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Volumn 6, Issue 11, 2013, Pages 252-263

Muscle Proteomics of the Indian Major Carp Catla (Catla catla, Hamilton)

Author keywords

2 D electrophoresis; Catla catla; Indian major carp; MALDI TOF MS; Proteogenomics; Reference muscle proteome

Indexed keywords

ADENYLATE KINASE; APOLIPOPROTEIN A1; ASPARTATE AMINOTRANSFERASE; BETA ACTIN; ENOLASE; FRUCTOSE 1, 6 BISPHOSPHATE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; GLYCOGEN PHOSPHORYLASE; LACTATE DEHYDROGENASE; MUSCLE PROTEIN; PHOSPHOGLYCERATE KINASE; PROTEOME; PYRUVATE KINASE; UNCLASSIFIED DRUG;

EID: 84889680950     PISSN: None     EISSN: 0974276X     Source Type: Journal    
DOI: 10.4172/jpb.1000288     Document Type: Article
Times cited : (10)

References (45)
  • 1
    • 0035997269 scopus 로고    scopus 로고
    • Proteomics and its trends facing nature's complexity
    • Hochstrasser DF, Sanchez JC, Appel RD (2002) Proteomics and its trends facing nature's complexity. Proteomics 2: 807-812.
    • (2002) Proteomics , vol.2 , pp. 807-812
    • Hochstrasser, D.F.1    Sanchez, J.C.2    Appel, R.D.3
  • 2
    • 37249014081 scopus 로고    scopus 로고
    • The biological impact of massspectrometry-based proteomics
    • Cravatt BF, Simon GM, Yates JR 3rd (2007) The biological impact of massspectrometry-based proteomics. Nature 450: 991-1000.
    • (2007) Nature , vol.450 , pp. 991-1000
    • Cravatt, B.F.1    Simon, G.M.2    Yates III, J.R.3
  • 4
    • 33750093325 scopus 로고    scopus 로고
    • The underappreciated role of muscle in health and disease
    • Wolfe RR (2006) The underappreciated role of muscle in health and disease. Am J ClinNutr 84: 475-482.
    • (2006) Am J ClinNutr , vol.84 , pp. 475-482
    • Wolfe, R.R.1
  • 5
    • 84866269085 scopus 로고    scopus 로고
    • Proteomic Profiling of Fast-To-Slow Muscle Transitions during Aging
    • Ohlendieck K (2011) Proteomic Profiling of Fast-To-Slow Muscle Transitions during Aging. Front Physiol 2: 105.
    • (2011) Front Physiol , vol.2 , pp. 105
    • Ohlendieck, K.1
  • 6
    • 0034059761 scopus 로고    scopus 로고
    • Regulation of contraction in striated muscle
    • Gordon AM, Homsher E, Regnier M (2000) Regulation of contraction in striated muscle. Physiol Rev 80: 853-924.
    • (2000) Physiol Rev , vol.80 , pp. 853-924
    • Gordon, A.M.1    Homsher, E.2    Regnier, M.3
  • 7
    • 77952503211 scopus 로고    scopus 로고
    • Pathogenesis of insulin resistance in skeletal muscle
    • Abdul-Ghani MA, DeFronzo RA (2010) Pathogenesis of insulin resistance in skeletal muscle. J Biomed Biotech 2010: 476279.
    • (2010) J Biomed Biotech , vol.2010 , pp. 476279
    • Abdul-Ghani, M.A.1    DeFronzo, R.A.2
  • 8
    • 34247881871 scopus 로고    scopus 로고
    • Proteomic profiling of pathological and aged skeletal muscle fibres by peptide mass fingerprinting (Review)
    • Doran P, Donoghue P, O'Connell K, Gannon J, Ohlendieck K (2007) Proteomic profiling of pathological and aged skeletal muscle fibres by peptide mass fingerprinting (Review). Int J Mol Med 19: 547-564.
    • (2007) Int J Mol Med , vol.19 , pp. 547-564
    • Doran, P.1    Donoghue, P.2    O'Connell, K.3    Gannon, J.4    Ohlendieck, K.5
  • 9
    • 39749097121 scopus 로고    scopus 로고
    • Characterization of the human skeletal muscle proteome by one-dimensional gel electrophoresis and HPLC-ESI-MS/MS
    • Højlund K, Yi Z, Hwang H, Bowen B, Lefort N, et al. (2008) Characterization of the human skeletal muscle proteome by one-dimensional gel electrophoresis and HPLC-ESI-MS/MS. Mol Cell Proteomics 7: 257-267.
    • (2008) Mol Cell Proteomics , vol.7 , pp. 257-267
    • Højlund, K.1    Yi, Z.2    Hwang, H.3    Bowen, B.4    Lefort, N.5
  • 10
    • 21744437938 scopus 로고    scopus 로고
    • Differential proteome analysis of aging in rat skeletal muscle
    • Piec I, Listrat A, Alliot J, Chambon C, Taylor RG, et al. (2005) Differential proteome analysis of aging in rat skeletal muscle. FASEB J 19: 1143-1145.
    • (2005) FASEB J , vol.19 , pp. 1143-1145
    • Piec, I.1    Listrat, A.2    Alliot, J.3    Chambon, C.4    Taylor, R.G.5
  • 11
    • 67650429974 scopus 로고    scopus 로고
    • Establishment of a proteomic reference map for the gastrocnemius muscle in the rabbit (Oryctolaguscuniculus)
    • Almeida AM, Campos A, van Harten S, Cardoso LA, Coelho AV (2009) Establishment of a proteomic reference map for the gastrocnemius muscle in the rabbit (Oryctolaguscuniculus). Res Vet Sci 87: 196-199.
    • (2009) Res Vet Sci , vol.87 , pp. 196-199
    • Almeida, A.M.1    Campos, A.2    van Harten, S.3    Cardoso, L.A.4    Coelho, A.V.5
  • 12
    • 2642568030 scopus 로고    scopus 로고
    • The proteome of chicken skeletal muscle: Changes in Soluble protein expression during growth in a layer strain
    • Doherty MK, McLean L, Hayter JR, Pratt JM, Robertson DHL, et al. (2004) The proteome of chicken skeletal muscle: Changes in Soluble protein expression during growth in a layer strain. Proteomics 4: 2082-2089.
    • (2004) Proteomics , vol.4 , pp. 2082-2089
    • Doherty, M.K.1    McLean, L.2    Hayter, J.R.3    Pratt, J.M.4    Robertson, D.H.L.5
  • 13
    • 17044399794 scopus 로고    scopus 로고
    • Protein expression patterns in zebrafish skeletal muscle: Initial characterization and the effects of hypoxic exposure
    • Bosworth CA 4th, Chou CW, Cole RB, Rees BB (2005) Protein expression patterns in zebrafish skeletal muscle: initial characterization and the effects of hypoxic exposure. Proteomics 5: 1362-1371.
    • (2005) Proteomics , vol.5 , pp. 1362-1371
    • Bosworth IV, C.A.1    Chou, C.W.2    Cole, R.B.3    Rees, B.B.4
  • 14
    • 34547872702 scopus 로고    scopus 로고
    • Global cooling: Cold acclimation and the expression of soluble proteins in carp skeletal muscle
    • McLean L, Young IS, Doherty MK, Robertson DH, Cossins AR, et al. (2007) Global cooling: cold acclimation and the expression of soluble proteins in carp skeletal muscle. Proteomics 7: 2667-2681.
    • (2007) Proteomics , vol.7 , pp. 2667-2681
    • McLean, L.1    Young, I.S.2    Doherty, M.K.3    Robertson, D.H.4    Cossins, A.R.5
  • 15
    • 78049529463 scopus 로고    scopus 로고
    • Proteomic analysis of muscle tissue from gilthead sea bream (Sparus aurata, L.) farmed in offshore floating cages
    • Addis MF, Cappuccinelli R, Tedde V, Pagnozzi D, Porcu MC, et al. (2010) Proteomic analysis of muscle tissue from gilthead sea bream (Sparus aurata, L.) farmed in offshore floating cages. Aquaculture 309: 245-252.
    • (2010) Aquaculture , vol.309 , pp. 245-252
    • Addis, M.F.1    Cappuccinelli, R.2    Tedde, V.3    Pagnozzi, D.4    Porcu, M.C.5
  • 16
    • 78649644187 scopus 로고    scopus 로고
    • Cod (Gadusmorhua) muscle proteome cataloging using 1D-PAGE protein separation, nano-liquid chromatography peptide fractionation, and Linear Trap Quadrupole (LTQ) Mass Spectrometry
    • Gebriel M, Uleberg KE, Larssen E, HjelleBjørnstad A, Sivertsvik M, et al. (2010) Cod (Gadusmorhua) muscle proteome cataloging using 1D-PAGE protein separation, nano-liquid chromatography peptide fractionation, and Linear Trap Quadrupole (LTQ) Mass Spectrometry. J Agric Food Chem 58: 12307-12312.
    • (2010) J Agric Food Chem , vol.58 , pp. 12307-12312
    • Gebriel, M.1    Uleberg, K.E.2    Larssen, E.3    HjelleBjørnstad, A.4    Sivertsvik, M.5
  • 17
    • 79959591891 scopus 로고    scopus 로고
    • Proteomic analysis of Snakehead fish (Channastriata) muscle tissue
    • Gam LH, Leow CY, Baie S (2006) Proteomic analysis of Snakehead fish (Channastriata) muscle tissue. Malaysian J BiochemMolBiol 14: 25-32.
    • (2006) Malaysian J BiochemMolBiol , vol.14 , pp. 25-32
    • Gam, L.H.1    Leow, C.Y.2    Baie, S.3
  • 18
    • 0033168987 scopus 로고    scopus 로고
    • Muscle development and growth: Potential implications for flesh quality in fish
    • Johnston IA (1999) Muscle development and growth: potential implications for flesh quality in fish. Aquaculture 177: 99-115.
    • (1999) Aquaculture , vol.177 , pp. 99-115
    • Johnston, I.A.1
  • 19
    • 16244376499 scopus 로고    scopus 로고
    • Genetic analysis of three river populations ofCatlacatla(Hamilton) using randomly amplified polymorphic DNA markers
    • Islam MS, Ahmed ASI, Azam MS, Alam MS (2005) Genetic analysis of three river populations ofCatlacatla(Hamilton) using randomly amplified polymorphic DNA markers. Asian-Aust J AnimSci 18: 453-457.
    • (2005) Asian-Aust J AnimSci , vol.18 , pp. 453-457
    • Islam, M.S.1    Ahmed, A.S.I.2    Azam, M.S.3    Alam, M.S.4
  • 20
    • 84885178676 scopus 로고    scopus 로고
    • Proteomic analysis of sarcoplasmic peptides of two related fish species for food authentication
    • Barik SK, Banerjee S, Bhattacharjee S, Das Gupta SK, Mohanty S, et al. (2013) Proteomic analysis of sarcoplasmic peptides of two related fish species for food authentication. ApplBiochemBiotechnol 171: 1011-1021.
    • (2013) ApplBiochemBiotechnol , vol.171 , pp. 1011-1021
    • Barik, S.K.1    Banerjee, S.2    Bhattacharjee, S.3    Das Gupta, S.K.4    Mohanty, S.5
  • 21
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 22
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 23
    • 0016711037 scopus 로고
    • High resolution two-dimensional electrophoresis of proteins
    • O'Farrell PH (1975) High resolution two-dimensional electrophoresis of proteins. J BiolChem 250: 4007-4021.
    • (1975) J BiolChem , vol.250 , pp. 4007-4021
    • O'Farrell, P.H.1
  • 24
    • 41149100569 scopus 로고    scopus 로고
    • Proteomic analysis of the venom of Heterometruslongimanus (Asian black scorpion)
    • Bringans S, Eriksen S, Kendrick T, Gopalakrishnakone P, Livk A, et al. (2008) Proteomic analysis of the venom of Heterometruslongimanus (Asian black scorpion). Proteomics 8: 1081-1096.
    • (2008) Proteomics , vol.8 , pp. 1081-1096
    • Bringans, S.1    Eriksen, S.2    Kendrick, T.3    Gopalakrishnakone, P.4    Livk, A.5
  • 25
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins DN, Pappin DJ, Creasy DM, Cottrell JS (1999) Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 20: 3551-3567.
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 27
    • 84889640596 scopus 로고    scopus 로고
    • http://www.cifri.ernet.in/fishprot.html
  • 28
    • 68249113501 scopus 로고    scopus 로고
    • Cloning, nucleotide sequence and phylogenetic analyses and tissue-specific expression of the transferrin gene in Cirrhinusmrigala infected with Aeromonashydrophila
    • Sahoo PK, Mohanty BR, Kumari J, Barat A, Sarangi N (2009) Cloning, nucleotide sequence and phylogenetic analyses and tissue-specific expression of the transferrin gene in Cirrhinusmrigala infected with Aeromonashydrophila. Comp ImmunolMicrobiol Infect Dis 6: 527-537
    • (2009) Comp ImmunolMicrobiol Infect Dis , vol.6 , pp. 527-537
    • Sahoo, P.K.1    Mohanty, B.R.2    Kumari, J.3    Barat, A.4    Sarangi, N.5
  • 29
    • 80053641874 scopus 로고    scopus 로고
    • Effect of storage temperature as a preanalytical variable on the lens crystallins protein quality for proteomic studies
    • Bhattacharjee S, Mohanty S, Sharma AP, Mohanty BP (2011) Effect of storage temperature as a preanalytical variable on the lens crystallins protein quality for proteomic studies. Proteomics ClinAppl 5: 504-512.
    • (2011) Proteomics ClinAppl , vol.5 , pp. 504-512
    • Bhattacharjee, S.1    Mohanty, S.2    Sharma, A.P.3    Mohanty, B.P.4
  • 30
    • 74849108510 scopus 로고    scopus 로고
    • Proteomic signature of muscle atrophy in rainbow trout
    • Salem M, Kenney PB, Rexroad CE 3rd, Yao J (2010) Proteomic signature of muscle atrophy in rainbow trout. J Proteomics 73: 778-789.
    • (2010) J Proteomics , vol.73 , pp. 778-789
    • Salem, M.1    Kenney, P.B.2    Rexroad III, C.E.3    Yao, J.4
  • 31
    • 17444381547 scopus 로고    scopus 로고
    • Apolipoprotein AI could be a significant determinant of epithelial integrity in rainbow trout gill cell cultures: A study in functional proteomics
    • Smith RW, Wood CM, Cash P, Diao L, Pärt P (2005) Apolipoprotein AI could be a significant determinant of epithelial integrity in rainbow trout gill cell cultures: a study in functional proteomics. BiochimBiophysActa 1749: 81-93.
    • (2005) BiochimBiophysActa , vol.1749 , pp. 81-93
    • Smith, R.W.1    Wood, C.M.2    Cash, P.3    Diao, L.4    Pärt, P.5
  • 33
    • 0024538866 scopus 로고
    • Optic nerve regeneration in adult fish and apolipoprotein A-I
    • Harel A, Fainaru M, Shafer Z, Hernandez M, Cohen A, et al. (1989) Optic nerve regeneration in adult fish and apolipoprotein A-I. J Neurochem 52: 1218-1228.
    • (1989) J Neurochem , vol.52 , pp. 1218-1228
    • Harel, A.1    Fainaru, M.2    Shafer, Z.3    Hernandez, M.4    Cohen, A.5
  • 34
    • 0037341220 scopus 로고    scopus 로고
    • Local expression of apolipoprotein A-I gene and a possible role for HDL in primary defence in the carp skin
    • Concha MI, Molina S, Oyarzún C, Villanueva J, Amthauer R (2003) Local expression of apolipoprotein A-I gene and a possible role for HDL in primary defence in the carp skin. Fish Shellfish Immunol 14: 259-273.
    • (2003) Fish Shellfish Immunol , vol.14 , pp. 259-273
    • Concha, M.I.1    Molina, S.2    Oyarzún, C.3    Villanueva, J.4    Amthauer, R.5
  • 35
    • 10744224229 scopus 로고    scopus 로고
    • Is ApolipoproteinA-I a regulating protein for the complement system of cod (Gadusmorhua L)?
    • Magnadóttir B, Lange S (2004) Is ApolipoproteinA-I a regulating protein for the complement system of cod (Gadusmorhua L)? Fish Shellfish Immunol 16: 265-269.
    • (2004) Fish Shellfish Immunol , vol.16 , pp. 265-269
    • Magnadóttir, B.1    Lange, S.2
  • 36
    • 0015509365 scopus 로고
    • Patterns of the isoenzymes of creatine kinase in teleostean fish
    • Scholl A, Eppenberger HM (1972) Patterns of the isoenzymes of creatine kinase in teleostean fish. CompBiochemPhysiol B 42: 221-226.
    • (1972) CompBiochemPhysiol B , vol.42 , pp. 221-226
    • Scholl, A.1    Eppenberger, H.M.2
  • 37
    • 0037379434 scopus 로고    scopus 로고
    • Isolation, characterization and nucleotide sequence of the muscle isoforms of creatine kinase from the Antarctic teleost Chaenocephalus aceratus
    • Winnard P, Cashon RE, Sidell BD, Vayda ME (2003) Isolation, characterization and nucleotide sequence of the muscle isoforms of creatine kinase from the Antarctic teleost Chaenocephalus aceratus. Comp Biochem Physiol B Biochem Mol Biol 134: 651-667.
    • (2003) Comp Biochem Physiol B Biochem Mol Biol , vol.134 , pp. 651-667
    • Winnard, P.1    Cashon, R.E.2    Sidell, B.D.3    Vayda, M.E.4
  • 38
    • 14844336887 scopus 로고    scopus 로고
    • Characterization of creatine kinase isoforms in herring (Clupeaharengus) skeletal muscle
    • Grzyb K, Skorkowski EF (2005) Characterization of creatine kinase isoforms in herring (Clupeaharengus) skeletal muscle. Comp BiochemPhysiol B BiochemMolBiol 140: 629-634.
    • (2005) Comp BiochemPhysiol B BiochemMolBiol , vol.140 , pp. 629-634
    • Grzyb, K.1    Skorkowski, E.F.2
  • 39
    • 0032509537 scopus 로고    scopus 로고
    • Cloning, characterization, and expression in Escherichia coli of three creatine kinase muscle isoenzymecDNAs from carp (Cyprinuscarpio) striated muscle
    • Sun HW, Hui CF, Wu JL (1998) Cloning, characterization, and expression in Escherichia coli of three creatine kinase muscle isoenzymecDNAs from carp (Cyprinuscarpio) striated muscle. J BiolChem 273: 33774-33780.
    • (1998) J BiolChem , vol.273 , pp. 33774-33780
    • Sun, H.W.1    Hui, C.F.2    Wu, J.L.3
  • 40
    • 0029374716 scopus 로고
    • Origin of PDZ (DHR, GLGF) domains
    • Kennedy MB (1995) Origin of PDZ (DHR, GLGF) domains. Trends BiochemSci 20: 350.
    • (1995) Trends BiochemSci , vol.20 , pp. 350
    • Kennedy, M.B.1
  • 41
    • 0034004352 scopus 로고    scopus 로고
    • The LIM domain: Regulation by association
    • Bach I (2000) The LIM domain: regulation by association. MechDev 91: 5-17.
    • (2000) MechDev , vol.91 , pp. 5-17
    • Bach, I.1
  • 44
    • 84889638214 scopus 로고    scopus 로고
    • Meat and fish flesh quality improvement with proteomic applications
    • Picard B, Lefèvre F, Lebret B (2010) Meat and fish flesh quality improvement with proteomic applications. Animal Front 2: 18-25
    • (2010) Animal Front , vol.2 , pp. 18-25
    • Picard, B.1    Lefèvre, F.2    Lebret, B.3
  • 45
    • 0038353381 scopus 로고    scopus 로고
    • Proteome analysis elucidating post-mortem changes in cod (Gadus morhua) muscle proteins
    • Kjaersgård IV, Jessen F (2003) Proteome analysis elucidating post-mortem changes in cod (Gadus morhua) muscle proteins. J Agric Food Chem 51: 3985-3991.
    • (2003) J Agric Food Chem , vol.51 , pp. 3985-3991
    • Kjaersgård, I.V.1    Jessen, F.2


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