Are there inositol 1,4,5-triphosphate (IP3) receptors in human sperm?

Kuroda, Yukako; Kaneko, Satoru; Yoshimura, Yasunori; Nozawa, Shiro; Mikoshiba, Katsuhiko

doi:10.1016/s0024-3205(99)00230-1

Cited by 43 publications

(26 citation statements)

References 19 publications

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“…From previous experimental studies, it has been shown that bovine sperm IP 3 receptors have properties similar to that of IP 3 receptors on the bovine adrenal cortex and adrenal medullar chromaffin cells (Minelli et al, 2000). It has also been observed that the IP 3 receptors in sperm have a high density, with IP 3 binding affinities that range from 0.026-0.75 µM in different mammalian species of sperm (Kuroda et al, 1999;Minelli et al, 2000;Walensky and Snyder, 1995). Staining studies have identified type I (Minelli et al, 2000;Ho and Suarez, 2001a;Walensky and Snyder, 1995) and type III (Kuroda et al, 1999) IP 3 receptors in mammalian sperm.…”

Section: Numerical Methods and Parametersmentioning

confidence: 95%

“…It has also been observed that the IP 3 receptors in sperm have a high density, with IP 3 binding affinities that range from 0.026-0.75 µM in different mammalian species of sperm (Kuroda et al, 1999;Minelli et al, 2000;Walensky and Snyder, 1995). Staining studies have identified type I (Minelli et al, 2000;Ho and Suarez, 2001a;Walensky and Snyder, 1995) and type III (Kuroda et al, 1999) IP 3 receptors in mammalian sperm. The SPCA pump has been observed to transport Ca 2+ with an affinity similar to that of ER SERCA pumps (Wuytack et al, 2002).…”

Section: Numerical Methods and Parametersmentioning

confidence: 99%

“…Studies have also shown that cAMP can mediate or trigger stimulation of PLC to generate IP 3 (Schmidt et al, 2001). Several isoforms of PLC have been identified in mammalian sperm, including PLCδ4 (Fukami et al, 2003), PLCζ (Swann et al, 2004), and PLCβ in the head and midpiece (Kuroda et al, 1999;Walensky and Snyder, 1995).…”

Section: Additional Fluxes Degradation and Synthesismentioning

confidence: 99%

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A Model of CatSper Channel Mediated Calcium Dynamics in Mammalian Spermatozoa

2010

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CatSpers are calcium (Ca(2+)) channels that are located along the principal piece of mammalian sperm flagella and are directly linked to sperm motility and hyperactivation. It has been observed that Ca(2+) entry through CatSper channels triggers a tail to head Ca(2+) propagation in mouse sperm, as well as a sustained increase of Ca(2+) in the head. Here, we develop a mathematical model to investigate this propagation and sustained increase in the head. A 1-d reaction-diffusion model tracking intracellular Ca(2+) with flux terms for the CatSper channels, a leak flux, and plasma membrane Ca(2+) clearance mechanism is studied. Results of this simple model exhibit tail to head Ca(2+) propagation, but no sustained increase in the head. Therefore, in this model, a simple plasma membrane pump-leak system with diffusion in the cytosol cannot account for these experimentally observed results. It has been proposed that Ca(2+) influx from the CatSper channels induce additional Ca(2+) release from an internal store. We test this hypothesis by examining the possible role of Ca(2+) release from the redundant nuclear envelope (RNE), an inositol 1,4,5-trisphosphate (IP(3)) gated Ca(2+) store in the neck. The simple model is extended to include an equation for IP(3) synthesis, degradation, and diffusion, as well as flux terms for Ca(2+) in the RNE. When IP(3) and the RNE are accounted for, the results of the model exhibit a tail to head Ca(2+) propagation as well as a sustained increase of Ca(2+) in the head.

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Section: Numerical Methods and Parametersmentioning

confidence: 95%

Section: Numerical Methods and Parametersmentioning

confidence: 99%

Section: Additional Fluxes Degradation and Synthesismentioning

confidence: 99%

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A Model of CatSper Channel Mediated Calcium Dynamics in Mammalian Spermatozoa

2010

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“…In the mammalian sperm, IP 3 receptor is located on the acrosomal vesicle, which is considered as the internal Ca 2ϩ stores (21,39). On the other hand, whereas the spermatozoon has a large mitochondrion that has been proposed as internal Ca 2ϩ stores (38), the IP 3 receptor has never been found in the mitochondria of any cells.…”

Section: Discussionmentioning

confidence: 99%

Store-operated calcium channel regulates the chemotactic behavior of ascidian sperm

Yoshida

Ishikawa

Izumi

et al. 2002

Proc. Natl. Acad. Sci. U.S.A.

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The sperm-activating and -attracting factor released from the eggs of the ascidians Ciona intestinalis and Ciona savignyi requires extracellular Ca 2؉ for activating sperm motility and eliciting chemotactic behavior of the activated sperm toward the egg. Here, we show that modulators of the store-operated Ca 2؉ channel, SK&F96365, Ni 2؉ , 2-aminoethoxydiphenylborane, and thapsigargin inhibit the chemotactic behavior of the ascidian sperm; on the other hand, blockers of voltage-dependent Ca 2؉ channels did not inhibit the chemotaxis, even though they inhibited the sperm activation operated by voltage-dependent Ca 2؉ channels. The blockers of store-operated Ca 2؉ channels also inhibited the asymmetrical flagellar beating and turning movements of the ascidian sperm, which are typical signs of sperm chemotaxis. Depletion of internal Ca 2؉ stores by thapsigargin induced capacitative Ca 2؉ entry into the sperm, which was blocked by SK&F96365. These results suggest that the intracellular Ca 2؉ concentration increase through the store-operated Ca 2؉ channels induces asymmetrical flagellar movements to establish the chemotactic behavior of the sperm. I t is now well known that many cells, e.g., leukocytes, starved amoebae of Dictyostelium discoideum, bacteria, and migrating axon cells during development, can detect an extracellular chemical gradient and migrate toward the source of the chemicals, that is, exhibit chemotactic behavior. There is a variety of factors inducing chemotaxis of cells, e.g., food, pathogens, partner cells, etc., and chemotactic behavior of cells is one of the important communication systems between separated cells. Chemotactic behavior of the sperm toward an egg during fertilization in animal species is a typical case, first reported in hydrozoans (1). This phenomenon is now widely known to occur, from sponges to humans (2-4), and much effort has been devoted to clarifying the mechanisms underlying sperm chemotaxis.Extracellular Ca 2ϩ is generally accepted as being an important factor in the induction of chemotactic behavior of sperm in many plant and animal species (5-8). In the case of the sea urchin, Arbacia punctulata, a peptide named resact in the jelly layer of the egg has been shown to have sperm-activating and -attracting activities (7). The peptide increases the intracellular Ca 2ϩ concentration ([Ca 2ϩ ] i ) via cAMP-gated Ca 2ϩ channels (9, 10), which, in turn, induces asymmetrical flagellum movements (5, 11, 12) that result in reorientation of the sperm swimming direction (13). The role of extracellular Ca 2ϩ -induced asymmetrical flagellar movement in inducing sperm chemotaxis has also been reported in hydrozoan species (14). Ascidian sperm chemotactic behavior is also characterized by abrupt turning movements of the sperm (15, 16). Furthermore, it has been shown that the sperm-attracting activity in the ascidians Ciona intestinalis and Ciona savignyi does not originate from the overall surface of the egg coats, such as follicle cells, but from the vegetal pole of the egg (17). We al...

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“…Receptors for inositol trisphosphate (IP3) have been localised to the acrosomal membrane (Walensky and Snyder, 1995;Kuroda et al, 1999) and IP3-mediated release of Ca 2+ from the acrosome has been demonstrated in permeabilised human spermatozoa (De Blas et al, 2002). Recently, the existence of a second Ca 2+ store in the redundant nuclear envelope has been proposed (NaabyHansen et al, 2001;Ho and Suarez, 2003).…”

Section: Introductionmentioning

confidence: 99%

Secretory pathway Ca2+-ATPase (SPCA1) Ca2+ pumps, not SERCAs, regulate complex [Ca2+]i signals in human spermatozoa

Harper

Wootton

Michelangeli

et al. 2005

Journal of Cell Science

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The sarcoplasmic-endoplasmic reticulum Ca2+-ATPase (SERCA) inhibitors thapsigargin (0.1-1 μM) and cyclopiazonic acid (10 μM), failed to affect resting [Ca2+] in human spermatozoa. Slow progesterone-induced [Ca2+ i]i oscillations in human spermatozoa, which involve cyclic emptying-refilling of an intracellular Ca2+ store were also insensitive to these inhibitors. Non-selective doses of thapsigargin (5-30 μM, 50-300 times the saturating dose for SERCA inhibition), caused elevation of resting [Ca2+]i and partial, dose-dependent disruption of oscillations. A 10-40 μM concentration of bis(2-hydroxy-3-tert-butyl-5-methyl-phenyl)methane (bis-phenol), which inhibits both thapsigargin-sensitive and -insensitive microsomal Ca2+ ATPases, caused elevation of resting [Ca2+]i and inhibition of [Ca2+]i oscillations at doses consistent with inhibition of thapsigargin-resistant, microsomal ATPase and liberation of stored Ca2+. Low doses of bis-phenol had marked effects on [Ca2+]i oscillation kinetics. Application of the drug to cells previously stimulated with progesterone had effects very similar to those observed when it was applied to unstimulated cells, suggesting that the sustained Ca2+ influx induced by progesterone is not mediated via mobilisation of Ca2+ stores. Western blotting for human sperm proteins showed expression of secretory pathway Ca2+ ATPase (SPCA1). Immunolocalisation studies revealed expression of SPCA1 in all cells in an area behind the nucleus, extending into the midpiece. Staining for SERCA, carried out in parallel, detected no expression with either technique. We conclude that: (1) intracellular Ca2+ store(s) and store-dependent [Ca2+]i oscillations in human spermatozoa rely primarily on a thapsigargin/cyclopiazonic acid-insensitive Ca2+ pump, which is not a SERCA as characterised in somatic cells; (2) effects of high-dose thapsigargin on spermatozoa primarily reflect non-specific actions on non-SERCAs and; (3) secretory pathway Ca2+ ATPases contribute at least part of this non-SERCA Ca2+ pump activity.

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Are there inositol 1,4,5-triphosphate (IP3) receptors in human sperm?

Cited by 43 publications

References 19 publications

A Model of CatSper Channel Mediated Calcium Dynamics in Mammalian Spermatozoa

A Model of CatSper Channel Mediated Calcium Dynamics in Mammalian Spermatozoa

Store-operated calcium channel regulates the chemotactic behavior of ascidian sperm

Secretory pathway Ca2+-ATPase (SPCA1) Ca2+ pumps, not SERCAs, regulate complex [Ca2+]i signals in human spermatozoa

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