메뉴 건너뛰기




Volumn 5, Issue 5, 2010, Pages

Calpain 4 is not necessary for LFA-1-Mediated Function in CD4+ T Cells

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; CALPAIN; CALPAIN 1; CALPAIN 2; CALPAIN 4; CASEIN; CD28 ANTIGEN; CD3 ANTIGEN; CD4 ANTIGEN; INTERCELLULAR ADHESION MOLECULE 1; LYMPHOCYTE FUNCTION ASSOCIATED ANTIGEN 1; PROTEIN KINASE C THETA; UNCLASSIFIED DRUG; CAPNS1 PROTEIN, MOUSE;

EID: 77956295909     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0010513     Document Type: Article
Times cited : (5)

References (34)
  • 1
    • 0032480279 scopus 로고    scopus 로고
    • Threedimensional segregation of supramolecular activation clusters in T cells
    • Monks CR, Freiberg BA, Kupfer H, Sciaky N, Kupfer A (1998) Threedimensional segregation of supramolecular activation clusters in T cells. Nature 395: 82-86.
    • (1998) Nature , vol.395 , pp. 82-86
    • Monks, C.R.1    Freiberg, B.A.2    Kupfer, H.3    Sciaky, N.4    Kupfer, A.5
  • 2
    • 4644312322 scopus 로고    scopus 로고
    • LFA-1 on CD4+ T cells is required for optimal antigen-dependent activation in vivo
    • Kandula S, Abraham C (2004) LFA-1 on CD4+ T cells is required for optimal antigen-dependent activation in vivo. J Immunol 173: 4443-4451.
    • (2004) J Immunol , vol.173 , pp. 4443-4451
    • Kandula, S.1    Abraham, C.2
  • 3
    • 21844450244 scopus 로고    scopus 로고
    • Intracellular signalling controlling integrin activation in lymphocytes
    • Kinashi T (2005) Intracellular signalling controlling integrin activation in lymphocytes. Nat Rev Immunol 5: 546-559.
    • (2005) Nat Rev Immunol , vol.5 , pp. 546-559
    • Kinashi, T.1
  • 4
    • 33751578411 scopus 로고    scopus 로고
    • Talin1 regulates TCRmediated LFA-1 function
    • Simonson WT, Franco SJ, Huttenlocher A (2006) Talin1 regulates TCRmediated LFA-1 function. J Immunol 177: 7707-7714.
    • (2006) J Immunol , vol.177 , pp. 7707-7714
    • Simonson, W.T.1    Franco, S.J.2    Huttenlocher, A.3
  • 6
    • 26244434596 scopus 로고    scopus 로고
    • Regulating cell migration: Calpains make the cut
    • Franco SJ, Huttenlocher A (2005) Regulating cell migration: calpains make the cut. J Cell Sci 118: 3829-3838.
    • (2005) J Cell Sci , vol.118 , pp. 3829-3838
    • Franco, S.J.1    Huttenlocher, A.2
  • 7
    • 33745826605 scopus 로고    scopus 로고
    • Ubiquitous calpains promote both apoptosis and survival signals in response to different cell death stimuli
    • Tan Y, Wu C, De Veyra T, Greer PA (2006) Ubiquitous calpains promote both apoptosis and survival signals in response to different cell death stimuli. J Biol Chem 281: 17689-17698.
    • (2006) J Biol Chem , vol.281 , pp. 17689-17698
    • Tan, Y.1    Wu, C.2    De Veyra, T.3    Greer, P.A.4
  • 8
    • 0034116930 scopus 로고    scopus 로고
    • Disruption of the murine calpain small subunit gene, Capn4: Calpain is essential for embryonic development but not for cell growth and division
    • Arthur JS, Elce JS, Hegadorn C, Williams K, Greer PA (2000) Disruption of the murine calpain small subunit gene, Capn4: calpain is essential for embryonic development but not for cell growth and division. Mol Cell Biol 20: 4474-4481.
    • (2000) Mol Cell Biol , vol.20 , pp. 4474-4481
    • Arthur, J.S.1    Elce, J.S.2    Hegadorn, C.3    Williams, K.4    Greer, P.A.5
  • 9
    • 0035930548 scopus 로고    scopus 로고
    • Reduced cell migration and disruption of the actin cytoskeleton in calpain-deficient embryonic fibroblasts
    • Dourdin N, Bhatt AK, Dutt P, Greer PA, Arthur JS, et al. (2001) Reduced cell migration and disruption of the actin cytoskeleton in calpain-deficient embryonic fibroblasts. J Biol Chem 276: 48382-48388.
    • (2001) J Biol Chem , vol.276 , pp. 48382-48388
    • Dourdin, N.1    Bhatt, A.K.2    Dutt, P.3    Greer, P.A.4    Arthur, J.S.5
  • 11
    • 0035971155 scopus 로고    scopus 로고
    • A single amino acid in the cytoplasmic domain of the beta 2 integrin lymphocyte function-associated antigen-1 regulates avidity-dependent inside-out signaling
    • Bleijs DA, van Duijnhoven GC, van Vliet SJ, Thijssen JP, Figdor CG, et al. (2001) A single amino acid in the cytoplasmic domain of the beta 2 integrin lymphocyte function-associated antigen-1 regulates avidity-dependent inside-out signaling. J Biol Chem 276: 10338-10346.
    • (2001) J Biol Chem , vol.276 , pp. 10338-10346
    • Bleijs, D.A.1    van Duijnhoven, G.C.2    van Vliet, S.J.3    Thijssen, J.P.4    Figdor, C.G.5
  • 12
    • 33747091892 scopus 로고    scopus 로고
    • Cytoskeletal regulation couples LFA-1 conformational changes to receptor lateral mobility and clustering
    • Cairo CW, Mirchev R, Golan DE (2006) Cytoskeletal regulation couples LFA-1 conformational changes to receptor lateral mobility and clustering. Immunity 25: 297-308.
    • (2006) Immunity , vol.25 , pp. 297-308
    • Cairo, C.W.1    Mirchev, R.2    Golan, D.E.3
  • 13
    • 0034715731 scopus 로고    scopus 로고
    • Beta1 integrin-mediated T cell adhesion and cell spreading are regulated by calpain
    • Rock MT, Dix AR, Brooks WH, Roszman TL (2000) Beta1 integrin-mediated T cell adhesion and cell spreading are regulated by calpain. Exp Cell Res 261: 260-270.
    • (2000) Exp Cell Res , vol.261 , pp. 260-270
    • Rock, M.T.1    Dix, A.R.2    Brooks, W.H.3    Roszman, T.L.4
  • 14
    • 33947183752 scopus 로고    scopus 로고
    • Activation of LFA-1 by ionomycin is independent of calpain-mediated talin cleavage
    • Dreolini L, Takei F (2007) Activation of LFA-1 by ionomycin is independent of calpain-mediated talin cleavage. Biochem Biophys Res Commun 356: 207-212.
    • (2007) Biochem Biophys Res Commun , vol.356 , pp. 207-212
    • Dreolini, L.1    Takei, F.2
  • 15
    • 33745686005 scopus 로고    scopus 로고
    • Conditional disruption of ubiquitous calpains in the mouse
    • Tan Y, Dourdin N, Wu C, De Veyra T, Elce JS, et al. (2006) Conditional disruption of ubiquitous calpains in the mouse. Genesis 44: 297-303.
    • (2006) Genesis , vol.44 , pp. 297-303
    • Tan, Y.1    Dourdin, N.2    Wu, C.3    De Veyra, T.4    Elce, J.S.5
  • 17
    • 68249135245 scopus 로고    scopus 로고
    • Calpain inhibition induces activation of the distinct signalling pathways and cell migration in human monocytes
    • Noma H, Kato T, Fujita H, Kitagawa M, Yamano T, et al. (2009) Calpain inhibition induces activation of the distinct signalling pathways and cell migration in human monocytes. Immunology 128: e487-496.
    • (2009) Immunology , vol.128
    • Noma, H.1    Kato, T.2    Fujita, H.3    Kitagawa, M.4    Yamano, T.5
  • 19
    • 0035889958 scopus 로고    scopus 로고
    • Superantigen-induced T cell:B cell conjugation is mediated by LFA-1 and requires signaling through Lck, but not ZAP-70
    • Morgan MM, Labno CM, Van Seventer GA, Denny MF, Straus DB, et al. (2001) Superantigen-induced T cell:B cell conjugation is mediated by LFA-1 and requires signaling through Lck, but not ZAP-70. J Immunol 167: 5708-5718.
    • (2001) J Immunol , vol.167 , pp. 5708-5718
    • Morgan, M.M.1    Labno, C.M.2    Van Seventer, G.A.3    Denny, M.F.4    Straus, D.B.5
  • 21
    • 0031024011 scopus 로고    scopus 로고
    • A cysteine protease inhibitor prevents activation-induced T-cell apoptosis and death of peripheral blood cells from human immunodeficiency virus-infected individuals by inhibiting upregulation of Fas ligand
    • Yang Y, Liu ZH, Ware CF, Ashwell JD (1997) A cysteine protease inhibitor prevents activation-induced T-cell apoptosis and death of peripheral blood cells from human immunodeficiency virus-infected individuals by inhibiting upregulation of Fas ligand. Blood 89: 550-557.
    • (1997) Blood , vol.89 , pp. 550-557
    • Yang, Y.1    Liu, Z.H.2    Ware, C.F.3    Ashwell, J.D.4
  • 22
    • 0027425110 scopus 로고
    • Protease inhibitors selectively block T cell receptor-triggered programmed cell death in a murine T cell hybridoma and activated peripheral T cells
    • Sarin A, Adams DH, Henkart PA (1993) Protease inhibitors selectively block T cell receptor-triggered programmed cell death in a murine T cell hybridoma and activated peripheral T cells. J Exp Med 178: 1693-1700.
    • (1993) J Exp Med , vol.178 , pp. 1693-1700
    • Sarin, A.1    Adams, D.H.2    Henkart, P.A.3
  • 23
    • 0034938978 scopus 로고    scopus 로고
    • The role of calpain in caspase activation during etoposide induced apoptosis in T cells
    • Varghese J, Radhika G, Sarin A (2001) The role of calpain in caspase activation during etoposide induced apoptosis in T cells. Eur J Immunol 31: 2035-2041.
    • (2001) Eur J Immunol , vol.31 , pp. 2035-2041
    • Varghese, J.1    Radhika, G.2    Sarin, A.3
  • 24
    • 0031569532 scopus 로고    scopus 로고
    • Calpain, an upstream regulator of thymocyte apoptosis
    • Squier MK, Cohen JJ (1997) Calpain, an upstream regulator of thymocyte apoptosis. J Immunol 158: 3690-3697.
    • (1997) J Immunol , vol.158 , pp. 3690-3697
    • Squier, M.K.1    Cohen, J.J.2
  • 25
    • 0025099366 scopus 로고
    • Inhibitory effect of di- and tripeptidyl aldehydes on calpains and cathepsins
    • Sasaki T, Kishi M, Saito M, Tanaka T, Higuchi N, et al. (1990) Inhibitory effect of di- and tripeptidyl aldehydes on calpains and cathepsins. J Enzyme Inhib 3: 195-201.
    • (1990) J Enzyme Inhib , vol.3 , pp. 195-201
    • Sasaki, T.1    Kishi, M.2    Saito, M.3    Tanaka, T.4    Higuchi, N.5
  • 26
    • 0023784467 scopus 로고
    • The design of peptidyldiazomethane inhibitors to distinguish between the cysteine proteinases calpain II, cathepsin L and cathepsin B
    • Crawford C, Mason RW, Wikstrom P, Shaw E (1988) The design of peptidyldiazomethane inhibitors to distinguish between the cysteine proteinases calpain II, cathepsin L and cathepsin B. Biochem J 253: 751-758.
    • (1988) Biochem J , vol.253 , pp. 751-758
    • Crawford, C.1    Mason, R.W.2    Wikstrom, P.3    Shaw, E.4
  • 27
    • 0029987453 scopus 로고    scopus 로고
    • An alpha-mercaptoacrylic acid derivative is a selective nonpeptide cell-permeable calpain inhibitor and is neuroprotective
    • Wang KK, Nath R, Posner A, Raser KJ, Buroker-Kilgore M, et al. (1996) An alpha-mercaptoacrylic acid derivative is a selective nonpeptide cell-permeable calpain inhibitor and is neuroprotective. Proc Natl Acad Sci USA 93: 6687-6692.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 6687-6692
    • Wang, K.K.1    Nath, R.2    Posner, A.3    Raser, K.J.4    Buroker-Kilgore, M.5
  • 28
    • 0027980319 scopus 로고
    • Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules
    • Rock KL, Gramm C, Rothstein L, Clark K, Stein R, et al. (1994) Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules. Cell 78: 761-771.
    • (1994) Cell , vol.78 , pp. 761-771
    • Rock, K.L.1    Gramm, C.2    Rothstein, L.3    Clark, K.4    Stein, R.5
  • 29
    • 0042681786 scopus 로고    scopus 로고
    • Bidirectional transmembrane signaling by cytoplasmic domain separation in integrins
    • Kim M, Carman CV, Springer TA (2003) Bidirectional transmembrane signaling by cytoplasmic domain separation in integrins. Science 301: 1720-1725.
    • (2003) Science , vol.301 , pp. 1720-1725
    • Kim, M.1    Carman, C.V.2    Springer, T.A.3
  • 30
    • 0020010505 scopus 로고
    • Fibronectin: Purification, immunochemical properties, and biological activities
    • Ruoslahti E, Hayman EG, Pierschbacher M, Engvall E (1992) Fibronectin: purification, immunochemical properties, and biological activities. Methods Enzymol 82: 803-831.
    • (1992) Methods Enzymol , vol.82 , pp. 803-831
    • Ruoslahti, E.1    Hayman, E.G.2    Pierschbacher, M.3    Engvall, E.4
  • 31
    • 0029048989 scopus 로고
    • Casein zymography: A method to study mu-calpain, m-calpain, and their inhibitory agents
    • Raser KJ, Posner A, Wang KK (1995) Casein zymography: a method to study mu-calpain, m-calpain, and their inhibitory agents. Arch Biochem Biophys 319: 211-216.
    • (1995) Arch Biochem Biophys , vol.319 , pp. 211-216
    • Raser, K.J.1    Posner, A.2    Wang, K.K.3
  • 32
    • 0014862141 scopus 로고
    • The locomotion of mouse fibroblasts in tissue culture
    • Gail MH, Boone CW (1970) The locomotion of mouse fibroblasts in tissue culture. Biophys J 10: 980-993.
    • (1970) Biophys J , vol.10 , pp. 980-993
    • Gail, M.H.1    Boone, C.W.2
  • 33
    • 54249122300 scopus 로고    scopus 로고
    • The PCH family member proline-serine-threonine phosphatase-interacting protein 1 targets to the leukocyte uropod and regulates directed cell migration
    • Cooper KM, Bennin DA, Huttenlocher A (2008) The PCH family member proline-serine-threonine phosphatase-interacting protein 1 targets to the leukocyte uropod and regulates directed cell migration. Mol Biol Cell 19: 3180-3191.
    • (2008) Mol Biol Cell , vol.19 , pp. 3180-3191
    • Cooper, K.M.1    Bennin, D.A.2    Huttenlocher, A.3
  • 34
    • 0037380628 scopus 로고    scopus 로고
    • Essential role for caspase 8 in T-cell homeostasis and T-cell-mediated immunity
    • Salmena L, Lemmers B, Hakem A, Matysiak-Zablocki E, Murakami K, et al. (2003) Essential role for caspase 8 in T-cell homeostasis and T-cell-mediated immunity. Genes Dev 17: 883-895.
    • (2003) Genes Dev , vol.17 , pp. 883-895
    • Salmena, L.1    Lemmers, B.2    Hakem, A.3    Matysiak-Zablocki, E.4    Murakami, K.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.