메뉴 건너뛰기




Volumn 31, Issue 2, 1999, Pages 363-375

Interactions at the NH2-terminal interface of cardiac troponin I modulate myofilament activation

Author keywords

Actin binding proteins; Actomyosin ATPase activity; Ca2+ sensitivity; Myofilaments; Thin filament; Tropomyosin; Troponin C; Troponin I; Troponin T

Indexed keywords

ACTIN BINDING PROTEIN; ADENOSINE TRIPHOSPHATASE (MAGNESIUM); F ACTIN; MUSCLE PROTEIN; REGULATOR PROTEIN; TROPOMYOSIN; TROPONIN C; TROPONIN I; TROPONIN T; ACTIN; ADENOSINE TRIPHOSPHATASE (CALCIUM); HYBRID PROTEIN;

EID: 0033068167     PISSN: 00222828     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmcc.1998.0870     Document Type: Article
Times cited : (22)

References (47)
  • 1
    • 0017230650 scopus 로고
    • Separation and characterization of the troponin components from bovine cardiac muscle
    • Brekke CJ, Greaser ML, 1976. Separation and characterization of the troponin components from bovine cardiac muscle. J Biol Chem 251: 866-871.
    • (1976) J Biol Chem , vol.251 , pp. 866-871
    • Brekke, C.J.1    Greaser, M.L.2
  • 2
    • 0020681165 scopus 로고
    • Inorganic phosphate assay with malachite green: An improvement and evaluation
    • Carter SG, Karl DW, 1982. Inorganic phosphate assay with malachite green: An improvement and evaluation. J Biochem Biophys Method 7: 7-13.
    • (1982) J Biochem Biophys Method , vol.7 , pp. 7-13
    • Carter, S.G.1    Karl, D.W.2
  • 3
    • 0020478670 scopus 로고
    • Proximity of sulfhydryl groups to the sites of interaction between components of the troponin complex from rabbit skeletal muscle
    • Chong PCS, Hodges RS, 1982. Proximity of sulfhydryl groups to the sites of interaction between components of the troponin complex from rabbit skeletal muscle. J Biol Chem 257: 2549-2555.
    • (1982) J Biol Chem , vol.257 , pp. 2549-2555
    • Chong, P.C.S.1    Hodges, R.S.2
  • 4
    • 0030815460 scopus 로고    scopus 로고
    • Effects of protein kinase A phosphorylation on signalling between cardiac troponin I and the N-terminal domain of cardiac troponin C
    • Chandra M, Dong W-J, Pan B-S, Cheung HC, Solaro RJ, 1997. Effects of protein kinase A phosphorylation on signalling between cardiac troponin I and the N-terminal domain of cardiac troponin C. Biochemistry 36: 13305-13310.
    • (1997) Biochemistry , vol.36 , pp. 13305-13310
    • Chandra, M.1    Dong, W.-J.2    Pan, B.-S.3    Cheung, H.C.4    Solaro, R.J.5
  • 5
    • 0016805050 scopus 로고
    • Phosphorylation of troponin I from cardiac muscle
    • Cole HA, Perry SV, 1975. Phosphorylation of troponin I from cardiac muscle. Biochem J 149: 525-533.
    • (1975) Biochem J , vol.149 , pp. 525-533
    • Cole, H.A.1    Perry, S.V.2
  • 8
    • 0027340391 scopus 로고
    • 2+ binding activity in mutated EF-hands of cardiac troponin C
    • 2+ binding activity in mutated EF-hands of cardiac troponin C. J Biol Chem 268: 24067-24073.
    • (1993) J Biol Chem , vol.268 , pp. 24067-24073
    • Dotson, D.G.1    Putkey, J.A.2
  • 9
    • 0017885455 scopus 로고
    • Effects of pH on the myofilaments and the sarcoplasmic reticulum of skinned cells from cardiac and skeletal muscles
    • Fabiato A, Fabiato F, 1978. Effects of pH on the myofilaments and the sarcoplasmic reticulum of skinned cells from cardiac and skeletal muscles. J Physiol 276: 233-255.
    • (1978) J Physiol , vol.276 , pp. 233-255
    • Fabiato, A.1    Fabiato, F.2
  • 11
    • 0029031198 scopus 로고
    • The troponin complex and regulation of muscle contraction
    • Farah CS, Reinach FC, 1995. The troponin complex and regulation of muscle contraction. FASEB J 9: 755-767.
    • (1995) FASEB J , vol.9 , pp. 755-767
    • Farah, C.S.1    Reinach, F.C.2
  • 12
    • 0019951710 scopus 로고
    • Proton-magnetic resonance studies on the interaction of rabbit skeletal-muscle troponin I with troponin C and actin
    • Grand RJA, Levine BA, Perry SV, 1982. Proton-magnetic resonance studies on the interaction of rabbit skeletal-muscle troponin I with troponin C and actin. Biochem J 203: 61-68.
    • (1982) Biochem J , vol.203 , pp. 61-68
    • Grand, R.J.A.1    Levine, B.A.2    Perry, S.V.3
  • 13
    • 0015935352 scopus 로고
    • Purification and properties of the components from troponin
    • Greaser M, Gergely J, 1973. Purification and properties of the components from troponin. J Biol Chem 248: 2125-2140.
    • (1973) J Biol Chem , vol.248 , pp. 2125-2140
    • Greaser, M.1    Gergely, J.2
  • 15
    • 0026579645 scopus 로고
    • 2+-activated tension development of single glycerinated rabbit skeletal muscle fibers
    • 2+-activated tension development of single glycerinated rabbit skeletal muscle fibers. Eur J Biochem 205: 985-993.
    • (1992) Eur J Biochem , vol.205 , pp. 985-993
    • Hatakenaka, M.1    Ohtsuki, I.2
  • 16
    • 0020479286 scopus 로고
    • Study of the structure of troponin-I by measuring the relative reactivities of lysines with acetic anhydride
    • Hitchcock-Degregori SE, 1982. Study of the structure of troponin-I by measuring the relative reactivities of lysines with acetic anhydride. J Biol Chem 257: 7372-7380.
    • (1982) J Biol Chem , vol.257 , pp. 7372-7380
    • Hitchcock-Degregori, S.E.1
  • 17
    • 0019293605 scopus 로고
    • The calcium and magnesium binding sites on cardiac troponin and their role in the regulation of myofibrillar adenosine triphosphatase
    • Holroyde MJ, Robertson SP, Johnson JD, Solaro RJ, Potter JD, 1980. The calcium and magnesium binding sites on cardiac troponin and their role in the regulation of myofibrillar adenosine triphosphatase. J Biol Chem 255: 11688-11693.
    • (1980) J Biol Chem , vol.255 , pp. 11688-11693
    • Holroyde, M.J.1    Robertson, S.P.2    Johnson, J.D.3    Solaro, R.J.4    Potter, J.D.5
  • 18
    • 0023821821 scopus 로고
    • 2+ and subunit interactions on surface accessibility of cysteine residues in cardiac troponin
    • 2+ and subunit interactions on surface accessibility of cysteine residues in cardiac troponin. Biochemistry 27: 5891-5898.
    • (1988) Biochemistry , vol.27 , pp. 5891-5898
    • Ingraham, R.H.1    Hodges, R.S.2
  • 20
    • 0028801148 scopus 로고
    • Cardiac troponin I-induced conformational changes in cardiac troponin C as monitored by NMR using site directed spin and isotope labeling
    • Kleerekoper Q, Howarth JW, Quo X, Solaro RJ, Rosevear PR, 1995. Cardiac troponin I-induced conformational changes in cardiac troponin C as monitored by NMR using site directed spin and isotope labeling. Biochemistry 34: 13343-13352.
    • (1995) Biochemistry , vol.34 , pp. 13343-13352
    • Kleerekoper, Q.1    Howarth, J.W.2    Quo, X.3    Solaro, R.J.4    Rosevear, P.R.5
  • 21
    • 0028016156 scopus 로고
    • NMR studies delineating spatial relationships within the cardiac troponin I-troponin C complex
    • Krudy G, Kleerekoper Q, Guo X, Howarth JW, Solaro RJ, Rosevear PR, 1994. NMR studies delineating spatial relationships within the cardiac troponin I-troponin C complex. J Biol Chem 269: 23731-23735.
    • (1994) J Biol Chem , vol.269 , pp. 23731-23735
    • Krudy, G.1    Kleerekoper, Q.2    Guo, X.3    Howarth, J.W.4    Solaro, R.J.5    Rosevear, P.R.6
  • 22
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage
    • Laemmli UK, 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 26
    • 78651163419 scopus 로고
    • Disc electrophoresis-I: Background and theory
    • Ornstein L, 1964. Disc electrophoresis-I: Background and theory. Ann NY Acad Sci 121: 321-325.
    • (1964) Ann NY Acad Sci , vol.121 , pp. 321-325
    • Ornstein, L.1
  • 27
    • 0008392486 scopus 로고    scopus 로고
    • Interaction of cardiotonic thiadiazinone derivatives with cardiac troponin C
    • Pan B-S., Johnson RG Jr, 1996. Interaction of cardiotonic thiadiazinone derivatives with cardiac troponin C. J Biol Chem 271: 817-823.
    • (1996) J Biol Chem , vol.271 , pp. 817-823
    • Pan, B.-S.1    Johnson R.G., Jr.2
  • 29
    • 0018193791 scopus 로고
    • Troponin T fragments: Physical properties and binding to troponin C
    • Pearlstone JR, Smillie LB, 1978. Troponin T fragments: Physical properties and binding to troponin C. Can J Biochem 56: 521-527.
    • (1978) Can J Biochem , vol.56 , pp. 521-527
    • Pearlstone, J.R.1    Smillie, L.B.2
  • 30
    • 0020015131 scopus 로고
    • Preparations of troponin and its sub-units
    • Potter JD, 1982. Preparations of troponin and its sub-units. Methods Enzymol 85: 241-263.
    • (1982) Methods Enzymol , vol.85 , pp. 241-263
    • Potter, J.D.1
  • 32
    • 0024413451 scopus 로고
    • Site-directed mutation of the trigger calcium-binding sites in cardiac troponin C
    • Putkey JA, Sweeney HL, Campbell ST, 1989. Site-directed mutation of the trigger calcium-binding sites in cardiac troponin C. J Biol Chem 264: 12370-12378.
    • (1989) J Biol Chem , vol.264 , pp. 12370-12378
    • Putkey, J.A.1    Sweeney, H.L.2    Campbell, S.T.3
  • 33
    • 0029861093 scopus 로고    scopus 로고
    • An essential myosin light chain peptide stimulates cardiac mofibrillar ATPase activity
    • Rarick HM, Opgenorth TJ, Wu-wong J, von Geldern TW, Solaro RJ, 1996. An essential myosin light chain peptide stimulates cardiac mofibrillar ATPase activity. J Biol Chem 271: 27039-27043.
    • (1996) J Biol Chem , vol.271 , pp. 27039-27043
    • Rarick, H.M.1    Opgenorth, T.J.2    Wu-Wong, J.3    Von Geldern, T.W.4    Solaro, R.J.5
  • 36
    • 0032494188 scopus 로고    scopus 로고
    • Troponin and tropomyosin: Proteins that switch on and tune in the activity of cardiac myofilaments
    • Solaro RJ, Rarick HR, 1998. Troponin and tropomyosin: Proteins that switch on and tune in the activity of cardiac myofilaments. Circ Res 83: 471-480.
    • (1998) Circ Res , vol.83 , pp. 471-480
    • Solaro, R.J.1    Rarick, H.R.2
  • 38
    • 0032477852 scopus 로고    scopus 로고
    • Identification and mutagenesis of a highly conserved domain in troponin T responsible for troponin I binding: Potential role for coiled coil interaction
    • Stefancsik R, Jha PK, Sarkar S, 1998. Identification and mutagenesis of a highly conserved domain in troponin T responsible for troponin I binding: Potential role for coiled coil interaction. Proc Natl Acad Sci USA 95: 957-962.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 957-962
    • Stefancsik, R.1    Jha, P.K.2    Sarkar, S.3
  • 39
    • 0023676443 scopus 로고
    • Cardiac troponin I, isolated from bovine heart, contains two adjacent phosphoserines: A first example of phosphoserine determination by derivatization to S-ethylcysteine
    • Swiderek K, Jaquet K, Meyer HE, Heilmeyer Jr LMG, 1988. Cardiac troponin I, isolated from bovine heart, contains two adjacent phosphoserines: A first example of phosphoserine determination by derivatization to S-ethylcysteine. Eur J Biochem 176: 335-342.
    • (1988) Eur J Biochem , vol.176 , pp. 335-342
    • Swiderek, K.1    Jaquet, K.2    Meyer, H.E.3    Heilmeyer L.M.G., Jr.4
  • 40
    • 0017280755 scopus 로고
    • The relationship between biological activity and primary structure of troponin I from skeletal muscle of the rabbit
    • Syska H, Wilkinson JM, Grand RJA, Perry SV, 1976. The relationship between biological activity and primary structure of troponin I from skeletal muscle of the rabbit. Biochem J 153: 375-387.
    • (1976) Biochem J , vol.153 , pp. 375-387
    • Syska, H.1    Wilkinson, J.M.2    Grand, R.J.A.3    Perry, S.V.4
  • 41
    • 0019474543 scopus 로고
    • Synthetic studies on the inhibitory region of rabbit skeletal troponin I
    • Talbot JA, Hodges RS, 1981. Synthetic studies on the inhibitory region of rabbit skeletal troponin I. J Biol Chem 25: 2798-2802.
    • (1981) J Biol Chem , vol.25 , pp. 2798-2802
    • Talbot, J.A.1    Hodges, R.S.2
  • 42
    • 0030004861 scopus 로고    scopus 로고
    • Thin-filament-mediated regulation of cardiac contraction
    • Tobacman LS, 1996. Thin-filament-mediated regulation of cardiac contraction. Annu Rev Physiol 58: 447-481.
    • (1996) Annu Rev Physiol , vol.58 , pp. 447-481
    • Tobacman, L.S.1
  • 43
    • 0023930339 scopus 로고
    • The biological importance of each amino acid residue of the troponin I inhibitory sequence 104-115 in the interaction with troponin C and tropomyosin-actin
    • Van Eyk JE, Hodges RS, 1988. The biological importance of each amino acid residue of the troponin I inhibitory sequence 104-115 in the interaction with troponin C and tropomyosin-actin. J Biol Chem 263: 1726-1732.
    • (1988) J Biol Chem , vol.263 , pp. 1726-1732
    • Van Eyk, J.E.1    Hodges, R.S.2
  • 45
    • 0029146873 scopus 로고
    • The unique amino-terminal peptide of cardiac troponin I regulates myofibrillar ATPase activity only when it is phosphorylated
    • Wattanapermpool J, Guo X, Solaro RJ, 1995. The unique amino-terminal peptide of cardiac troponin I regulates myofibrillar ATPase activity only when it is phosphorylated. J Mol Cell Cardiol 27: 1383-1391.
    • (1995) J Mol Cell Cardiol , vol.27 , pp. 1383-1391
    • Wattanapermpool, J.1    Guo, X.2    Solaro, R.J.3
  • 46
    • 0020013525 scopus 로고
    • Special instrumentation and techniques for kinetic studies of contractile systems
    • White HD, 1982. Special instrumentation and techniques for kinetic studies of contractile systems. Methods Enzymol 85: 698-708.
    • (1982) Methods Enzymol , vol.85 , pp. 698-708
    • White, H.D.1
  • 47
    • 0017919767 scopus 로고
    • Comparison of amino acid sequence of troponin I from different striated muscles
    • Wilkinson JM, Grand RJA, 1978. Comparison of amino acid sequence of troponin I from different striated muscles. Nature 231: 31-35.
    • (1978) Nature , vol.231 , pp. 31-35
    • Wilkinson, J.M.1    Grand, R.J.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.