The Diagnostic Value of Seminal Proteins

Authors

  • A. J. Montes Department of Large Animal Surgery and Medicine, Auburn University, Auburn University, AL 36849
  • D. F. Wolfe Department of Large Animal Surgery and Medicine, Auburn University, Auburn University, AL 36849
  • J. G. W. Wenzel Department of Large Animal Surgery and Medicine, Auburn University, Auburn University, AL 36849
  • J. T. Bradley Department of Zoology and Wildlife Science, Auburn University, Auburn University, AL 36849
  • B. H. Estridge Department of Zoology and Wildlife Science, Auburn University, Auburn University, AL 36849

Keywords:

temperature, cellular response, stress response, stress protein, heat shock proteins, spermatozoa, scrotal hyperthermia

Abstract

It is well known that immediately following a sudden increase in temperature, all types of cells increase the production of a class of compounds that appears to enhance the cell's ability to recover from stress. A similar cellular response occurs with exposure to a wide variety of environmental assaults such as toxic metals, alcohols, anoxia, and many metabolic poisons. Due to the fact that so many different types of stimuli elicit the same cellular defense mechanism in virtually all organisms - from Escherichia coli to man - it is also commonly referred to as "the stress response" and the expressed proteins, "stress proteins" or "heat shock proteins" (HSP; 1).

The enhanced production of HSPs has been reported to occur in germ cells. Members of the HSP 70 and HSP 90 families have recently been isolated from rat spermatogenic cells,2,3 human ejaculated spermatozoa4 and bovine testicular tissue homogenates.5 The purpose of this study was to identify the presence of two HSPs, HSP 70 and ubiquitin, from ejaculated bovine spermatozoa following prolonged exposure to scrotal hyperthermia.

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Published

2020-04-09

Issue

Section

Society for Theriogenology