Motility Stimulant Effects of Prostasome Inclusion in Swim-Up Medium on Cryopreserved Human Spermatozoa

Carlsson, Lena; Ronquist, Gunnar; Stridsberg, Mats; Johansson, Lars

doi:10.3109/01485019708994880

Cited by 45 publications

(32 citation statements)

References 22 publications

(14 reference statements)

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“…Sperm are then in contact with seminal secretions and encounter prostasomes produced by the prostate (Ronquist et al 1978, Breitbart & Rubinstein 1982. Interactions with prostasomes increase sperm motility (Stegmayr & Ronquist 1982, Carlsson et al 1997, have a role in the sperm capacitation process (Cross & Mahasreshti 1997) and in the stabilisation of their plasma membrane (Saez et al 2003). Once in the female genital tract, spermatozoa transiently bind to the epithelial cells of the caudal isthmus leading to the concept of 'sperm reservoir' (Suarez 1987, Baillie et al 1997.…”

Section: Discussionmentioning

confidence: 99%

Membrane transfer from oocyte to sperm occurs in two CD9-independent ways that do not supply the fertilising ability of Cd9-deleted oocytes

Barraud-Lange¹,

Boissonnas²,

Serres³

et al. 2012

Reproduction

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Spermatozoa undergo regulation of their functions along their lifespan through exchanges via vesicles or interactions with epithelial cells, in the epididymis, in the seminal fluid and in the female genital tract. Two different ways of oocyte membrane transfer to spermatozoa have been described: trogocytosis and exosomes. We here report an analysis of in vitro exchanges between the membranes of unfertilised oocytes and capacitated spermatozoa. We showed that optimum conditions are fulfilled when unfertilised oocytes interact with acrosome-reacted spermatozoa, a scenario mimicking the events occurring when the fertilising spermatozoon is inside the perivitelline space. Although CD9 tetraspanin is an essential molecule for fertilisation, exosome and trogocytosis transfer persists in Cd9-null oocytes in spite of their dramatic fusion failure. These exchanges are CD9 tetraspanin independent. We also confirm that mice sperm express CD9 tetraspanin and that when Cd9-null oocytes were inseminated with sperm covered with oocyte membrane materials, including CD9 tetraspanin, no rescue of the oocytes' fertilisability could be obtained. Thus, the existence of two ways of exchange between gametes during fertilisation suggests that these events could be of a physiological importance in this process.

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Section: Discussionmentioning

confidence: 99%

Membrane transfer from oocyte to sperm occurs in two CD9-independent ways that do not supply the fertilising ability of Cd9-deleted oocytes

Barraud-Lange¹,

Boissonnas²,

Serres³

et al. 2012

Reproduction

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show abstract

“…The presence of TMPRSS2 in prostasomes suggests that it may also regulate prostasome functions. Prostasomes have been proposed to be involved in protection of the spermatozoa in the acidic milieu of the vagina, 29,30 stabilization of sperm plasma membrane and delay of acrosome reaction, [31][32][33][34] enhancement of sperm motility, 30,[35][36][37][38][39] protection of spermatozoa from phagocytosis and complement attack, and inhibition of viral activity. Many of the proposed biological functions of the prostasomes facilitate sperm function and enhance male reproduction.…”

Section: Discussionmentioning

confidence: 99%

TMPRSS2, a Serine Protease Expressed in the Prostate on the Apical Surface of Luminal Epithelial Cells and Released into Semen in Prostasomes, Is Misregulated in Prostate Cancer Cells

Chen

Lee

Lucht

et al. 2010

The American Journal of Pathology

147

152

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TMPRSS2, a type II transmembrane serine protease, is highly expressed by the epithelium of the human prostate gland. To explore the regulation and function of TMPRSS2 in the prostate, a panel of monoclonal antibodies with high sensitivity and specificity were generated. Immunodetection showed TMPRSS2 on the apical plasma membrane of the prostate luminal cells and demonstrated its release into semen as a component of prostasomes, organelle-like vesicles that may facilitate sperm function and enhance male reproduction. In prostate cancer cells, TMPRSS2 expression was increased and the protein mislocalized over the entire tumor cell membrane. In both LNCaP prostate cancer cells and human semen, TMPRSS2 protein was detected predominantly as inactive zymogen forms as part of an array of multiple noncovalent and disulfide-linked complexes, suggesting that TM-PRSS2 activity may be regulated by unconventional mechanisms. Our data suggested that TMPRSS2, an apical surface serine protease, may have a normal role in male reproduction as a component of prostasomes.The aberrant cellular localization, and increased expression of the protease seen in cancer, may contribute to prostate tumorigenesis by providing access of the enzyme to nonphysiological substrates and binding

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“…The motility of spermatozoa is enhanced by prostasomes [25,[32][33][34][35][36][37] and antibacterial prop- …”

Section: Physiological Roles Of Prostasomesmentioning

confidence: 99%

Role of human prostasomes in the activation of spermatozoa

Arienti¹,

Carlini²,

Saccardi

et al. 2004

J Cellular Molecular Medi

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Prostasomes are small vesicles of prostatic origin contained in human semen. Their composition is peculiar under many aspects. Cholesterol is abundant and many proteins are endowed with enzymatic or other activities. The function of prostasomes has been amply debated and several hypotheses have been put forward. The liquefaction of semen, spermatozoa motility, antibacterial activity and immunological functions have been related to prostasomes. Under certain aspects, prostasomes resemble synaptosomes. The fusion of prostasomes to spermatozoa enriches spermatozoa with cholesterol and causes bursts of cytoplasmic sperm calcium. The interaction of spermatozoa and prostasomes should be limited to vagina since prostasomes are immobile and do not follow spermatozoa in the superior female genital tract. Calcium bursts would increase spermatozoa motility, where cholesterol would decapacitate spermatozoa, so preventing untimely activation. Since spermatozoa receive many different molecules from prostasomes, additional effects are also possible. Prostasomes makes spermatozoa more apt to be activated by progesterone in the proximity of the ovum. Therefore, the fusion between spermatozoa and prostasomes would influence spermatozoa behaviour under many aspects and might be relevant for fecundation. The richness of molecular species in prostasomes is amazing and these small vesicles are expected to lead to many more discoveries in the field of human reproduction.

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Motility Stimulant Effects of Prostasome Inclusion in Swim-Up Medium on Cryopreserved Human Spermatozoa

Cited by 45 publications

References 22 publications

Membrane transfer from oocyte to sperm occurs in two CD9-independent ways that do not supply the fertilising ability of Cd9-deleted oocytes

Membrane transfer from oocyte to sperm occurs in two CD9-independent ways that do not supply the fertilising ability of Cd9-deleted oocytes

TMPRSS2, a Serine Protease Expressed in the Prostate on the Apical Surface of Luminal Epithelial Cells and Released into Semen in Prostasomes, Is Misregulated in Prostate Cancer Cells

Role of human prostasomes in the activation of spermatozoa

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