دورية أكاديمية
أعرض في EDS

Binding of Equine Seminal Lactoferrin/Superoxide Dismutase (SOD-3) Complex Is Biased towards Dead Spermatozoa.

التفاصيل البيبلوغرافية
العنوان: Binding of Equine Seminal Lactoferrin/Superoxide Dismutase (SOD-3) Complex Is Biased towards Dead Spermatozoa.
المؤلفون: Alghamdi AS; Departments of Agriculture and Natural Resources, University of Minnesota Crookston, Crookston, MN 56716, USA., Fedorka CE; Gluck Equine Research Center, University of Kentucky, Lexington, KY 40546, USA., Scoggin KE; Gluck Equine Research Center, University of Kentucky, Lexington, KY 40546, USA., Esteller-Vico A; Gluck Equine Research Center, University of Kentucky, Lexington, KY 40546, USA., Beatty K; Departments of Agriculture and Natural Resources, University of Minnesota Crookston, Crookston, MN 56716, USA., Davolli G; Gluck Equine Research Center, University of Kentucky, Lexington, KY 40546, USA., Ball BA; Gluck Equine Research Center, University of Kentucky, Lexington, KY 40546, USA., Troedsson MHT; Gluck Equine Research Center, University of Kentucky, Lexington, KY 40546, USA.
المصدر: Animals : an open access journal from MDPI [Animals (Basel)] 2022 Dec 23; Vol. 13 (1). Date of Electronic Publication: 2022 Dec 23.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: Molecular Diversity Preservation International Country of Publication: Switzerland NLM ID: 101635614 Publication Model: Electronic Cited Medium: Print ISSN: 2076-2615 (Print) Linking ISSN: 20762615 NLM ISO Abbreviation: Animals (Basel) Subsets: PubMed not MEDLINE
أسماء مطبوعة: Original Publication: Basel, Switzerland : Molecular Diversity Preservation International, 2011-
مستخلص: Sperm-neutrophil binding is an important facet of breeding and significantly impacts fertility. While a specific seminal plasma protein has been found to reduce this binding and improve fertility (CRISP-3), additional molecule(s) appear to promote binding between defective sperm and neutrophils. Recent work has suggested one of these proteins is lactoferrin (LF), an 80 kDa iron-binding protein found throughout the body, but the purity of the protein was not confirmed. It is unknown if LF binds to sperm selectively based on viability, and if receptors for LF are located on equine sperm. To evaluate this, we attempted to purify equine seminal LF from five stallions (n = 5), biotinylate LF, and evaluate potential binding site(s) on spermatozoa. LF was consistently associated with superoxide dismutase (SOD-3), and all attempts to separate the two proteins were unsuccessful. Flow cytometric and microscopic analyses were used to compare LF/SOD-3 binding to viable and nonviable spermatozoa. Additionally, various methods of biotinylation were assessed to optimize this methodology. Biotinylation of seminal plasma protein was an effective and efficient method to study seminal plasma protein properties, and the binding site for LF/SOD-3 was found to be broadly localized to the entire sperm cell surface as well as selective towards nonviable/defective sperm. Although we were not able to determine if the binding to equine spermatozoa was through LF or SOD-3, we can conclude that equine seminal LF is tightly bound to SOD-3 and this protein complex binds selectively to nonviable spermatozoa, possibly to mark them for elimination by neutrophil phagocytosis.
References: Hum Reprod. 2013 May;28(5):1297-308. (PMID: 23427237)
Urology. 2000 Jun;55(6):922-6. (PMID: 10840110)
J Vet Med Sci. 2002 Jan;64(1):75-7. (PMID: 11853152)
Cell Tissue Res. 1999 Jun;296(3):511-6. (PMID: 10370137)
Adv Exp Med Biol. 1994;357:61-70. (PMID: 7762447)
Equine Vet J. 2015 Jul;47(4):384-9. (PMID: 25537084)
Andrology. 2015 Nov;3(6):1068-75. (PMID: 26445132)
Reprod Domest Anim. 2012 Aug;47 Suppl 5:31-41. (PMID: 22913558)
Curr Pharm Des. 2009;15(17):1956-73. (PMID: 19519436)
Proc Soc Exp Biol Med. 1997 Dec;216(3):404-9. (PMID: 9402146)
J Vet Med Sci. 2003 Nov;65(11):1273-4. (PMID: 14665762)
Anim Reprod Sci. 2005 Oct;89(1-4):171-86. (PMID: 16102920)
Reprod Biomed Online. 2011 Feb;22(2):155-61. (PMID: 21195028)
Biol Reprod. 2015 Apr;92(4):94. (PMID: 25695722)
Cell Mol Life Sci. 2005 Nov;62(22):2560-75. (PMID: 16261254)
Science. 1977 Jul 15;197(4300):263-5. (PMID: 327545)
Reproduction. 2004 May;127(5):593-600. (PMID: 15129015)
Biometals. 2010 Jun;23(3):569-78. (PMID: 20195887)
Mol Reprod Dev. 1997 Aug;47(4):490-6. (PMID: 9211434)
Anim Reprod Sci. 2005 Oct;89(1-4):242-5. (PMID: 16265727)
Theriogenology. 2018 Jul 1;114:63-69. (PMID: 29597125)
J Histochem Cytochem. 1997 Aug;45(8):1053-7. (PMID: 9267466)
Biomol Eng. 2007 Sep;24(3):283-91. (PMID: 17379573)
Res Vet Sci. 2007 Oct;83(2):165-70. (PMID: 17222435)
Anim Reprod Sci. 2009 Sep;114(4):331-44. (PMID: 19081210)
Biol Reprod. 2011 Jul;85(1):157-64. (PMID: 21389342)
Tuberculosis (Edinb). 2009 Dec;89 Suppl 1:S49-54. (PMID: 20006305)
Int Immunol. 2009 Oct;21(10):1185-97. (PMID: 19692539)
Int J Antimicrob Agents. 2009 Apr;33(4):301.e1-8. (PMID: 18842395)
Vet Immunol Immunopathol. 2006 Nov 15;114(1-2):159-67. (PMID: 16973221)
Cancer Res. 1994 May 1;54(9):2310-2. (PMID: 8162571)
فهرسة مساهمة: Keywords: binding; equine; lactoferrin; seminal plasma; spermatozoa
تواريخ الأحداث: Date Created: 20230108 Latest Revision: 20230111
رمز التحديث: 20231215
مُعرف محوري في PubMed: PMC9817809
DOI: 10.3390/ani13010052
PMID: 36611662
قاعدة البيانات: MEDLINE
الوصف
تدمد:2076-2615
DOI:10.3390/ani13010052