메뉴 건너뛰기




Volumn 1720, Issue 1-2, 2005, Pages 110-116

Stabilization of trypsin by association to plasma membranes: Implications for tryptic cleavage of membrane-bound Na,K-ATPase

Author keywords

Membrane; Membrane bound protein; Na,K ATPase; P type ATPase; Trypsin

Indexed keywords

ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM); ANION; BICARBONATE; CHOLESTEROL; ION; MEMBRANE LIPID; MEMBRANE PROTEIN; POTASSIUM CHLORIDE; SODIUM CHLORIDE; TRYPSIN;

EID: 32044448709     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2005.11.001     Document Type: Article
Times cited : (8)

References (32)
  • 1
    • 3242701547 scopus 로고    scopus 로고
    • Biology, structure and mechanism of P-type ATPases
    • W. Kühlbrandt Biology, structure and mechanism of P-type ATPases Nat. Rev. 5 2004 282 295
    • (2004) Nat. Rev. , vol.5 , pp. 282-295
    • Kühlbrandt, W.1
  • 3
    • 0001409028 scopus 로고
    • The influence of some cations on an adenosine triphosphatase from peripheral nerves
    • J.C. Skou The influence of some cations on an adenosine triphosphatase from peripheral nerves Biochim. Biophys. Acta 23 1957 394 401
    • (1957) Biochim. Biophys. Acta , vol.23 , pp. 394-401
    • Skou, J.C.1
  • 4
    • 0038621773 scopus 로고    scopus 로고
    • Structure and mechanism of Na,K-ATPase: Functional sites and their interactions
    • P.L. Jorgensen, K.O. Hakansson, and S.J. Karlish Structure and mechanism of Na,K-ATPase: functional sites and their interactions Annu. Rev. Physiol. 65 2003 817 849
    • (2003) Annu. Rev. Physiol. , vol.65 , pp. 817-849
    • Jorgensen, P.L.1    Hakansson, K.O.2    Karlish, S.J.3
  • 5
    • 0016786376 scopus 로고
    • Purification and characterization of (Na+, K+)-ATPase. V. Conformational changes in the enzyme. Transitions between the Na-form and the K-form studied with tryptic digestion as a tool
    • P.L. Jørgensen Purification and characterization of (Na+, K+)-ATPase. V. Conformational changes in the enzyme. Transitions between the Na-form and the K-form studied with tryptic digestion as a tool Biochim. Biophys. Acta 410 1975 399 415
    • (1975) Biochim. Biophys. Acta , vol.410 , pp. 399-415
    • Jørgensen, P.L.1
  • 6
    • 0022553624 scopus 로고
    • Tryptic and chymotryptic cleavage sites in sequence of alpha-subunit of (Na+ + K+)-ATPase from outer medulla of mammalian kidney
    • P.L. Jørgensen, and J.H. Collins Tryptic and chymotryptic cleavage sites in sequence of alpha-subunit of (Na+ + K+)-ATPase from outer medulla of mammalian kidney Biochim. Biophys. Acta 860 1986 570 576
    • (1986) Biochim. Biophys. Acta , vol.860 , pp. 570-576
    • Jørgensen, P.L.1    Collins, J.H.2
  • 7
    • 0022375157 scopus 로고
    • +)-ATPase: Effects on enzymatic properties, ligand binding and cation exchange
    • +)-ATPase: effects on enzymatic properties, ligand binding and cation exchange Biochim. Biophys. Acta 821 1985 319 333
    • (1985) Biochim. Biophys. Acta , vol.821 , pp. 319-333
    • Jørgensen, P.L.1    Petersen, J.2
  • 8
    • 0141844566 scopus 로고    scopus 로고
    • Regulation of Na,K-ATPase by PLMS, the phospholemman-like protein from shark: Molecular cloning, sequence, expression, cellular distribution, and functional effects of PLMS
    • Y.A. Mahmmoud, G. Cramb, A.B. Maunsbach, C.P. Cutler, L. Meischke, and F. Cornelius Regulation of Na,K-ATPase by PLMS, the phospholemman-like protein from shark: molecular cloning, sequence, expression, cellular distribution, and functional effects of PLMS J. Biol. Chem. 278 2003 37427 37438
    • (2003) J. Biol. Chem. , vol.278 , pp. 37427-37438
    • Mahmmoud, Y.A.1    Cramb, G.2    Maunsbach, A.B.3    Cutler, C.P.4    Meischke, L.5    Cornelius, F.6
  • 9
    • 0022977090 scopus 로고
    • Proteolytic activation of the canine cardiac sarcoplasmic reticulum calcium pump
    • M.A. Krichberger, D. Borchman, and C. Kasinathan Proteolytic activation of the canine cardiac sarcoplasmic reticulum calcium pump Biochemistry 25 1986 5484 5492
    • (1986) Biochemistry , vol.25 , pp. 5484-5492
    • Krichberger, M.A.1    Borchman, D.2    Kasinathan, C.3
  • 12
    • 0028200088 scopus 로고
    • Structural integrity of the membrane domains in extensively trypsinized Na,K-ATPase from shark rectal glands
    • M. Esmann, S.J. Karlish, L. Sottrup-Jensen, and D. Marsh Structural integrity of the membrane domains in extensively trypsinized Na,K-ATPase from shark rectal glands Biochemistry 33 1994 8044 8050
    • (1994) Biochemistry , vol.33 , pp. 8044-8050
    • Esmann, M.1    Karlish, S.J.2    Sottrup-Jensen, L.3    Marsh, D.4
  • 13
    • 0036213233 scopus 로고    scopus 로고
    • Protein kinase C phosphorylation of purified Na,K-ATPase: C-terminal phosphorylation sites at the alpha- and gamma-subunits close to the inner face of the plasma membrane
    • Y.A. Mahmmoud, and F. Cornelius Protein kinase C phosphorylation of purified Na,K-ATPase: C-terminal phosphorylation sites at the alpha- and gamma-subunits close to the inner face of the plasma membrane Biophys. J. 82 2002 1907 1919
    • (2002) Biophys. J. , vol.82 , pp. 1907-1919
    • Mahmmoud, Y.A.1    Cornelius, F.2
  • 14
    • 0016184723 scopus 로고
    • +)-ATPase. 3. Purification from the outer medulla of mammalian kidney after selective removal of membrane components by sodium dodecylsulphate
    • +)-ATPase. 3. Purification from the outer medulla of mammalian kidney after selective removal of membrane components by sodium dodecylsulphate Biochim. Biophys. Acta 356 1974 36 52
    • (1974) Biochim. Biophys. Acta , vol.356 , pp. 36-52
    • Jørgensen, P.L.1
  • 15
    • 0017613512 scopus 로고
    • A simplification of the protein assay method of Lowry et al. which is more generally applicable
    • G.L. Peterson A simplification of the protein assay method of Lowry et al. which is more generally applicable Anal. Biochem. 83 1977 346 356
    • (1977) Anal. Biochem. , vol.83 , pp. 346-356
    • Peterson, G.L.1
  • 16
    • 0025978278 scopus 로고
    • Functional reconstitution of the sodium pump. Kinetics of exchange reactions performed by reconstituted Na/K-ATPase
    • F. Cornelius Functional reconstitution of the sodium pump. Kinetics of exchange reactions performed by reconstituted Na/K-ATPase Biochim. Biophys. Acta 1071 1991 19 66
    • (1991) Biochim. Biophys. Acta , vol.1071 , pp. 19-66
    • Cornelius, F.1
  • 17
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 18
    • 0034680861 scopus 로고    scopus 로고
    • Identification of a phospholemman-like protein from shark rectal glands. Evidence for indirect regulation of Na,K-ATPase by protein kinase C via a novel member of the FXYD family
    • Y.A. Mahmmoud, H. Vorum, and F. Cornelius Identification of a phospholemman-like protein from shark rectal glands. Evidence for indirect regulation of Na,K-ATPase by protein kinase C via a novel member of the FXYD family J. Biol. Chem. 275 2000 35969 35977
    • (2000) J. Biol. Chem. , vol.275 , pp. 35969-35977
    • Mahmmoud, Y.A.1    Vorum, H.2    Cornelius, F.3
  • 19
    • 0022977068 scopus 로고
    • A unique trypsin-like protease associated with plasma membranes of rat liver. Purification and characterization
    • K. Tanaka, T. Nakamura, and A. Ichihara A unique trypsin-like protease associated with plasma membranes of rat liver. Purification and characterization J. Biol. Chem. 261 1986 2610 2615
    • (1986) J. Biol. Chem. , vol.261 , pp. 2610-2615
    • Tanaka, K.1    Nakamura, T.2    Ichihara, A.3
  • 20
    • 0023969680 scopus 로고
    • Membrane-bound trypsin-like enzyme functioning in degradation of dynorphin in neuroblastoma cells. Purification and characterization
    • M. Satoh, H. Yokosawa, and S.-I. Ishii Membrane-bound trypsin-like enzyme functioning in degradation of dynorphin in neuroblastoma cells. Purification and characterization J. Biochem. 103 1988 493 498
    • (1988) J. Biochem. , vol.103 , pp. 493-498
    • Satoh, M.1    Yokosawa, H.2    Ishii, S.-I.3
  • 21
    • 0024788289 scopus 로고
    • Further studies on the ionic strength-dependent proteolytic activation of protein kinase C in rat liver plasma membranes by endogenous trypsin-like protease
    • E. Hashimoto, and H. Yamamura Further studies on the ionic strength-dependent proteolytic activation of protein kinase C in rat liver plasma membranes by endogenous trypsin-like protease J. Biochem. 106 1989 1041 1048
    • (1989) J. Biochem. , vol.106 , pp. 1041-1048
    • Hashimoto, E.1    Yamamura, H.2
  • 22
    • 0030114707 scopus 로고    scopus 로고
    • Trypsin secretion in Musca domestica larval midguts: A biochemical and immunocytochemical study
    • B.P. Jordao, W.R. Terra, A.F. Ribeiro, M.J. Lehane, and C. Ferreira Trypsin secretion in Musca domestica larval midguts: a biochemical and immunocytochemical study Insect Biochem. Mol. Biol. 26 1996 337 346
    • (1996) Insect Biochem. Mol. Biol. , vol.26 , pp. 337-346
    • Jordao, B.P.1    Terra, W.R.2    Ribeiro, A.F.3    Lehane, M.J.4    Ferreira, C.5
  • 24
    • 0029977459 scopus 로고    scopus 로고
    • Solubilization of a complex of tryptic fragments of Na,K-ATPase containing occluded Rb ions and bound ouabain
    • E. Or, E.D. Goldshleger, D.M. Tal, and S.J. Karlish Solubilization of a complex of tryptic fragments of Na,K-ATPase containing occluded Rb ions and bound ouabain Biochemistry 35 1996 6853 6864
    • (1996) Biochemistry , vol.35 , pp. 6853-6864
    • Or, E.1    Goldshleger, E.D.2    Tal, D.M.3    Karlish, S.J.4
  • 25
    • 0028264177 scopus 로고
    • Evidence that the cation occlusion domain of Na,K-ATPase consists of a complex of membrane-spanning segments. Analysis of limit membrane-embedded tryptic fragments
    • A. Shainskaya, and S.J.D. Karlish Evidence that the cation occlusion domain of Na,K-ATPase consists of a complex of membrane-spanning segments. Analysis of limit membrane-embedded tryptic fragments J. Biol. Chem. 269 1994 10780 10789
    • (1994) J. Biol. Chem. , vol.269 , pp. 10780-10789
    • Shainskaya, A.1    Karlish, S.J.D.2
  • 26
    • 0027981252 scopus 로고
    • Molecular events in close proximity to the membrane associated with the binding of ligands to the Na,K-ATPase
    • S. Lutsenko, and J.H. Kaplan Molecular events in close proximity to the membrane associated with the binding of ligands to the Na,K-ATPase J. Biol. Chem. 269 1994 4555 4564
    • (1994) J. Biol. Chem. , vol.269 , pp. 4555-4564
    • Lutsenko, S.1    Kaplan, J.H.2
  • 27
    • 0032571311 scopus 로고    scopus 로고
    • Interaction between fragments of trypsinized Na,K-ATPase detected by thermal inactivation of Rb+ occlusion and dissociation of the M5M6 fragment
    • A. Shainskaya, V. Nesaty, and S.J.D. Karlish Interaction between fragments of trypsinized Na,K-ATPase detected by thermal inactivation of Rb+ occlusion and dissociation of the M5M6 fragment J. Biol. Chem. 273 1998 7311 7319
    • (1998) J. Biol. Chem. , vol.273 , pp. 7311-7319
    • Shainskaya, A.1    Nesaty, V.2    Karlish, S.J.D.3
  • 28
    • 0034779892 scopus 로고    scopus 로고
    • Molecular and functional studies of the gamma subunit of the sodium pump
    • A.G. Therien, H.X. Pu, S.J. Karlish, and R. Blostein Molecular and functional studies of the gamma subunit of the sodium pump J. Bioenerg. Biomembr. 33 2001 407 414
    • (2001) J. Bioenerg. Biomembr. , vol.33 , pp. 407-414
    • Therien, A.G.1    Pu, H.X.2    Karlish, S.J.3    Blostein, R.4
  • 29
    • 0031434245 scopus 로고    scopus 로고
    • Tissue-specific distribution and modulatory role of the gamma subunit of the Na,K-ATPase
    • A.G. Therien, R. Goldshleger, S.J. Karlish, and R. Blostein Tissue-specific distribution and modulatory role of the gamma subunit of the Na,K-ATPase J. Biol. Chem. 272 1997 32628 32634
    • (1997) J. Biol. Chem. , vol.272 , pp. 32628-32634
    • Therien, A.G.1    Goldshleger, R.2    Karlish, S.J.3    Blostein, R.4
  • 30
    • 0038116611 scopus 로고    scopus 로고
    • Modulation of Na,K-ATPase by phospholipids and cholesterol. II. Steady-state and pre-steady state kinetics
    • F. Cornelius, N. Turner, and H.R.Z. Christensen Modulation of Na,K-ATPase by phospholipids and cholesterol. II. Steady-state and pre-steady state kinetics Biochemistry 42 2003 8541 8549
    • (2003) Biochemistry , vol.42 , pp. 8541-8549
    • Cornelius, F.1    Turner, N.2    Christensen, H.R.Z.3
  • 31
    • 0034609542 scopus 로고    scopus 로고
    • Modulation of pig kidney Na,K-ATPase activity by cholesterol: Role of hydration
    • C.P. Sotomayor, L.F. Aguilar, F.J. Cuevas, M.K. Helms, and D.M. Jameson Modulation of pig kidney Na,K-ATPase activity by cholesterol: role of hydration Biochemistry 39 2000 10928 10935
    • (2000) Biochemistry , vol.39 , pp. 10928-10935
    • Sotomayor, C.P.1    Aguilar, L.F.2    Cuevas, F.J.3    Helms, M.K.4    Jameson, D.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.