PL EN


Preferencje help
Widoczny [Schowaj] Abstrakt
Liczba wyników
2007 | 54 | 2 |

Tytuł artykułu

Calcium- and proton-dependent relocation of annexin A6 in Jurkat T cells stimulated for interleukin-2 secretion

Warianty tytułu

Języki publikacji

EN

Abstrakty

EN
Annexin A6 (AnxA6) is a Ca2+-dependent membrane-binding protein involved in vesicular traffic. The likely participation of AnxA6 in the response of lymphocytes to Ca2+ signals has not been investigated yet. The present study focuses on intracellular relocation of AnxA6 in human Jurkat T lymphoblasts upon stimulation followed by transient increase of intracellular [Ca2+] and exocytosis of interleukin-2 (IL-2). Stimulation of the cells under different experimental conditions (by lowering pH and/or by rising extracellular [Ca2+] in the presence of ionomycin) induced time-dependent transients of intracellular [Ca2+] and concomitant changes in AnxA6 intracellular localization and in IL-2 secretion, with only minor effects on cell viability and apoptosis. In resting conditions (in the presence of EGTA or with no ionophore) AnxA6 was localized uniformly in the cytosol, whereas it translocated to vesicular structures beneath the plasma membrane within 5 min following stimulation of Jurkat T cells and rise of intracellular [Ca2+] at pH 7.4. Lowering the extracellular pH value from 7.4 to 6.0 significantly enhanced this process. AnxA6 changed its location from the cytosol to the secretory granules and early endosomes which seem to represent membranous targets for annexin. In conclusion, AnxA6 is sensitive to variations in intracellular [Ca2+] upon stimulation of Jurkat T cells, as manifested by a switch in its intracellular localization from the cytosol to vesicular structures located in close proximity to the plasma membrane, suggestive of participation of AnxA6 in calcium- and proton-dependent secretion of cytokines by lymphocytes.

Wydawca

-

Rocznik

Tom

54

Numer

2

Opis fizyczny

p.261-271,fig.,ref.

Twórcy

  • Nencki Institute of Experimental Biology, 02-093 Warsaw, Poland
autor

Bibliografia

  • Abudara V, Jiang RG, Eyzaguirre C (2001) Acidic regulation of junction channel between glomus cells in the rat carotic body. Possible role of [Ca2+]i. Brain Res 916: 50–60.
  • Andersson S, Coleclough C (1993) Regulation of CD4+ and CD8+ expression on mouse T-cells. J Immunol 151: 5123–5134.
  • Babiychuk EB, Drager A (2000) Annexins in cell membrane dynamics. Ca2+-regulated association of lipid microdomains. J Cell Biol 150: 1113–1124.
  • Bandorowicz J, Pikula S, Sobota A (1992) Annexins IV (p32) and VI (p68) interact with erythrocyte membrane in a calcium-dependent manner. Biochim Biophys Acta 1105: 201–206.
  • Batliwalla FM, Rufer N, Lansdorp PM, Gregersen PK (2000) Oligoclonal expansion in the CD8+CD28– T cells largely explain the shorter telomeres detected in this subset: analysis by flow FISH. Human Immunol 61: 951–958.
  • Casas J, Gijon MA, Vigo AG, Crespo MS, Balsinde J, Balboa MA (2006) Overexpression of cytosolic group IVA phospholipase A2 protects cells from Ca2+-dependent death. J Biol Chem 281: 6106–6116.
  • Chander A, Sen N, Naidu DG, Spitzer AR (2003) Calcium ionophore and phorbol ester increase membrane binding of annexin A7 in alveolar type II cells. Cell Calcium 33: 11–17.
  • Clemen CS, Herr C, Lie AA, Noegel AA, Schröder R (2001) Annexin VII: an astrogial protein exhibiting a Ca2+-dependent subcellular distribution. NeuroReport 12: 1139–1144.
  • Creutz CE (1992) The annexins and exocytosis. Science 258: 924–951.
  • de Diego I, Schwartz F, Siegfried H, Dauterstedt P, Heeren J, Beisiegel U, Enrich C, Grewal T (2002) Cholesterol modulates the membrane binding and intracellular distribution of annexin 6. J Biol Chem 277: 32187–32194.
  • Donnelly SR, Moss SE (1997) Annexins in the secretory pathway. Cell Mol Life Sci 53: 533–538.
  • Donnelly SR, Moss SE (1998) Functional analysis of the human annexin I and VI gene promoters. Biochem J 332: 681–687.
  • Dubois T, Soula M, Moss SE, Russo-Marie F, Rothhut B (1995) Potential interaction between annexin VI and a 56-kDa protein kinase in T cells. Biochem Biophys Res Commun 212: 270–278.
  • Edwards HC, Moss SE (1995) Functional and genetic analysis of annexin VI. Mol Cell Biochem 149/150: 293–299.
  • Esser MT, Haverstick DM, Fuller CL, Gullo CA, Braciale VL (1998) Ca2+ signaling modulates cytolytic T lymphocyte effector functions. J Exp Med 187: 1057–1067.
  • Fleet A, Ashworth R, Kubista H, Edwards H, Bolsover S, Mobbs P, Moss SE (1999) Inhibition of EGF-dependent calcium influx by annexin VI is splice form-specific. Biochem Biophys Res Commun 260: 540–546.
  • Gerke V, Moss SE (1997) Annexins and membrane dynamics. Biochim Biophys Acta 1357: 129–154.
  • Gerke V, Moss SE (2002) Annexins: from structure to function. Physiol Rev 82: 331–371.
  • Gerke V, Creutz CE, Moss SE (2005) Annexins: linking Ca2+ signalling to membrane dynamics. Nat Rev Mol Cell Biol 6: 449–461.
  • Golczak M, Kicinska A, Bandorowicz-Pikula J, Buchet R, Szewczyk A, Pikula S (2001a) Acidic pH-induced folding of annexin VI is a prerequisite for its insertion into lipid bilayers and formation of ion channels by the protein molecule. FASEB J 15: 1083–1085.
  • Golczak M, Kirilenko A, Bandorowicz-Pikula J, Pikula S (2001b) Conformational states of annexin VI in solution induced by acidic pH. FEBS Lett 496: 49–54.
  • Grewal T, Enrich C (2006) Molecular mechanisms involved in Ras inactivation: the annexin A6–p120GAP complex. BioEssays 28: 1211–1220.
  • Grewal T, Heeren J, Mewawala D, Schnitgerhans T, Wendt D, Salomon G, Enrich C, Beisiegel U, Jackle S (2000) Annexin VI stimulates endocytosis and is involved in the trafficking of low density lipoprotein to the prelysosomal compartment. J Biol Chem 275: 33806–33813.
  • Grynkiewicz G, Poenie M, Tsien RY (1985) A new generation of Ca2+ indicators with greatly improved fluorescence properties. J Biol Chem 260: 3440–3450.
  • Hawkins TE, Roes D, Monkhouse J, Moss SE (1999) Immunological development and cardiovascular function are normal in annexin VI null mutant mice. Mol Cell Biol 19: 8028–8032.
  • Hayes MJ, Rescher U, Gerke V, Moss SE (2004) Annexinactin interactions. Traffic 5: 571–576.
  • Jhun BS, Oh YT, Lee JY, Kong Y, Yoon K-S, Kim SS, Baik HH, Ha J, Kang I (2005) AICAR suppresses IL-2 expression through inhibition of GSK-3 phosphorylation and NF-AT activation in Jurkat T cells. Biochem Biophys Res Commun 332: 339–346.
  • Jones PG, Fitzpatrick S, Waismann DM (1994) Chromaffin granules release calcium on contact with annexin VI: implications for exocytosis. Biochemistry 33: 8180–8187.
  • Kaetzel MA, Pula G, Campos B, Uhrin P, Horseman N, Dedman JR (1994) Annexin VI isoforms are differentially expressed in mammalian tissues. Biochim Biophys Acta 1223: 368–374.
  • Kester HA, van der Leede BM, van der Saag PT, van der Burg B (1997) Novel progesterone target genes identified by an improved differential display technique suggest that progestin-induced growth inhibition of breast cancer cells coincides with enhancement of differentiation. J Biol Chem 272: 16637–16643.
  • Kirilenko A, Golczak M, Pikula S, Buchet R, Bandorowicz-Pikula J (2002) GTP-induced membrane binding and ion channel activity of annexin VI: is annexin VI a GTP biosensor? Biophys J 82: 2737–2745.
  • Kubista H, Sacre S, Moss SE (2000) Annexins and membrane fusion. Subcell Biochim 34: 73–131.
  • Marti F, Krause A, Post NH, Lyddane C, Dupont B, Sadelain M, King PD (2001) Negative-feedback regulation of CD28 costimulation by a novel mitogen-activated protein kinase phosphatase, MKP6. J Immunol 166: 197–206.
  • Moss SE, Morgan RO (2004) The annexins. Genome Biology 5: 219–226.
  • Nell AE (2002) T-cell activation through the antygen receptor. Part 2: signaling components, signaling pathways, and signal integration at the T-cell antygen receptor synapse. J Allergy Clin Immunol 109: 758–770.
  • Pardo J, Buferne M, Martinez-Lorenzo MJ, Naval J, Schmitt-Verhulst AM, Boyer C, Anel A (2003) Differential implication of protein kinase C isoforms in cytotoxic T lymphocyte degranulation and TCR-induced Fas ligand expression. Int Immunol 15: 1441–1450.
  • Pons M, Grewal T, Rius E, Schnitgerhans T, Jackle S, Enrich C (2001) Evidence for the involvement of annexin 6 in the trafficking between the andocytic compartment and lysosomes. Exp Cell Res 269: 13–22.
  • Rambotti MG, Spreca A, Donato R (1993) Immunocytochemical localization of annexins V and VI in human placentae of different gestational ages. Cell Mol Biol Res 39: 579–588.
  • Rescher U, Gerke V (2004) Annexins – unique membrane binding proteins with diverse functions. J Cell Sci 117: 2631–2639.
  • Rink TJ, Tsien RY, Pozzan T (1982) Cytoplasmic pH and free Mg2+ in lymphocytes. J Cell Biol 95: 189–196.
  • Russo-Marie F (1999) Annexin V and phospholipid metabolism. Clin Chem Lab Med 37: 287–291.
  • Sen N, Spitzer AR, Chander A (1997) Calcium-dependence of synexin binding may determine aggregation and fusion of lamellar bodies. Biochem J 322: 103–109.
  • Song G, Harding SE, Duchen MR, Tunwell R, O’Gara P, Hawkins TE, Moss SE (2002) Altered mechanical properties and intracellular calcium signaling in cardiomyocytes from annexin 6 null-mutant mice. FASEB J 16: 622–624.
  • Sullivan KE, Cutilli J, Piliero LM, Ghavimi-Alagha D, Starr SE, Campbell DE, Douglas SD (2000) Measurement of cytokine secretion, intracellular protein expression, and mRNA in resting and stimulated peripheral blood mononuclear cells. Clin Diag Lab Immunol 7: 920–924.
  • Walker D, Jason J, Wallance K, Slaughter J, Whatley V, Han A, Nwanyanwu OC, Kazembe PN, Dobbie H, Archibald L, Jarvis WR (2002) Spontaneous cytokine production and its effect on induced production. Clin Diag Lab Immunol 9: 1049–1056.
  • Zaks WJ, Creutz CE (1990) Annexin-chromaffin granule membrane interactions: a comparative study of synexin, p37 and p67. Biochim Biophys Acta 1020: 149–160.

Typ dokumentu

Bibliografia

Identyfikatory

Identyfikator YADDA

bwmeta1.element.agro-article-26cdabff-0095-4932-a141-3352a08dad80
JavaScript jest wyłączony w Twojej przeglądarce internetowej. Włącz go, a następnie odśwież stronę, aby móc w pełni z niej korzystać.