Functional Expression of P2UReceptors in Rat Spermatogenic Cells: Dual Modulation of a Ca2+-Activated K+Channel

Wu, Wei; So, S.C.; Sun, Yuanzhi; Chung, Yiu Wa; Grima, J; Wong, Patrick; Yan, Yizhong; Chan, Hsiao Chang

doi:10.1006/bbrc.1998.9051

Cited by 15 publications

(9 citation statements)

References 23 publications

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“…More will be said about SLO3 later in this review. Biochemical, molecular biology, and electrophysiological data support the presence of several of the above mentioned K + channels in spermatogenic cells and sperm (Acevedo et al, 2006; Chan et al, 1998; Felix et al, 2002; Hagiwara & Kawa, 1984; Jacob, Hurley, Goodwin, Cooper, & Benoff, 2000; Martinez-Lopez et al, 2009; Munoz-Garay et al, 2001; Navarro et al, 2007; Salvatore, D’Adamo, Polishchuk, Salmona, & Pessia, 1999; Santi et al, 2010; Schreiber et al, 1998; Wu et al, 1998). …”

Section: Capacitationmentioning

confidence: 86%

“…Various compounds with structurally different characteristics considered to be Cl − -channel blockers, such as NFA, anthracene-9-carboxylate, and ethacrynic acid, enhance K Ca 1.1 currents (Greenwood & Large, 1995; Ottolia & Toro, 1994; Toma, Greenwood, Helliwell, & Large, 1996). Since there are evidences of the presence of K Ca 1.1 channels in mammalian sperm (Rossato, Di Virgilio, Rizzuto, Galeazzi, & Foresta, 2001; Wu et al, 1998), the combined effects of anion-channel blockers such as NFA on CaCCs and K Ca 1.1s could account for their potent ability to inhibit the AR. The large [Ca 2+ ]i changes that occur during the AR result in significant morphological sperm head alterations which seem to involve acrosome swelling and an RVD in which CaCCs may participate.…”

Section: Acrosome Reactionmentioning

confidence: 99%

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K+ and Cl− Channels and Transporters in Sperm Function

Santi

Orta

Salkoff

et al. 2013

Current Topics in Developmental Biology

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To succeed in fertilization, spermatozoa must decode environmental cues which require a set of ion channels. Recent findings have revealed that K+ and Cl− channels participate in some of the main sperm functions. This work reviews the evidence indicating the involvement of K+ and Cl− channels in motility, maturation, and the acrosome reaction, and the advancement in identifying their molecular identity and modes of regulation. Improving our insight on how these channels operate will strengthen our ability to surmount some infertility problems, improve animal breeding, preserve biodiversity, and develop selective and secure male contraceptives.

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Section: Capacitationmentioning

confidence: 86%

Section: Acrosome Reactionmentioning

confidence: 99%

K+ and Cl− Channels and Transporters in Sperm Function

Santi

Orta

Salkoff

et al. 2013

Current Topics in Developmental Biology

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“…For example, ATP inhibits KCNQ1 channels in vestibular dark cells of the inner ear, M-type K + currents in sympathetic neurons, GIRK channels, ROMK2 channels in renal cells and Ca 2+ -activated K + currents in spermatogenetic cells [7,8,24,[26][27][28]45]. Various regulatory mechanisms have been proposed to explain inhibition of such K + channels, including crossregulation by the G i/o and G q pathways, regulation via PKC, PKG and via phosphatase PP2A [7,24,25,27].…”

Section: Discussionmentioning

confidence: 99%

P2Y2 and P2Y4 receptors regulate pancreatic Ca2+-activated K+ channels differently

Hede

Amstrup

Klærke

et al. 2005

Pflugers Arch - Eur J Physiol

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Extracellular ATP is an important regulator of transepithelial transport in a number of tissues. In pancreatic ducts, we have shown that ATP modulates epithelial K+ channels via purinergic receptors, most likely the P2Y2 and P2Y4 receptors, but the identity of the involved K+ channels was not clear. In this study, we show by RT-PCR analysis that rat pancreatic ducts express Ca(2+)-activated K+ channels of intermediate conductance (IK) and big conductance (BK), but not small conductance (SK). Possible interactions between P2Y receptors and these Ca(2+)-activated K+ channels were examined in co-expression experiments in Xenopus laevis oocytes. K+ channel activity was measured electrophysiologically in oocytes stimulated with UTP (0.1 mM). UTP stimulation of oocytes expressing P2Y4 receptors and BK channels resulted in a 30% increase in the current through the expressed channels. In contrast, stimulation of P2Y2 receptors led to a 20% inhibition of co-expressed BK channel activity, a response that was sensitive to TEA. Furthermore, co-expression of IK channels with P2Y4 and P2Y2 receptors resulted in a large hyperpolarization and 22-fold and 5-fold activation of currents by UTP, respectively. Taken together, this study shows that there are different interactions between the subtypes of P2Y purinergic receptors and different Ca(2+)-activated K+ channels.

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“…The P 2y2 type, for example, is more specific for pyrimidine nucleotides, in which the order for activation is: uridine triphosphate (UTP) ϭ ATP k 2-methylthio-ATP [35]. Because purinergic receptors of the type P 2u , which are specific for UTP, have been identified in rat sperm [36], we determined the effect of UTP on bovine sperm AR. As shown in Figure 2, UTP (1.0 mM) stimulated the AR most prominently.…”

Section: Induction Of Ar By Atpe and Various Nucleotidesmentioning

confidence: 99%

Extracellular Adenosine Triphosphate Stimulates Acrosomal Exocytosis in Bovine Spermatozoa via P2 Purinoceptor1

Luria

Rubinstein

Lax

et al. 2002

Biology of Reproduction

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The presence of ATP in the genital tract fluid of mammals provokes questions regarding its function in the fertilization process. We investigated the effect of extracellular ATP (ATPe) on the activation of bovine spermatozoa. A signal transduction mechanism for ATP involving the receptor-mediated release of second messengers is described. Treatment of spermatozoa with ATP, uridine triphosphate (UTP), or 2-methylthio-ATP resulted in a concentration-dependent increase of acrosomal exocytosis, whereas treatment with either AMP or adenosine induced little exocytosis. This suggested that the receptor involved is of the P2 and not the P1 type. Several lines of evidence also suggest that the ATP purinoceptor is of the P2y and not the P2x type. First, the acrosome reaction was induced by the P2y-agonists ATP, UTP, or 2-methylthio-ATP, but no effects were shown by the P2x-agonists alpha,beta-methylene-ATP or beta,gamma-methylene-ATP. Second, ATP-induced acrosomal exocytosis was inhibited by the P2y antagonists, but not by the P2x antagonists. Third, enhanced Ca2+ uptake into the cells was observed with ATP and 2-methylthio-ATP, but not with beta,gamma-methylene-ATP. Additionally, ATP induced elevation of intracellular Ca2+ and cAMP, and the effect on cAMP was predominantly enhanced by including Ca2+ and the Ca2+-ionophore A23187 in the incubation medium. Extracellular ATP also activates protein kinase Calpha (PKCalpha), and the acrosome reaction, stimulated by ATPe, is inhibited by a PKC-specific inhibitor. In summary, we suggest that ATPe activates the P2 purinoceptor that elevates [Ca2+]i, which leads to PKCalpha activation and culminates in acrosomal exocytosis.

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Functional Expression of P2UReceptors in Rat Spermatogenic Cells: Dual Modulation of a Ca2+-Activated K+Channel

Cited by 15 publications

References 23 publications

K+ and Cl− Channels and Transporters in Sperm Function

K+ and Cl− Channels and Transporters in Sperm Function

P2Y2 and P2Y4 receptors regulate pancreatic Ca2+-activated K+ channels differently

Extracellular Adenosine Triphosphate Stimulates Acrosomal Exocytosis in Bovine Spermatozoa via P2 Purinoceptor1

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