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Volumn 34, Issue 6, 2009, Pages 899-908

Proteomic analysis of heparin-binding proteins from human seminal plasma: A step towards identification of molecular markers of male fertility

Author keywords

2D gel electrophoresis; Heparin binding proteins; Human seminal plasma; MALDI TOF; Sperm capacitation

Indexed keywords

ANTIMICROBIAL CATIONIC PEPTIDE; BIOLOGICAL MARKER; CARRIER PROTEIN; CATIONIC ANTIMICROBIAL PROTEIN CAP 37, HUMAN; HEPARIN; PLASMA PROTEIN; PROTEOME;

EID: 77949899048     PISSN: 02505991     EISSN: 09737138     Source Type: Journal    
DOI: 10.1007/s12038-009-0104-5     Document Type: Article
Times cited : (65)

References (49)
  • 1
    • 27944461855 scopus 로고    scopus 로고
    • Bicarbonate and bovine serum albumin reversibly 'switch' capacitation-induced events in human spermatozoa
    • Bedu-Addo K, Lefievre L, Moseley F L, Barratt C L and Publicover S J 2005 Bicarbonate and bovine serum albumin reversibly 'switch' capacitation-induced events in human spermatozoa; Mol. Hum. Reprod. 11 683-691
    • (2005) Mol. Hum. Reprod , vol.11 , pp. 683-691
    • Bedu-Addo, K.1    Lefievre, L.2    Moseley, F.L.3    Barratt, C.L.4    Publicover, S.J.5
  • 2
    • 27544444578 scopus 로고    scopus 로고
    • The interaction between heparin and lys49 phospholipase A2 reveals the natural binding of heparin on the enzyme
    • Bugs M R, Bortoleto-Bugs R K and Cornelio M L 2005 The interaction between heparin and Lys49 phospholipase A2 reveals the natural binding of heparin on the enzyme; Int. J. Biol. Macromol. 37 21-27
    • (2005) Int. J. Biol. Macromol , vol.37 , pp. 21-27
    • Bugs, M.R.1    Bortoleto-Bugs, R.K.2    Cornelio, M.L.3
  • 3
    • 0031589138 scopus 로고    scopus 로고
    • Isolation and characterization of heparin- and phosphorylcholine-binding proteins of boar and stallion seminal plasma. Primary structure of porcine pB1
    • Calvete J J, Raida M, Gentzel M, Urbanke C, Sanz L and Topfer-Petersen E 1997 Isolation and characterization of heparin- and phosphorylcholine-binding proteins of boar and stallion seminal plasma. Primary structure of porcine pB1; FEBS Lett. 407 201-206
    • (1997) FEBS Lett. , vol.407 , pp. 201-206
    • Calvete, J.J.1    Raida, M.2    Gentzel, M.3    Urbanke, C.4    Sanz, L.5    Topfer-Petersen, E.6
  • 4
    • 0029090785 scopus 로고
    • Effect of glycosylation on the heparin-binding capability of boar and stallion seminal plasma proteins
    • Calvete J J, Reinert M, Sanz L and Topfer-Petersen E 1995 Effect of glycosylation on the heparin-binding capability of boar and stallion seminal plasma proteins; J. Chromatogr. A711 167-173
    • (1995) J. Chromatogr. , vol.A711 , pp. 167-173
    • Calvete, J.J.1    Reinert, M.2    Sanz, L.3    Topfer-Petersen, E.4
  • 5
    • 34248352716 scopus 로고    scopus 로고
    • Sperm competition and the evolution of ejaculate composition
    • Cameron E, Day T and Rowe L 2007 Sperm competition and the evolution of ejaculate composition; Am. Nat. 169 E158-E172
    • (2007) Am. Nat. , vol.169
    • Cameron, E.1    Day, T.2    Rowe, L.3
  • 6
    • 0024584913 scopus 로고
    • Molecular modeling of protein-glycosaminoglycan interactions
    • Cardin A D and Weintraub H J 1989 Molecular modeling of protein-glycosaminoglycan interactions; Arteriosclerosis 9 21-32
    • (1989) Arteriosclerosis , vol.9 , pp. 21-32
    • Cardin, A.D.1    Weintraub, H.J.2
  • 7
    • 0017263315 scopus 로고
    • Characterization of the proteinase inhibitors from bull seminal plasma and spermatozoa
    • Cechova D and Fritz H 1976 Characterization of the proteinase inhibitors from bull seminal plasma and spermatozoa; Hoppe Seylers Z. Physiol. Chem. 357 401-408
    • (1976) Hoppe Seylers Z. Physiol. Chem. , vol.357 , pp. 401-408
    • Cechova, D.1    Fritz, H.2
  • 9
    • 24644503098 scopus 로고    scopus 로고
    • Blast2GO: A universal tool for annotation, visualization and analysis in functional genomics research
    • Conesa A, Gotz S, Garcia-Gomez J M, Terol J, Talon M and Robles M 2005 Blast2GO: a universal tool for annotation, visualization and analysis in functional genomics research; Bioinformatics 21 3674-3676
    • (2005) Bioinformatics , vol.21 , pp. 3674-3676
    • Conesa, A.1    Gotz, S.2    Garcia-Gomez, J.M.3    Terol, J.4    Talon, M.5    Robles, M.6
  • 11
    • 0025983879 scopus 로고
    • Functionally active protein C inhibitor/plasminogen activator inhibitor-3 (PCI/PAI-3) is secreted in seminal vesicles, occurs at high concentrations in human seminal plasma and complexes with prostate-specific antigen
    • Espana F, Gilabert J, Estelles A, Romeu A, Aznar J and Cabo A 1991 Functionally active protein C inhibitor/plasminogen activator inhibitor-3 (PCI/PAI-3) is secreted in seminal vesicles, occurs at high concentrations in human seminal plasma and complexes with prostate-specific antigen; Thromb. Res. 64 309-320
    • (1991) Thromb. Res. , vol.64 , pp. 309-320
    • Espana, F.1    Gilabert, J.2    Estelles, A.3    Romeu, A.4    Aznar, J.5    Cabo, A.6
  • 12
    • 0031880170 scopus 로고    scopus 로고
    • Molecular mechanisms of sperm-egg interactions and egg activation
    • Evans J P and Kopf G S 1998 Molecular mechanisms of sperm-egg interactions and egg activation; Andrologia 30 297-307
    • (1998) Andrologia , vol.30 , pp. 297-307
    • Evans, J.P.1    Kopf, G.S.2
  • 13
    • 0025040329 scopus 로고
    • Amino acid sequence elucidation of human acrosin-trypsin inhibitor (HUSI-II) reveals that kazal-type proteinase inhibitors are structurally related to beta-subunits of glycoprotein hormones
    • Fink E, Hehlein-Fink C and Eulitz M 1990 Amino acid sequence elucidation of human acrosin-trypsin inhibitor (HUSI-II) reveals that Kazal-type proteinase inhibitors are structurally related to beta-subunits of glycoprotein hormones; FEBS Lett. 270 222-224
    • (1990) FEBS Lett. , vol.270 , pp. 222-224
    • Fink, E.1    Hehlein-Fink, C.2    Eulitz, M.3
  • 14
    • 0017242086 scopus 로고
    • Proteinase inhibitors from boar seminal plasma
    • Fritz H, Tschesche H and Fink E 1976 Proteinase inhibitors from boar seminal plasma; Methods Enzymol. 45 834-847
    • (1976) Methods Enzymol , vol.45 , pp. 834-847
    • Fritz, H.1    Tschesche, H.2    Fink, E.3
  • 16
    • 0019826523 scopus 로고
    • Immunological identification of lactoferrin as a shared antigen on radioiodinated human sperm surface and in radioiodinated human seminal plasma
    • Goodman S A and Young L G 1981 Immunological identification of lactoferrin as a shared antigen on radioiodinated human sperm surface and in radioiodinated human seminal plasma; J. Reprod. Immunol. 3 99-108
    • (1981) J. Reprod. Immunol. , vol.3 , pp. 99-108
    • Goodman, S.A.1    Young, L.G.2
  • 17
    • 0020363444 scopus 로고
    • Structural comparisons among glycosaminoglycans to promote an acrosome reaction in bovine spermatozoa
    • Handrow R R, Lenz R W and Ax R L 1982 Structural comparisons among glycosaminoglycans to promote an acrosome reaction in bovine spermatozoa; Biochem. Biophys. Res. Commun. 107 1326-1332
    • (1982) Biochem. Biophys. Res. Commun. , vol.107 , pp. 1326-1332
    • Handrow, R.R.1    Lenz, R.W.2    Ax, R.L.3
  • 18
    • 34547828095 scopus 로고    scopus 로고
    • Proteomic approach for purification of seminal plasma proteins involved in tumor proliferation
    • Hassan M I, Kumar V, Kashav T, Alam N, Singh T P and Yadav S 2007 Proteomic approach for purification of seminal plasma proteins involved in tumor proliferation; J. Sep. Sci. 30 1979-1988
    • (2007) J. Sep. Sci. , vol.30 , pp. 1979-1988
    • Hassan, M.I.1    Kumar, V.2    Kashav, T.3    Alam, N.4    Singh, T.P.5    Yadav, S.6
  • 19
    • 0344172844 scopus 로고    scopus 로고
    • Inhibitors of chymase as mast cell-stabilizing agents: Contribution of chymase in the activation of human mast cells
    • He S, Gaca M D, McEuen A R and Walls A F 1999 Inhibitors of chymase as mast cell-stabilizing agents: contribution of chymase in the activation of human mast cells; J. Pharmacol. Exp. Ther. 291 517-523
    • (1999) J. Pharmacol. Exp. Ther. , vol.291 , pp. 517-523
    • He, S.1    Gaca, M.D.2    McEuen, A.R.3    Walls, A.F.4
  • 22
    • 0018340741 scopus 로고
    • Effects of human seminal plasma on fertilizing capacity of human spermatozoa
    • Kanwar K C, Yanagimachi R and Lopata A 1979 Effects of human seminal plasma on fertilizing capacity of human spermatozoa; Fertil. Steril. 31 321-327
    • (1979) Fertil. Steril. , vol.31 , pp. 321-327
    • Kanwar, K.C.1    Yanagimachi, R.2    Lopata, A.3
  • 23
    • 0034866204 scopus 로고    scopus 로고
    • Heparin-binding proteins of human seminal plasma homologous with boar spermadhesins
    • Kraus M, Ticha M and Jonakova V 2001 Heparin-binding proteins of human seminal plasma homologous with boar spermadhesins; J. Reprod. Immunol. 51 131-144
    • (2001) J. Reprod. Immunol. , vol.51 , pp. 131-144
    • Kraus, M.1    Ticha, M.2    Jonakova, V.3
  • 24
    • 56449129804 scopus 로고    scopus 로고
    • Heparin-binding proteins of human seminal plasma: Purification and characterization
    • Kumar V, Hassan M I, Kashav T, Singh T P and Yadav S 2008 Heparin-binding proteins of human seminal plasma: purification and characterization; Mol. Reprod. Dev. 75 1767-1774
    • (2008) Mol. Reprod. Dev. , vol.75 , pp. 1767-1774
    • Kumar, V.1    Hassan, M.I.2    Kashav, T.3    Singh, T.P.4    Yadav, S.5
  • 25
    • 0020536794 scopus 로고
    • Chondroitin sulfate facilitates an acrosome reaction in bovine spermatozoa as evidenced by light microscopy, electron microscopy and in vitro fertilization
    • Lenz R W, Ball G D, Lohse J K, First N L and Ax R L 1983 Chondroitin sulfate facilitates an acrosome reaction in bovine spermatozoa as evidenced by light microscopy, electron microscopy and in vitro fertilization; Biol. Reprod. 28 683-690
    • (1983) Biol. Reprod , vol.28 , pp. 683-690
    • Lenz, R.W.1    Ball, G.D.2    Lohse, J.K.3    First, N.L.4    Ax, R.L.5
  • 26
    • 0036899102 scopus 로고    scopus 로고
    • KRAB zinc finger proteins: An analysis of the molecular mechanisms governing their increase in numbers and complexity during evolution
    • Looman C, Abrink M, Mark C and Hellman L 2002 KRAB zinc finger proteins: an analysis of the molecular mechanisms governing their increase in numbers and complexity during evolution; Mol. Biol. Evol. 19 2118-2130
    • (2002) Mol. Biol. Evol. , vol.19 , pp. 2118-2130
    • Looman, C.1    Abrink, M.2    Mark, C.3    Hellman, L.4
  • 27
    • 0027978954 scopus 로고
    • Delineation of the glycosaminoglycan-binding site in human inflammatory response protein lactoferrin
    • Mann D M, Romm E and Migliorini M 1994 Delineation of the glycosaminoglycan-binding site in human inflammatory response protein lactoferrin; J. Biol. Chem. 269 23661-23667
    • (1994) J. Biol. Chem. , vol.269 , pp. 23661-23667
    • Mann, D.M.1    Romm, E.2    Migliorini, M.3
  • 28
    • 0025284297 scopus 로고
    • Heparin-binding proteins from seminal plasma bind to bovine spermatozoa and modulate capacitation by heparin
    • Miller D J, Winer M A and Ax R L 1990 Heparin-binding proteins from seminal plasma bind to bovine spermatozoa and modulate capacitation by heparin; Biol. Reprod. 42 899-915
    • (1990) Biol. Reprod. , vol.42 , pp. 899-915
    • Miller, D.J.1    Winer, M.A.2    Ax, R.L.3
  • 29
    • 0023492126 scopus 로고
    • Isolation and characterization of seminal fluid proteins that bind heparin
    • Miller D J, First N L and Ax R L 1987 Isolation and characterization of seminal fluid proteins that bind heparin; Adv. Exp. Med. Biol. 219 597-601
    • (1987) Adv. Exp. Med. Biol. , vol.219 , pp. 597-601
    • Miller, D.J.1    First, N.L.2    Ax, R.L.3
  • 30
    • 0031712111 scopus 로고    scopus 로고
    • Effect of seminal plasma on capacitation and hyperactivation in human spermatozoa
    • Mortimer S T, Swan M A and Mortimer D 1998 Effect of seminal plasma on capacitation and hyperactivation in human spermatozoa; Hum. Reprod. 13 2139-2146
    • (1998) Hum. Reprod. , vol.13 , pp. 2139-2146
    • Mortimer, S.T.1    Swan, M.A.2    Mortimer, D.3
  • 31
    • 34447635697 scopus 로고    scopus 로고
    • New insights into the molecular mechanisms of sperm-egg interaction
    • Nixon B, Aitken R J and McLaughlin E A 2007 New insights into the molecular mechanisms of sperm-egg interaction; Cell Mol. Life Sci. 64 1805-1823
    • (2007) Cell Mol. Life Sci. , vol.64 , pp. 1805-1823
    • Nixon, B.1    Aitken, R.J.2    McLaughlin, E.A.3
  • 33
    • 33745104040 scopus 로고    scopus 로고
    • Large-scale and high-confidence proteomic analysis of human seminal plasma
    • Pilch B and Mann M 2006 Large-scale and high-confidence proteomic analysis of human seminal plasma; Genome Biol. 7 R40
    • (2006) Genome Biol. , vol.7
    • Pilch, B.1    Mann, M.2
  • 34
    • 34250547694 scopus 로고
    • Enzyme localization in proteins separated by paper electrophoresis in human seminal plasma
    • Povoa H Jr 1962 Enzyme localization in proteins separated by paper electrophoresis in human seminal plasma; Experientia 18 552
    • (1962) Experientia , vol.18 , pp. 552
    • Povoa Jr., H.1
  • 35
    • 0037150651 scopus 로고    scopus 로고
    • Penetration, adhesion, and fusion in mammalian sperm-egg interaction
    • Primakoff P and Myles D G 2002 Penetration, adhesion, and fusion in mammalian sperm-egg interaction; Science 296 2183-2185
    • (2002) Science , vol.296 , pp. 2183-2185
    • Primakoff, P.1    Myles, D.G.2
  • 37
    • 0021173834 scopus 로고
    • Posttesticular surface modifications and contributions of reproductive tract fluids to the surface polypeptide composition of boar spermatozoa
    • Russell L D, Peterson R N, Hunt W and Strack L E 1984 Posttesticular surface modifications and contributions of reproductive tract fluids to the surface polypeptide composition of boar spermatozoa; Biol. Reprod. 30 959-978
    • (1984) Biol. Reprod. , vol.30 , pp. 959-978
    • Russell, L.D.1    Peterson, R.N.2    Hunt, W.3    Strack, L.E.4
  • 38
    • 0031002920 scopus 로고    scopus 로고
    • Heparin binding and oligomerization of hepatocyte growth factor/scatter factor isoforms. Heparan sulfate glycosaminoglycan requirement for met binding and signaling
    • Sakata H, Stahl S J, Taylor W G, Rosenberg J M, Sakaguchi K, Wingfield P T and Rubin J S 1997 Heparin binding and oligomerization of hepatocyte growth factor/scatter factor isoforms. Heparan sulfate glycosaminoglycan requirement for Met binding and signaling; J. Biol. Chem. 272 9457-9463
    • (1997) J. Biol. Chem. , vol.272 , pp. 9457-9463
    • Sakata, H.1    Stahl, S.J.2    Taylor, W.G.3    Rosenberg, J.M.4    Sakaguchi, K.5    Wingfield, P.T.6    Rubin, J.S.7
  • 39
    • 0017245826 scopus 로고
    • Acid-stable proteinase inhibitors from human seminal plasma
    • Schiessler H, Fink E and Fritz H 1976 Acid-stable proteinase inhibitors from human seminal plasma; Methods Enzymol. 45 847-859
    • (1976) Methods Enzymol , vol.45 , pp. 847-859
    • Schiessler, H.1    Fink, E.2    Fritz, H.3
  • 40
    • 0029897025 scopus 로고    scopus 로고
    • Heparin induces dimerization and confers proliferative activity onto the hepatocyte growth factor antagonists NK1 and NK2
    • Schwall R H, Chang L Y, Godowski P J, Kahn D W, Hillan K J, Bauer K D and Zioncheck T F 1996 Heparin induces dimerization and confers proliferative activity onto the hepatocyte growth factor antagonists NK1 and NK2; J. Cell Biol. 133 709-718
    • (1996) J. Cell Biol. , vol.133 , pp. 709-718
    • Schwall, R.H.1    Chang, L.Y.2    Godowski, P.J.3    Kahn, D.W.4    Hillan, K.J.5    Bauer, K.D.6    Zioncheck, T.F.7
  • 41
    • 33846627841 scopus 로고    scopus 로고
    • The interaction among protein C inhibitor, prostate-specific antigen, and the semenogelin system
    • Suzuki K, Kise H, Nishioka J and Hayashi 2007 The interaction among protein C inhibitor, prostate-specific antigen, and the semenogelin system; Semin. Thromb. Hemost. 33 46-52
    • (2007) Semin. Thromb. Hemost. , vol.33 , pp. 46-52
    • Suzuki, K.1    Kise, H.2    Nishioka, J.3    Hayashi4
  • 43
    • 0346274978 scopus 로고    scopus 로고
    • KRAB-containing zinc-finger repressor proteins
    • Urrutia R 2003 KRAB-containing zinc-finger repressor proteins; Genome Biol. 4 231
    • (2003) Genome Biol. , vol.4 , pp. 231
    • Urrutia, R.1
  • 45
    • 0021870401 scopus 로고
    • A kunitz type of proteinase inhibitor isolated from boar seminal vesicle fluid
    • Veselsky L, Jonakova V and Cechova D 1985 A Kunitz type of proteinase inhibitor isolated from boar seminal vesicle fluid; Andrologia 17 352-358
    • (1985) Andrologia , vol.17 , pp. 352-358
    • Veselsky, L.1    Jonakova, V.2    Cechova, D.3
  • 46
    • 0029846488 scopus 로고    scopus 로고
    • Structural domains of heparan sulphate for specific recognition of the C-terminal heparin-binding domain of human plasma fibronectin (HEPII)
    • Walker A and Gallagher J T 1996 Structural domains of heparan sulphate for specific recognition of the C-terminal heparin-binding domain of human plasma fibronectin (HEPII); Biochem. J. 317 871-877
    • (1996) Biochem. J. , vol.317 , pp. 871-877
    • Walker, A.1    Gallagher, J.T.2
  • 47
    • 0033593530 scopus 로고    scopus 로고
    • Mammalian fertilization: Molecular aspects of gamete adhesion, exocytosis, and fusion
    • Wassarman P M 1999 Mammalian fertilization: molecular aspects of gamete adhesion, exocytosis, and fusion; Cell 96 175-183
    • (1999) Cell , vol.96 , pp. 175-183
    • Wassarman, P.M.1
  • 48
    • 34547850913 scopus 로고    scopus 로고
    • Mechanism of sperm-zona pellucida penetration during mammalian fertilization: 26S proteasome as a candidate egg coat lysine
    • Yi Y J, Manandhar G, Oko R J, Breed W G and Sutovsky P 2007 Mechanism of sperm-zona pellucida penetration during mammalian fertilization: 26S proteasome as a candidate egg coat lysine; Soc. Reprod. Fertil. Suppl. 63 385-408
    • (2007) Soc. Reprod. Fertil. , vol.63 , Issue.SUPPL. , pp. 385-408
    • Yi, Y.J.1    Manandhar, G.2    Oko, R.J.3    Breed, W.G.4    Sutovsky, P.5


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