Characterization of extracellular Ca2+ -dependent full-type hyperactivation in ejaculated boar spermatozoa preincubated with a cAMP analog

2017 ◽  
Vol 84 (11) ◽  
pp. 1203-1217 ◽  
Author(s):  
Nagisa Otsuka ◽  
Hiroshi Harayama
Keyword(s):  
Camp Analog ◽  
Boar Spermatozoa

Characterization of the glycoconjugates of boar testis and epididymis

Reproduction ◽  
2000 ◽  
pp. 325-335 ◽  
Author(s):  
A Calvo ◽  
LM Pastor ◽  
S Bonet ◽  
E Pinart ◽  
M Ventura
Keyword(s):  
Ricinus Communis ◽  
Lectin Histochemistry ◽  
Apical Part ◽  
Seminiferous Tubules ◽  
In Situ Characterization ◽  
Intense Staining ◽  
Terminal Galactose ◽  
Boar Spermatozoa

Lectin histochemistry was used to perform in situ characterization of the glycoconjugates present in boar testis and epididymis. Thirteen horseradish peroxidase- or digoxigenin-labelled lectins were used in samples obtained from healthy fertile boars. The acrosomes of the spermatids were stained intensely by lectins with affinity for galactose and N-acetyl-galactosamine residues, these being soybean, peanut and Ricinus communis agglutinins. Sertoli cells were stained selectively by Maackia ammurensis agglutinin. The lamina propria of seminiferous tubules showed the most intense staining with fucose-binding lectins. The Golgi area and the apical part of the principal cells of the epididymis were stained intensely with many lectins and their distribution was similar in the three zones of the epididymis. On the basis of lectin affinity, both testis and epididymis appear to have N- and O-linked glycoconjugates. Spermatozoa from different epididymal regions showed different expression of terminal galactose and N-acetyl-galactosamine. Sialic acid (specifically alpha2,3 neuraminic-5 acid) was probably incorporated into spermatozoa along the extratesticular ducts. These findings indicate that the development and maturation of boar spermatozoa are accompanied by changes in glycoconjugates. As some lectins stain cellular or extracellular compartments specifically, these lectins could be useful markers in histopathological evaluation of diseases of boar testis and epididymis.

Immunological approach to the characterization of the outer acrosomal membrane of boar spermatozoa

1985 ◽  
Vol 11 (2) ◽  
pp. 143-155 ◽  
Author(s):  
Adriana C. Hinrichsen ◽  
Edda Töpfer-Petersen ◽  
Thomas Dietl ◽  
Christian Schmoeckel ◽  
Wolf-B. Schill
Keyword(s):  
Acrosomal Membrane ◽  
Immunological Approach ◽  
Boar Spermatozoa

scholarly journals Kinetic characterization of the changes in protein tyrosine phosphorylation of membranes, cytosolic Ca2+ concentration and viability in boar sperm populations selected by binding to oviductal epithelial cells

Reproduction ◽  
2001 ◽  
pp. 469-480 ◽  
Author(s):  
AM Petrunkina ◽  
J Friedrich ◽  
W Drommer ◽  
G Bicker ◽  
D Waberski ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Tyrosine Phosphorylation ◽  
Membrane Integrity ◽  
Free Swimming ◽  
Sperm Binding ◽  
Preferential Binding ◽  
Functional Modulation ◽  
And Control ◽  
Boar Spermatozoa

On reaching the oviduct, spermatozoa are retained in the isthmic region of the oviduct until ovulation occurs. The essential steps of capacitation are co-ordinated in this region. In this study, a primary cell culture system of oviductal epithelial cells was established to investigate sperm binding to oviductal epithelium and modulation of sperm function during incubation under capacitating conditions in co-culture with oviductal epithelial cells. Epithelial cells were stripped from the oviducts of sows and cultivated for 5-7 days on Lab-Tek Chamber slides on Matrigel. The preparations on chamber slides and suspensions of control spermatozoa were incubated for 3 h in Tyrode's albumin lactate pyruvate (TALP) medium. At 3, 30, 60, 90 and 180 min the free-swimming spermatozoa were collected by washing, and membrane integrity, tyrosine phosphorylation patterns and [Ca(2+)](i) of bound, unbound and control spermatozoa were assessed with fluorescent probes (propidium iodide, Cy-3 and fluo-3-AM). The cells bound to oviductal epithelial cells showed reduced cytosolic Ca(2+) concentration, reduced and almost absent tyrosine phosphorylation of membrane proteins and higher viability at the time of the first sampling. Increases in Ca(2+) concentration and cell death occurred much more slowly during incubation in cells bound to oviductal epithelial cells compared with free-swimming spermatozoa, and no changes in tyrosine phosphorylation were observed. The preferential binding of viable, low-Ca(2+) cells with suppressed tyrosine phosphorylation and slower functional modulation of boar spermatozoa attached to oviductal epithelial cells might represent a mechanism for selecting functionally competent spermatozoa and prolonging their lifespan by delaying capacitation in the oviductal reservoir.

Characterization of actin isoforms in ejaculated boar spermatozoa

1988 ◽  
Vol 20 (2) ◽  
pp. 133-144 ◽  
Author(s):  
Antonella Casale ◽  
Marina Camatini ◽  
Omar Skalli ◽  
Giulio Gabbiani
Keyword(s):  
Actin Isoforms ◽  
Boar Spermatozoa

Characterization of membrane-associated actin in boar spermatozoa

1990 ◽  
Vol 253 (2) ◽  
pp. 202-214 ◽  
Author(s):  
R. N. Peterson ◽  
J. J. Bozzola ◽  
W. P. Hunt ◽  
A. Darabi
Keyword(s):  
Boar Spermatozoa
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