Capacitated and acrosome reacted spermatozoa of goat (Capra indicus): a fluorescence and electron microscopic study.
Plasma membrane alterations accompanying in vitro capacitation and acrosome reaction of goat spermatozoa were studied using lectin labelling, scanning electron microscopy, and freeze-fracture methods. Fluorescein isothiocyanate linked lectins namely; Canavalia ensiformis (ConA), Maclura pomifera (MPA), Arachis hypogaea (PNA), Glycine max (SBA) and Triticum vulgaris (WGA) agglutinin were used to examine the distribution of surface carbohydrates during these two events. The head and the sperm tail reveal altered lectin labelling features after capacitation and acrosome reaction. After capacitation the surface coat components for MPA, SBA, and WGA are shed from the spermatozoon head. ConA receptors on the head are retained after capacitation but are partially shed in the acrosome reacted spermatozoa. SBA receptor sites appear on the sperm tail of the capacitated spermatozoa. Unusual morphological changes attending capacitation involve the sperm tail-end which develops a novel entity, which we have termed 'spatula'. The 'spatula' shows strong binding with ConA and WGA only. In the acrosome reacted spermatozoa the spatulated tail-end unwinds with a concomitant loss of lectin labelling. Highly ordered membrane particles, 'ladders' of the middle piece of the epididymal sperm tail, disappear and IMP clearings appear on the middle piece and in the spatulated ends of the capacitated spermatozoa. But in the acrosome reacted sperm IMPs reappear and are randomly disposed on the middle-piece and are clustered in small patches on the principal-piece. IMP free areas appear on the plasma membrane covering the acrosome and the outer acrosomal membrane (OAM) of the capacitated spermatozoa. The plasma membrane and OAM fuse at multiple foci and appear as acrosomal 'ghosts' which remain associated with the sperm head even after acrosome reaction.
Department of Biophysics, Panjab University, Chandigarh, India.
S R
SR
Bawa
M A
MA
Pabst
G
G
Werner
H K
HK
Bains
D000177:Acrosome / Q000502:physiology*; D000818:Animals; D002462:Cell Membrane / Q000502:physiology / Q000648:ultrastructure*; D003208:Concanavalin A; D016650:Fluorescein-5-isothiocyanate; D005456:Fluorescent Dyes; D005614:Freeze Fracturing; D006041:Goats / Q000502:physiology*; D037102:Lectins; D008297:Male; D008854:Microscopy, Electron; D008855:Microscopy, Electron, Scanning; D019887:Peanut Agglutinin; D037121:Plant Lectins; D013075:Sperm Capacitation; D013094:Spermatozoa / Q000502:physiology / Q000648:ultrastructure*; D014909:Wheat Germ Agglutinins
D005456:Fluorescent Dyes; D037102:Lectins; D019887:Peanut Agglutinin; D037121:Plant Lectins; D014909:Wheat Germ Agglutinins; D003208:Concanavalin A; C034551:maclurin; D016650:Fluorescein-5-isothiocyanate