The Presence of Progressive Motility Sustaining Factor (PMSF) in Human Epididymis

Sheth, A. R.; Gunjikar, A.N.; Shah, Girish V.

doi:10.1111/j.1439-0272.1981.tb00021.x

Cited by 11 publications

(3 citation statements)

References 14 publications

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“…As reviewed in the Introduction Section, earlier investigators have reported the occurrence of multiple sperm motility regulating undefined protein factors in the male reproductive fluids (Morton and Chang, 1973;Gaur and Talwar, 1975;Acott and Hoskins, 1978;Hoskins et al, 1978;Sheth et al, 1981;Pinto et al, 1984;Jaiswal and Majumder, 1998;Ding et al, 2007;Tso and Lee, 2008). However, none of these motility proteins have been purified to apparent homogeneity and characterized.…”

Section: Discussionmentioning

confidence: 92%

“…The biochemical mechanism of sperm forward initiation in epididymis and its regulation is largely unknown. As reviewed earlier (Mandal et al, 1989;Majumder and Mandal, 1992;Majumder et al, 2001), early workers have reported the occurrence of various types of uncharacterized motility regulating protein factors in male reproductive fluids/ reproductive organs (Morton and Chang, 1973;Gaur and Talwar, 1975;Sheth et al, 1981;Tso and Lee, 2008). Hoskins and his associates Hoskins et al, 1978) have developed a novel in vitro model that permitted initiation of forward motility in the immature (immotile) sperm derived from bovine caput-epididymis when incubated in presence of epididymal plasma/seminal plasma and theophylline.…”

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confidence: 94%

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Purification and characterization of a motility initiating protein from caprine epididymal plasma

Jaiswal

Das

Saha

et al. 2009

Journal Cellular Physiology

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Numerous reports have appeared on the occurrence of undefined protein factors in male reproductive fluids that promote motility of mature sperm and initiate forward motility in the immature (immotile) caput-epididymal sperm. This study reports for the first time purification to apparent homogeneity of a motility initiating protein (MIP) from epididymal plasma and its characterization using the caprine sperm model. It is a 125 kDa (approximately) dimeric protein made up of two subunits: 70 and 54 kDa. MIP is an acidic protein with an isoelectric point of 4.75. The motility protein at 30 microg/ml (240 nM) level showed nearly maximal motility-promoting activity. MIP is heat stable and it is maximally active at pH 8. It is a glycoprotein that binds with high affinity to concanavalin A and it contains mannose, galactose, and N-acetyl glucosamine approximately in the ratios of 6:1:6. It is sensitive to the actions of alpha-mannosidase and beta-N-acetylglucoseaminidase thereby demonstrating that the sugar side chain of the glycoprotein is essential for its biological activity. Epididymal plasma is its richest source. It is also capable of enhancing forward motility of mature cauda-sperm. Its antibody markedly inhibits sperm motility. MIP antibody is highly immunospecific and it recognizes both the subunits. MIP causes significant increase of the intrasperm level of cyclic AMP. MIP: the physiological motility-activating protein has potential for use as a contraceptive vaccine and for solving some of the problems of human infertility and animal breeding.

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Section: Discussionmentioning

confidence: 92%

mentioning

confidence: 94%

Purification and characterization of a motility initiating protein from caprine epididymal plasma

Jaiswal

Das

Saha

et al. 2009

Journal Cellular Physiology

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“…This characteristic of forward motility of male gamete cells is primarily achieved during the epididymal transit [3] ; however the cells attain the ultimate kinetic potential inside the female genital tract [4] . Reports of various types of extracellular sperm motility promoting factors in male reproductive fluids and blood serum of different animals, as well as human, have been part of the scientific literature for the last four decades [2] , [5] , [6] , [7] , [8] , [9] , [10] . But, none of these motility-regulatory entities were sufficiently purified and characterized.…”

Section: Introductionmentioning

confidence: 99%

Extracellular Regulation of Sperm Transmembrane Adenylyl Cyclase by a Forward Motility Stimulating Protein

et al. 2014

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Forward motility stimulating factor (FMSF), a glycoprotein isolated from buffalo serum, binds to the surface of the mature sperm cells to promote their progressive motility. This article reports the mode of signal transduction of this extracellular factor in goat sperm. The mechanism was investigated by assaying intracellular second messenger level and forward motility in presence of different pharmacological modulators. Mg++-dependent Forskolin responsive form of transmembrane adenylyl cyclase (tmAC) of goat spermatozoa was probed for its involvement in FMSF action. Dideoxyadenosine, a selective inhibitor of tmACs, was used to identify the role of this enzyme in the scheme of FMSF-signaling. Involvement of the α-subunit of G-protein in this regard has been inspected using GTPγS. Participation of protein kinase A (PKA) and tyrosine kinase was checked using IP20 and genistein, respectively. FMSF promotes tmAC activity in a dose-dependent manner through receptor/G-protein activation to enhance intracellular cAMP and forward motility. Motility boosting effects of this glycoprotein are almost lost in presence of dideoxyadenosine. But, FMSF displayed substantial motility promoting activity when movement of spermatozoa was inhibited with KH7, the specific inhibitor of soluble adenylyl cyclase indicating tmAC to be the primary target of FMSF action. Involvement of cAMP in mediating FMSF action was confirmed by the application of dibutyryl cAMP. Observed motility regulatory effects with IP20 and genistein indicate contribution of PKA and tyrosine kinase in FMSF activity; enhanced phosphorylation of a tyrosine containing ≈50 kDa protein was detected in this regard. FMSF initiates a novel signaling cascade to stimulate tmAC activity that augments intracellular cAMP, which through downstream crosstalk of phosphokinases leads to enhanced forward motility in mature spermatozoa. Thus, this article for the first time describes conventional tmAC-dependent profound activation of progressive motility by a physiologic extracellular factor in a mammalian species.

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Identification and characterization of a sperm motility promoting glycoprotein from buffalo blood serum

Mandal

Saha

Ghosh

et al. 2006

Journal Cellular Physiology

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Early investigators reported the occurrence of unidentified protein factors in biological fluids that may regulate sperm motility essential for fertility potential. This study reports for the first time purification of a forward motility stimulating protein (FMSF-I), to apparent homogeneity, from a biological fluid (buffalo blood serum) and its characterization. FMSF-I is the major motility protein of buffalo serum: a rich source of the factor. FMSF showed high protein specificity and affinity for activating forward motility of goat cauda epididymal spermatozoa. The motility promoter at 0.5 microM level showed maximal activity when nearly 60%-70% of spermatozoa expressed forward motility. It is a 66 kDa monomeric acidic protein rich in aspartate, glutamate, and leucine with isoelectric point of 3.7. FMSF: a Mg2+ -dependent protein binds to concanavalin A-agarose and the glycoprotein nature of FMSF has been confirmed by PAS staining. The factor lost activity completely when treated with alpha-mannosidase showing that the sugar part of the protein is essential for its biological activity. FMSF has no species specificity for its motility-activating potential. Sperm surface has specific receptors of FMSF, which is strongly immunogenic. The factor is present in testis and epididymis although liver is its richest source. Motility promoting efficacy of FMSF is markedly higher than the well-known non-protein motility activators: theophylline and bicarbonate or their combination. FMSF is a physiological activator of sperm motility and as a slaughterhouse byproduct it has potentiality for solving some of the problems of animal breeding, conservation of endangered species, and human infertility: a global social problem.

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The Presence of Progressive Motility Sustaining Factor (PMSF) in Human Epididymis

Cited by 11 publications

References 14 publications

Purification and characterization of a motility initiating protein from caprine epididymal plasma

Purification and characterization of a motility initiating protein from caprine epididymal plasma

Extracellular Regulation of Sperm Transmembrane Adenylyl Cyclase by a Forward Motility Stimulating Protein

Identification and characterization of a sperm motility promoting glycoprotein from buffalo blood serum

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