JAM-A is present in mammalian spermatozoa where it is essential for normal motility

Shao, Minghai; Ghosh, Ananya; Cooke, Vesselina G.; Naik, Ulhas P.; Martin‐DeLeon, Patricia A.

doi:10.1016/j.ydbio.2007.10.013

Cited by 49 publications

(55 citation statements)

References 31 publications

(47 reference statements)

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“…indicates that JAM-A is found on both Sertoli and a subset of basal GCs in the testis, a finding that is supported by microarray data from Sertoli and GC isolates (Chalmel et al 2007), as well as the identification of JAM-A protein in spermatozoa from the caudal epididymis (Shao et al 2008). Together, these data suggest a novel role for JAM-A in spermatogenesis.…”

Section: Discussionmentioning

confidence: 52%

“…JAM family members (JAM-B and JAM-C) have been identified on both Sertoli and GCs in rodents, while claudins and occludin have been localised exclusively to inter-Sertoli cell TJs in this species . To date, JAM-A has been identified at inter-Sertoli cell junctions and the tails of elongated spermatids within the epididymis of rodents (Shao et al 2008).…”

Section: Introductionmentioning

confidence: 99%

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Regulation of testicular tight junctions by gonadotrophins in the adult Djungarian hamster in vivo

Tarulli¹,

Meachem²,

Schlatt³

et al. 2008

Reproduction

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This study aimed to assess the effect of gonadotrophin suppression and FSH replacement on testicular tight junction dynamics and blood-testis barrier (BTB) organisation in vivo, utilising the seasonal breeding Djungarian hamster. Confocal immunohistology was used to assess the cellular organisation of tight junction proteins and real-time PCR to quantify tight junction mRNA. The effect of tight junction protein organisation on the BTB permeability was also investigated using a biotin-linked tracer. Tight junction protein (claudin-3, junctional adhesion molecule (JAM)-A and occludin) localisation was present but disorganised after gonadotrophin suppression, while mRNA levels (claudin-11, claudin-3 and occludin) were significantly (two-to threefold) increased. By contrast, both protein localisation and mRNA levels for the adaptor protein zona occludens-1 decreased after gonadotrophin suppression. FSH replacement induced a rapid reorganisation of tight junction protein localisation. The functionality of the BTB (as inferred by biotin tracer permeation) was found to be strongly associated with the organisation and localisation of claudin-11. Surprisingly, JAM-A was also recognised on spermatogonia, suggesting an additional novel role for this protein in trans-epithelial migration of germ cells across the BTB. It is concluded that gonadotrophin regulation of tight junction proteins forming the BTB occurs primarily at the level of protein organisation and not gene transcription in this species, and that immunolocalisation of the organised tight junction protein claudin-11 correlates with BTB functionality.

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Section: Discussionmentioning

confidence: 52%

Section: Introductionmentioning

confidence: 99%

Regulation of testicular tight junctions by gonadotrophins in the adult Djungarian hamster in vivo

Tarulli¹,

Meachem²,

Schlatt³

et al. 2008

Reproduction

View full text Add to dashboard Cite

show abstract

“…This difference could be related to the mode of fertilization, in vivo or in vitro. JAM-A is present in elongated spermatids and in the plasma membrane of the head and flagellum of sperm [20], and plays an important role in cell adhesion [21]. Since in vitro fertilization occurs in fish, the high expression of JAM-A in fish eggs may be more conducive to egg and sperm cell adhesion and subsequent sperm penetration into the egg membrane.…”

Section: Discussionmentioning

confidence: 99%

Cloning and preliminary functional studies of the JAM-A gene in grass carp (Ctenopharyngodon idellus)

Huang

et al. 2013

Fish & Shellfish Immunology

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“…lacking Jam-A (Shao, Ghosh, Cooke, Naik, & Martin-DeLeon, 2008) and have shown that it is associated with decreased activity of PMCA4 (Aravindan et al, 2012).…”

mentioning

confidence: 99%

“…Breeding and genotyping of these mice were described previously (Okunade et al, 2004). Jam-A null sperm were generated and genotyped as described (Shao et al, 2008). …”

mentioning

confidence: 99%

Plasma membrane calcium ATPase 4 (PMCA4) co‐ordinates calcium and nitric oxide signaling in regulating murine sperm functional activity

Olli

Galileo

et al. 2017

Journal Cellular Physiology

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Reduced sperm motility (asthenospermia) and resulting infertility arise from deletion of the Plasma Membrane Ca 2+ -ATPase 4 (Pmca4) gene which encodes the highly conserved Ca 2+ efflux pump, PMCA4. This is the major Ca 2+ clearance protein in murine sperm. Since the mechanism underlying asthenospermia in PMCA4's absence or reduced activity is unknown, we investigated if sperm PMCA4 negatively regulates nitric oxide synthases (NOSs) and when absent NO, peroxynitrite, and oxidative stress levels are increased. Using co-immunoprecipitation (Co-IP) and Fluorescence Resonance Energy Transfer (FRET), we show an association of PMCA4 with the NOSs in elevated cytosolic [Ca 2+ ] in capacitated and Ca 2+ ionophore-treated sperm and with neuronal (nNOS) at basal [Ca 2+ ] (ucapacitated sperm). FRET efficiencies for PMCA4-eNOS were 35% and 23% in capacitated and uncapacitated sperm, significantly (p < 0.01) different, with the molecules being <10 nm apart. For PMCA4-nNOS, this interaction was seen only for capacitated sperm where FRET efficiency was 24%, significantly (p < 0.05) higher than in uncapacitated sperm (6%). PMCA4 and the NOSs were identified as interacting partners in a quaternary complex that includes Caveolin1, which co-immunoprecipitated with eNOS in a Ca 2+ -dependent manner. In Pmca4 −/− sperm NOS activity was elevated twofold in capacitated/uncapacitated sperm (vs. wild-type), accompanied by a twofold increase in peroxynitrite levels and significantly (p < 0.001) increased numbers of apoptotic germ cells. The data support a quaternary complex model in which PMCA4 co-ordinates Ca 2+ and NO signaling to maintain motility, with increased NO levels resulting in asthenospermia in Pmca4 −/− males.They suggest the involvement of PMCA4 mutations in human asthenospermia, with diagnostic relevance.asthenospermia, calcium efflux pump, infertility, oxidative stress, sperm damageCapacitation is the series of changes that occur in the final maturation of mammalian sperm in the female in order for them to gain fertilizing competence, and subsequently undergo the acrosome reaction. Both of these processes are dependent on elevated levels of cytosolic Ca 2+ concentration ([Ca 2+ ] c ) (de Lamirande, Leclerc, & Gagnon, 1997;Fraser, 1987). After the calcium influx required to meet this high calcium demand, there needs to be a return to resting cytosolic calcium concentration ([Ca 2+ ] c ) levels (50-100 nM [Herrick et al., 2005]). In mice, in the absence of the major calcium efflux pump, Plasma Membrane Calcium ATPase 4 (PMCA4) (Wennemuth, Babcock, & Hille, 2003), calcium levels remain elevated with loss of sperm motility (Asthenospermia, AS) and resulting male infertility (Okunade et al., 2004;Schuh et al., 2004 (de Lamirande et al., 1997;Fraser, 1987) which rapidly activates them (Knowles & Moncada, 1994). Thus, as PMCA4 extrudes Ca 2+ , the NOSs are held in a locale or microdomain with a relatively low [Ca 2+ ] c, compared to the surrounding environment where it is globally high. In this Ca 2+ -extruding locale, NO...

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JAM-A is present in mammalian spermatozoa where it is essential for normal motility

Cited by 49 publications

References 31 publications

Regulation of testicular tight junctions by gonadotrophins in the adult Djungarian hamster in vivo

Regulation of testicular tight junctions by gonadotrophins in the adult Djungarian hamster in vivo

Cloning and preliminary functional studies of the JAM-A gene in grass carp (Ctenopharyngodon idellus)

Plasma membrane calcium ATPase 4 (PMCA4) co‐ordinates calcium and nitric oxide signaling in regulating murine sperm functional activity

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