedman JR, Weinman S: Annexins I–VI in secretory ameloblasts and odontoblasts of rat incisor. J Biol Buccale 18: 289–298, 1990Google Scholar
  187. 187.
    Schafer T, Karli UO, Gratwohl EK, Schweizer FE, Burger MM: Digitonin-permeabilized cells are exocytosis competent. J Neurochem 49: 1697–1707, 1987PubMedGoogle Scholar
  188. 188.
    Holz RW: Control of exocytosis from adrenal chromaffin cells. Cell Mol Neurobiol 8: 259–268, 1988PubMedGoogle Scholar
  189. 189.
    Grant NJ, Aunis D, Bader MF: Morphology and secretory activity of digitonin-and alpha-toxin-permeabilized chromaffin cells. Neuroscience 23: 1143–1155, 1987PubMedGoogle Scholar
  190. 190.
    Morita K, Ishii S, Uda H, Oka M: Requirement of ATP for exocytotic release of catecholamines from digitonin-permeabilized adrenal chromaffin cells. J Neurochem 50: 644–648, 1988PubMedGoogle Scholar
  191. 191.
    Dunn LA, Holz RW: Catecholamine secretion from digitonin-treated adrenal medullary chromaffin cells. J Biol Chem 258: 4989–4993, 1983PubMedGoogle Scholar
  192. 192.
    Wilson SP, Kirshner N: Calcium-evoked secretion from digitonin-permeabilized adrenal medullary chromaffin cells. J Biol Chem 258: 4994–5000, 1983PubMedGoogle Scholar
  193. 193.
    Vitale ML, Rodriguez-Del-Castillo A, Trifaro JM: Loss and Ca(2+)-dependent retention of scinderin in digitonin-permeabilized chromaffin cells: correlation with Ca(2+)-evoked catecholamine release. J Neurochem 59: 1717–1728, 1992PubMedGoogle Scholar
  194. 194.
    Sarafian T, Aunis D, Bader MF: Loss of proteins from digitonin-permeabilized adrenal chromaffin cells essential for exocytosis. J Biol Chem 262: 16671–16676, 1987PubMedGoogle Scholar
  195. 195.
    Augustine GJ, Neher E: Calcium requirements for secretion in bovine chromaffin cells. J Physiol Lond 450: 247–271, 1992PubMedGoogle Scholar
  196. 196.
    Nishizaki T, Walent JH, Kowalchyk JA, Martin TF: A key role for a 145-kDa cytosolic protein in the stimulation of Ca(2+)-dependent secretion by protein kinase C. J Biol Chem 267: 23972–23981, 1992PubMedGoogle Scholar
  197. 197.
    Jones PG, Damji A, Waisman DM: Inability of annexin II tetramer to stimulate exocytosis in detergent permeabilized adrenal medulla cells. FASEB J A 1317: 1994Google Scholar
  198. 198.
    Bennett MK, Scheller RH: The molecular machinery for secretion is conserved from yeast to neurons. Proc Natl Acad Sci U S A 90: 2559–2563, 1993PubMedGoogle Scholar
  199. 199.
    Sollner T, Bennett MK, Whiteheart SW, Scheller RH, Rothman JE: A protein assembly-disassembly pathwayin vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion. Cell 75: 409–418, 1993PubMedGoogle Scholar
  200. 200.
    Sudhof TC, Petrenko AG, Whittaker VP, Jahn R: Molecular approaches to synaptic vesicle exocytosis. Prog Brain Res 98: 235–240, 1993PubMedGoogle Scholar
  201. 201.
    Elferink LA, Scheller RH: Synaptic vesicle proteins and regulated exocytosis. J Cell Sci Suppl 17: 75–79, 1993Google Scholar
  202. 202.
    Calakos N, Bennett MK, Peterson KE, Scheller RH: Protein-protein interactions contributing to the specificity of intracellular vesicular trafficking. Science 263: 1146–1149, 1994PubMedGoogle Scholar
  203. 203.
    Whiteheart SW, Griff IC, Brunner M, Clary DO, Mayer T, Buhrow SA, Rothman JE: SNAP family of NSF attachment proteins includes a brain-specific isoform [see comments]. Nature 362: 353–355, 1993PubMedGoogle Scholar
  204. 204.
    Alder J, Poo MM: Reconstitution of transmiter secretion. Curr Opin Neurobiol 3: 322–328, 1993PubMedGoogle Scholar
  205. 205.
    Walch Solimena C, Jahn R, Sudhof TC: Synaptic vesicle proteins in exocytosis: what do we know? Curr Opin Neurobiol 3: 329–336, 1993PubMedGoogle Scholar
  206. 206.
    Roth D, Burgoyne RD: SNAP-25 is present in a SNARE complex in adrenal chromaffin cells. FEBS Letters 351: 207–210, 1994PubMedGoogle Scholar
  207. 207.
    Christmas P, Callaway J, Fallon J, Jones J, Haigler HT: Selective secretion of annexin 1, a protein without a signal sequence, by the human prostate gland. J Biol Chem 266: 2499–2507, 1991PubMedGoogle Scholar
  208. 208.
    Cesarman GM, Guevara CA, Hajjar KA: An endothelial cell receptor for plasminogen/tissue plasminogen activator (t-PA). II. Annexin II-mediated enhancement of t-PA-dependent plasminogen activation. J Biol Chem 269: 21198–21203, 1994PubMedGoogle Scholar
  209. 209.
    Ma AS, Bell DJ, Mittal AA, Harrison HH: Immunocytochemical detection of extracellular annexin II in cultures human skin keratinocytes and isolation of annexin II isoforms enriched in the extracellular pool. J Cell Sci 107: 1973–1984, 1994PubMedGoogle Scholar
  210. 210.
    Wirl G, Schwartz-Albiez R: Collagen-binding proteins of mammary epithelial cells are related to Ca2(+)-and phospholipid-binding annexins. J Cell Physiol 144: 511–522, 1990PubMedGoogle Scholar
  211. 211.
    Robitzki A, Schroder HC, Ugarkovic D, Pfeifer K, Uhlenbruck G, Muller WE. Demonstration of an endocrine signaling circuit for insulin in the sponge Geodia cydonim. EMBO J 8: 2905–2909, 1989PubMedGoogle Scholar
  212. 212.
    Nicolson GL: Cancer metastasis: tumor cell and host organ properties important in metastasis to specific secondary sites. Biochim Biophys Acta 948: 175–224, 1988PubMedGoogle Scholar
  213. 213.
    Nicolson GL: Tumor and host molecules important in the organ preference of metastasis. Semin Cancer Biol 2: 143–154, 1991PubMedGoogle Scholar
  214. 214.
    Zetter BR: The cellular basis of site-specific tumor metastasis. N Engl J Med 322: 605–612, 1990PubMedGoogle Scholar
  215. 215.
    Chung CY, Erickson HP: Cell surface annexin II is a high affinity receptor for the alternatively spliced segment of tenascin-C. J Cell Biol 126: 539–548, 1994PubMedGoogle Scholar

Copyright information

© Kluwer Academic Publishers 1995

Authors and Affiliations

  • David M. Waisman
    • 1
  1. 1.Department of Medical Biochemistry, Faculty of MedicineUniversity of CalgaryCalgaryCanada

Personalised recommendations