메뉴 건너뛰기




Volumn 43, Issue 1, 1996, Pages 82-93

Properties and localization of a tyrosine phosphorylated form of hexokinase in mouse sperm

Author keywords

Hexokinase; Mouse; Protein tyrosine phosphorylation; Sperm

Indexed keywords

COMPLEMENTARY DNA; HEXOKINASE; MEMBRANE PROTEIN; PHOSPHOTYROSINE; PORIN; TYROSINE;

EID: 0030071292     PISSN: 1040452X     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1098-2795(199601)43:1<82::AID-MRD11>3.0.CO;2-6     Document Type: Article
Times cited : (45)

References (48)
  • 2
    • 0025796715 scopus 로고
    • Porin interaction with hexokinase and glycerol kinase metabolic microcompartmentation at the outer mitochondrial membrane
    • Adams V, Griffin L, Towbin J, Gelb B, Worley K, McCabe ERB (1991b): Porin interaction with hexokinase and glycerol kinase metabolic microcompartmentation at the outer mitochondrial membrane. Biochem Med Metab Biol 45:271-291.
    • (1991) Biochem Med Metab Biol , vol.45 , pp. 271-291
    • Adams, V.1    Griffin, L.2    Towbin, J.3    Gelb, B.4    Worley, K.5    McCabe, E.R.B.6
  • 3
    • 0024237766 scopus 로고
    • Functional significance of mitochondrial bound hexokinase in tumor cell metabolism
    • Arora K, Pedersen P (1988): Functional significance of mitochondrial bound hexokinase in tumor cell metabolism. J Biol Chem 263: 17422-17428.
    • (1988) J Biol Chem , vol.263 , pp. 17422-17428
    • Arora, K.1    Pedersen, P.2
  • 4
    • 0027180056 scopus 로고
    • Glucose utilization by tumor cells: The enzyme hexokinase autophosphorylates both its N- and C- terminal halves
    • Arora K, Pedersen P (1993): Glucose utilization by tumor cells: The enzyme hexokinase autophosphorylates both its N- and C- terminal halves. Arch Biochem Biophys 304:515-518.
    • (1993) Arch Biochem Biophys , vol.304 , pp. 515-518
    • Arora, K.1    Pedersen, P.2
  • 5
    • 0025218127 scopus 로고
    • Glucose phosphorylation in tumor cells: Cloning, sequencing, and overexpression in active form of a full length cDNA encoding a mitochondrial bindable form of hexokinase
    • Arora KK, Fanciulli M, Pedersen PL (1990): Glucose phosphorylation in tumor cells: Cloning, sequencing, and overexpression in active form of a full length cDNA encoding a mitochondrial bindable form of hexokinase. J Biol Chem 265:6481-6488.
    • (1990) J Biol Chem , vol.265 , pp. 6481-6488
    • Arora, K.K.1    Fanciulli, M.2    Pedersen, P.L.3
  • 6
    • 0017717734 scopus 로고
    • Dissociation of the mouse testis and characterization of isolated spermatogenic cells
    • Bellvé AR, Millette CF, Bhatnagar YM, O'Brien DA (1977): Dissociation of the mouse testis and characterization of isolated spermatogenic cells. J Histochem Cytochem 25:480-494.
    • (1977) J Histochem Cytochem , vol.25 , pp. 480-494
    • Bellvé, A.R.1    Millette, C.F.2    Bhatnagar, Y.M.3    O'Brien, D.A.4
  • 7
    • 0018873552 scopus 로고
    • Compartmentation of hexokinase and creatine phosphokinase, cellular regulation, and insulin action
    • Bessman SP, Geiger PJ (1980): Compartmentation of hexokinase and creatine phosphokinase, cellular regulation, and insulin action. Curr Top Cell Regul 16:55-86.
    • (1980) Curr Top Cell Regul , vol.16 , pp. 55-86
    • Bessman, S.P.1    Geiger, P.J.2
  • 8
    • 0020665468 scopus 로고
    • Sperm-egg interactions in the mouse: Sequence of events and induction of the acrosome reaction by a zona pellucida glycoprotein
    • Bleil JD, Wassarman PM (1983): Sperm-egg interactions in the mouse: Sequence of events and induction of the acrosome reaction by a zona pellucida glycoprotein. Dev Biol 95:317-324.
    • (1983) Dev Biol , vol.95 , pp. 317-324
    • Bleil, J.D.1    Wassarman, P.M.2
  • 9
    • 0025075878 scopus 로고
    • Identification of a ZP3-binding protein on acrosome-intact mouse sperm by photoaffinity crosslinking
    • Bleil JD, Wassarman PM (1990): Identification of a ZP3-binding protein on acrosome-intact mouse sperm by photoaffinity crosslinking. Proc Natl Acad Sci USA 87:6778-6782.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 6778-6782
    • Bleil, J.D.1    Wassarman, P.M.2
  • 10
    • 0019887744 scopus 로고
    • Phase separation of integral membrane proteins in Triton X-114 solution
    • Bordier C (1981): Phase separation of integral membrane proteins in Triton X-114 solution. J Biol Chem 256:1604-1607.
    • (1981) J Biol Chem , vol.256 , pp. 1604-1607
    • Bordier, C.1
  • 11
    • 0025854703 scopus 로고
    • Generation of a mouse sperm membrane fraction with a zona receptor activity
    • Bunch DO, Saling PM (1991): Generation of a mouse sperm membrane fraction with a zona receptor activity. Biol Reprod 44:672-680.
    • (1991) Biol Reprod , vol.44 , pp. 672-680
    • Bunch, D.O.1    Saling, P.M.2
  • 13
    • 0028227343 scopus 로고
    • Sperm-egg recognition in the mouse: Characterization of sp56, a sperm protein having specific affinity for ZP3
    • Cheng A, Le T, Palacios M, Bookbinder LH, Wassarman PM, Suzuki F, Bleil JD (1994): Sperm-egg recognition in the mouse: Characterization of sp56, a sperm protein having specific affinity for ZP3. J Cell Biol 125:867-378.
    • (1994) J Cell Biol , vol.125 , pp. 867-1378
    • Cheng, A.1    Le, T.2    Palacios, M.3    Bookbinder, L.H.4    Wassarman, P.M.5    Suzuki, F.6    Bleil, J.D.7
  • 14
    • 0018639079 scopus 로고
    • Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease
    • Chirgwin JM, Przybila AE, MacDonald RJ, Rutter WJ (1979): Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease. Biochemistry 18:5294-5299.
    • (1979) Biochemistry , vol.18 , pp. 5294-5299
    • Chirgwin, J.M.1    Przybila, A.E.2    MacDonald, R.J.3    Rutter, W.J.4
  • 15
    • 0025335432 scopus 로고
    • Evidence for export of a muscle lectin from cytosol to extracellular matrix and for a novel secretory mechanism
    • Cooper DN, Barondes SH (1990): Evidence for export of a muscle lectin from cytosol to extracellular matrix and for a novel secretory mechanism. J Cell Biol 110:1681-1691.
    • (1990) J Cell Biol , vol.110 , pp. 1681-1691
    • Cooper, D.N.1    Barondes, S.H.2
  • 16
    • 0023522461 scopus 로고
    • 2+ uptake by guinea pig epididymal spermatozoa
    • 2+ uptake by guinea pig epididymal spermatozoa. Biol Reprod 37:1097-1107.
    • (1987) Biol Reprod , vol.37 , pp. 1097-1107
    • Coronel, C.E.1    Lardy, H.A.2
  • 17
    • 0017381295 scopus 로고
    • Effect of neutrat salts on the interaction of the rat brain hexokinase with the outer mitochondrial membrane
    • Feigner P, Wilson J (1977): Effect of neutrat salts on the interaction of the rat brain hexokinase with the outer mitochondrial membrane. Arch Biochem Biophys 182:282-294.
    • (1977) Arch Biochem Biophys , vol.182 , pp. 282-294
    • Feigner, P.1    Wilson, J.2
  • 18
    • 0018801012 scopus 로고
    • Purification of a hexokinase binding protein from outer mitochondrial membrane
    • Felgner PL, Messer JL, Wilson JE (1979): Purification of a hexokinase binding protein from outer mitochondrial membrane. J Biol Chem 254:4946-4949.
    • (1979) J Biol Chem , vol.254 , pp. 4946-4949
    • Felgner, P.L.1    Messer, J.L.2    Wilson, J.E.3
  • 20
    • 0020039866 scopus 로고
    • Isolation of intracellular membranes by means of sodium carbonate treatment: Application to endoplasmic reticulum
    • Fujiki Y, Hubbard A, Fowler S, Lazarow P (1982): Isolation of intracellular membranes by means of sodium carbonate treatment: Application to endoplasmic reticulum. J Cell Biol 93:97-102.
    • (1982) J Cell Biol , vol.93 , pp. 97-102
    • Fujiki, Y.1    Hubbard, A.2    Fowler, S.3    Lazarow, P.4
  • 22
    • 0024312610 scopus 로고
    • The hexokinase isoenzyme PII of Saccharomyces cerevisiae is a protein kinase
    • Herrero P, Fernandez R, Moreno F (1989): The hexokinase isoenzyme PII of Saccharomyces cerevisiae is a protein kinase. J Gen Microbiol 135:1209-1216.
    • (1989) J Gen Microbiol , vol.135 , pp. 1209-1216
    • Herrero, P.1    Fernandez, R.2    Moreno, F.3
  • 23
    • 0017087721 scopus 로고
    • Glucose requirement for mouse sperm capacitation in vitro
    • Hoppe PC (1976): Glucose requirement for mouse sperm capacitation in vitro. Biol Reprod 15:39-45.
    • (1976) Biol Reprod , vol.15 , pp. 39-45
    • Hoppe, P.C.1
  • 24
    • 0028964265 scopus 로고
    • Sperm from mice carrying one or two t haplotypes are deficient in investment and oocyte penetration
    • Johnson LR, Pilder SH, Bailey JL, Olds-Clarke P (1995): Sperm from mice carrying one or two t haplotypes are deficient in investment and oocyte penetration. Dev Biol 168:138-149.
    • (1995) Dev Biol , vol.168 , pp. 138-149
    • Johnson, L.R.1    Pilder, S.H.2    Bailey, J.L.3    Olds-Clarke, P.4
  • 25
    • 0028111490 scopus 로고
    • p95, the major phosphotyrosine-containing protein in mouse spermatozoa, is a hexokinase with unique properties
    • Kalab P, Visconti P, Leclerc P, Kopf GS (1994): p95, the major phosphotyrosine-containing protein in mouse spermatozoa, is a hexokinase with unique properties. J Biol Chem 269:3810-3817.
    • (1994) J Biol Chem , vol.269 , pp. 3810-3817
    • Kalab, P.1    Visconti, P.2    Leclerc, P.3    Kopf, G.S.4
  • 26
    • 0025812781 scopus 로고
    • Zona pellucidamediated acrosomal exocytosis in mouse spermatozoa: Characterization of an intermediate stage prior to the completion of the acrosome reaction
    • Kligman I, Glassner M, Storey BT. Kopf GS (1991): Zona pellucidamediated acrosomal exocytosis in mouse spermatozoa: Characterization of an intermediate stage prior to the completion of the acrosome reaction. Dev Biol 145:344-355.
    • (1991) Dev Biol , vol.145 , pp. 344-355
    • Kligman, I.1    Glassner, M.2    Storey, B.T.3    Kopf, G.S.4
  • 27
    • 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 227:680-385.
    • (1970) Nature , vol.227 , pp. 680-1385
    • Laemmli, U.K.1
  • 28
    • 0022650341 scopus 로고
    • Bicarbonate is essential for fertilization of mouse eggs; mouse sperm require it to undergo the acrosome reaction
    • Lee MA, Storey BT (1986): Bicarbonate is essential for fertilization of mouse eggs; mouse sperm require it to undergo the acrosome reaction. Biol Reprod 34:349-356.
    • (1986) Biol Reprod , vol.34 , pp. 349-356
    • Lee, M.A.1    Storey, B.T.2
  • 29
    • 0024356430 scopus 로고
    • 95 kD sperm proteins bind ZP3 and serve as tyrosine kinase substrates in response to zona binding
    • Leyton L, Saling PM (1989a): 95 kD sperm proteins bind ZP3 and serve as tyrosine kinase substrates in response to zona binding. Cell 57:123-130.
    • (1989) Cell , vol.57 , pp. 123-130
    • Leyton, L.1    Saling, P.M.2
  • 30
    • 0024356204 scopus 로고
    • Evidence that aggregation of mouse sperm receptors by ZP3 triggers the acrosome reaction
    • Leyton L, Saling PM (1989b): Evidence that aggregation of mouse sperm receptors by ZP3 triggers the acrosome reaction. J Cell Biol 108:2163-2168.
    • (1989) J Cell Biol , vol.108 , pp. 2163-2168
    • Leyton, L.1    Saling, P.M.2
  • 31
    • 0027080725 scopus 로고
    • Regulation of mouse gamete interaction by a sperm tyrosine kinase
    • Leyton L, LeGuen P, Bunch D, Saling PM (1992): Regulation of mouse gamete interaction by a sperm tyrosine kinase. Proc Natl Acad Sci USA 89:11692-11695.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 11692-11695
    • Leyton, L.1    LeGuen, P.2    Bunch, D.3    Saling, P.M.4
  • 32
    • 0026611050 scopus 로고
    • Complementarity between sperm surface β-1,4-galactosyltransferase and egg-coat ZP3 mediates sperm-egg binding
    • Miller DJ, Macek MB, Shur BD (1992): Complementarity between sperm surface β-1,4-galactosyltransferase and egg-coat ZP3 mediates sperm-egg binding. Nature 357:589-593.
    • (1992) Nature , vol.357 , pp. 589-593
    • Miller, D.J.1    Macek, M.B.2    Shur, B.D.3
  • 33
    • 0026488395 scopus 로고
    • Proteins containing an uncleaved signal for glycophosphatidyhnositol membrane anchor attachment are retained in a post-ER compartment
    • Moran P, Caras IW (1992): Proteins containing an uncleaved signal for glycophosphatidyhnositol membrane anchor attachment are retained in a post-ER compartment. J Cell Biol 119:763-772.
    • (1992) J Cell Biol , vol.119 , pp. 763-772
    • Moran, P.1    Caras, I.W.2
  • 34
    • 0027169570 scopus 로고
    • Unique hexokinase messenger ribonucleic acids lacking the porin-binding domain are developmentally expressed in mouse spermatogenic cells
    • Mori C, Welch JE, Fulcher KD, O'Brien DA, Eddy EM (1993): Unique hexokinase messenger ribonucleic acids lacking the porin-binding domain are developmentally expressed in mouse spermatogenic cells. Biol Reprod 49:191-203.
    • (1993) Biol Reprod , vol.49 , pp. 191-203
    • Mori, C.1    Welch, J.E.2    Fulcher, K.D.3    O'Brien, D.A.4    Eddy, E.M.5
  • 35
    • 0030031745 scopus 로고
    • Sperm from mice carrying two t haplotypes do not possess a tyrosine phosphorylated form of hexokinase
    • Olds-Clarke P, Pilder SH, Visconti PE, Moss SB, Orth JM, Kopf GS (1995): Sperm from mice carrying two t haplotypes do not possess a tyrosine phosphorylated form of hexokinase. Mol Reprod Dev 43: 94-104.
    • (1995) Mol Reprod Dev , vol.43 , pp. 94-104
    • Olds-Clarke, P.1    Pilder, S.H.2    Visconti, P.E.3    Moss, S.B.4    Orth, J.M.5    Kopf, G.S.6
  • 36
    • 0023820803 scopus 로고
    • 14C]-valine incorporation and its relation to hexokinase activity in developing brain
    • 14C]-valine incorporation and its relation to hexokinase activity in developing brain. Biochem Biophys Res Commun 154:450-454.
    • (1988) Biochem Biophys Res Commun , vol.154 , pp. 450-454
    • Pal, N.1    Bessman, S.P.2
  • 37
    • 0024828501 scopus 로고
    • Capacitation of bovine sperm by heparin: Inhibitory effect of glucose and role of intracellular pH
    • Parrish JJ, Susko-Parrish JL, First NL (1989): Capacitation of bovine sperm by heparin: Inhibitory effect of glucose and role of intracellular pH. Biol Reprod 41:683-699.
    • (1989) Biol Reprod , vol.41 , pp. 683-699
    • Parrish, J.J.1    Susko-Parrish, J.L.2    First, N.L.3
  • 38
    • 0021966411 scopus 로고
    • An intact hydrophobic N-terminal sequence is critical for binding of rat brain hexokinase to mitochondria
    • Polakis PG, Wilson JE (1985): An intact hydrophobic N-terminal sequence is critical for binding of rat brain hexokinase to mitochondria. Arch Biochem Biophys 236:328-337.
    • (1985) Arch Biochem Biophys , vol.236 , pp. 328-337
    • Polakis, P.G.1    Wilson, J.E.2
  • 39
    • 0026471714 scopus 로고
    • Transport of proteins across the endoplasmic reticulum membrane
    • Rapoport TA (1992): Transport of proteins across the endoplasmic reticulum membrane. Science 258:931-936.
    • (1992) Science , vol.258 , pp. 931-936
    • Rapoport, T.A.1
  • 40
    • 0017225975 scopus 로고
    • Separation of mouse spermatogenic cells by sedimentation velocity
    • Romrell LJ, Bellvé AR, Fawcett DW (1976): Separation of mouse spermatogenic cells by sedimentation velocity. Dev Biol 49:119-131.
    • (1976) Dev Biol , vol.49 , pp. 119-131
    • Romrell, L.J.1    Bellvé, A.R.2    Fawcett, D.W.3
  • 41
    • 0025726129 scopus 로고
    • Disposition of mitochondrially bound hexokinase at the membrane surface, deduced from reactivity with monoclonal antibodies recognizing epitopes of defined location
    • Smith AD, Wilson JE (1991a): Disposition of mitochondrially bound hexokinase at the membrane surface, deduced from reactivity with monoclonal antibodies recognizing epitopes of defined location. Arch Biochem Biophys 287:359-366.
    • (1991) Arch Biochem Biophys , vol.287 , pp. 359-366
    • Smith, A.D.1    Wilson, J.E.2
  • 42
    • 0025751596 scopus 로고
    • Effect of ligand binding on the tryptic digestion pattern of rat brain hexokinase: Relationship of ligand-induced conformational changes to catalytic and regulatory functions
    • Smith AD, Wilson JE (1991b): Effect of ligand binding on the tryptic digestion pattern of rat brain hexokinase: Relationship of ligand-induced conformational changes to catalytic and regulatory functions. Arch Biochem Biophys 29:59-68.
    • (1991) Arch Biochem Biophys , vol.29 , pp. 59-68
    • Smith, A.D.1    Wilson, J.E.2
  • 43
    • 0028957362 scopus 로고
    • Capacitation of mouse spermatozoa I. Correlation between the capacitation state and protein tyrosine phosphorylation
    • Visconti PE, Bailey JL, Moore GD, Pan D, Olds-Clarke P, Kopf GS (1995a): Capacitation of mouse spermatozoa I. Correlation between the capacitation state and protein tyrosine phosphorylation. Development 121:1129-1137.
    • (1995) Development , vol.121 , pp. 1129-1137
    • Visconti, P.E.1    Bailey, J.L.2    Moore, G.D.3    Pan, D.4    Olds-Clarke, P.5    Kopf, G.S.6
  • 44
    • 0028936801 scopus 로고
    • Capacitation of mouse spermatozoa II. Protein tyrosine phosphorylation and capacitation are regulated by a cAMP-dependent pathway
    • Visconti PE, Moore GD, Bailey JL, Leclerc P, Connors SA, Pan D, Olds-Clarke P, Kopf GS (1995b): Capacitation of mouse spermatozoa II. Protein tyrosine phosphorylation and capacitation are regulated by a cAMP-dependent pathway. Development 121:1139-1150.
    • (1995) Development , vol.121 , pp. 1139-1150
    • Visconti, P.E.1    Moore, G.D.2    Bailey, J.L.3    Leclerc, P.4    Connors, S.A.5    Pan, D.6    Olds-Clarke, P.7    Kopf, G.S.8
  • 45
    • 0008886238 scopus 로고
    • Molecular events mediating sperm activation
    • Ward CR, Kopf GS (1993): Molecular events mediating sperm activation. Dev Biol 104:287-296
    • (1993) Dev Biol , vol.104 , pp. 287-296
    • Ward, C.R.1    Kopf, G.S.2
  • 46
    • 0025044472 scopus 로고
    • Profile of a mammalian sperm receptor
    • Wassarman PM (1990): Profile of a mammalian sperm receptor. Development 108:1-17.
    • (1990) Development , vol.108 , pp. 1-17
    • Wassarman, P.M.1
  • 47
    • 0017900492 scopus 로고
    • Ambiquitous enzymes: Variation in intracellular distribution as a regulatory mechanism
    • Wilson JE (1978): Ambiquitous enzymes: Variation in intracellular distribution as a regulatory mechanism Trends Biochem Sci 3:124-125.
    • (1978) Trends Biochem Sci , vol.3 , pp. 124-125
    • Wilson, J.E.1
  • 48
    • 85132263639 scopus 로고
    • Regulation of mammalian hexokinase activity
    • R Beither (ed): Boca Raton, FL: CRC Press
    • Wilson JE (1984) Regulation of mammalian hexokinase activity. In R Beither (ed): Regulation of Carbohydrate Metabolism, Vol. I, Boca Raton, FL: CRC Press, pp 45-85.
    • (1984) Regulation of Carbohydrate Metabolism , vol.1 , pp. 45-85
    • Wilson, J.E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.