메뉴 건너뛰기




Volumn 58, Issue 1, 2015, Pages 105-113

Flagellar ion channels of sperm: similarities and differences between species

Author keywords

Flagellar calcium; Sperm ion channels

Indexed keywords

CALCIUM; CALCIUM CHANNEL; CALCIUM CHANNEL CATSPER; ION CHANNEL; P2X2 ION CHANNEL; POTASSIUM CHANNEL; POTASSIUM CHANNEL SLO; TRANSIENT RECEPTOR POTENTIAL CHANNEL A1; TRANSIENT RECEPTOR POTENTIAL CHANNEL M8; UNCLASSIFIED DRUG; VANILLOID RECEPTOR 1; VANILLOID RECEPTOR 2; VANILLOID RECEPTOR 3; VANILLOID RECEPTOR 4; VOLTAGE GATED PROTON CHANNEL 1; HV1 CHANNEL, HUMAN; SODIUM PROTON EXCHANGE PROTEIN;

EID: 84930542515     PISSN: 01434160     EISSN: 15321991     Source Type: Journal    
DOI: 10.1016/j.ceca.2014.10.009     Document Type: Review
Times cited : (89)

References (158)
  • 1
    • 0000029613 scopus 로고
    • Letter of 1677 to the Royal Society: De natis è semine genital animalculis
    • Leeuwenhoek A.v. Letter of 1677 to the Royal Society: De natis è semine genital animalculis. R. Soc. London 1678, 12:1040-1043.
    • (1678) R. Soc. London , vol.12 , pp. 1040-1043
    • Leeuwenhoek, A.1
  • 2
    • 0016833934 scopus 로고
    • Structural and transcriptional features of the mouse spermatid genome
    • Kierszenbaum A.L., Tres L.L. Structural and transcriptional features of the mouse spermatid genome. J. Cell Biol. 1975, 65:258-270.
    • (1975) J. Cell Biol. , vol.65 , pp. 258-270
    • Kierszenbaum, A.L.1    Tres, L.L.2
  • 3
    • 0031155076 scopus 로고    scopus 로고
    • RNA in spermatozoa: implications for the alternative haploid genome
    • Kramer J.A., Krawetz S.A. RNA in spermatozoa: implications for the alternative haploid genome. Mol. Hum. Reprod. 1997, 3:473-478.
    • (1997) Mol. Hum. Reprod. , vol.3 , pp. 473-478
    • Kramer, J.A.1    Krawetz, S.A.2
  • 4
    • 0027314707 scopus 로고
    • Intracellular calcium increases with hyperactivation in intact, moving hamster sperm and oscillates with the flagellar beat cycle
    • Suarez S.S., Varosi S.M., Dai X. Intracellular calcium increases with hyperactivation in intact, moving hamster sperm and oscillates with the flagellar beat cycle. Proc. Natl. Acad. Sci. U.S.A. 1993, 90:4660-4664.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 4660-4664
    • Suarez, S.S.1    Varosi, S.M.2    Dai, X.3
  • 5
    • 29544450106 scopus 로고    scopus 로고
    • Sperm transport in the female reproductive tract
    • Suarez S.S., Pacey A.A. Sperm transport in the female reproductive tract. Hum. Reprod. Update 2006, 12:23-37.
    • (2006) Hum. Reprod. Update , vol.12 , pp. 23-37
    • Suarez, S.S.1    Pacey, A.A.2
  • 8
    • 36549022192 scopus 로고    scopus 로고
    • External Ca2+ acts upstream of adenylyl cyclase SACY in the bicarbonate signaled activation of sperm motility
    • Carlson A.E., Hille B., Babcock D.F. External Ca2+ acts upstream of adenylyl cyclase SACY in the bicarbonate signaled activation of sperm motility. Dev. Biol. 2007, 312:183-192.
    • (2007) Dev. Biol. , vol.312 , pp. 183-192
    • Carlson, A.E.1    Hille, B.2    Babcock, D.F.3
  • 11
    • 0021227119 scopus 로고
    • Inhibition of bovine spermatozoa by caudal epididymal fluid: I. Studies of a sperm motility quiescence factor
    • Carr D.W., Acott T.S. Inhibition of bovine spermatozoa by caudal epididymal fluid: I. Studies of a sperm motility quiescence factor. Biol. Reprod. 1984, 30:913-925.
    • (1984) Biol. Reprod. , vol.30 , pp. 913-925
    • Carr, D.W.1    Acott, T.S.2
  • 12
    • 0024788833 scopus 로고
    • Intracellular pH regulates bovine sperm motility and protein phosphorylation
    • Carr D.W., Acott T.S. Intracellular pH regulates bovine sperm motility and protein phosphorylation. Biol. Reprod. 1989, 41:907-920.
    • (1989) Biol. Reprod. , vol.41 , pp. 907-920
    • Carr, D.W.1    Acott, T.S.2
  • 13
    • 0021891926 scopus 로고
    • Effects of pH, lactate, and viscoelastic drag on sperm motility: a species comparison
    • Carr D.W., Usselman M.C., Acott T.S. Effects of pH, lactate, and viscoelastic drag on sperm motility: a species comparison. Biol. Reprod. 1985, 33:588-595.
    • (1985) Biol. Reprod. , vol.33 , pp. 588-595
    • Carr, D.W.1    Usselman, M.C.2    Acott, T.S.3
  • 15
    • 80055094651 scopus 로고    scopus 로고
    • Rediscovering sperm ion channels with the patch-clamp technique
    • Kirichok Y., Lishko P.V. Rediscovering sperm ion channels with the patch-clamp technique. Mol. Hum. Reprod. 2011, 17:478-499.
    • (2011) Mol. Hum. Reprod. , vol.17 , pp. 478-499
    • Kirichok, Y.1    Lishko, P.V.2
  • 16
    • 29844448212 scopus 로고    scopus 로고
    • Whole-cell patch-clamp measurements of spermatozoa reveal an alkaline-activated Ca2+ channel
    • Kirichok Y., Navarro B., Clapham D.E. Whole-cell patch-clamp measurements of spermatozoa reveal an alkaline-activated Ca2+ channel. Nature 2006, 439:737-740.
    • (2006) Nature , vol.439 , pp. 737-740
    • Kirichok, Y.1    Navarro, B.2    Clapham, D.E.3
  • 17
    • 75749122696 scopus 로고    scopus 로고
    • Acid extrusion from human spermatozoa is mediated by flagellar voltage-gated proton channel
    • Lishko P.V., Botchkina I.L., Fedorenko A., Kirichok Y. Acid extrusion from human spermatozoa is mediated by flagellar voltage-gated proton channel. Cell 2010, 140:327-337.
    • (2010) Cell , vol.140 , pp. 327-337
    • Lishko, P.V.1    Botchkina, I.L.2    Fedorenko, A.3    Kirichok, Y.4
  • 18
    • 79952800026 scopus 로고    scopus 로고
    • Progesterone activates the principal Ca2+ channel of human sperm
    • Lishko P.V., Botchkina I.L., Kirichok Y. Progesterone activates the principal Ca2+ channel of human sperm. Nature 2011, 471:387-391.
    • (2011) Nature , vol.471 , pp. 387-391
    • Lishko, P.V.1    Botchkina, I.L.2    Kirichok, Y.3
  • 20
  • 23
    • 33646172012 scopus 로고    scopus 로고
    • Insights into sperm cell motility signaling through sNHE and the CatSpers
    • Quill T.A., Wang D., Garbers D.L. Insights into sperm cell motility signaling through sNHE and the CatSpers. Mol. Cell. Endocrinol. 2006, 250:84-92.
    • (2006) Mol. Cell. Endocrinol. , vol.250 , pp. 84-92
    • Quill, T.A.1    Wang, D.2    Garbers, D.L.3
  • 26
    • 0032488843 scopus 로고    scopus 로고
    • Slo3, a novel pH-sensitive K+ channel from mammalian spermatocytes
    • Schreiber M., Wei A., Yuan A., Gaut J., Saito M., Salkoff L. Slo3, a novel pH-sensitive K+ channel from mammalian spermatocytes. J. Biol. Chem. 1998, 273:3509-3516.
    • (1998) J. Biol. Chem. , vol.273 , pp. 3509-3516
    • Schreiber, M.1    Wei, A.2    Yuan, A.3    Gaut, J.4    Saito, M.5    Salkoff, L.6
  • 28
    • 0023275696 scopus 로고
    • The activating effects of bicarbonate on sperm motility and respiration at ejaculation
    • Tajima Y., Okamura N., Sugita Y. The activating effects of bicarbonate on sperm motility and respiration at ejaculation. Biochim. Biophys. Acta 1987, 924:519-529.
    • (1987) Biochim. Biophys. Acta , vol.924 , pp. 519-529
    • Tajima, Y.1    Okamura, N.2    Sugita, Y.3
  • 29
    • 75649114270 scopus 로고    scopus 로고
    • Block of mouse Slo1 and Slo3 K+ channels by CTX, IbTX, TEA, 4-AP and quinidine
    • Tang Q.Y., Zhang Z., Xia X.M., Lingle C.J. Block of mouse Slo1 and Slo3 K+ channels by CTX, IbTX, TEA, 4-AP and quinidine. Channels (Austin, TX) 2010, 4:22-41.
    • (2010) Channels (Austin, TX) , vol.4 , pp. 22-41
    • Tang, Q.Y.1    Zhang, Z.2    Xia, X.M.3    Lingle, C.J.4
  • 30
    • 84883224923 scopus 로고    scopus 로고
    • Simultaneous knockout of Slo3 and CatSper1 abolishes all alkalization- and voltage-activated current in mouse spermatozoa
    • Zeng X.H., Navarro B., Xia X.M., Clapham D.E., Lingle C.J. Simultaneous knockout of Slo3 and CatSper1 abolishes all alkalization- and voltage-activated current in mouse spermatozoa. J. Gen. Physiol. 2013, 142:305-313.
    • (2013) J. Gen. Physiol. , vol.142 , pp. 305-313
    • Zeng, X.H.1    Navarro, B.2    Xia, X.M.3    Clapham, D.E.4    Lingle, C.J.5
  • 31
    • 79955032438 scopus 로고    scopus 로고
    • Deletion of the Slo3 gene abolishes alkalization-activated K+ current in mouse spermatozoa
    • Zeng X.H., Yang C., Kim S.T., Lingle C.J., Xia X.M. Deletion of the Slo3 gene abolishes alkalization-activated K+ current in mouse spermatozoa. Proc. Natl. Acad. Sci. U.S.A. 2011, 108:5879-5884.
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 5879-5884
    • Zeng, X.H.1    Yang, C.2    Kim, S.T.3    Lingle, C.J.4    Xia, X.M.5
  • 32
    • 0030024773 scopus 로고    scopus 로고
    • 3(-)-dependent and arylaminobenzoate-dependent regulatory mechanisms and characterization of their roles in sperm capacitation
    • 3(-)-dependent and arylaminobenzoate-dependent regulatory mechanisms and characterization of their roles in sperm capacitation. Dev. Biol. 1996, 173:510-520.
    • (1996) Dev. Biol. , vol.173 , pp. 510-520
    • Zeng, Y.1    Oberdorf, J.A.2    Florman, H.M.3
  • 33
    • 33748120061 scopus 로고    scopus 로고
    • Slo3 K+ channels: voltage and pH dependence of macroscopic currents
    • Zhang X., Zeng X., Lingle C.J. Slo3 K+ channels: voltage and pH dependence of macroscopic currents. J. Gen. Physiol. 2006, 128:317-336.
    • (2006) J. Gen. Physiol. , vol.128 , pp. 317-336
    • Zhang, X.1    Zeng, X.2    Lingle, C.J.3
  • 34
    • 0000860764 scopus 로고
    • Electron microscopy of the sperm tail; results obtained with a new fixative
    • Afzelius B. Electron microscopy of the sperm tail; results obtained with a new fixative. J. Biophys. Biochem. Cytol. 1959, 5:269-278.
    • (1959) J. Biophys. Biochem. Cytol. , vol.5 , pp. 269-278
    • Afzelius, B.1
  • 37
    • 79960557909 scopus 로고    scopus 로고
    • Sperm flagella: comparative and phylogenetic perspectives of protein components
    • Inaba K. Sperm flagella: comparative and phylogenetic perspectives of protein components. Mol. Hum. Reprod. 2011, 17:524-538.
    • (2011) Mol. Hum. Reprod. , vol.17 , pp. 524-538
    • Inaba, K.1
  • 38
    • 78650966258 scopus 로고    scopus 로고
    • The epididymis, cytoplasmic droplets and male fertility
    • Cooper T.G. The epididymis, cytoplasmic droplets and male fertility. Asian J. Androl. 2011, 13:130-138.
    • (2011) Asian J. Androl. , vol.13 , pp. 130-138
    • Cooper, T.G.1
  • 39
    • 34250563621 scopus 로고
    • Histochemistry of the cytoplasmic droplet in the mammalian spermatozoon
    • Guraya S.S. Histochemistry of the cytoplasmic droplet in the mammalian spermatozoon. Experientia 1963, 19:94-95.
    • (1963) Experientia , vol.19 , pp. 94-95
    • Guraya, S.S.1
  • 40
    • 0037405925 scopus 로고    scopus 로고
    • Acquisition of volume regulatory response of sperm upon maturation in the epididymis and the role of the cytoplasmic droplet
    • Cooper T.G., Yeung C.H. Acquisition of volume regulatory response of sperm upon maturation in the epididymis and the role of the cytoplasmic droplet. Microsc. Res. Tech. 2003, 61:28-38.
    • (2003) Microsc. Res. Tech. , vol.61 , pp. 28-38
    • Cooper, T.G.1    Yeung, C.H.2
  • 41
    • 0032227096 scopus 로고    scopus 로고
    • Interactions between epididymal secretions and spermatozoa
    • Cooper T.G. Interactions between epididymal secretions and spermatozoa. J. Reprod. Fertil. 1998, 53(Supplement):119-136.
    • (1998) J. Reprod. Fertil. , vol.53 , pp. 119-136
    • Cooper, T.G.1
  • 42
    • 84887249573 scopus 로고    scopus 로고
    • The cytoplasmic droplet may be indicative of sperm motility and normal spermiogenesis
    • Xu H., Yuan S.Q., Zheng Z.H., Yan W. The cytoplasmic droplet may be indicative of sperm motility and normal spermiogenesis. Asian J. Androl. 2013, 15:799-805.
    • (2013) Asian J. Androl. , vol.15 , pp. 799-805
    • Xu, H.1    Yuan, S.Q.2    Zheng, Z.H.3    Yan, W.4
  • 44
    • 0015463197 scopus 로고
    • The distribution of negative surface charges on mammalian spermatozoa
    • Yanagimachi R., Noda Y.D., Fujimoto M., Nicolson G.L. The distribution of negative surface charges on mammalian spermatozoa. Am. J. Anat. 1972, 135:497-519.
    • (1972) Am. J. Anat. , vol.135 , pp. 497-519
    • Yanagimachi, R.1    Noda, Y.D.2    Fujimoto, M.3    Nicolson, G.L.4
  • 45
    • 0015579907 scopus 로고
    • Electrophysiology of bull spermatozoa: correlations with motility
    • McGrady A.V., Nelson L. Electrophysiology of bull spermatozoa: correlations with motility. Exp. Cell Res. 1973, 76:349-352.
    • (1973) Exp. Cell Res. , vol.76 , pp. 349-352
    • McGrady, A.V.1    Nelson, L.2
  • 46
    • 0018777649 scopus 로고
    • Electrophysiology of differentiating mouse spermatozoa
    • McGrady A. Electrophysiology of differentiating mouse spermatozoa. J. Cell Physiol. 1979, 99:223-232.
    • (1979) J. Cell Physiol. , vol.99 , pp. 223-232
    • McGrady, A.1
  • 47
    • 35848969340 scopus 로고    scopus 로고
    • Patch-clamp 'mapping' of ion channel activity in human sperm reveals regionalisation and co-localisation into mixed clusters
    • Jimenez-Gonzalez M.C., Gu Y., Kirkman-Brown J., Barratt C.L., Publicover S. Patch-clamp 'mapping' of ion channel activity in human sperm reveals regionalisation and co-localisation into mixed clusters. J. Cell Physiol. 2007, 213:801-808.
    • (2007) J. Cell Physiol. , vol.213 , pp. 801-808
    • Jimenez-Gonzalez, M.C.1    Gu, Y.2    Kirkman-Brown, J.3    Barratt, C.L.4    Publicover, S.5
  • 48
    • 78649702915 scopus 로고    scopus 로고
    • The role of Hv1 and CatSper channels in sperm activation
    • Lishko P.V., Kirichok Y. The role of Hv1 and CatSper channels in sperm activation. J. Physiol. 2010, 588:4667-4672.
    • (2010) J. Physiol. , vol.588 , pp. 4667-4672
    • Lishko, P.V.1    Kirichok, Y.2
  • 49
    • 77955538603 scopus 로고    scopus 로고
    • Calcium signaling through CatSper channels in mammalian fertilization
    • Ren D., Xia J. Calcium signaling through CatSper channels in mammalian fertilization. Physiology (Bethesda) 2010, 25:165-175.
    • (2010) Physiology (Bethesda) , vol.25 , pp. 165-175
    • Ren, D.1    Xia, J.2
  • 50
    • 37149029370 scopus 로고    scopus 로고
    • Calcium signaling
    • Clapham D.E. Calcium signaling. Cell 2007, 131:1047-1058.
    • (2007) Cell , vol.131 , pp. 1047-1058
    • Clapham, D.E.1
  • 51
    • 58149391013 scopus 로고    scopus 로고
    • A novel neuronal calcium sensor family protein, calaxin, is a potential Ca(2+)-dependent regulator for the outer arm dynein of metazoan cilia and flagella
    • under the auspices of the European Cell Biology Organization
    • Mizuno K., Padma P., Konno A., Satouh Y., Ogawa K., Inaba K. A novel neuronal calcium sensor family protein, calaxin, is a potential Ca(2+)-dependent regulator for the outer arm dynein of metazoan cilia and flagella. Biol. Cell 2009, 101:91-103. under the auspices of the European Cell Biology Organization.
    • (2009) Biol. Cell , vol.101 , pp. 91-103
    • Mizuno, K.1    Padma, P.2    Konno, A.3    Satouh, Y.4    Ogawa, K.5    Inaba, K.6
  • 53
    • 58049202801 scopus 로고    scopus 로고
    • Ca2+ bursts occur around a local minimal concentration of attractant and trigger sperm chemotactic response
    • Shiba K., Baba S.A., Inoue T., Yoshida M. Ca2+ bursts occur around a local minimal concentration of attractant and trigger sperm chemotactic response. Proc. Natl. Acad. Sci. U.S.A. 2008, 105:19312-19317.
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 19312-19317
    • Shiba, K.1    Baba, S.A.2    Inoue, T.3    Yoshida, M.4
  • 54
    • 0024359610 scopus 로고
    • Relationship between calcium, cyclic AMP, ATP, and intracellular pH and the capacity of hamster spermatozoa to express hyperactivated motility
    • White D.R., Aitken R.J. Relationship between calcium, cyclic AMP, ATP, and intracellular pH and the capacity of hamster spermatozoa to express hyperactivated motility. Gamete Res. 1989, 22:163-177.
    • (1989) Gamete Res. , vol.22 , pp. 163-177
    • White, D.R.1    Aitken, R.J.2
  • 55
    • 0036389888 scopus 로고    scopus 로고
    • Hyperactivated motility of bull sperm is triggered at the axoneme by Ca2+ and not cAMP
    • Ho H.C., Granish K.A., Suarez S.S. Hyperactivated motility of bull sperm is triggered at the axoneme by Ca2+ and not cAMP. Dev. Biol. 2002, 250:208-217.
    • (2002) Dev. Biol. , vol.250 , pp. 208-217
    • Ho, H.C.1    Granish, K.A.2    Suarez, S.S.3
  • 57
    • 0024366051 scopus 로고
    • An adhesion-associated agonist from the zona pellucida activates G protein-promoted elevations of internal Ca2+ and pH that mediate mammalian sperm acrosomal exocytosis
    • Florman H.M., Tombes R.M., First N.L., Babcock D.F. An adhesion-associated agonist from the zona pellucida activates G protein-promoted elevations of internal Ca2+ and pH that mediate mammalian sperm acrosomal exocytosis. Dev. Biol. 1989, 135:133-146.
    • (1989) Dev. Biol. , vol.135 , pp. 133-146
    • Florman, H.M.1    Tombes, R.M.2    First, N.L.3    Babcock, D.F.4
  • 59
    • 34249816501 scopus 로고    scopus 로고
    • Sperm phospholipases and acrosomal exocytosis
    • Roldan E.R., Shi Q.X. Sperm phospholipases and acrosomal exocytosis. Front. Biosci. 2007, 12:89-104.
    • (2007) Front. Biosci. , vol.12 , pp. 89-104
    • Roldan, E.R.1    Shi, Q.X.2
  • 60
    • 0016132946 scopus 로고
    • Calcium dependence of the acrosome reaction and activation of guinea pig spermatozoa
    • Yanagimachi R., Usui N. Calcium dependence of the acrosome reaction and activation of guinea pig spermatozoa. Exp. Cell Res. 1974, 89:161-174.
    • (1974) Exp. Cell Res. , vol.89 , pp. 161-174
    • Yanagimachi, R.1    Usui, N.2
  • 61
    • 0030591315 scopus 로고    scopus 로고
    • T-type Ca2+ channels and alpha1E expression in spermatogenic cells, and their possible relevance to the sperm acrosome reaction
    • Lievano A., Santi C.M., Serrano C.J., Trevino C.L., Bellve A.R., Hernandez-Cruz A., Darszon A. T-type Ca2+ channels and alpha1E expression in spermatogenic cells, and their possible relevance to the sperm acrosome reaction. FEBS Lett. 1996, 388:150-154.
    • (1996) FEBS Lett. , vol.388 , pp. 150-154
    • Lievano, A.1    Santi, C.M.2    Serrano, C.J.3    Trevino, C.L.4    Bellve, A.R.5    Hernandez-Cruz, A.6    Darszon, A.7
  • 62
    • 0029847170 scopus 로고    scopus 로고
    • A dihydropyridine-sensitive T-type Ca2+ current is the main Ca2+ current carrier in mouse primary spermatocytes
    • Santi C.M., Darszon A., Hernandez-Cruz A. A dihydropyridine-sensitive T-type Ca2+ current is the main Ca2+ current carrier in mouse primary spermatocytes. Am. J. Physiol. 1996, 271:C1583-C1593.
    • (1996) Am. J. Physiol. , vol.271 , pp. C1583-C1593
    • Santi, C.M.1    Darszon, A.2    Hernandez-Cruz, A.3
  • 63
    • 0034647343 scopus 로고    scopus 로고
    • CaV2.2 and CaV2.3 (N- and R-type) Ca2+ channels in depolarization-evoked entry of Ca2+ into mouse sperm
    • Wennemuth G., Westenbroek R.E., Xu T., Hille B., Babcock D.F. CaV2.2 and CaV2.3 (N- and R-type) Ca2+ channels in depolarization-evoked entry of Ca2+ into mouse sperm. J. Biol. Chem. 2000, 275:21210-21217.
    • (2000) J. Biol. Chem. , vol.275 , pp. 21210-21217
    • Wennemuth, G.1    Westenbroek, R.E.2    Xu, T.3    Hille, B.4    Babcock, D.F.5
  • 65
    • 34547940325 scopus 로고    scopus 로고
    • Expression, localization and functions in acrosome reaction and sperm motility of Ca(V)3.1 and Ca(V)3.2 channels in sperm cells: an evaluation from Ca(V)3.1 and Ca(V)3.2 deficient mice
    • Escoffier J., Boisseau S., Serres C., Chen C.C., Kim D., Stamboulian S., Shin H.S., Campbell K.P., De Waard M., Arnoult C. Expression, localization and functions in acrosome reaction and sperm motility of Ca(V)3.1 and Ca(V)3.2 channels in sperm cells: an evaluation from Ca(V)3.1 and Ca(V)3.2 deficient mice. J. Cell Physiol. 2007, 212:753-763.
    • (2007) J. Cell Physiol. , vol.212 , pp. 753-763
    • Escoffier, J.1    Boisseau, S.2    Serres, C.3    Chen, C.C.4    Kim, D.5    Stamboulian, S.6    Shin, H.S.7    Campbell, K.P.8    De Waard, M.9    Arnoult, C.10
  • 67
    • 0034879821 scopus 로고    scopus 로고
    • Lack of the burst firing of thalamocortical relay neurons and resistance to absence seizures in mice lacking alpha(1G) T-type Ca(2+) channels
    • Kim D., Song I., Keum S., Lee T., Jeong M.J., Kim S.S., McEnery M.W., Shin H.S. Lack of the burst firing of thalamocortical relay neurons and resistance to absence seizures in mice lacking alpha(1G) T-type Ca(2+) channels. Neuron 2001, 31:35-45.
    • (2001) Neuron , vol.31 , pp. 35-45
    • Kim, D.1    Song, I.2    Keum, S.3    Lee, T.4    Jeong, M.J.5    Kim, S.S.6    McEnery, M.W.7    Shin, H.S.8
  • 70
    • 4344665636 scopus 로고    scopus 로고
    • Identification of human and mouse CatSper3 and CatSper4 genes: characterisation of a common interaction domain and evidence for expression in testis
    • Lobley A., Pierron V., Reynolds L., Allen L., Michalovich D. Identification of human and mouse CatSper3 and CatSper4 genes: characterisation of a common interaction domain and evidence for expression in testis. Reprod. Biol. Endocrinol. 2003, 1:53.
    • (2003) Reprod. Biol. Endocrinol. , vol.1 , pp. 53
    • Lobley, A.1    Pierron, V.2    Reynolds, L.3    Allen, L.4    Michalovich, D.5
  • 71
    • 78651358912 scopus 로고    scopus 로고
    • A novel gene required for male fertility and functional CATSPER channel formation in spermatozoa
    • Chung J.J., Navarro B., Krapivinsky G., Krapivinsky L., Clapham D.E. A novel gene required for male fertility and functional CATSPER channel formation in spermatozoa. Nat. Commun. 2011, 2:153.
    • (2011) Nat. Commun. , vol.2 , pp. 153
    • Chung, J.J.1    Navarro, B.2    Krapivinsky, G.3    Krapivinsky, L.4    Clapham, D.E.5
  • 72
    • 34547096281 scopus 로고    scopus 로고
    • CatSperbeta, a novel transmembrane protein in the CatSper channel complex
    • Liu J., Xia J., Cho K.H., Clapham D.E., Ren D. CatSperbeta, a novel transmembrane protein in the CatSper channel complex. J. Biol. Chem. 2007, 282:18945-18952.
    • (2007) J. Biol. Chem. , vol.282 , pp. 18945-18952
    • Liu, J.1    Xia, J.2    Cho, K.H.3    Clapham, D.E.4    Ren, D.5
  • 73
    • 69849084741 scopus 로고    scopus 로고
    • A novel, single, transmembrane protein CATSPERG is associated with CATSPER1 channel protein
    • Wang H., Liu J., Cho K.H., Ren D. A novel, single, transmembrane protein CATSPERG is associated with CATSPER1 channel protein. Biol. Reprod. 2009, 81:539-544.
    • (2009) Biol. Reprod. , vol.81 , pp. 539-544
    • Wang, H.1    Liu, J.2    Cho, K.H.3    Ren, D.4
  • 74
    • 84900327987 scopus 로고    scopus 로고
    • Structurally distinct Ca(2+) signaling domains of sperm flagella orchestrate tyrosine phosphorylation and motility
    • Chung J.J., Shim S.H., Everley R.A., Gygi S.P., Zhuang X., Clapham D.E. Structurally distinct Ca(2+) signaling domains of sperm flagella orchestrate tyrosine phosphorylation and motility. Cell 2014, 157:808-822.
    • (2014) Cell , vol.157 , pp. 808-822
    • Chung, J.J.1    Shim, S.H.2    Everley, R.A.3    Gygi, S.P.4    Zhuang, X.5    Clapham, D.E.6
  • 77
    • 84930542781 scopus 로고
    • In: R.A. Pagon, M.P. Adam, H.H. Ardinger, T.D. Bird, C.R. Dolan, C.T. Fong, R.J.H. Smith, K. Stephens (Eds.), GeneReviews® [Internet], Seattle (WA): University of Washington, Seattle, 2009 Dec 03.
    • M.S. Hildebrand, M.R. Avenarius, R.J.H. Smith, CATSPER-related male infertility. In: R.A. Pagon, M.P. Adam, H.H. Ardinger, T.D. Bird, C.R. Dolan, C.T. Fong, R.J.H. Smith, K. Stephens (Eds.), GeneReviews® [Internet], Seattle (WA): University of Washington, Seattle; 1993-2014, 2009 Dec 03.
    • (1993)
    • Hildebrand, M.S.1    Avenarius, M.R.2    Smith, R.J.H.3
  • 80
    • 84898769805 scopus 로고    scopus 로고
    • Chromosome microarray analysis: a case report of infertile brothers with CATSPER gene deletion
    • Jaiswal D., Singh V., Dwivedi U.S., Trivedi S., Singh K. Chromosome microarray analysis: a case report of infertile brothers with CATSPER gene deletion. Gene 2014, 542:263-265.
    • (2014) Gene , vol.542 , pp. 263-265
    • Jaiswal, D.1    Singh, V.2    Dwivedi, U.S.3    Trivedi, S.4    Singh, K.5
  • 82
    • 34250844962 scopus 로고    scopus 로고
    • Catsper3 and Catsper4 are essential for sperm hyperactivated motility and male fertility in the mouse
    • Jin J., Jin N., Zheng H., Ro S., Tafolla D., Sanders K.M., Yan W. Catsper3 and Catsper4 are essential for sperm hyperactivated motility and male fertility in the mouse. Biol. Reprod. 2007, 77:37-44.
    • (2007) Biol. Reprod. , vol.77 , pp. 37-44
    • Jin, J.1    Jin, N.2    Zheng, H.3    Ro, S.4    Tafolla, D.5    Sanders, K.M.6    Yan, W.7
  • 83
    • 59849088171 scopus 로고    scopus 로고
    • CatSper-null mutant spermatozoa are unable to ascend beyond the oviductal reservoir
    • Ho K., Wolff C.A., Suarez S.S. CatSper-null mutant spermatozoa are unable to ascend beyond the oviductal reservoir. Reprod., Fertil. Dev. 2009, 2(1):345-350.
    • (2009) Reprod., Fertil. Dev. , vol.2 , Issue.1 , pp. 345-350
    • Ho, K.1    Wolff, C.A.2    Suarez, S.S.3
  • 84
    • 0025095406 scopus 로고
    • Progesterone and 17 alpha-hydroxyprogesterone. Novel stimulators of calcium influx in human sperm
    • Blackmore P.F., Beebe S.J., Danforth D.R., Alexander N. Progesterone and 17 alpha-hydroxyprogesterone. Novel stimulators of calcium influx in human sperm. J. Biol. Chem. 1990, 265:1376-1380.
    • (1990) J. Biol. Chem. , vol.265 , pp. 1376-1380
    • Blackmore, P.F.1    Beebe, S.J.2    Danforth, D.R.3    Alexander, N.4
  • 85
    • 0025943491 scopus 로고
    • Intracellular calcium accumulation and responsiveness to progesterone in capacitating human spermatozoa
    • Baldi E., Casano R., Falsetti C., Krausz C., Maggi M., Forti G. Intracellular calcium accumulation and responsiveness to progesterone in capacitating human spermatozoa. J. Androl. 1991, 12:323-330.
    • (1991) J. Androl. , vol.12 , pp. 323-330
    • Baldi, E.1    Casano, R.2    Falsetti, C.3    Krausz, C.4    Maggi, M.5    Forti, G.6
  • 88
    • 0026621839 scopus 로고
    • Direct effects of progesterone and antiprogesterone on human sperm hyperactivated motility and acrosome reaction
    • Uhler M.L., Leung A., Chan S.Y., Wang C. Direct effects of progesterone and antiprogesterone on human sperm hyperactivated motility and acrosome reaction. Fertil. Steril. 1992, 58:1191-1198.
    • (1992) Fertil. Steril. , vol.58 , pp. 1191-1198
    • Uhler, M.L.1    Leung, A.2    Chan, S.Y.3    Wang, C.4
  • 89
    • 0028650360 scopus 로고
    • Exocytosis in spermatozoa in response to progesterone and zona pellucida
    • Roldan E.R., Murase T., Shi Q.X. Exocytosis in spermatozoa in response to progesterone and zona pellucida. Science 1994, 266:1578-1581.
    • (1994) Science , vol.266 , pp. 1578-1581
    • Roldan, E.R.1    Murase, T.2    Shi, Q.X.3
  • 90
    • 0032539925 scopus 로고    scopus 로고
    • A new prostaglandin E receptor mediates calcium influx and acrosome reaction in human spermatozoa
    • Schaefer M., Hofmann T., Schultz G., Gudermann T. A new prostaglandin E receptor mediates calcium influx and acrosome reaction in human spermatozoa. Proc. Natl. Acad. Sci. U.S.A. 1998, 95:3008-3013.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 3008-3013
    • Schaefer, M.1    Hofmann, T.2    Schultz, G.3    Gudermann, T.4
  • 94
    • 3543003538 scopus 로고    scopus 로고
    • Human spermatozoa as a model for studying membrane receptors mediating rapid nongenomic effects of progesterone and estrogens
    • Luconi M., Francavilla F., Porazzi I., Macerola B., Forti G., Baldi E. Human spermatozoa as a model for studying membrane receptors mediating rapid nongenomic effects of progesterone and estrogens. Steroids 2004, 69:553-559.
    • (2004) Steroids , vol.69 , pp. 553-559
    • Luconi, M.1    Francavilla, F.2    Porazzi, I.3    Macerola, B.4    Forti, G.5    Baldi, E.6
  • 95
    • 84863982468 scopus 로고    scopus 로고
    • Nongenomic actions of aldosterone and progesterone revisited
    • Wendler A., Albrecht C., Wehling M. Nongenomic actions of aldosterone and progesterone revisited. Steroids 2012, 77:1002-1006.
    • (2012) Steroids , vol.77 , pp. 1002-1006
    • Wendler, A.1    Albrecht, C.2    Wehling, M.3
  • 96
    • 55849098087 scopus 로고    scopus 로고
    • Evolutionary genomics reveals lineage-specific gene loss and rapid evolution of a sperm-specific ion channel complex: CatSpers and CatSperbeta
    • Cai X., Clapham D.E. Evolutionary genomics reveals lineage-specific gene loss and rapid evolution of a sperm-specific ion channel complex: CatSpers and CatSperbeta. PLoS One 2008, 3:e3569.
    • (2008) PLoS One , vol.3 , pp. e3569
    • Cai, X.1    Clapham, D.E.2
  • 97
    • 84903782213 scopus 로고    scopus 로고
    • Activation of the Pi3k/Akt pathway and modulation of phosphodiesterase activity via membrane progestin receptor-alpha (mPRalpha) regulate progestin-initiated sperm hypermotility in Atlantic croaker
    • Tan W., Thomas P. Activation of the Pi3k/Akt pathway and modulation of phosphodiesterase activity via membrane progestin receptor-alpha (mPRalpha) regulate progestin-initiated sperm hypermotility in Atlantic croaker. Biol. Reprod. 2014, 90:105.
    • (2014) Biol. Reprod. , vol.90 , pp. 105
    • Tan, W.1    Thomas, P.2
  • 98
    • 0014487695 scopus 로고
    • In vitro capacitation of hamster spermatozoa by follicular fluid
    • Yanagimachi R. In vitro capacitation of hamster spermatozoa by follicular fluid. J. Reprod. Fertil. 1969, 18:275-286.
    • (1969) J. Reprod. Fertil. , vol.18 , pp. 275-286
    • Yanagimachi, R.1
  • 99
    • 0028936801 scopus 로고
    • Capacitation of mouse spermatozoa. II. Protein tyrosine phosphorylation and capacitation are regulated by a cAMP-dependent pathway
    • Visconti P.E., Moore G.D., Bailey J.L., Leclerc P., Connors S.A., Pan D., Olds-Clarke P., Kopf G.S. Capacitation of mouse spermatozoa. II. Protein tyrosine phosphorylation and capacitation are regulated by a cAMP-dependent pathway. Development 1995, 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
  • 100
    • 71149104896 scopus 로고    scopus 로고
    • The BSA-induced Ca2+ influx during sperm capacitation is CATSPER channel-dependent
    • Xia J., Ren D. The BSA-induced Ca2+ influx during sperm capacitation is CATSPER channel-dependent. Reprod. Biol. Endocrinol. 2009, 7:119.
    • (2009) Reprod. Biol. Endocrinol. , vol.7 , pp. 119
    • Xia, J.1    Ren, D.2
  • 102
    • 84901256099 scopus 로고    scopus 로고
    • P,p'-DDE activates CatSper and compromises human sperm function at environmentally relevant concentrations
    • Tavares R.S., Mansell S., Barratt C.L., Wilson S.M., Publicover S.J., Ramalho-Santos J. p,p'-DDE activates CatSper and compromises human sperm function at environmentally relevant concentrations. Hum. Reprod. 2013, 28:3167-3177.
    • (2013) Hum. Reprod. , vol.28 , pp. 3167-3177
    • Tavares, R.S.1    Mansell, S.2    Barratt, C.L.3    Wilson, S.M.4    Publicover, S.J.5    Ramalho-Santos, J.6
  • 103
    • 85013734929 scopus 로고    scopus 로고
    • NIH National Institute of Child and Human Development (NICHD), http://grants.nih.gov/grants/guide/rfa-files/RFA-HD-09-032.html.
  • 104
    • 33947515264 scopus 로고    scopus 로고
    • Bovine sperm hyperactivation is promoted by alkaline-stimulated Ca2+ influx
    • Marquez B., Suarez S.S. Bovine sperm hyperactivation is promoted by alkaline-stimulated Ca2+ influx. Biol. Reprod. 2007, 76:660-665.
    • (2007) Biol. Reprod. , vol.76 , pp. 660-665
    • Marquez, B.1    Suarez, S.S.2
  • 106
    • 0020541910 scopus 로고
    • Examination of the intracellular ionic environment and of ionophore action by null point measurements employing the fluorescein chromophore
    • Babcock D.F. Examination of the intracellular ionic environment and of ionophore action by null point measurements employing the fluorescein chromophore. J. Biol. Chem. 1983, 258:6380-6389.
    • (1983) J. Biol. Chem. , vol.258 , pp. 6380-6389
    • Babcock, D.F.1
  • 107
    • 0020532581 scopus 로고
    • Potassium-dependent increases in cytosolic pH stimulate metabolism and motility of mammalian sperm
    • Babcock D.F., Rufo G.A., Lardy H.A. Potassium-dependent increases in cytosolic pH stimulate metabolism and motility of mammalian sperm. Proc. Natl. Acad. Sci. U.S.A. 1983, 80:1327-1331.
    • (1983) Proc. Natl. Acad. Sci. U.S.A. , vol.80 , pp. 1327-1331
    • Babcock, D.F.1    Rufo, G.A.2    Lardy, H.A.3
  • 108
    • 0032924197 scopus 로고    scopus 로고
    • Regulation of intracellular pH in capacitated human spermatozoa by a Na+/H+ exchanger
    • Garcia M.A., Meizel S. Regulation of intracellular pH in capacitated human spermatozoa by a Na+/H+ exchanger. Mol. Reprod. Dev. 1999, 52:189-195.
    • (1999) Mol. Reprod. Dev. , vol.52 , pp. 189-195
    • Garcia, M.A.1    Meizel, S.2
  • 109
    • 0036015195 scopus 로고    scopus 로고
    • Roles of the Na,K-ATPase alpha4 isoform and the Na+/H+ exchanger in sperm motility
    • Woo A.L., James P.F., Lingrel J.B. Roles of the Na,K-ATPase alpha4 isoform and the Na+/H+ exchanger in sperm motility. Mol. Reprod. Dev. 2002, 62:348-356.
    • (2002) Mol. Reprod. Dev. , vol.62 , pp. 348-356
    • Woo, A.L.1    James, P.F.2    Lingrel, J.B.3
  • 110
    • 0344668550 scopus 로고    scopus 로고
    • A new sperm-specific Na+/H+ exchanger required for sperm motility and fertility
    • Wang D., King S.M., Quill T.A., Doolittle L.K., Garbers D.L. A new sperm-specific Na+/H+ exchanger required for sperm motility and fertility. Nat. Cell Biol. 2003, 5:1117-1122.
    • (2003) Nat. Cell Biol. , vol.5 , pp. 1117-1122
    • Wang, D.1    King, S.M.2    Quill, T.A.3    Doolittle, L.K.4    Garbers, D.L.5
  • 111
    • 34547231222 scopus 로고    scopus 로고
    • A sperm-specific Na+/H+ exchanger (sNHE) is critical for expression and in vivo bicarbonate regulation of the soluble adenylyl cyclase (sAC)
    • Wang D., Hu J., Bobulescu I.A., Quill T.A., McLeroy P., Moe O.W., Garbers D.L. A sperm-specific Na+/H+ exchanger (sNHE) is critical for expression and in vivo bicarbonate regulation of the soluble adenylyl cyclase (sAC). Proc. Natl. Acad. Sci. U.S.A. 2007, 104:9325-9330.
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 9325-9330
    • Wang, D.1    Hu, J.2    Bobulescu, I.A.3    Quill, T.A.4    McLeroy, P.5    Moe, O.W.6    Garbers, D.L.7
  • 113
    • 84875204528 scopus 로고    scopus 로고
    • SLC9/NHE gene family, a plasma membrane and organellar family of Na(+)/H(+) exchangers
    • Donowitz M., Ming Tse C., Fuster D. SLC9/NHE gene family, a plasma membrane and organellar family of Na(+)/H(+) exchangers. Mol. Aspects Med. 2013, 34:236-251.
    • (2013) Mol. Aspects Med. , vol.34 , pp. 236-251
    • Donowitz, M.1    Ming Tse, C.2    Fuster, D.3
  • 114
    • 33646358260 scopus 로고    scopus 로고
    • A voltage-gated proton-selective channel lacking the pore domain
    • Ramsey I.S., Moran M.M., Chong J.A., Clapham D.E. A voltage-gated proton-selective channel lacking the pore domain. Nature 2006, 440:1213-1216.
    • (2006) Nature , vol.440 , pp. 1213-1216
    • Ramsey, I.S.1    Moran, M.M.2    Chong, J.A.3    Clapham, D.E.4
  • 115
    • 33646229810 scopus 로고    scopus 로고
    • A voltage sensor-domain protein is a voltage-gated proton channel
    • Sasaki M., Takagi M., Okamura Y. A voltage sensor-domain protein is a voltage-gated proton channel. Science 2006, 312:589-592.
    • (2006) Science , vol.312 , pp. 589-592
    • Sasaki, M.1    Takagi, M.2    Okamura, Y.3
  • 119
    • 0015302470 scopus 로고
    • Bioluminescence: mechanism and mode of control of scintillon activity
    • Fogel M., Hastings J.W. Bioluminescence: mechanism and mode of control of scintillon activity. Proc. Natl. Acad. Sci. U.S.A. 1972, 69:690-693.
    • (1972) Proc. Natl. Acad. Sci. U.S.A. , vol.69 , pp. 690-693
    • Fogel, M.1    Hastings, J.W.2
  • 120
    • 0019936907 scopus 로고
    • Hydrogen ion currents and intracellular pH in depolarized voltage-clamped snail neurones
    • Thomas R.C., Meech R.W. Hydrogen ion currents and intracellular pH in depolarized voltage-clamped snail neurones. Nature 1982, 299:826-828.
    • (1982) Nature , vol.299 , pp. 826-828
    • Thomas, R.C.1    Meech, R.W.2
  • 121
    • 0025723509 scopus 로고
    • Hydrogen ion currents in rat alveolar epithelial cells
    • DeCoursey T.E. Hydrogen ion currents in rat alveolar epithelial cells. Biophys. J. 1991, 60:1243-1253.
    • (1991) Biophys. J. , vol.60 , pp. 1243-1253
    • DeCoursey, T.E.1
  • 122
    • 0027375484 scopus 로고
    • Potential, pH, and arachidonate gate hydrogen ion currents in human neutrophils
    • DeCoursey T.E., Cherny V.V. Potential, pH, and arachidonate gate hydrogen ion currents in human neutrophils. Biophys. J. 1993, 65:1590-1598.
    • (1993) Biophys. J. , vol.65 , pp. 1590-1598
    • DeCoursey, T.E.1    Cherny, V.V.2
  • 123
    • 0029034117 scopus 로고
    • The voltage-activated hydrogen ion conductance in rat alveolar epithelial cells is determined by the pH gradient
    • Cherny V.V., Markin V.S., DeCoursey T.E. The voltage-activated hydrogen ion conductance in rat alveolar epithelial cells is determined by the pH gradient. J. Gen. Physiol. 1995, 105:861-896.
    • (1995) J. Gen. Physiol. , vol.105 , pp. 861-896
    • Cherny, V.V.1    Markin, V.S.2    DeCoursey, T.E.3
  • 124
    • 84878507905 scopus 로고    scopus 로고
    • Voltage-gated proton channels: molecular biology, physiology, and pathophysiology of the H(V) family
    • DeCoursey T.E. Voltage-gated proton channels: molecular biology, physiology, and pathophysiology of the H(V) family. Physiol. Rev. 2013, 93:599-652.
    • (2013) Physiol. Rev. , vol.93 , pp. 599-652
    • DeCoursey, T.E.1
  • 125
    • 0024312499 scopus 로고
    • Characterization of proton currents in neurones of the snail, Lymnaea stagnalis
    • Byerly L., Suen Y. Characterization of proton currents in neurones of the snail, Lymnaea stagnalis. J. Physiol. 1989, 413:75-89.
    • (1989) J. Physiol. , vol.413 , pp. 75-89
    • Byerly, L.1    Suen, Y.2
  • 126
    • 84872735337 scopus 로고    scopus 로고
    • Voltage-sensing domain of voltage-gated proton channel Hv1 shares mechanism of block with pore domains
    • Hong L., Pathak M.M., Kim I.H., Ta D., Tombola F. Voltage-sensing domain of voltage-gated proton channel Hv1 shares mechanism of block with pore domains. Neuron 2013, 77:274-287.
    • (2013) Neuron , vol.77 , pp. 274-287
    • Hong, L.1    Pathak, M.M.2    Kim, I.H.3    Ta, D.4    Tombola, F.5
  • 127
    • 83055176497 scopus 로고    scopus 로고
    • Aspartate 112 is the selectivity filter of the human voltage-gated proton channel
    • Musset B., Smith S.M., Rajan S., Morgan D., Cherny V.V., Decoursey T.E. Aspartate 112 is the selectivity filter of the human voltage-gated proton channel. Nature 2011, 480:273-277.
    • (2011) Nature , vol.480 , pp. 273-277
    • Musset, B.1    Smith, S.M.2    Rajan, S.3    Morgan, D.4    Cherny, V.V.5    Decoursey, T.E.6
  • 129
    • 45549106075 scopus 로고    scopus 로고
    • Dimeric subunit stoichiometry of the human voltage-dependent proton channel Hv1
    • Lee S.Y., Letts J.A., Mackinnon R. Dimeric subunit stoichiometry of the human voltage-dependent proton channel Hv1. Proc. Natl. Acad. Sci. U.S.A. 2008, 105:7692-7695.
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 7692-7695
    • Lee, S.Y.1    Letts, J.A.2    Mackinnon, R.3
  • 130
    • 43449139690 scopus 로고    scopus 로고
    • The voltage-gated proton channel Hv1 has two pores, each controlled by one voltage sensor
    • Tombola F., Ulbrich M.H., Isacoff E.Y. The voltage-gated proton channel Hv1 has two pores, each controlled by one voltage sensor. Neuron 2008, 58:546-556.
    • (2008) Neuron , vol.58 , pp. 546-556
    • Tombola, F.1    Ulbrich, M.H.2    Isacoff, E.Y.3
  • 131
    • 77954346297 scopus 로고    scopus 로고
    • Function of the HVCN1 proton channel in airway epithelia and a naturally occurring mutation, M91T
    • Iovannisci D., Illek B., Fischer H. Function of the HVCN1 proton channel in airway epithelia and a naturally occurring mutation, M91T. J. Gen. Physiol. 2010, 136:35-46.
    • (2010) J. Gen. Physiol. , vol.136 , pp. 35-46
    • Iovannisci, D.1    Illek, B.2    Fischer, H.3
  • 132
    • 0032763120 scopus 로고    scopus 로고
    • PH-dependent inhibition of voltage-gated H(+) currents in rat alveolar epithelial cells by Zn(2+) and other divalent cations
    • Cherny V.V., DeCoursey T.E. pH-dependent inhibition of voltage-gated H(+) currents in rat alveolar epithelial cells by Zn(2+) and other divalent cations. J. Gen. Physiol. 1999, 114:819-838.
    • (1999) J. Gen. Physiol. , vol.114 , pp. 819-838
    • Cherny, V.V.1    DeCoursey, T.E.2
  • 135
    • 28144460084 scopus 로고    scopus 로고
    • A tale of two cells: endocannabinoid-signaling regulates functions of neurons and sperm
    • Schuel H., Burkman L.J. A tale of two cells: endocannabinoid-signaling regulates functions of neurons and sperm. Biol. Reprod. 2005, 73:1078-1086.
    • (2005) Biol. Reprod. , vol.73 , pp. 1078-1086
    • Schuel, H.1    Burkman, L.J.2
  • 136
    • 77949315267 scopus 로고    scopus 로고
    • Identification of Thr29 as a critical phosphorylation site that activates the human proton channel Hvcn1 in leukocytes
    • Musset B., Capasso M., Cherny V.V., Morgan D., Bhamrah M., Dyer M.J., DeCoursey T.E. Identification of Thr29 as a critical phosphorylation site that activates the human proton channel Hvcn1 in leukocytes. J. Biol. Chem. 2010, 285:5117-5121.
    • (2010) J. Biol. Chem. , vol.285 , pp. 5117-5121
    • Musset, B.1    Capasso, M.2    Cherny, V.V.3    Morgan, D.4    Bhamrah, M.5    Dyer, M.J.6    DeCoursey, T.E.7
  • 137
    • 0035371374 scopus 로고    scopus 로고
    • Inwardly rectifying K(+) channels in spermatogenic cells: functional expression and implication in sperm capacitation
    • Munoz-Garay C., De la Vega-Beltran J.L., Delgado R., Labarca P., Felix R., Darszon A. Inwardly rectifying K(+) channels in spermatogenic cells: functional expression and implication in sperm capacitation. Dev. Biol. 2001, 234:261-274.
    • (2001) Dev. Biol. , vol.234 , pp. 261-274
    • Munoz-Garay, C.1    De la Vega-Beltran, J.L.2    Delgado, R.3    Labarca, P.4    Felix, R.5    Darszon, A.6
  • 138
    • 34250624097 scopus 로고    scopus 로고
    • KSper, a pH-sensitive K+ current that controls sperm membrane potential
    • Navarro B., Kirichok Y., Clapham D.E. KSper, a pH-sensitive K+ current that controls sperm membrane potential. Proc. Natl. Acad. Sci. U.S.A. 2007, 104:7688-7692.
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 7688-7692
    • Navarro, B.1    Kirichok, Y.2    Clapham, D.E.3
  • 140
    • 82755195901 scopus 로고    scopus 로고
    • LRRC52 (leucine-rich-repeat-containing protein 52), a testis-specific auxiliary subunit of the alkalization-activated Slo3 channel
    • Yang C., Zeng X.H., Zhou Y., Xia X.M., Lingle C.J. LRRC52 (leucine-rich-repeat-containing protein 52), a testis-specific auxiliary subunit of the alkalization-activated Slo3 channel. Proc. Natl. Acad. Sci. U.S.A. 2011, 108:19419-19424.
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 19419-19424
    • Yang, C.1    Zeng, X.H.2    Zhou, Y.3    Xia, X.M.4    Lingle, C.J.5
  • 141
    • 67650324103 scopus 로고    scopus 로고
    • Interactions between beta subunits of the KCNMB family and Slo3: beta4 selectively modulates Slo3 expression and function
    • Yang C.T., Zeng X.H., Xia X.M., Lingle C.J. Interactions between beta subunits of the KCNMB family and Slo3: beta4 selectively modulates Slo3 expression and function. PLoS One 2009, 4:e6135.
    • (2009) PLoS One , vol.4 , pp. e6135
    • Yang, C.T.1    Zeng, X.H.2    Xia, X.M.3    Lingle, C.J.4
  • 142
    • 84869806054 scopus 로고    scopus 로고
    • Functional and structural analysis of the human SLO3 pH- and voltage-gated K+ channel
    • Leonetti M.D., Yuan P., Hsiung Y., Mackinnon R. Functional and structural analysis of the human SLO3 pH- and voltage-gated K+ channel. Proc. Natl. Acad. Sci. U.S.A. 2012, 109:19274-19279.
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 19274-19279
    • Leonetti, M.D.1    Yuan, P.2    Hsiung, Y.3    Mackinnon, R.4
  • 143
    • 77953503613 scopus 로고    scopus 로고
    • Phosphatidylinositol 4,5-bisphosphate activates Slo3 currents and its hydrolysis underlies the epidermal growth factor-induced current inhibition
    • Tang Q.Y., Zhang Z., Xia J., Ren D., Logothetis D.E. Phosphatidylinositol 4,5-bisphosphate activates Slo3 currents and its hydrolysis underlies the epidermal growth factor-induced current inhibition. J. Biol. Chem. 2010, 285:19259-19266.
    • (2010) J. Biol. Chem. , vol.285 , pp. 19259-19266
    • Tang, Q.Y.1    Zhang, Z.2    Xia, J.3    Ren, D.4    Logothetis, D.E.5
  • 145
    • 84899795576 scopus 로고    scopus 로고
    • Patch clamp studies of human sperm under physiological ionic conditions reveal three functionally and pharmacologically distinct cation channels
    • Mansell S.A., Publicover S.J., Barratt C.L., Wilson S.M. Patch clamp studies of human sperm under physiological ionic conditions reveal three functionally and pharmacologically distinct cation channels. Mol. Hum. Reprod. 2014, 20:392-408.
    • (2014) Mol. Hum. Reprod. , vol.20 , pp. 392-408
    • Mansell, S.A.1    Publicover, S.J.2    Barratt, C.L.3    Wilson, S.M.4
  • 147
    • 0027161159 scopus 로고
    • MSlo, a complex mouse gene encoding "maxi" calcium-activated potassium channels
    • Butler A., Tsunoda S., McCobb D.P., Wei A., Salkoff L. mSlo, a complex mouse gene encoding "maxi" calcium-activated potassium channels. Science 1993, 261:221-224.
    • (1993) Science , vol.261 , pp. 221-224
    • Butler, A.1    Tsunoda, S.2    McCobb, D.P.3    Wei, A.4    Salkoff, L.5
  • 148
    • 0037422013 scopus 로고    scopus 로고
    • Molecular identification of the Na+-activated K+ channel
    • Dryer S.E. Molecular identification of the Na+-activated K+ channel. Neuron 2003, 37:727-728.
    • (2003) Neuron , vol.37 , pp. 727-728
    • Dryer, S.E.1
  • 150
    • 0034717111 scopus 로고    scopus 로고
    • HKCNMB3 and hKCNMB4, cloning and characterization of two members of the large-conductance calcium-activated potassium channel beta subunit family
    • Behrens R., Nolting A., Reimann F., Schwarz M., Waldschutz R., Pongs O. hKCNMB3 and hKCNMB4, cloning and characterization of two members of the large-conductance calcium-activated potassium channel beta subunit family. FEBS Lett. 2000, 474:99-106.
    • (2000) FEBS Lett. , vol.474 , pp. 99-106
    • Behrens, R.1    Nolting, A.2    Reimann, F.3    Schwarz, M.4    Waldschutz, R.5    Pongs, O.6
  • 151
    • 77954954506 scopus 로고    scopus 로고
    • LRRC26 auxiliary protein allows BK channel activation at resting voltage without calcium
    • Yan J., Aldrich R.W. LRRC26 auxiliary protein allows BK channel activation at resting voltage without calcium. Nature 2010, 466:513-516.
    • (2010) Nature , vol.466 , pp. 513-516
    • Yan, J.1    Aldrich, R.W.2
  • 152
    • 80052181424 scopus 로고    scopus 로고
    • ATP-activated P2X2 current in mouse spermatozoa
    • Epub 2011, Aug 10
    • Navarro B., Miki K., Clapham D.E. ATP-activated P2X2 current in mouse spermatozoa. Proc. Natl. Acad. Sci. U.S.A. 2011, 108(34):14342-14347. Epub 2011, Aug 10. 10.1073/pnas.1111695108.
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , Issue.34 , pp. 14342-14347
    • Navarro, B.1    Miki, K.2    Clapham, D.E.3
  • 154
    • 84861715725 scopus 로고    scopus 로고
    • Human spermatozoa possess a calcium-dependent chloride channel that may participate in the acrosomal reaction
    • Orta G., Ferreira G., Jose O., Trevino C.L., Beltran C., Darszon A. Human spermatozoa possess a calcium-dependent chloride channel that may participate in the acrosomal reaction. J. Physiol. 2012, 590:2659-2675.
    • (2012) J. Physiol. , vol.590 , pp. 2659-2675
    • Orta, G.1    Ferreira, G.2    Jose, O.3    Trevino, C.L.4    Beltran, C.5    Darszon, A.6
  • 155
    • 79960038352 scopus 로고    scopus 로고
    • Aquaporin3 is a sperm water channel essential for postcopulatory sperm osmoadaptation and migration
    • Chen Q., Peng H., Lei L., Zhang Y., Kuang H., Cao Y., Shi Q.X., Ma T., Duan E. Aquaporin3 is a sperm water channel essential for postcopulatory sperm osmoadaptation and migration. Cell Res. 2011, 21:922-933.
    • (2011) Cell Res. , vol.21 , pp. 922-933
    • Chen, Q.1    Peng, H.2    Lei, L.3    Zhang, Y.4    Kuang, H.5    Cao, Y.6    Shi, Q.X.7    Ma, T.8    Duan, E.9
  • 156
    • 0345059360 scopus 로고    scopus 로고
    • International Union of International Union of Pharmacology. XLIII. Compendium of voltage-gated ion channels: transient receptor potential channels
    • Clapham D.E., Montell C., Schultz G., Julius D. International Union of International Union of Pharmacology. XLIII. Compendium of voltage-gated ion channels: transient receptor potential channels. Pharmacol. Rev. 2003, 55:591-596.
    • (2003) Pharmacol. Rev. , vol.55 , pp. 591-596
    • Clapham, D.E.1    Montell, C.2    Schultz, G.3    Julius, D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.