메뉴 건너뛰기




Volumn 98, Issue 3, 2001, Pages 681-687

Interaction of calmodulin with the cytoplasmic domain of the platelet membrane glycoprotein Ib-IX-V complex

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBODIES,ANTISERA AND IMMUNOGLOBULINS; CALCIUM CHANNEL; CALCIUM ION; CALMODULIN; DODECYL SULFATE SODIUM; GLYCOPROTEIN IB; GLYCOPROTEIN IB IX V COMPLEX; L SELECTIN; MEMBRANE PROTEIN; POLYACRYLAMIDE GEL; UNCLASSIFIED DRUG; VON WILLEBRAND FACTOR;

EID: 0035437184     PISSN: 00064971     EISSN: None     Source Type: Journal    
DOI: 10.1182/blood.V98.3.681     Document Type: Article
Times cited : (100)

References (43)
  • 2
    • 0032483550 scopus 로고    scopus 로고
    • Synergy of multiple substrate-receptor interactions in platelet thrombus formation under flow
    • Savage B, Almus-Jacobs F, Ruggeri ZM. Synergy of multiple substrate-receptor interactions in platelet thrombus formation under flow. Cell. 1998;94:657-666.
    • (1998) Cell , vol.94 , pp. 657-666
    • Savage, B.1    Almus-Jacobs, F.2    Ruggeri, Z.M.3
  • 4
    • 17444444169 scopus 로고    scopus 로고
    • A revised model of platelet aggregation
    • Kulkarni S, Dopheide SM, Yap CL, et al. A revised model of platelet aggregation. J Clin Invest. 2000;105;783-791.
    • (2000) J Clin Invest , vol.105 , pp. 783-791
    • Kulkarni, S.1    Dopheide, S.M.2    Yap, C.L.3
  • 5
    • 0033615963 scopus 로고    scopus 로고
    • Analysis of the roles of 14-3-3 in the platelet glycoprotein Ib-IX-mediated activation of integrin αIIbβ3 using a reconstituted mammalian cell expression model
    • Gu M, Xi X, Englund GD, Berndt MC, Du X. Analysis of the roles of 14-3-3 in the platelet glycoprotein Ib-IX-mediated activation of integrin αIIbβ3 using a reconstituted mammalian cell expression model. J Cell Biol. 1999;147:1085-1096.
    • (1999) J Cell Biol , vol.147 , pp. 1085-1096
    • Gu, M.1    Xi, X.2    Englund, G.D.3    Berndt, M.C.4    Du, X.5
  • 6
    • 0034595818 scopus 로고    scopus 로고
    • Signaling across the platelet adhesion receptor glycoprotein Ib-IX induces αIIbβ3 activation both in platelets and a transfected Chinese hamster ovary cell system
    • Zaffran Y, Meyer SC, Negrescu E, Reddy KB, Fox JEB. Signaling across the platelet adhesion receptor glycoprotein Ib-IX induces αIIbβ3 activation both in platelets and a transfected Chinese hamster ovary cell system. J Biol Chem. 2000;275:16779-16787.
    • (2000) J Biol Chem , vol.275 , pp. 16779-16787
    • Zaffran, Y.1    Meyer, S.C.2    Negrescu, E.3    Reddy, K.B.4    Fox, J.E.B.5
  • 7
    • 0034731480 scopus 로고    scopus 로고
    • Synergistic adhesive interactions and signaling mechanisms operating between platelet glycoprotein Ib/IX and integrin αIIbβ3 studies in human platelets and transfected Chinese hamster ovary cells
    • Yap CL, Hughan SC, Cranmer SL, et al. Synergistic adhesive interactions and signaling mechanisms operating between platelet glycoprotein Ib/IX and integrin αIIbβ3 studies in human platelets and transfected Chinese hamster ovary cells. J Biol Chem. 2000;275:41377-41388.
    • (2000) J Biol Chem , vol.275 , pp. 41377-41388
    • Yap, C.L.1    Hughan, S.C.2    Cranmer, S.L.3
  • 8
    • 0022376248 scopus 로고
    • Purification and preliminary characterization of the glycoprotein Ib complex in the human platelet membrane
    • Berndt MC, Gregory C, Kabral A, Zola H, Fournier D, Castaldi PA. Purification and preliminary characterization of the glycoprotein Ib complex in the human platelet membrane. Eur J Biochem. 1985;151:637-649.
    • (1985) Eur J Biochem , vol.151 , pp. 637-649
    • Berndt, M.C.1    Gregory, C.2    Kabral, A.3    Zola, H.4    Fournier, D.5    Castaldi, P.A.6
  • 10
    • 12944317287 scopus 로고    scopus 로고
    • Requirement of leucine-rich repeats of GP Ibα for shear-dependent and static binding of von Willebrand factor to the platelet membrane GP Ib-IX-V complex
    • Shen Y, Romo GM, Dong J-F, et al. Requirement of leucine-rich repeats of GP Ibα for shear-dependent and static binding of von Willebrand factor to the platelet membrane GP Ib-IX-V complex. Blood. 2000;95:903-910.
    • (2000) Blood , vol.95 , pp. 903-910
    • Shen, Y.1    Romo, G.M.2    Dong, J.-F.3
  • 11
    • 0028335858 scopus 로고
    • Association of a phospholipase A2 (14-3-3 protein) with the platelet glycoprotein Ib-IX complex
    • Du X, Harris SJ, Tetaz TJ, Ginsberg MH, Berndt MC. Association of a phospholipase A2 (14-3-3 protein) with the platelet glycoprotein Ib-IX complex. J Biol Chem. 1994;269:18287-18290.
    • (1994) J Biol Chem , vol.269 , pp. 18287-18290
    • Du, X.1    Harris, S.J.2    Tetaz, T.J.3    Ginsberg, M.H.4    Berndt, M.C.5
  • 12
    • 0029922841 scopus 로고    scopus 로고
    • Identification of a binding sequence for the 14-3-3 protein within the cytoplasmic domain of the adhesion receptor, platelet glycoprotein Ibα
    • Du X, Fox JE, Pei S. Identification of a binding sequence for the 14-3-3 protein within the cytoplasmic domain of the adhesion receptor, platelet glycoprotein Ibα. J Biol Chem. 1996;269:7362-7367.
    • (1996) J Biol Chem , vol.269 , pp. 7362-7367
    • Du, X.1    Fox, J.E.2    Pei, S.3
  • 13
    • 0032512413 scopus 로고    scopus 로고
    • Binding of purified 14-3-3 ζ signaling protein to discrete amino acid sequences within the cytoplasmic domain of the platelet membrane glycoprotein Ib-IX-V complex
    • Andrews RK, Harris SJ, McNally T, Berndt MC. Binding of purified 14-3-3 ζ signaling protein to discrete amino acid sequences within the cytoplasmic domain of the platelet membrane glycoprotein Ib-IX-V complex. Biochemistry. 1998;37:638-647.
    • (1998) Biochemistry , vol.37 , pp. 638-647
    • Andrews, R.K.1    Harris, S.J.2    McNally, T.3    Berndt, M.C.4
  • 14
    • 0032519507 scopus 로고    scopus 로고
    • Human signaling protein 14-3-3ζ interacts with platelet glycoprotein Ib subunits Ibα and Ibα
    • Calverly DC, Kavanagh TJ, Roth GJ. Human signaling protein 14-3-3ζ interacts with platelet glycoprotein Ib subunits Ibα and Ibα. Blood. 1998;91:1295-1303.
    • (1998) Blood , vol.91 , pp. 1295-1303
    • Calverly, D.C.1    Kavanagh, T.J.2    Roth, G.J.3
  • 15
    • 0034649783 scopus 로고    scopus 로고
    • Cytoplasmic domains of GPIbα and GPIbβ regulate 14-3-3ζ binding to GPIb/IX/V
    • Feng S, Christodoulides N, Resendiz JC, Berndt MC, Kroll MH. Cytoplasmic domains of GPIbα and GPIbβ regulate 14-3-3ζ binding to GPIb/IX/V. Blood. 2000;95:551-557.
    • (2000) Blood , vol.95 , pp. 551-557
    • Feng, S.1    Christodoulides, N.2    Resendiz, J.C.3    Berndt, M.C.4    Kroll, M.H.5
  • 16
    • 0034661839 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase forms a complex with platelet membrane glycoprotein Ib-IX-V complex and 14-3-3ζ
    • Munday AD, Berndt MC, Mitchell CA. Phosphoinositide 3-kinase forms a complex with platelet membrane glycoprotein Ib-IX-V complex and 14-3-3ζ. Blood. 2000;96:577-584.
    • (2000) Blood , vol.96 , pp. 577-584
    • Munday, A.D.1    Berndt, M.C.2    Mitchell, C.A.3
  • 17
    • 0024121629 scopus 로고
    • The α and β chains of human platelet glycoprotein Ib are both transmembrane proteins containing a leucine-rich amino acid sequence
    • López JA, Chung DW, Fujikawa K, Hagen FS, Davie EW, Roth GJ. The α and β chains of human platelet glycoprotein Ib are both transmembrane proteins containing a leucine-rich amino acid sequence. Proc Natl Acad Sci U S A. 1988;85:2135-2139.
    • (1988) Proc Natl Acad Sci U S A , vol.85 , pp. 2135-2139
    • López, J.A.1    Chung, D.W.2    Fujikawa, K.3    Hagen, F.S.4    Davie, E.W.5    Roth, G.J.6
  • 18
    • 0027385345 scopus 로고
    • Cloning and characterization of the gene encoding the human platelet glycoprotein V: A member of the leucine-rich glycoprotein family cleaved during thrombin-induced platelet activation
    • Lanza F, Morales M, de La Salle C, et al. Cloning and characterization of the gene encoding the human platelet glycoprotein V: a member of the leucine-rich glycoprotein family cleaved during thrombin-induced platelet activation. J Biol Chem. 1993;268:20801-20807.
    • (1993) J Biol Chem , vol.268 , pp. 20801-20807
    • Lanza, F.1    Morales, M.2    De La Salle, C.3
  • 19
    • 0033616619 scopus 로고    scopus 로고
    • The inositol polyphosphate 4-phosphatase forms a complex with phosphatidylinositol 3-kinase in human platelet cytosol
    • Munday AD, Norris FA, Caldwell KK, Brown S, Majerus PW, Mitchell CA. The inositol polyphosphate 4-phosphatase forms a complex with phosphatidylinositol 3-kinase in human platelet cytosol. Proc Natl Acad Sci U S A. 1999;96:3640-3645.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 3640-3645
    • Munday, A.D.1    Norris, F.A.2    Caldwell, K.K.3    Brown, S.4    Majerus, P.W.5    Mitchell, C.A.6
  • 20
    • 0027985446 scopus 로고
    • Adhesion receptor activation of phosphatidylinositol 3-kinase von Willebrand factor stimulates the cytoskeletal association and activation of phosphatidylinositol 3-kinase and pp60c-src in human platelets
    • Jackson SP, Schoenwaelder SM, Yuan Y, Rabinowitz I, Salem HH, Mitchell CA. Adhesion receptor activation of phosphatidylinositol 3-kinase von Willebrand factor stimulates the cytoskeletal association and activation of phosphatidylinositol 3-kinase and pp60c-src in human platelets. J Biol Chem. 1994;269:27093-27099.
    • (1994) J Biol Chem , vol.269 , pp. 27093-27099
    • Jackson, S.P.1    Schoenwaelder, S.M.2    Yuan, Y.3    Rabinowitz, I.4    Salem, H.H.5    Mitchell, C.A.6
  • 21
    • 0345465665 scopus 로고    scopus 로고
    • Calmodulin supports both inactivation and facilitation of L-type ion channels
    • Zühlke RD, Pitt GS, Deisseroth K, Tsien RW, Reuter H. Calmodulin supports both inactivation and facilitation of L-type ion channels. Nature. 1999;399:159-162.
    • (1999) Nature , vol.399 , pp. 159-162
    • Zühlke, R.D.1    Pitt, G.S.2    Deisseroth, K.3    Tsien, R.W.4    Reuter, H.5
  • 22
    • 0033551361 scopus 로고    scopus 로고
    • 2+/calmodulin binds to modulates P/Q-type calcium channels
    • 2+/calmodulin binds to modulates P/Q-type calcium channels. Nature. 1999;399:155-159.
    • (1999) Nature , vol.399 , pp. 155-159
    • Lee, A.1    Wong, S.T.2    Gallagher, D.3
  • 23
    • 0032587550 scopus 로고    scopus 로고
    • 2+/calmodulin-binding domain within the carboxyl-terminus of the angiotensin II (AT1A) receptor
    • 2+/calmodulin-binding domain within the carboxyl-terminus of the angiotensin II (AT1A) receptor. FEBS Lett. 1999;45:367-371.
    • (1999) FEBS Lett , vol.45 , pp. 367-371
    • Thomas, W.G.1    Pipolo, L.2    Qian, H.3
  • 24
    • 0029963871 scopus 로고    scopus 로고
    • Mocarhagin, a novel cobra venom metalloproteinase, cleaves the platelet von Willebrand factor receptor glycoprotein Ibα binding site for von Willebrand factor and α-thrombin
    • Ward CM, Andrews RK, Smith AI, Berndt MC. Mocarhagin, a novel cobra venom metalloproteinase, cleaves the platelet von Willebrand factor receptor glycoprotein Ibα binding site for von Willebrand factor and α-thrombin. Biochemistry. 1996;35:4929-4938.
    • (1996) Biochemistry , vol.35 , pp. 4929-4938
    • Ward, C.M.1    Andrews, R.K.2    Smith, A.I.3    Berndt, M.C.4
  • 25
    • 0024336047 scopus 로고
    • cAMP-dependent phosphorylation of glycoprotein Ib inhibits collagen-induced polymerization of actin in platelets
    • Fox JEB, Berndt MC. cAMP-dependent phosphorylation of glycoprotein Ib inhibits collagen-induced polymerization of actin in platelets. J Biol Chem. 1989;264:9520-9526.
    • (1989) J Biol Chem , vol.264 , pp. 9520-9526
    • Fox, J.E.B.1    Berndt, M.C.2
  • 26
    • 0023226103 scopus 로고
    • Fluorescence properties of calmodulin-binding peptides reflect α-helical periodicity
    • O'Neil KT, Wolfe HR Jr, Erickson-Viitanen S, De-Grado WF. Fluorescence properties of calmodulin-binding peptides reflect α-helical periodicity. Science. 1987;236:1454-1456.
    • (1987) Science , vol.236 , pp. 1454-1456
    • O'Neil, K.T.1    Wolfe H.R., Jr.2    Erickson-Viitanen, S.3    De-Grado, W.F.4
  • 27
    • 0032549712 scopus 로고    scopus 로고
    • Calmodulin regulates L-selectin adhesion molecule expression and function through a protease-dependent mechanism
    • Kahn J, Walcheck B, Migaki GI, Jutila MA, Kishimoto TK. Calmodulin regulates L-selectin adhesion molecule expression and function through a protease-dependent mechanism. Cell. 1998;92:809-818.
    • (1998) Cell , vol.92 , pp. 809-818
    • Kahn, J.1    Walcheck, B.2    Migaki, G.I.3    Jutila, M.A.4    Kishimoto, T.K.5
  • 28
    • 0033527687 scopus 로고    scopus 로고
    • Calmodulin dependence of presynaptic metabotropic glutamate receptor signaling
    • O'Connor V, El Far O, Bofill-Cardona E, et al. Calmodulin dependence of presynaptic metabotropic glutamate receptor signaling. Science. 1999;286:1180-1183.
    • (1999) Science , vol.286 , pp. 1180-1183
    • O'Connor, V.1    El Far, O.2    Bofill-Cardona, E.3
  • 29
    • 0023811919 scopus 로고
    • Multiple divergent mRNAs code for a single human calmodulin
    • Fischer R, Koller M, Flura M, et al. Multiple divergent mRNAs code for a single human calmodulin. J Biol Chem. 1988;263:17055-17062.
    • (1988) J Biol Chem , vol.263 , pp. 17055-17062
    • Fischer, R.1    Koller, M.2    Flura, M.3
  • 30
    • 0024278735 scopus 로고
    • Identification and characterization of the calmodulin-binding domain of neuromedulin, a neurospecific calmodulin-binding protein
    • Alexander KA, Wakim BT, Doyle GS, Walsh KA, Storm DR. Identification and characterization of the calmodulin-binding domain of neuromedulin, a neurospecific calmodulin-binding protein. J Biol Chem. 1988;263:7544-7549.
    • (1988) J Biol Chem , vol.263 , pp. 7544-7549
    • Alexander, K.A.1    Wakim, B.T.2    Doyle, G.S.3    Walsh, K.A.4    Storm, D.R.5
  • 32
    • 0025961398 scopus 로고
    • Purification and characterization of a brain-specific protein kinase C substrate, neurogranin (p17): Identification of a consensus amino acid sequence between neurogranin and neuromodulin (GAP43) that corresponds to the protein kinase C phosphorylation site and the calmodulin-binding domain
    • Baudier J, Deloulme JC, Van Dorsselaer A, Black D, Matthes HW. Purification and characterization of a brain-specific protein kinase C substrate, neurogranin (p17): identification of a consensus amino acid sequence between neurogranin and neuromodulin (GAP43) that corresponds to the protein kinase C phosphorylation site and the calmodulin-binding domain. J Biol Chem. 1991;266:229-237.
    • (1991) J Biol Chem , vol.266 , pp. 229-237
    • Baudier, J.1    Deloulme, J.C.2    Van Dorsselaer, A.3    Black, D.4    Matthes, H.W.5
  • 33
    • 0028921581 scopus 로고
    • Calmodulin-binding domains: Just two faced or multi-faceted?
    • James P, Vorherr T, Carafoli E. Calmodulin-binding domains: just two faced or multi-faceted? Trends Biochem Sci. 1995;20:38-42.
    • (1995) Trends Biochem Sci , vol.20 , pp. 38-42
    • James, P.1    Vorherr, T.2    Carafoli, E.3
  • 34
    • 0026472164 scopus 로고
    • The MARCKS brothers: A family of protein kinase C substrates
    • Aderem A. The MARCKS brothers: a family of protein kinase C substrates. Cell. 1992;71:713-716.
    • (1992) Cell , vol.71 , pp. 713-716
    • Aderem, A.1
  • 35
    • 0024424515 scopus 로고
    • Platelet glycoprotein Ib β is phosphorylated on serine 166 by cyclic AMP-dependent protein kinase
    • Wardell MR, Reynolds CC, Berndt MC, Wallace RW, Fox JEB. Platelet glycoprotein Ib β is phosphorylated on serine 166 by cyclic AMP-dependent protein kinase. J Biol Chem. 1989;264:15656-15661.
    • (1989) J Biol Chem , vol.264 , pp. 15656-15661
    • Wardell, M.R.1    Reynolds, C.C.2    Berndt, M.C.3    Wallace, R.W.4    Fox, J.E.B.5
  • 36
    • 0026687701 scopus 로고
    • Identification of a region from the cytoplasmic domain of the platelet membrane GP Ib-IX complex that binds to purified actin-binding protein
    • Andrews RK, Fox JEB. Identification of a region from the cytoplasmic domain of the platelet membrane GP Ib-IX complex that binds to purified actin-binding protein. J Biol Chem. 1992;267:18605-18611.
    • (1992) J Biol Chem , vol.267 , pp. 18605-18611
    • Andrews, R.K.1    Fox, J.E.B.2
  • 37
    • 0029950954 scopus 로고    scopus 로고
    • The cytoplasmic domain of the α-subunit of glycoprotein (GP) Ib mediates attachment of the entire G P Ib-IX complex to the cytoskeleton and regulates von Willebrand factor-induced changes in cell morphology
    • Cunningham JG, Meyer SC, Fox JEB. The cytoplasmic domain of the α-subunit of glycoprotein (GP) Ib mediates attachment of the entire G P Ib-IX complex to the cytoskeleton and regulates von Willebrand factor-induced changes in cell morphology. J Biol Chem. 1996;271:11581-11587.
    • (1996) J Biol Chem , vol.271 , pp. 11581-11587
    • Cunningham, J.G.1    Meyer, S.C.2    Fox, J.E.B.3
  • 38
    • 0024348536 scopus 로고
    • Glycoprotein Ib and glycoprotein IX in human platelets are acylated with palmitic acid through thioester linkages
    • Muszbek L, Laposata M. Glycoprotein Ib and glycoprotein IX in human platelets are acylated with palmitic acid through thioester linkages. J Biol Chem. 1989;264:9716-9719.
    • (1989) J Biol Chem , vol.264 , pp. 9716-9719
    • Muszbek, L.1    Laposata, M.2
  • 39
    • 0031009292 scopus 로고    scopus 로고
    • Modulation of actin filament behavior by GAP-43 (neuromodulin) is dependent on the phosphorylation status of serine 41, the protein kinase C site
    • He Q, Dent EW, Meiri KF. Modulation of actin filament behavior by GAP-43 (neuromodulin) is dependent on the phosphorylation status of serine 41, the protein kinase C site. J Neurosci. 1997;17:3515-3524.
    • (1997) J Neurosci , vol.17 , pp. 3515-3524
    • He, Q.1    Dent, E.W.2    Meiri, K.F.3
  • 40
    • 0032588515 scopus 로고    scopus 로고
    • 2+-calmodulin and protein kinase Cs: A hypothetical synthesis of their conflicting convergences on shared substrate domains
    • 2+-calmodulin and protein kinase Cs: a hypothetical synthesis of their conflicting convergences on shared substrate domains. Trends Neurosci. 1999;22:12-16.
    • (1999) Trends Neurosci , vol.22 , pp. 12-16
    • Chakravarthy, B.1    Morley, P.2    Whitfield, J.3
  • 41
    • 0034617183 scopus 로고    scopus 로고
    • Interaction between actin and the effector peptide of MARCKS-related protein: Identification of functional amino acid segments
    • Wohnsland F, Schmitz AAP, Steinmetz MO, Aebi U, Vergeres G. Interaction between actin and the effector peptide of MARCKS-related protein: identification of functional amino acid segments. J Biol Chem. 2000;275:20873-20879.
    • (2000) J Biol Chem , vol.275 , pp. 20873-20879
    • Wohnsland, F.1    Schmitz, A.A.P.2    Steinmetz, M.O.3    Aebi, U.4    Vergeres, G.5
  • 42
    • 0034717707 scopus 로고    scopus 로고
    • Gap43, MARCKS CAP23 modulate PI(4,5)P(2) at plasmalemmal rafts, and regulate cell cortex actin dynamics through a common mechanism
    • Laux T, Fukami K, Thelen M, Golub T, Frey D, Caroni P. GAP43, MARCKS, and CAP23 modulate PI(4,5)P(2) at plasmalemmal rafts, and regulate cell cortex actin dynamics through a common mechanism. J Cell Biol. 2000;149:1455-1471.
    • (2000) J Cell Biol , vol.149 , pp. 1455-1471
    • Laux, T.1    Fukami, K.2    Thelen, M.3    Golub, T.4    Frey, D.5    Caroni, P.6
  • 43
    • 0030917921 scopus 로고    scopus 로고
    • Expression of a constitutively active phosphatidylinositol 3-kinase induces process formation in rat PC 12 cells: Use of Cre/IoxP recombination system
    • Kobayashi M, Nagata S, Kita Y, et al. Expression of a constitutively active phosphatidylinositol 3-kinase induces process formation in rat PC 12 cells: use of Cre/IoxP recombination system. J Biol Chem. 1997;272:16089-16092.
    • (1997) J Biol Chem , vol.272 , pp. 16089-16092
    • Kobayashi, M.1    Nagata, S.2    Kita, Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.