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  • Sperm surface proteomics: from protein lists to biological function
  • Brewis IA; Gadella BM
  • Mol Hum Reprod 2010[Feb]; 16 (2): 68-79
  • Proteomics technologies have matured significantly in recent years and proteomics driven research articles in reproductive biology and medicine are increasingly common. The key challenge is to move from lists of identified proteins to informed understanding of biological function. This review introduces the range of proteomics workflows most commonly used for protein identification before focusing on the mammalian sperm cell at fertilization as an exemplar for proteomic studies. We review the work of others on entire cells but then argue that proper subcellular fractionation and proper solubilization strategies offers critical advantages to achieving increased biological understanding. In relation to understanding initial gamete recognition events at fertilization (capacitation, zona binding and acrosomal exocytosis) it is imperative to study the sperm surface proteome by using purified plasma membrane fractions. Although this task is challenging there are now strategies at our disposal to achieve comprehensive coverage of the proteins at the sperm surface. Within this context it is also important to understand the milieu of the sperm cell during transit from the testis to the oviduct as proteins (or other entities) from the genital tract epithelia and fluids may also affect the composition and organization of proteins on the sperm surface. Finally the arguments presented for studying the cell plasma membrane proteome to understand the role of the cell surface equally apply to all cell types with important roles in reproductive function.
  • |*Proteomics[MESH]
  • |Animals[MESH]
  • |Cell Membrane/metabolism[MESH]
  • |Humans[MESH]
  • |Male[MESH]
  • |Models, Biological[MESH]
  • |Proteins/*metabolism[MESH]
  • |Spermatozoa/*metabolism[MESH]

  • *{{pmid19717474}}
    *<b>[ Sperm surface proteomics: from protein lists to biological function ]</b> Mol Hum Reprod 2010; 16(2) ; 68-79 Brewis IA; Gadella BM


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    Mol Hum Reprod

    68 2.16 2010