title: Involvement of sperm plasma membrane and cytoskeletal proteins in human male infertility.
abstract: OBJECTIVE
  To assess the physicochemical characteristics of sperm plasma membrane and to evaluate the immunohistochemical expression of transmembrane and cytoskeletal proteins in spermatozoa isolated from normospermic fertile donors and asthenozoospermic infertile patients.
  
  
  METHODS
  Case-control study.
  
  
  METHODS
  Academic male infertility center.
  
  
  METHODS
  Twenty-five infertile patients affected by idiopathic asthenozoospermia and 21 age-matched normospermic fertile donors.
  
  
  METHODS
  Sperm parameters were evaluated; membrane fluidity and hydration studies, and immunohistochemical analysis were performed in isolated spermatozoa.
  
  
  METHODS
  Semen analyses to ascertain volume, sperm count, motility, and morphology; then membrane fluidity and hydration studies and immunohistochemical analysis were performed on isolated spermatozoa.
  
  
  RESULTS
  Spermatozoa from the asthenozoospermic group exhibited a reduced fluidity at the lipid-water interface level, an increased fluidity of the deeper portion of the bilayer, and a lower plasma membrane hydration than normospermic cells. Moreover, the immunohistochemical expression of ezrin, Cdc42, CD9, F-actin, and β-tubulin was higher in normospermic samples.
  
  
  CONCLUSIONS
  Our results together assume that a cytoskeletal reorganization induced by a disturbance in the physicochemical features of sperm plasma membrane, and potentially mediated by ezrin, Cdc42, and tetraspanin CD9, could have a role in idiopathic asthenozoospermia.
authors.affiliation: Department of Clinical and Molecular Sciences-Histology, Polytechnic University of Marche, Ancona, Italy. e.salvolini@univpm.it
authors.forename: Eleonora
authors.initials: E
authors.lastname: Salvolini
authors.forename: Eddi
authors.initials: E
authors.lastname: Buldreghini
authors.forename: Guendalina
authors.initials: G
authors.lastname: Lucarini
authors.forename: Arianna
authors.initials: A
authors.lastname: Vignini
authors.forename: Andrea
authors.initials: A
authors.lastname: Lenzi
authors.forename: Roberto
authors.initials: R
authors.lastname: Di Primio
authors.forename: Giancarlo
authors.initials: G
authors.lastname: Balercia
mesh_terms: D000199:Actins / Q000378:metabolism; D000328:Adult; D053627:Asthenozoospermia / Q000378:metabolism* / Q000473:pathology / Q000503:physiopathology*; D016022:Case-Control Studies; D002462:Cell Membrane / Q000378:metabolism*; D003598:Cytoskeletal Proteins / Q000378:metabolism; D003599:Cytoskeleton / Q000378:metabolism*; D006801:Humans; D007150:Immunohistochemistry; D007248:Infertility, Male / Q000378:metabolism / Q000473:pathology / Q000503:physiopathology; D008297:Male; D008560:Membrane Fluidity / Q000502:physiology; D008565:Membrane Proteins / Q000378:metabolism*; D008875:Middle Aged; D008954:Models, Biological; D018384:Oxidative Stress / Q000502:physiology; D013075:Sperm Capacitation / Q000502:physiology; D013094:Spermatozoa / Q000166:cytology / Q000378:metabolism*; D060245:Tetraspanin 29 / Q000378:metabolism; D014404:Tubulin / Q000378:metabolism; D014867:Water / Q000378:metabolism; D020764:cdc42 GTP-Binding Protein / Q000378:metabolism; D000099149:Ezrin
chemical_list: D000199:Actins; D003598:Cytoskeletal Proteins; D008565:Membrane Proteins; D060245:Tetraspanin 29; D014404:Tubulin; D014867:Water; D020764:cdc42 GTP-Binding Protein; D000099149:Ezrin; C554869:CD9 protein, human