Decapacitation factor (DF) is composed of sperm surface-associated proteins which modulate the fertilizing ability of spermatozoa.[1] Decapacitation is a reversible process that converts fertile, capacitated sperm to less-fertile uncapacitated sperm.[2][3] This activity is achieved by interaction between cholesterol, phospholipids and fibronectin-like substances and delivered via small vesicles in seminal plasma. DF prevents onset of capacitation. Many DFs are released in secretions from the epididymis and accessory organs of the male reproductive system.[1] However, some DFs have been identified that are located on the acrosome of sperm.[4] Normally, capacitation is initiated through the loss of DF[5] before the spermatozoa can perform the acrosomal reaction.[6] Physiologically decapacitation will inhibit the acrosomal reaction as DFs reassociate onto the sperm surface.[6] For example, one way this can be achieved is through spermatozoal membrane stabilization by maintaining physiological cholesterol/phospholipid ratio.

The study of DFs can help understand male infertility and has possible role in reversible male contraception. DFs are potent, but can be removed from sperm by gentle centrifugation to produce extremely fertile sperm.[2] DFs have been found in bull, rabbit, boar, stallion, monkey,[3] mouse,[6] and human[4] semen. Purification to obtain DFs and subsequent injection into a uterus with capacitated sperm decreases the efficiency of fertilization and converts sperm to an uncapacitated form.[1][2][5] In natural conditions, the uterus has the ability to inactivate or remove DF, allowing capacitation to occur. In vitro incubation of DF with β-amylase was demonstrated to destroy DF activity, and Dukelow hypothesized that uterine amylase would similarly be able to destroy DF activity and allow capacitation to occur.[3] In addition, the DF factors can be removed from the seminal plasma by gentle centrifugation to cause capacitation and can be added back to cause decapacitation.[3]

Various DFs have been found and characterized. One DF was removed by gentle centrifugation from rabbit seminal plasma and is an anionic polypeptide with an MR ~40,000 and is heat stable, cannot be destroyed by proteases at pH 8, and is stable when incubated other enzymes like lysozyme and glucose oxidase.[6] Some other DFs, such as DF10 and DF-R, have been reported as alternative forms of other proteins found in sperm.[1][5] NYD-SP27 is a unique DF as it is intrinsic to the sperm acrosome and inhibits the action of phospholipase C that is necessary for capacitation.[4] SERPINE2 is a proposed DF, as it is present in high concentrations on uncapacitated sperm and is lost during the capacitation process.[7] Platelet-activating factor acetylhydrolase is another proposed DF due to the negative correlation between its concentration and the motility of sperm.[8] Recently, the mechanisms of DFs such as SPINK3 had been demonstrated [9]

References

  1. 1 2 3 4 Nixon, Brett; MacIntyre, David A.; Mitchell, Lisa A.; Gibbs, Gerard M.; O’Bryan, Moira; Aitken, R. John (2006-02-01). "The Identification of Mouse Sperm-Surface-Associated Proteins and Characterization of Their Ability to Act as Decapacitation Factors1". Biology of Reproduction. 74 (2): 275–287. doi:10.1095/biolreprod.105.044644. ISSN 0006-3363. PMID 16221991.
  2. 1 2 3 Bedford, J. M.; Chang, M. C. (1962-01-01). "Removal of decapacitation factor from seminal plasma by high-speed centrifugation". American Journal of Physiology. Legacy Content. 202 (1): 179–181. doi:10.1152/ajplegacy.1962.202.1.179. ISSN 0002-9513. PMID 13866460.
  3. 1 2 3 4 Dukelow, W. Richard; Chernoff, H. N.; Williams, W. L. (1967-12-01). "PROPERTIES OF DECAPACITATION FACTOR AND PRESENCE IN VARIOUS SPECIES". Reproduction. 14 (3): 393–399. doi:10.1530/jrf.0.0140393. ISSN 0022-4251. PMID 4965247.
  4. 1 2 3 Bi, Ye; Xu, Wen-Ming; Wong, Hau Yan; Zhu, Hui; Zhou, Zuo-Min; Chan, Hsiao Chang; Sha, Jia-Hao (March 2009). "NYD-SP27, a novel intrinsic decapacitation factor in sperm". Asian Journal of Andrology. 11 (2): 229–239. doi:10.1038/aja.2009.6. ISSN 1008-682X. PMC 3735031. PMID 19252507.
  5. 1 2 3 Gibbons, Rachel; Adeoya-Osiguwa, Susan A.; Fraser, Lynn R. (2005-10-01). "A mouse sperm decapacitation factor receptor is phosphatidylethanolamine-binding protein 1". Reproduction. 130 (4): 497–508. doi:10.1530/rep.1.00792. ISSN 1741-7899. PMID 16183867.
  6. 1 2 3 4 Fraser, Lynn R.; Harrison, R. a. P.; Herod, Jane E. (1990-05-01). "Characterization of a decapacitation factor associated with epididymal mouse spermatozoa". Reproduction. 89 (1): 135–148. doi:10.1530/jrf.0.0890135. ISSN 0022-4251. PMID 2197409.
  7. ↑ Lu, Chung-Hao; Lee, Robert Kuo-Kuang; Hwu, Yuh-Ming; Chu, Shian-Ling; Chen, Ying-Jie; Chang, Wei-Chao; Lin, Shau-Ping; Li, Sheng-Hsiang (2011-03-01). "SERPINE2, a Serine Protease Inhibitor Extensively Expressed in Adult Male Mouse Reproductive Tissues, May Serve as a Murine Sperm Decapacitation Factor1". Biology of Reproduction. 84 (3): 514–525. doi:10.1095/biolreprod.110.085100. ISSN 0006-3363. PMID 21084713.
  8. ↑ Zhu, Jiuming; Massey, Joe B.; Mitchell-Leef, Dorothy; Elsner, Carlene W.; Kort, Hilton I.; Roudebush, William E. (February 2006). "Platelet-activating factor acetylhydrolase activity affects sperm motility and serves as a decapacitation factor". Fertility and Sterility. 85 (2): 391–394. doi:10.1016/j.fertnstert.2005.07.1303. PMID 16595216.
  9. ↑ Zalazar, Lucia; Stival, Cintia; Nicolli, Anabella R.; De Blas, Gerardo; Krapf, Dario; Cesari, Andreina (September 2020). "Male Decapacitation Factor SPINK3 Blocks Membrane Hyperpolarization and Calcium Entry in Mouse Sperm". Frontiers in Cell and Developmental Biology. 8 (2): 1041. doi:10.3389/fcell.2020.575126. PMC 7554638. PMID 33102481.
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