Interaction of Extender Composition and Incubation Period on Cold Shock Susceptibility of Boar Spermatozoa

1972 ◽  
Vol 35 (3) ◽  
pp. 580-584 ◽  
Author(s):  
V. G. Pursel ◽  
L. A. Johnson ◽  
L. L. Schulman
Keyword(s):  
Incubation Period ◽  
Cold Shock ◽  
Boar Spermatozoa

INFLUENCE OF CARBON DIOXIDE ABSORBENT AND PERCENTAGE ATMOSPHERIC CARBON DIOXIDE ON OXYGEN UPTAKE BY BOAR SPERMATOZOA

1972 ◽  
Vol 52 (1) ◽  
pp. 57-63
Author(s):  
L. M. SANFORD ◽  
G. J. KING
Keyword(s):  
Carbon Dioxide ◽  
Oxygen Uptake ◽  
Incubation Period ◽  
Potassium Hydroxide ◽  
Atmospheric Carbon Dioxide ◽  
Initial Value ◽  
Atmospheric Carbon ◽  
Cell Motion ◽  
Boar Spermatozoa ◽  
Carbon Dioxide Absorbent

Boar spermatozoa were diluted in Ringer’s fructose or sulfate buffer and incubated aerobically for 4 hr at 37 C (a) in the presence of potassium hydroxide (KOH), hyamine hydroxide, or diethanolamine (DEA) absorbents, and (b) in 1, 2, or 3% atmospheric levels of carbon dioxide. Oxygen uptake by boar spermatozoa was enhanced by the presence of DEA compared with KOH and hyamine hydroxide. Incubation with DEA resulted in increased spermatozoan livability, more desirable cell motion, and smaller increases in buffer pH. Oxygen uptake by boar spermatozoa was optimum with 1 or 2% carbon dioxide, depending upon which buffer cells were diluted in. Levels of 2 and 3% carbon dioxide maintained oxygen uptake and livability of boar spermatozoa during later stages of the incubation period equally as well as 1% carbon dioxide. As the level of atmospheric carbon dioxide increased, buffer pH remained closer to the initial value.

Effect of Incubation and Cold Shock on Motility of Boar Spermatozoa and Their Relationship to Lipid Content

1967 ◽  
Vol 26 (5) ◽  
pp. 1078-1081 ◽  
Author(s):  
R. W. Benson ◽  
B. W. Pickett ◽  
R. J. Komarek ◽  
J. J. Lucas
Keyword(s):  
Lipid Content ◽  
Cold Shock ◽  
Boar Spermatozoa

Biochemical appraisal of a milk diluent for semen

1960 ◽  
Vol 54 (2) ◽  
pp. 166-169
Author(s):  
K. Friis Jakobsen ◽  
T. Mann
Keyword(s):  
Lactic Acid ◽  
Oxygen Uptake ◽  
Incubation Period ◽  
Milk Fat ◽  
Acid Production ◽  
Marked Effect ◽  
Lactic Acid Production ◽  
Milk Product ◽  
Bull Semen ◽  
Boar Spermatozoa

1. A study was made of the effects of a milk diluent on bull, ram and boar spermatozoa. Respiration and fructolysis of spermatozoa were used as the two main criteria of sperm activity. The milk diluent was a standardized and commercially available milk product, consisting of sterilized and homogenized milk, supplemented with milk fat.2. The rate of oxygen uptake measured manometrically in the presence of air was increased by the addition of the milk diluent throughout the entire incubation period. Fructose utilization was assessed by the rate of lactic-acid production. The rate of the anaerobic lactic-acid formation was higher in the presence of the milk diluent during the later stages of incubation.3. The effect of the milk diluent on sperm respiration was most striking in experiments with the sperm-rich portion of boar ejaculate obtained by fractionated collection. A somewhat less marked effect was observed with bull semen, and in ram semen the effect was comparatively weak.

INFLUENCE OF GLYCEROL CONCENTRATION AND FREEZING TO −79 C ON OXYGEN UPTAKE AND LIVABILITY OF BOAR AND BULL SPERMATOZOA

1972 ◽  
Vol 52 (1) ◽  
pp. 65-72 ◽  
Author(s):  
L. M. SANFORD ◽  
G. J. KING ◽  
J. W. MACPHERSON
Keyword(s):  
Oxygen Uptake ◽  
Incubation Period ◽  
Skim Milk ◽  
Egg Yolk ◽  
Freezing Process ◽  
Glycerol Concentration ◽  
Motile Cells ◽  
Boar Semen ◽  
Boar Spermatozoa

Boar and bull spermatozoa were diluted in a skim milk–egg yolk–glucose extender containing 0, 7.5, or 15% glycerol (v/v) and incubated aerobically for 6 hr at 37 C. Other partially diluted boar semen samples were cooled to 5 C. Glycerol was added to a final concentration of 0, 7.5, and 15%. Samples were frozen to −79 C, rewarmed, and incubated for 3 hr at 37 C. The presence of glycerol in the extender depressed (P < 0.01) the oxygen uptake by nonfrozen boar and bull spermatozoa during the 6-hr incubation period. The reduction of oxygen uptake by semen samples increased as the level of glycerol in the extender increased. There was a corresponding decrease (P < 0.01) in the number of motile cells at the conclusion of the incubation period. Glycerol appeared to have more of a detrimental effect on boar spermatozoan oxygen uptake. The rate of oxygen uptake by boar semen samples postfreezing was extremely depressed, suggesting that spermatozoa surviving the freezing process metabolize at a much lower rate than normal. Active progressive motility of most of the surviving boar spermatozoa ceased within 1–2 hr of incubation under the in vitro conditions of this experiment.

In vitro phagocytosis of boar spermatozoa by neutrophils from peripheral blood of sows

Reproduction ◽  
2000 ◽  
pp. 265-273 ◽  
Author(s):  
A Matthijs ◽  
W Harkema ◽  
B Engel ◽  
H Woelders
Keyword(s):  
Cold Shock ◽  
Female Genital Tract ◽  
Polymorphonuclear Leucocytes ◽  
Freezing And Thawing ◽  
Phagocytosis Assay ◽  
Acrosomal Exocytosis ◽  
Boar Spermatozoa ◽  
Female Genital ◽  
Serum Components

A considerable number of spermatozoa are used in each sow in routine artificial insemination. However, within a few hours after insemination, many spermatozoa are phagocytosed by polymorphonuclear leucocytes. Some aspects of sperm transport in the female genital tract in the sow have been thoroughly investigated, whereas little is known about the mechanisms involved in the phagocytosis of spermatozoa, or about which spermatozoa (fresh, capacitated or dead) are the most susceptible to ingestion by polymorphonuclear leucocytes. In this study, phagocytosis was investigated by use of an in vitro phagocytosis assay. Polymorphonuclear leucocytes were challenged with either untreated, cold-shocked or frozen-thawed spermatozoa, or with spermatozoa that had been treated to induce capacitation in vitro. The influence of serum on phagocytosis was also investigated. Treatment of the semen to induce capacitation in vitro considerably reduced the phagocytosis of spermatozoa, whereas crude treatments like cold-shock or freezing and thawing reduced phagocytosis only in the first 15-30 min of incubation with polymorphonuclear leucocytes. Viable spermatozoa were phagocytosed mainly through a pathway that was independent of complement or other serum components (for example, antibodies). Complement had little effect on phagocytosis of spermatozoa, but did cause acrosomal exocytosis and cell death.

scholarly journals Properties of spermatozoal superoxide dismutase and lack of involvement of superoxides in metal-ion-catalysed lipid-peroxidation and reactions in semen

1980 ◽  
Vol 191 (2) ◽  
pp. 289-297 ◽  
Author(s):  
M R F Mennella ◽  
R Jones
Keyword(s):  
Lipid Peroxidation ◽  
Superoxide Dismutase ◽  
Metal Ion ◽  
Cold Shock ◽  
Total Activity ◽  
Cellular Damage ◽  
Purification And Characterization ◽  
Boar Spermatozoa

1. The distribution and properties of superoxide dismutase were examined in mammalian semen, and the enzyme was used to investigate the role of superoxides in metal-ion-catalysed lipid-peroxidation reactions in spermatozoa. 2. Superoxide dismutase activity was detected in seminal plasma and spermatozoa from all species studied, exceptionally high activity being found in donkey semen. The enzyme is easily solubilized from spermatozoa, as 85-90% of the total activity is released by cold shock, a relatively mild form of cellular damage. 3. Purification and characterization of the enzyme from supernatant fractions prepared from cold-shocked boar spermatozoa showed it to be cyanide-sensitive, to have a mol.wt. of 31 000, a pI of 5.9 and to contain 1.85 g-atoms of copper and 1.91 g-atoms of zinc per mol of protein. However, extensive sonication of spermatozoa released a small amount of a cyanide-insensitive enzyme, presumably a mangano superoxide dismutase, from the mitochondrial matrix. 4. The presence of superoxide dismutase in spermatozoa, either intracellularly or extracellularly, did not inhibit ascorbate/Fe2+-catalysed lipid-peroxidation reactions, suggesting that superoxides are not essential intermediates in this system.

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