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Volumn 31, Issue 1, 2014, Pages 51-60

Changes in fucosylation of human seminal IgG and secretory component of IgA in leukocytospermic patients

Author keywords

Fucosylation; Immunoglobulin G; Leukocytospermia; Male infertility; Secretory component

Indexed keywords

FUCOSE; IMMUNOGLOBULIN A; IMMUNOGLOBULIN G; LECTIN;

EID: 84893367312     PISSN: 02820080     EISSN: 15734986     Source Type: Journal    
DOI: 10.1007/s10719-013-9501-y     Document Type: Article
Times cited : (15)

References (60)
  • 3
    • 0034175752 scopus 로고    scopus 로고
    • Does leukocytospermia associate with poor semen parameters and sperm functions in male infertility? the role of different seminal leukocyte concentrations
    • 1:STN:280:DC%2BD3c7ptFOjsQ%3D%3D 10725581 10.1016/S0301-2115(99)00204-3
    • Kaleli, S., Oçer, F., Irez, T., Budak, E., Aksu, M.F.: Does leukocytospermia associate with poor semen parameters and sperm functions in male infertility? The role of different seminal leukocyte concentrations. Eur. J. Obstet. Gynecol. Reprod. Biol. 89, 185-191 (2000)
    • (2000) Eur. J. Obstet. Gynecol. Reprod. Biol. , vol.89 , pp. 185-191
    • Kaleli, S.1    Oçer, F.2    Irez, T.3    Budak, E.4    Aksu, M.F.5
  • 4
    • 0018923182 scopus 로고
    • Diagnosis of accessory gland infection and its possible role in male infertility
    • 1:STN:280:DyaL3M%2Fgs1Sjtw%3D%3D 7409893 10.1111/j.1365-2605.1980. tb00093.x
    • Comhaire, F., Verschraegen, G., Vermeulen, L.: Diagnosis of accessory gland infection and its possible role in male infertility. Int. J. Androl. 3, 32-45 (1980)
    • (1980) Int. J. Androl. , vol.3 , pp. 32-45
    • Comhaire, F.1    Verschraegen, G.2    Vermeulen, L.3
  • 6
    • 0029084014 scopus 로고
    • Seminal leukocytes: Passengers, terrorists or good samaritans?
    • 1:STN:280:DyaK28%2FjtlWgug%3D%3D 8582971
    • Aitken, R.J., Baker, H.W.: Seminal leukocytes: passengers, terrorists or good samaritans? Hum. Reprod. 10, 1736-1739 (1995)
    • (1995) Hum. Reprod. , vol.10 , pp. 1736-1739
    • Aitken, R.J.1    Baker, H.W.2
  • 7
    • 0034941928 scopus 로고    scopus 로고
    • Relationship between seminal white blood cell counts and oxidative stress in men treated at an infertility clinic
    • 1:STN:280:DC%2BD38%2FitFarug%3D%3D 11451354
    • Sharma, R.K., Pasqualalotto, A.E., Nelson, D.R., Thomas Jr., A.J., Agarwal, A.: Relationship between seminal white blood cell counts and oxidative stress in men treated at an infertility clinic. J. Androl. 22, 575-583 (2001)
    • (2001) J. Androl. , vol.22 , pp. 575-583
    • Sharma, R.K.1    Pasqualalotto, A.E.2    Nelson, D.R.3    Thomas, Jr.A.J.4    Agarwal, A.5
  • 8
    • 0042885757 scopus 로고    scopus 로고
    • The limit of leucocytospermia from the microbiological viewpoint
    • 14535854
    • Punab, M., Lõivukene, K., Kermes, K., Mändar, R.: The limit of leucocytospermia from the microbiological viewpoint. Andrologia 35, 271-278 (2003)
    • (2003) Andrologia , vol.35 , pp. 271-278
    • Punab, M.1    Lõivukene, K.2    Kermes, K.3    Mändar, R.4
  • 9
    • 28344457575 scopus 로고    scopus 로고
    • Effects of leukocytospermia on semen parameters and outcomes of intracytoplasmic sperm injection
    • 16300665 10.1111/j.1365-2605.2005.00562.x
    • Yilmaz, S., Koyuturk, M., Kilic, G., Alpak, O., Aytoz, A.: Effects of leukocytospermia on semen parameters and outcomes of intracytoplasmic sperm injection. Int. J. Androl. 28, 337-342 (2005)
    • (2005) Int. J. Androl. , vol.28 , pp. 337-342
    • Yilmaz, S.1    Koyuturk, M.2    Kilic, G.3    Alpak, O.4    Aytoz, A.5
  • 10
    • 0031823336 scopus 로고    scopus 로고
    • Quantitation of the oligosaccharides of human serum IgG from patients with rheumatoid arthritis: A critical evaluation of different methods
    • 1:CAS:528:DyaK1cXjvVSksLk%3D 9692845 10.1016/S0022-1759(98)00032-5
    • Routier, F.H., Hounsell, E.F., Rudd, P.M., Takahashi, N., Bond, A., Hay, F.C., Alavi, A., Axford, J.S., Jefferis, R.: Quantitation of the oligosaccharides of human serum IgG from patients with rheumatoid arthritis: a critical evaluation of different methods. J. Immunol. Methods 213, 113-130 (1998)
    • (1998) J. Immunol. Methods , vol.213 , pp. 113-130
    • Routier, F.H.1    Hounsell, E.F.2    Rudd, P.M.3    Takahashi, N.4    Bond, A.5    Hay, F.C.6    Alavi, A.7    Axford, J.S.8    Jefferis, R.9
  • 12
    • 0037178791 scopus 로고    scopus 로고
    • Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human Fcgamma RIII and antibody-dependent cellular toxicity
    • 1:CAS:528:DC%2BD38XlvV2isrk%3D 11986321 10.1074/jbc.M202069200
    • Shields, R.L., Lai, J., Keck, R., O'Connell, L.Y., Hong, K., Meng, Y.G., Weikert, S.H., Presta, L.G.: Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human Fcgamma RIII and antibody-dependent cellular toxicity. J. Biol. Chem. 277, 26733-26740 (2002)
    • (2002) J. Biol. Chem. , vol.277 , pp. 26733-26740
    • Shields, R.L.1    Lai, J.2    Keck, R.3    O'Connell, L.Y.4    Hong, K.5    Meng, Y.G.6    Weikert, S.H.7    Presta, L.G.8
  • 14
    • 0033401533 scopus 로고    scopus 로고
    • Regulation of the formation and external transport of secretory immunoglobulins
    • 1:CAS:528:DC%2BD3cXnvF2ksQ%3D%3D 10647747
    • Norderhaug, I.N., Johannes, F.E., Schijerven, H., Brandtzaeg, P.: Regulation of the formation and external transport of secretory immunoglobulins. Crit. Rev. Immunol. 19, 481-508 (1999)
    • (1999) Crit. Rev. Immunol. , vol.19 , pp. 481-508
    • Norderhaug, I.N.1    Johannes, F.E.2    Schijerven, H.3    Brandtzaeg, P.4
  • 15
    • 31144457922 scopus 로고    scopus 로고
    • The function of immunoglobulin A in immunity
    • 1:CAS:528:DC%2BD28XhsFKjsr0%3D 16362985 10.1002/path.1877
    • Woof, J.M., Kerr, M.A.: The function of immunoglobulin A in immunity. J. Pathol. 208, 270-282 (2006)
    • (2006) J. Pathol. , vol.208 , pp. 270-282
    • Woof, J.M.1    Kerr, M.A.2
  • 16
    • 0031830375 scopus 로고    scopus 로고
    • Immunoglobulin A supplementation abrogates bacterial translocation and preserves the architecture of the intestinal epithelium
    • 1:STN:280:DyaK1czntFCjtQ%3D%3D 9706150 10.1016/S0039-6060(98)70132-1
    • Dickinson, E.C., Gorga, J.C., Garrett, M., Tuncer, R., Boyle, P., Watkins, S.C., Alber, S.M., Parizhskaya, M., Trucco, M., Rowe, M.I., Ford, H.R.: Immunoglobulin A supplementation abrogates bacterial translocation and preserves the architecture of the intestinal epithelium. Surgery 124, 284-290 (1998)
    • (1998) Surgery , vol.124 , pp. 284-290
    • Dickinson, E.C.1    Gorga, J.C.2    Garrett, M.3    Tuncer, R.4    Boyle, P.5    Watkins, S.C.6    Alber, S.M.7    Parizhskaya, M.8    Trucco, M.9    Rowe, M.I.10    Ford, H.R.11
  • 18
    • 84882872365 scopus 로고    scopus 로고
    • Immunoglobulin transport and the polymeric immunoglobulin receptor
    • J. Mestecky J. Bienenstock M.E. Lamm L. Mayer J.R. McGhee W. Strober (eds) Elsevier/Academic Press Amsterdam 10.1016/B978-012491543-5/50016-4
    • Kaetzel, C.S., Mostov, K.: Immunoglobulin transport and the polymeric immunoglobulin receptor. In: Mestecky, J., Bienenstock, J., Lamm, M.E., Mayer, L., McGhee, J.R., Strober, W. (eds.) Mucosal Immunology, pp. 211-250. Elsevier/Academic Press, Amsterdam (2005)
    • (2005) Mucosal Immunology , pp. 211-250
    • Kaetzel, C.S.1    Mostov, K.2
  • 19
    • 0032533818 scopus 로고    scopus 로고
    • Secretory component delays the conversion of secretory IgA antigen-binding component F(ab')2: A possible implication for muscosal defence
    • 1:CAS:528:DyaK1cXnsVOrurc%3D 9820520
    • Crottet, P., Corthésy, B.: Secretory component delays the conversion of secretory IgA antigen-binding component F(ab')2: a possible implication for muscosal defence. J. Immunol. 161, 5445-5453 (1998)
    • (1998) J. Immunol. , vol.161 , pp. 5445-5453
    • Crottet, P.1    Corthésy, B.2
  • 20
    • 23344449309 scopus 로고    scopus 로고
    • Mucosal immunoglobulins
    • 1:CAS:528:DC%2BD2MXhtVWjsb7F 16048542 10.1111/j.0105-2896.2005.00290.x
    • Woof, J.M., Mestecky, J.: Mucosal immunoglobulins. Immunol. Rev. 206, 64-82 (2005)
    • (2005) Immunol. Rev. , vol.206 , pp. 64-82
    • Woof, J.M.1    Mestecky, J.2
  • 22
    • 0013797229 scopus 로고
    • Immunochemical quantitation of antigens by single radial immunodiffusion
    • 1:CAS:528:DyaF2MXltVaitrg%3D 4956917 10.1016/0019-2791(65)90004-2
    • Mancini, G., Carbonara, A.O., Heremans, J.F.: Immunochemical quantitation of antigens by single radial immunodiffusion. Immunochemistry 2, 235-254 (1965)
    • (1965) Immunochemistry , vol.2 , pp. 235-254
    • Mancini, G.1    Carbonara, A.O.2    Heremans, J.F.3
  • 23
    • 80955139701 scopus 로고    scopus 로고
    • 1 -acid glycoprotein associated with leukocytospermia of infertile men
    • 1:CAS:528:DC%2BC3MXhsVSqtLfI 22048274 10.1155/2011/914710
    • 1 -acid glycoprotein associated with leukocytospermia of infertile men. Dis. Markers 31, 317-325 (2011)
    • (2011) Dis. Markers , vol.31 , pp. 317-325
    • Kratz, E.M.1    Faundez, R.2    Katnik-Prastowska, I.3
  • 24
    • 0021893594 scopus 로고
    • Fractionation of L-fucose-containing oligosaccharides on immobilized Aleuria aurantia lectin
    • 1:CAS:528:DyaL2MXktVejtbk%3D 3988732
    • Yamashita, K., Kochibe, N., Ohkura, T., Ueda, I., Kobata, A.: Fractionation of L-fucose-containing oligosaccharides on immobilized Aleuria aurantia lectin. J. Biol. Chem. 260, 4688-4693 (1985)
    • (1985) J. Biol. Chem. , vol.260 , pp. 4688-4693
    • Yamashita, K.1    Kochibe, N.2    Ohkura, T.3    Ueda, I.4    Kobata, A.5
  • 25
    • 0034714160 scopus 로고    scopus 로고
    • Structural basis of carbohydrate recognition by lectin II from Ulex europaeus, a protein with a promiscuous carbohydrate-binding site
    • 1:CAS:528:DC%2BD3cXmtVKlsrw%3D 10966800 10.1006/jmbi.2000.4016
    • Loris, R., De Greve, H., Dao-Thi, M.H., Messens, J., Imberty, A., Wyns, L.: Structural basis of carbohydrate recognition by lectin II from Ulex europaeus, a protein with a promiscuous carbohydrate-binding site. J. Mol. Biol. 301, 987-1002 (2000)
    • (2000) J. Mol. Biol. , vol.301 , pp. 987-1002
    • Loris, R.1    De Greve, H.2    Dao-Thi, M.H.3    Messens, J.4    Imberty, A.5    Wyns, L.6
  • 26
    • 0033980308 scopus 로고    scopus 로고
    • Alpha(1,2)-fucosylation prevents sialyl Lewis x expression and E-selectin-mediated adhesion of fucosyltransferase VII-transfected cells
    • 1:CAS:528:DC%2BD3cXlt1WksQ%3D%3D 10601850 10.1046/j.1432-1327.2000.00958. x
    • Zerfaoui, M., Fukuda, M., Sbarra, V., Lombardo, D., El-Battari, A.: Alpha(1,2)-fucosylation prevents sialyl Lewis x expression and E-selectin-mediated adhesion of fucosyltransferase VII-transfected cells. Eur. J. Biochem. 267, 53-61 (2000)
    • (2000) Eur. J. Biochem. , vol.267 , pp. 53-61
    • Zerfaoui, M.1    Fukuda, M.2    Sbarra, V.3    Lombardo, D.4    El-Battari, A.5
  • 27
    • 0031059280 scopus 로고    scopus 로고
    • Immobilized Lotus tetragonolobus agglutinin binds oligosaccharides containing the Le(x) determinant
    • 1:CAS:528:DyaK2sXitVGlurg%3D 9076513 10.1023/A:1018508914551
    • Yan, L., Wilkins, P.P., Alvarez-Manilla, G., Do, S.I., Smith, D.F., Cummings, R.D.: Immobilized Lotus tetragonolobus agglutinin binds oligosaccharides containing the Le(x) determinant. Glycoconj. J. 14, 45-55 (1997)
    • (1997) Glycoconj. J. , vol.14 , pp. 45-55
    • Yan, L.1    Wilkins, P.P.2    Alvarez-Manilla, G.3    Do, S.I.4    Smith, D.F.5    Cummings, R.D.6
  • 28
    • 0001953630 scopus 로고
    • Investigating the glycosylation of normal and ovarian cancer haptoglobins using digoxigenin-labeled lectins
    • Ka̧tnik, I., Jadach, J., Krotkiewski, H., Gerber, J.: Investigating the glycosylation of normal and ovarian cancer haptoglobins using digoxigenin-labeled lectins. Glycosyl. Dis. 1, 97-104 (1994)
    • (1994) Glycosyl. Dis. , vol.1 , pp. 97-104
    • Ka̧tnik, I.1    Jadach, J.2    Krotkiewski, H.3    Gerber, J.4
  • 29
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the fead of bacteriophage T4
    • 1:CAS:528:DC%2BD3MXlsFags7s%3D 5432063 10.1038/227680a0
    • Laemmli, U.K.: Cleavage of structural proteins during the assembly of the fead of bacteriophage T4. Nature 227, 680-685 (1970)
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 30
    • 77955559567 scopus 로고    scopus 로고
    • Terminal monosaccharide screening of synovial immunoglobulins G and A for the early detection of rheumatoid arthritis
    • 1:CAS:528:DC%2BC3cXpt12msr4%3D 19816690 10.1007/s00296-009-1139-5
    • Kratz, E.M., Borysewicz, K., Ka̧tnik-Prastowska, I.: Terminal monosaccharide screening of synovial immunoglobulins G and A for the early detection of rheumatoid arthritis. Rheumatol. Int. 30, 1285-1292 (2010)
    • (2010) Rheumatol. Int. , vol.30 , pp. 1285-1292
    • Kratz, E.M.1    Borysewicz, K.2    Ka̧tnik-Prastowska, I.3
  • 32
    • 33947591554 scopus 로고    scopus 로고
    • Fucosylation in synovial fluid as a novel clinical marker for differentiating joint diseases-A preliminary study
    • 1:STN:280:DC%2BD2s3htlOmuw%3D%3D 17417997
    • Ferens-Sieczkowska, M., Kossowska, B., Gancarz, R., Dudzik, D., Knas, M., Popko, J., Zwierz, K.: Fucosylation in synovial fluid as a novel clinical marker for differentiating joint diseases-a preliminary study. Clin. Exp. Rheumatol. 25, 92-95 (2007)
    • (2007) Clin. Exp. Rheumatol. , vol.25 , pp. 92-95
    • Ferens-Sieczkowska, M.1    Kossowska, B.2    Gancarz, R.3    Dudzik, D.4    Knas, M.5    Popko, J.6    Zwierz, K.7
  • 34
    • 0035208122 scopus 로고    scopus 로고
    • Localization of sperm ligand carbohydrate chains in pig zona pellucida glycoproteins
    • 1:CAS:528:DC%2BD3cXptVeitb4%3D 11114588 10.1159/000016807
    • Nakano, M., Yonezawa, N.: Localization of sperm ligand carbohydrate chains in pig zona pellucida glycoproteins. Cells Tissues Organs 168, 65-75 (2001)
    • (2001) Cells Tissues Organs , vol.168 , pp. 65-75
    • Nakano, M.1    Yonezawa, N.2
  • 35
    • 0020580561 scopus 로고
    • Immunoglobulin in seminal fluid of fertile, infertile, vasectomy and vasectomy reversal patients
    • 6842728
    • Fowler Jr., J.E., Mariano, M.: Immunoglobulin in seminal fluid of fertile, infertile, vasectomy and vasectomy reversal patients. J. Urol. 129, 869-872 (1983)
    • (1983) J. Urol. , vol.129 , pp. 869-872
    • Fowler, Jr.J.E.1    Mariano, M.2
  • 36
    • 0031932967 scopus 로고    scopus 로고
    • Seminal plasma immunoglobulin concentrations in autoimmune male subfertility
    • 1:CAS:528:DyaK1cXhs1Gns70%3D 9571571 10.1016/S0165-0378(97)00080-6
    • Luckas, M.J.M., Buckett, W.M., Aird, I.A., Johnson, P.M., Lewis-Jones, D.I.: Seminal plasma immunoglobulin concentrations in autoimmune male subfertility. J. Reprod. Immunol. 37, 171-180 (1998)
    • (1998) J. Reprod. Immunol. , vol.37 , pp. 171-180
    • Luckas, M.J.M.1    Buckett, W.M.2    Aird, I.A.3    Johnson, P.M.4    Lewis-Jones, D.I.5
  • 37
    • 0032146864 scopus 로고    scopus 로고
    • Influence of sperm surface antibodies on spontaneous pregnancy rates
    • 1:STN:280:DyaK1czlvFChsQ%3D%3D 9696234 10.1016/S0015-0282(98)00154-X
    • Abshagen, K., Behre, H.M., Cooper, T.G., Nieschlag, E.: Influence of sperm surface antibodies on spontaneous pregnancy rates. Fertil. Steril. 70, 355-356 (1998)
    • (1998) Fertil. Steril. , vol.70 , pp. 355-356
    • Abshagen, K.1    Behre, H.M.2    Cooper, T.G.3    Nieschlag, E.4
  • 38
    • 38649143213 scopus 로고    scopus 로고
    • Double knockdown of alpha1,6-fucosyltransferase (FUT8) and GDP-mannose 4,6-dehydratase (GMD) in antibody-producing cells: A new strategy for generating fully non-fucosylated therapeutic antibodies with enhanced ADCC
    • 2216013 18047682 10.1186/1472-6750-7-84
    • Imai-Nishiya, H., Mori, K., Inoue, M., Wakitani, M., Iida, S., Shitara, K., Satoh, M.: Double knockdown of alpha1,6-fucosyltransferase (FUT8) and GDP-mannose 4,6-dehydratase (GMD) in antibody-producing cells: a new strategy for generating fully non-fucosylated therapeutic antibodies with enhanced ADCC. BMC Biotechnol. 7, 84 (2007)
    • (2007) BMC Biotechnol. , vol.7 , pp. 84
    • Imai-Nishiya, H.1    Mori, K.2    Inoue, M.3    Wakitani, M.4    Iida, S.5    Shitara, K.6    Satoh, M.7
  • 39
    • 33646070900 scopus 로고    scopus 로고
    • Modulation of therapeutic antibody effector functions by glycosylation engineering: Influence of Golgi enzyme localization domain and co-expression of heterologous beta1, 4-N-acetylglucosaminyltransferase III and Golgi alpha-mannosidase II
    • 1:CAS:528:DC%2BD28Xjt1GkurY%3D 16435400 10.1002/bit.20777
    • Ferrara, C., Brünker, P., Suter, T., Moser, S., Püntener, U., Umaña, P.: Modulation of therapeutic antibody effector functions by glycosylation engineering: influence of Golgi enzyme localization domain and co-expression of heterologous beta1, 4-N-acetylglucosaminyltransferase III and Golgi alpha-mannosidase II. Biotechnol. Bioeng. 93, 851-861 (2006)
    • (2006) Biotechnol. Bioeng. , vol.93 , pp. 851-861
    • Ferrara, C.1    Brünker, P.2    Suter, T.3    Moser, S.4    Püntener, U.5    Umaña, P.6
  • 40
    • 0346098179 scopus 로고    scopus 로고
    • History of antibody therapy for non-Hodgkin's lymphoma
    • 1:CAS:528:DC%2BD2cXhtVSitbg%3D 14710396 10.1053/j.seminoncol.2003.10.002
    • Forero, A., Lobuglio, A.F.: History of antibody therapy for non-Hodgkin's lymphoma. Semin. Oncol. 30, 1-5 (2003)
    • (2003) Semin. Oncol. , vol.30 , pp. 1-5
    • Forero, A.1    Lobuglio, A.F.2
  • 41
    • 0033427574 scopus 로고    scopus 로고
    • Fucosylation of IgG heavy chains is increased in rheumatoid arthritis
    • 1:CAS:528:DC%2BD3cXos12jtg%3D%3D 10638942 10.1016/S0009-9120(99)00060-0
    • Gornik, I., Maravić, G., Dumić, J., Flögel, M., Lauc, G.: Fucosylation of IgG heavy chains is increased in rheumatoid arthritis. Clin. Biochem. 32, 605-608 (1999)
    • (1999) Clin. Biochem. , vol.32 , pp. 605-608
    • Gornik, I.1    Maravić, G.2    Dumić, J.3    Flögel, M.4    Lauc, G.5
  • 42
    • 44849133511 scopus 로고    scopus 로고
    • Sweet and sour: The impact of sugars on disease
    • Alavi, A., Axford, J.S.: Sweet and sour: the impact of sugars on disease. Rheumatology (Oxford) 47, 760-770 (2008)
    • (2008) Rheumatology (Oxford) , vol.47 , pp. 760-770
    • Alavi, A.1    Axford, J.S.2
  • 44
    • 84879156795 scopus 로고    scopus 로고
    • Aberrant glycosylation of the anti-Thomsen-Friedenreich glycotope immunoglobulin G in gastric cancer patients
    • 1:CAS:528:DC%2BC3sXhtVGjurbO 23801858 10.3748/wjg.v19.i23.3573
    • Kodar, K., Izotova, J., Klaamas, K., Sergeyev, B., Järvekülg, L., Kurtenkov, O.: Aberrant glycosylation of the anti-Thomsen-Friedenreich glycotope immunoglobulin G in gastric cancer patients. World J. Gastroenterol. 19, 3573-3582 (2013)
    • (2013) World J. Gastroenterol. , vol.19 , pp. 3573-3582
    • Kodar, K.1    Izotova, J.2    Klaamas, K.3    Sergeyev, B.4    Järvekülg, L.5    Kurtenkov, O.6
  • 46
    • 0038495798 scopus 로고    scopus 로고
    • Fucose: Biosynthesis and biological function in mammals
    • 1:CAS:528:DC%2BD3sXks1Wqs7o%3D 12651883 10.1093/glycob/cwg054
    • Becker, D.J., Lowe, J.B.: Fucose: biosynthesis and biological function in mammals. Glycobiology 13, 41R-53R (2003)
    • (2003) Glycobiology , vol.13
    • Becker, D.J.1    Lowe, J.B.2
  • 47
    • 0025967952 scopus 로고
    • Nature of the inhibitory effect of complex saccharide moieties on the tight binding of human spermatozoa to the human zona pellucida
    • 1:STN:280:DyaK3M%2FpvFGnug%3D%3D 1702739
    • Oehninger, S., Clark, G.F., Acosta, A.A., Hodgen, G.D.: Nature of the inhibitory effect of complex saccharide moieties on the tight binding of human spermatozoa to the human zona pellucida. Fertil. Steril. 55, 165-169 (1991)
    • (1991) Fertil. Steril. , vol.55 , pp. 165-169
    • Oehninger, S.1    Clark, G.F.2    Acosta, A.A.3    Hodgen, G.D.4
  • 49
    • 0028010881 scopus 로고
    • Participation of glycosylated residues in the human sperm acrosome reaction: Possible role of N-acetylglucosaminidase
    • 1:CAS:528:DyaK2cXisVWit7w%3D 8305503 10.1016/0167-4889(94)90152-X
    • Brandelli, A., Miranda, P.V., Tezon, J.G.: Participation of glycosylated residues in the human sperm acrosome reaction: possible role of N-acetylglucosaminidase. Biochim. Biophys. Acta 1220, 299-304 (1994)
    • (1994) Biochim. Biophys. Acta , vol.1220 , pp. 299-304
    • Brandelli, A.1    Miranda, P.V.2    Tezon, J.G.3
  • 50
    • 0028003677 scopus 로고
    • A fucose-containing epitope potentially involved in gamete interaction on the human zona pellucida
    • 1:STN:280:DyaK2M%2FotFensg%3D%3D 7527423
    • Lucas, H., Bercegeay, S., Le Pendu, J., Jean, M., Mirallie, S., Barriere, P.: A fucose-containing epitope potentially involved in gamete interaction on the human zona pellucida. Hum. Reprod. 9, 1532-1538 (1994)
    • (1994) Hum. Reprod. , vol.9 , pp. 1532-1538
    • Lucas, H.1    Bercegeay, S.2    Le Pendu, J.3    Jean, M.4    Mirallie, S.5    Barriere, P.6
  • 51
    • 0028104575 scopus 로고
    • Distribution of carbohydrates in the zona pellucida of human oocytes
    • 1:CAS:528:DyaK2MXit12rt7Y%3D 7528279 10.1530/jrf.0.1020081
    • Maymon, B.B., Maymon, R., Ben-Nun, I., Ghetler, Y., Shalgi, R., Skutelsky, E.: Distribution of carbohydrates in the zona pellucida of human oocytes. J. Reprod. Fertil. 102, 81-86 (1994)
    • (1994) J. Reprod. Fertil. , vol.102 , pp. 81-86
    • Maymon, B.B.1    Maymon, R.2    Ben-Nun, I.3    Ghetler, Y.4    Shalgi, R.5    Skutelsky, E.6
  • 52
    • 0019969344 scopus 로고
    • Evidence suggesting that L-fucose is part of the recognition signal for sperm-zona pellucida attachment in mammals
    • 1:CAS:528:DyaL38Xkt1Wns7g%3D 10.1002/mrd.1120050406
    • Huang, T.T.F., Ohzu, E., Yanagimachi, R.: Evidence suggesting that L-fucose is part of the recognition signal for sperm-zona pellucida attachment in mammals. Gamete Res. 5, 355-361 (1982)
    • (1982) Gamete Res. , vol.5 , pp. 355-361
    • Huang, T.T.F.1    Ohzu, E.2    Yanagimachi, R.3
  • 54
    • 70449338884 scopus 로고    scopus 로고
    • Analysis of the human seminal plasma glycome reveals the presence of immunomodulatory carbohydrate functional groups
    • 1:CAS:528:DC%2BD1MXht1Sqt77I 19606896 10.1021/pr9001756
    • Pang, P.C., Tissot, B., Drobnis, E.Z., Morris, H.R., Dell, A., Clark, G.F.: Analysis of the human seminal plasma glycome reveals the presence of immunomodulatory carbohydrate functional groups. J. Proteome Res. 8, 4906-4915 (2009)
    • (2009) J. Proteome Res. , vol.8 , pp. 4906-4915
    • Pang, P.C.1    Tissot, B.2    Drobnis, E.Z.3    Morris, H.R.4    Dell, A.5    Clark, G.F.6
  • 55
    • 0036401130 scopus 로고    scopus 로고
    • Effects of blastocyst surface ligosaccharide LeY on secretion and expression of matrix metalloproteinase in vivo
    • Ge, C.H., Kong, Y., Wang, H., Zhu, Z.M.: Effects of blastocyst surface ligosaccharide LeY on secretion and expression of matrix metalloproteinase in vivo. Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai) 34, 45-49 (2002)
    • (2002) Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai) , vol.34 , pp. 45-49
    • Ge, C.H.1    Kong, Y.2    Wang, H.3    Zhu, Z.M.4
  • 56
    • 65649086034 scopus 로고    scopus 로고
    • LeY oligosaccharide upregulates DAG/PKC signaling pathway in the human endometrial cells
    • 1:CAS:528:DC%2BD1MXhtlCjs7bM 10.1007/s11010-009-0137-y
    • Li, Y., Ma, K., Sun, P., Liu, S., Qin, H., Zhu, Z., Wang, X., Yan, Q.: LeY oligosaccharide upregulates DAG/PKC signaling pathway in the human endometrial cells. Mol. Cel. Biochem. 331, 1-7 (2009)
    • (2009) Mol. Cel. Biochem. , vol.331 , pp. 1-7
    • Li, Y.1    Ma, K.2    Sun, P.3    Liu, S.4    Qin, H.5    Zhu, Z.6    Wang, X.7    Yan, Q.8
  • 57
    • 38349150936 scopus 로고    scopus 로고
    • Increased levels of galactose-deficient anti-Gal immunoglobulin G in the sera of hepatitis C virus-infected individuals with fibrosis and cirrhosis
    • 1:CAS:528:DC%2BD1cXhtFOktLo%3D 2224448 18045939 10.1128/JVI.01600-07
    • Mehta, A.S., Long, R.E., Comunale, M.A., Wang, M., Rodemich, L., Krakover, J., Philip, R., Marrero, J.A., Dwek, R.A., Block, T.M.: Increased levels of galactose-deficient anti-Gal immunoglobulin G in the sera of hepatitis C virus-infected individuals with fibrosis and cirrhosis. J. Virol. 82, 1259-1270 (2008)
    • (2008) J. Virol. , vol.82 , pp. 1259-1270
    • Mehta, A.S.1    Long, R.E.2    Comunale, M.A.3    Wang, M.4    Rodemich, L.5    Krakover, J.6    Philip, R.7    Marrero, J.A.8    Dwek, R.A.9    Block, T.M.10
  • 58
    • 84866385852 scopus 로고    scopus 로고
    • Aleuria Aurantia Lectin (AAL)-reactive immunoglobulin G rapidly appears in sera of animals following antigen exposure
    • 1:CAS:528:DC%2BC38XhsVSjtbfE 3443102 23024749 10.1371/journal.pone. 0044422
    • Chen, S., Lu, C., Gu, H., Mehta, A., Li, J., Romano, P.B., Horn, D., Hooper, D.C., Bazemore-Walker, C.R., Block, T.: Aleuria Aurantia Lectin (AAL)-reactive immunoglobulin G rapidly appears in sera of animals following antigen exposure. PLoS One 7, e44422 (2012)
    • (2012) PLoS One , vol.7 , pp. 44422
    • Chen, S.1    Lu, C.2    Gu, H.3    Mehta, A.4    Li, J.5    Romano, P.B.6    Horn, D.7    Hooper, D.C.8    Bazemore-Walker, C.R.9    Block, T.10
  • 59
    • 0031762948 scopus 로고    scopus 로고
    • Binding of Clostridium difficile toxin A to human milk secretory component
    • 1:CAS:528:DyaK1cXnt1Wgu7w%3D 9788811 10.1099/00222615-47-10-879
    • Dallas, S.D., Rolfe, R.D.: Binding of Clostridium difficile toxin A to human milk secretory component. J. Med. Microbiol. 47, 879-888 (1998)
    • (1998) J. Med. Microbiol. , vol.47 , pp. 879-888
    • Dallas, S.D.1    Rolfe, R.D.2
  • 60
    • 62549149383 scopus 로고    scopus 로고
    • Functional and structural characterisation of human colostrum free secretory component
    • 1:CAS:528:DC%2BD1MXjsVertbc%3D 19230975 10.1016/j.molimm.2008.12.022
    • Almogren, A., Bonner, A., Perkins, S.J., Kerr, M.A.: Functional and structural characterisation of human colostrum free secretory component. Mol. Immunol. 46, 1534-1541 (2009)
    • (2009) Mol. Immunol. , vol.46 , pp. 1534-1541
    • Almogren, A.1    Bonner, A.2    Perkins, S.J.3    Kerr, M.A.4


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