Persistent Link:
http://hdl.handle.net/10150/282670
Title:
Identification of seminal proteins related to fertility of bulls
Author:
McCauley, Tod Christopher, 1965-
Issue Date:
1998
Publisher:
The University of Arizona.
Rights:
Copyright © is held by the author. Digital access to this material is made possible by the University Libraries, University of Arizona. Further transmission, reproduction or presentation (such as public display or performance) of protected items is prohibited except with permission of the author.
Abstract:
These studies were conducted to determine the chemical identity of heparin binding proteins in semen that are related to fertility of bulls. The first study describes the isolation and identification of a 31,000 dalton fertility-associated antigen (FAA). FAA was found to have significant primary structure homology to a recently described novel DNase I-like protein. The physiological significance of the similarities between FAA and a protein homologous to DNase I is unknown at this time as no function has been described for the DNase I-like protein. The second study describes the isolation and identification of a 24,000 dalton seminal heparin binding protein. It was found to be similar, if not identical, to tissue inhibitor of metalloproteinase-2 (TIMP-2). TIMP-2 regulates matrix metalloprotease activity and therefore, potentially plays a key role in the structural makeup of the extracellular matrix. These findings suggest that regulation of enzymatic activity in seminal fluid is in large part a function of heparin binding proteins that have been correlated to fertility of bulls, one being a potentially novel extracellular nuclease and a second acting as a specific inhibitor of metalloprotease activity. In addition to the ability to modulate capacitation of sperm, seminal heparin binding proteins likely are key players in protecting sperm and male reproductive tract tissues from enzymatic hydrolysis. The proteins identified in this dissertation represent novel additions to the previously described seminal heparin binding protein families. Clearly, these data indicate a growing complexity of seminal fluid and implicate a novel Dnase I-like protein and TIMP-2 in affecting cellular events related to fertility potential of males.
Type:
text; Dissertation-Reproduction (electronic)
Keywords:
Biology, Animal Physiology.; Biology, Zoology.; Agriculture, Animal Culture and Nutrition.
Degree Name:
Ph.D.
Degree Level:
doctoral
Degree Program:
Graduate College; Animal Sciences
Degree Grantor:
University of Arizona
Advisor:
Ax, Roy L.

Full metadata record

DC FieldValue Language
dc.language.isoen_USen_US
dc.titleIdentification of seminal proteins related to fertility of bullsen_US
dc.creatorMcCauley, Tod Christopher, 1965-en_US
dc.contributor.authorMcCauley, Tod Christopher, 1965-en_US
dc.date.issued1998en_US
dc.publisherThe University of Arizona.en_US
dc.rightsCopyright © is held by the author. Digital access to this material is made possible by the University Libraries, University of Arizona. Further transmission, reproduction or presentation (such as public display or performance) of protected items is prohibited except with permission of the author.en_US
dc.description.abstractThese studies were conducted to determine the chemical identity of heparin binding proteins in semen that are related to fertility of bulls. The first study describes the isolation and identification of a 31,000 dalton fertility-associated antigen (FAA). FAA was found to have significant primary structure homology to a recently described novel DNase I-like protein. The physiological significance of the similarities between FAA and a protein homologous to DNase I is unknown at this time as no function has been described for the DNase I-like protein. The second study describes the isolation and identification of a 24,000 dalton seminal heparin binding protein. It was found to be similar, if not identical, to tissue inhibitor of metalloproteinase-2 (TIMP-2). TIMP-2 regulates matrix metalloprotease activity and therefore, potentially plays a key role in the structural makeup of the extracellular matrix. These findings suggest that regulation of enzymatic activity in seminal fluid is in large part a function of heparin binding proteins that have been correlated to fertility of bulls, one being a potentially novel extracellular nuclease and a second acting as a specific inhibitor of metalloprotease activity. In addition to the ability to modulate capacitation of sperm, seminal heparin binding proteins likely are key players in protecting sperm and male reproductive tract tissues from enzymatic hydrolysis. The proteins identified in this dissertation represent novel additions to the previously described seminal heparin binding protein families. Clearly, these data indicate a growing complexity of seminal fluid and implicate a novel Dnase I-like protein and TIMP-2 in affecting cellular events related to fertility potential of males.en_US
dc.typetexten_US
dc.typeDissertation-Reproduction (electronic)en_US
dc.subjectBiology, Animal Physiology.en_US
dc.subjectBiology, Zoology.en_US
dc.subjectAgriculture, Animal Culture and Nutrition.en_US
thesis.degree.namePh.D.en_US
thesis.degree.leveldoctoralen_US
thesis.degree.disciplineGraduate Collegeen_US
thesis.degree.disciplineAnimal Sciencesen_US
thesis.degree.grantorUniversity of Arizonaen_US
dc.contributor.advisorAx, Roy L.en_US
dc.identifier.proquest9831843en_US
dc.identifier.bibrecord.b38646791en_US
All Items in UA Campus Repository are protected by copyright, with all rights reserved, unless otherwise indicated.