Association of Eppin with Semenogelin on Human Spermatozoa1
Abstract
Eppin (SPINLW1; GeneID, 57119) is a single-copy gene encoding a cysteine-rich protein found only in the testis and epididymis, which contains both Kunitz-type and WAP-type four disulfide core protease inhibitor consensus sequences. This study demonstrates that, in seminal plasma and on human spermatozoa following ejaculation, Eppin is bound to semenogelin I (Sg). Six different experimental approaches: 1) immunoprecipitation from spermatozoa and seminal plasma with anti-Eppin, 2) colocalization in semen and spermatozoa, 3) incubation of recombinant Eppin (rEppin) and rSg and immunoprecipitation with either anti-Eppin or anti-Sg, 4) far-Western blotting of Eppin and Sg, 5) Saturation binding of 125I-Sg to Eppin, which is competed by unlabeled Sg, and 6) direct binding of 125I-Sg to Eppin on a blot, all demonstrate that Eppin and Sg bind to each other. To study the specificity of binding, recombinant fragments of Eppin and Sg were made and demonstrate that the Eppin(75-133) C-terminal fragment binds the Sg(164-283) fragment containing the only cysteine in human Sg I (Cys-239). Reduction and carboxymethylation of Cys239 blocks binding of 125I-rEppin, indicating that a disulfide bond may be necessary for Eppin binding. The physiological significance of the Eppin-semenogelin complex bound on the surface of ejaculate spermatozoa lies in its ability to provide antimicrobial activity for spermatozoa, which has been reported for both Eppin and semenogelin-derived peptides, and in its ability to provide for the survival and preparation of spermatozoa for fertility in the female reproductive tract.
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EPPIN harbors a HHMC and shows no HF changes on the archaic, but 27 such SNCs on the modern human lineage.
“Another gene harboring a HHMC with similar functions is EPPIN174, which shows no HF changes on the archaic, but 27 such SNCs on the modern human lineage.”
From A catalog of single nucleotide changes distinguishing modern humans from archaic hominins (2019) · cites this paper as [174]
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A catalog of single nucleotide changes distinguishing modern humans from archaic hominins
Kuhlwilm, M., & Boeckx, C. (2019) · Scientific Reports · doi:10.1038/s41598-019-44877-x · Cited by 108 · see citing works
- Authors
- Wang, Z., Widgren, E. E., Sivashanmugam, P., O’Rand, M. G., & Richardson, R. T.
- Affiliations
- University of North Carolina at Chapel Hill (US)
- Venue
- Biology of Reproduction
- Publisher
- Oxford University Press (OUP)
- Published
- 2005-05-01
- Volume
- 72
- Issue
- 5
- Pages
- 1064-1070
- ISSN
- 0006-3363 (ISSN-L)
- 1529-7268
- OpenAlex
- W2142323380
- Cited by
- 83
- References
- 19
- Citations by year
- 2025: 3 · 2024: 2 · 2023: 2 · 2022: 1 · 2021: 2 · 2020: 3 · 2019: 6 · 2018: 6 · 2017: 2 · 2016: 1 · 2015: 3 · 2014: 4 · 2013: 7 · 2012: 5
- FWCI
- 7.32
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biology of Reproduction (publishedVersion)
- PubMed (publishedVersion)
- BioOne Complete (BioOne) (submittedVersion)
- Funders
- National Institutes of Health (1z01hd000627-05)
- Fogarty International Center (D43 TW/HD 00627)
- Topics
- Health Sciences › Medicine › Reproductive Medicine › Sperm and Testicular Function
- Health Sciences › Medicine › Rheumatology › Urologic and reproductive health conditions
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
- Keywords
- Eppin, semenogelin I, spermatozoa, seminal plasma, protein-protein binding, cysteine-rich proteins, Kunitz-type inhibitor, disulfide bonds, sperm surface proteins, antimicrobial activity, sperm fertility, epididymis
- MeSH terms
- Female, Humans, Immunohistochemistry, Male, Membrane Proteins, Peptide Fragments, Protein Binding, Proteins, Recombinant Proteins, Semen, Spermatozoa, Seminal Vesicle Secretory Proteins, Multiprotein Complexes, Proteinase Inhibitory Proteins, Secretory, In Vitro Techniques
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