Physiology and endocrinology symposium: A proteome-based model for sperm mobility phenotype

D. P. Froman, A. J. Feltmann, K. Pendarvis, A. M. Cooksey, Shane C Burgess, D. D. Rhoads

Research output: Contribution to journalArticle

29 Citations (Scopus)

Abstract

Sperm mobility is defined as sperm movement against resistance at body temperature. Although all mobile sperm are motile, not all motile sperm are mobile. Sperm mobility is a primary determinant of male fertility in the chicken. Previous work explained phenotypic variation at the level of the sperm cell and the mitochondrion. The present work was conducted to determine if phenotypic variation could be explained at the level of the proteome using semen donors from lines of chickens selected for low or high sperm mobility. We began by testing the hypothesis that premature mitochondrial failure, and hence sperm immobility, arose from Ca 2+ overloading. The hypothesis was rejected because staining with a cell permeant Ca 2+-specific dye was not enhanced in the case of low mobility sperm. The likelihood that sperm require little energy before ejaculation and the realization that the mitochondrial permeability transition can be induced by oxidative stress arising from inadequate NADH led to the hypothesis that glycolytic enzymes might differ between lines. This possibility was confirmed by 2-dimensional electrophoresis for aldolase and phosphoglycerate kinase 1. This outcome warranted evaluation of the whole cell proteome by differential detergent fractionation and mass spectrometry. Bioinformatics evaluation of proteins with different expression levels confirmed the likelihood that ATP metabolism and glycolysis differ between lines. This experimental outcome corroborated differences observed between lines in previous work, which include mitochondrial ultrastructure, sperm cell oxygen consumption, and straight line velocity. Although glycolytic proteins were more abundant within highly mobile sperm, quantitative PCR of representative testis RNA, which included mRNA for phosphoglycerate kinase 1, found no difference between lines. In summary, we propose a proteome-based model for sperm mobility phenotype in which a genetic predisposition puts sperm cells at risk of premature mitochondrial failure as they pass through the excurrent ducts of the testis. In other words, we attribute mitochondrial failure to sperm cell and reproductive tract attributes that interact to affect sperm in a stochastic manner before ejaculation. In conclusion, our work provides a starting point for understanding chicken semen quality in terms of gene networks.

Original languageEnglish (US)
Pages (from-to)1330-1337
Number of pages8
JournalJournal of Animal Science
Volume89
Issue number5
DOIs
StatePublished - May 2011
Externally publishedYes

Fingerprint

endocrinology
Endocrinology
Proteome
proteome
Spermatozoa
physiology
spermatozoa
Phenotype
phenotype
phosphoglycerate kinase
Phosphoglycerate Kinase
Chickens
Ejaculation
ejaculation
cells
chickens
phenotypic variation
Testis
semen
testes

Keywords

  • Chicken
  • Glycolysis
  • Proteome
  • Sperm
  • Sperm motility

ASJC Scopus subject areas

  • Animal Science and Zoology
  • Food Science
  • Genetics

Cite this

Physiology and endocrinology symposium : A proteome-based model for sperm mobility phenotype. / Froman, D. P.; Feltmann, A. J.; Pendarvis, K.; Cooksey, A. M.; Burgess, Shane C; Rhoads, D. D.

In: Journal of Animal Science, Vol. 89, No. 5, 05.2011, p. 1330-1337.

Research output: Contribution to journalArticle

Froman, D. P. ; Feltmann, A. J. ; Pendarvis, K. ; Cooksey, A. M. ; Burgess, Shane C ; Rhoads, D. D. / Physiology and endocrinology symposium : A proteome-based model for sperm mobility phenotype. In: Journal of Animal Science. 2011 ; Vol. 89, No. 5. pp. 1330-1337.
@article{0d55d9ce85b8494584b7181157187d5b,
title = "Physiology and endocrinology symposium: A proteome-based model for sperm mobility phenotype",
abstract = "Sperm mobility is defined as sperm movement against resistance at body temperature. Although all mobile sperm are motile, not all motile sperm are mobile. Sperm mobility is a primary determinant of male fertility in the chicken. Previous work explained phenotypic variation at the level of the sperm cell and the mitochondrion. The present work was conducted to determine if phenotypic variation could be explained at the level of the proteome using semen donors from lines of chickens selected for low or high sperm mobility. We began by testing the hypothesis that premature mitochondrial failure, and hence sperm immobility, arose from Ca 2+ overloading. The hypothesis was rejected because staining with a cell permeant Ca 2+-specific dye was not enhanced in the case of low mobility sperm. The likelihood that sperm require little energy before ejaculation and the realization that the mitochondrial permeability transition can be induced by oxidative stress arising from inadequate NADH led to the hypothesis that glycolytic enzymes might differ between lines. This possibility was confirmed by 2-dimensional electrophoresis for aldolase and phosphoglycerate kinase 1. This outcome warranted evaluation of the whole cell proteome by differential detergent fractionation and mass spectrometry. Bioinformatics evaluation of proteins with different expression levels confirmed the likelihood that ATP metabolism and glycolysis differ between lines. This experimental outcome corroborated differences observed between lines in previous work, which include mitochondrial ultrastructure, sperm cell oxygen consumption, and straight line velocity. Although glycolytic proteins were more abundant within highly mobile sperm, quantitative PCR of representative testis RNA, which included mRNA for phosphoglycerate kinase 1, found no difference between lines. In summary, we propose a proteome-based model for sperm mobility phenotype in which a genetic predisposition puts sperm cells at risk of premature mitochondrial failure as they pass through the excurrent ducts of the testis. In other words, we attribute mitochondrial failure to sperm cell and reproductive tract attributes that interact to affect sperm in a stochastic manner before ejaculation. In conclusion, our work provides a starting point for understanding chicken semen quality in terms of gene networks.",
keywords = "Chicken, Glycolysis, Proteome, Sperm, Sperm motility",
author = "Froman, {D. P.} and Feltmann, {A. J.} and K. Pendarvis and Cooksey, {A. M.} and Burgess, {Shane C} and Rhoads, {D. D.}",
year = "2011",
month = "5",
doi = "10.2527/jas.2010-3367",
language = "English (US)",
volume = "89",
pages = "1330--1337",
journal = "Journal of Animal Science",
issn = "0021-8812",
publisher = "American Society of Animal Science",
number = "5",

}

TY - JOUR

T1 - Physiology and endocrinology symposium

T2 - A proteome-based model for sperm mobility phenotype

AU - Froman, D. P.

AU - Feltmann, A. J.

AU - Pendarvis, K.

AU - Cooksey, A. M.

AU - Burgess, Shane C

AU - Rhoads, D. D.

PY - 2011/5

Y1 - 2011/5

N2 - Sperm mobility is defined as sperm movement against resistance at body temperature. Although all mobile sperm are motile, not all motile sperm are mobile. Sperm mobility is a primary determinant of male fertility in the chicken. Previous work explained phenotypic variation at the level of the sperm cell and the mitochondrion. The present work was conducted to determine if phenotypic variation could be explained at the level of the proteome using semen donors from lines of chickens selected for low or high sperm mobility. We began by testing the hypothesis that premature mitochondrial failure, and hence sperm immobility, arose from Ca 2+ overloading. The hypothesis was rejected because staining with a cell permeant Ca 2+-specific dye was not enhanced in the case of low mobility sperm. The likelihood that sperm require little energy before ejaculation and the realization that the mitochondrial permeability transition can be induced by oxidative stress arising from inadequate NADH led to the hypothesis that glycolytic enzymes might differ between lines. This possibility was confirmed by 2-dimensional electrophoresis for aldolase and phosphoglycerate kinase 1. This outcome warranted evaluation of the whole cell proteome by differential detergent fractionation and mass spectrometry. Bioinformatics evaluation of proteins with different expression levels confirmed the likelihood that ATP metabolism and glycolysis differ between lines. This experimental outcome corroborated differences observed between lines in previous work, which include mitochondrial ultrastructure, sperm cell oxygen consumption, and straight line velocity. Although glycolytic proteins were more abundant within highly mobile sperm, quantitative PCR of representative testis RNA, which included mRNA for phosphoglycerate kinase 1, found no difference between lines. In summary, we propose a proteome-based model for sperm mobility phenotype in which a genetic predisposition puts sperm cells at risk of premature mitochondrial failure as they pass through the excurrent ducts of the testis. In other words, we attribute mitochondrial failure to sperm cell and reproductive tract attributes that interact to affect sperm in a stochastic manner before ejaculation. In conclusion, our work provides a starting point for understanding chicken semen quality in terms of gene networks.

AB - Sperm mobility is defined as sperm movement against resistance at body temperature. Although all mobile sperm are motile, not all motile sperm are mobile. Sperm mobility is a primary determinant of male fertility in the chicken. Previous work explained phenotypic variation at the level of the sperm cell and the mitochondrion. The present work was conducted to determine if phenotypic variation could be explained at the level of the proteome using semen donors from lines of chickens selected for low or high sperm mobility. We began by testing the hypothesis that premature mitochondrial failure, and hence sperm immobility, arose from Ca 2+ overloading. The hypothesis was rejected because staining with a cell permeant Ca 2+-specific dye was not enhanced in the case of low mobility sperm. The likelihood that sperm require little energy before ejaculation and the realization that the mitochondrial permeability transition can be induced by oxidative stress arising from inadequate NADH led to the hypothesis that glycolytic enzymes might differ between lines. This possibility was confirmed by 2-dimensional electrophoresis for aldolase and phosphoglycerate kinase 1. This outcome warranted evaluation of the whole cell proteome by differential detergent fractionation and mass spectrometry. Bioinformatics evaluation of proteins with different expression levels confirmed the likelihood that ATP metabolism and glycolysis differ between lines. This experimental outcome corroborated differences observed between lines in previous work, which include mitochondrial ultrastructure, sperm cell oxygen consumption, and straight line velocity. Although glycolytic proteins were more abundant within highly mobile sperm, quantitative PCR of representative testis RNA, which included mRNA for phosphoglycerate kinase 1, found no difference between lines. In summary, we propose a proteome-based model for sperm mobility phenotype in which a genetic predisposition puts sperm cells at risk of premature mitochondrial failure as they pass through the excurrent ducts of the testis. In other words, we attribute mitochondrial failure to sperm cell and reproductive tract attributes that interact to affect sperm in a stochastic manner before ejaculation. In conclusion, our work provides a starting point for understanding chicken semen quality in terms of gene networks.

KW - Chicken

KW - Glycolysis

KW - Proteome

KW - Sperm

KW - Sperm motility

UR - http://www.scopus.com/inward/record.url?scp=80051828658&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=80051828658&partnerID=8YFLogxK

U2 - 10.2527/jas.2010-3367

DO - 10.2527/jas.2010-3367

M3 - Article

C2 - 21036929

AN - SCOPUS:80051828658

VL - 89

SP - 1330

EP - 1337

JO - Journal of Animal Science

JF - Journal of Animal Science

SN - 0021-8812

IS - 5

ER -