Artificial Stimulation of Cryopreserved Human Spermatozoa by Sodium Nitroprusside, 2-Chloroadenosine, and 2-Deoxyadenosine

1997 ◽  
Vol 32 (3) ◽  
pp. 344-352 ◽  
Author(s):  
R.K. Sharma ◽  
A. Agarwal
Keyword(s):  
Sodium Nitroprusside ◽  
Human Spermatozoa ◽  
Stimulation Of

Stimulation of protein tyrosine phosphorylation by platelet-activating factor and progesterone in human spermatozoa

1995 ◽  
Vol 108 (1-2) ◽  
pp. 35-42 ◽  
Author(s):  
Michaela Luconi ◽  
Lorella Bonaccorsi ◽  
Csilla Krausz ◽  
Ginetta Gervasi ◽  
Gianni Forti ◽  
...  
Keyword(s):  
Tyrosine Phosphorylation ◽  
Platelet Activating Factor ◽  
Human Spermatozoa ◽  
Protein Tyrosine Phosphorylation ◽  
Protein Tyrosine ◽  
Stimulation Of

scholarly journals Prolactin Exerts a Prosurvival Effect on Human Spermatozoa via Mechanisms that Involve the Stimulation of Akt Phosphorylation and Suppression of Caspase Activation and Capacitation

Endocrinology ◽  
2009 ◽  
Vol 151 (3) ◽  
pp. 1269-1279 ◽  
Author(s):  
Dwi Ari Pujianto ◽  
Benjamin J. Curry ◽  
R. John Aitken
Keyword(s):  
Western Blot ◽  
Human Spermatozoa ◽  
Pcr Analysis ◽  
Dependent Manner ◽  
Sperm Capacitation ◽  
Caspase Activation ◽  
Apoptotic Pathway ◽  
Akt Phosphorylation ◽  
The Impact ◽  
Stimulation Of

The purpose of this study was to examine the impact of prolactin (PRL) on human sperm function, in light of a recent proteomic analysis indicating that these cells express the PRL receptor (PRLR). Immunocytochemical analyses confirmed the presence of PRLR in human spermatozoa and localized this receptor to the postacrosomal region of the sperm head as well as the neck, midpiece, and principal piece of the sperm tail. Nested PCR analysis indicated that these cells possess four splice variants of the PRLR: the long form and three short isoforms, one of which is reported for the first time. A combination of Western blot analyses and immunocytochemistry demonstrated that PRL inhibited sperm capacitation in a dose-dependent manner, suppressing SRC kinase activation and phosphotyrosine expression, two hallmarks of this process. The suppression of sperm capacitation was accompanied by a powerful prosurvival effect, supporting the prolonged motility of these cells and preventing the formation of spontaneous DNA strand breaks via mechanisms that involved the concomitant suppression of caspase activation. Western blot analyses indicated that the prosurvival effect of PRL on human spermatozoa involved the stimulation of Akt phosphorylation, whereas inhibitors of phosphatidylinositol-3-OH kinase and Akt negated this effect, as did the direct induction of sperm capacitation with cAMP analogues. We conclude that PRL is a prosurvival factor for human spermatozoa that prevents these cells from defaulting to an intrinsic apoptotic pathway associated with cell senescence. These findings have implications for preservation of sperm integrity in vivo and in vitro.

Stimulation of movement and acrosome reaction of human spermatozoa by PC12 liposomes encapsulating ATP

1995 ◽  
Vol 18 (5) ◽  
pp. 287-294 ◽  
Author(s):  
M. SKIBA-LAHIANI ◽  
J. AUGER ◽  
J. TERRIBILE ◽  
E. FATTAL ◽  
J. DELATTRE ◽  
...  
Keyword(s):  
Acrosome Reaction ◽  
Human Spermatozoa ◽  
Stimulation Of

scholarly journals Soluble guanylate cyclase in the molecular mechanism underlying the therapeutic action of drugs

2012 ◽  
Vol 58 (1) ◽  
pp. 32-42 ◽  
Author(s):  
N.V. Pyatakova ◽  
I.S. Severina
Keyword(s):  
Sodium Nitroprusside ◽  
Guanylate Cyclase ◽  
Soluble Guanylate Cyclase ◽  
Human Platelet ◽  
Dependent Manner ◽  
Therapeutic Action ◽  
Rat Lung ◽  
Concentration Dependent Manner ◽  
No Donors ◽  
Stimulation Of

The influence of ambroxol - a mucolytic drug - on the activity of human platelet soluble guanylate cyclase and rat lung soluble guanylate cyclase and activation of both enzymes by NO-donors (sodium nitroprusside and Sin-1) were investigated. Ambroxol in the concentration range from 0.1 to 10 μM had no effect on the basal activity of both enzymes. Ambroxol inhibited in a concentration-dependent manner the sodium nitroprusside-induced human platelet soluble guanylate cyclase and rat lung soluble guanylate cyclase with the IC50 values 3.9 and 2.1 μM, respectively. Ambroxol did not influence the stimulation of both enzymes by protoporphyrin IX.The influence of artemisinin - an antimalarial drug - on human platelet soluble guanylate cyclase activity and the enzyme activation by NO-donors were investigated. Artemisinin (0.1-100 μM) had no effect on the basal activity of the enzyme. Artemisinin inhibited in a concentration-dependent manner the sodium nitroprusside-induced activation of human platelet guanylate cyclase with an IC50 value 5.6 μM. Artemisinin (10 μM) also inhibited (by 71±4.0%) the activation of the enzyme by thiol-dependent NO-donor the derivative of furoxan, 3,4-dicyano-1,2,5-oxadiazolo-2-oxide (10 μM), but did not influence the stimulation of soluble guanylate cyclase by protoporphyrin IX. It was concluded that the sygnalling system NO-soluble guanylate cyclase-cGMP is involved in the molecular mechanism of the therapeutic action of ambroxol and artemisinin.

scholarly journals Atrial natriuretic factor and sodium nitroprusside increase cyclic GMP in cultured rat lung fibroblasts by activating different forms of guanylate cyclase

1987 ◽  
Vol 244 (1) ◽  
pp. 69-74 ◽  
Author(s):  
D C Leitman ◽  
V L Agnost ◽  
J J Tuan ◽  
J W Andresen ◽  
F Murad
Keyword(s):  
Sodium Nitroprusside ◽  
Guanylate Cyclase ◽  
Cyclic Gmp ◽  
Atrial Natriuretic Factor ◽  
Soluble Guanylate Cyclase ◽  
Fold Increase ◽  
Lung Fibroblasts ◽  
Rat Lung ◽  
Natriuretic Factor ◽  
Stimulation Of

We used cultured rat lung fibroblasts to evaluate the role of particulate and soluble guanylate cyclase in the atrial natriuretic factor (ANF)-induced stimulation of cyclic GMP. ANF receptors were identified by binding of 125I-ANF to confluent cells at 37 degrees C. Specific ANF binding was rapid and saturable with increasing concentrations of ANF. The equilibrium dissociation constant (KD) was 0.66 +/- 0.077 nM and the Bmax. was 216 +/- 33 fmol bound/10(6) cells, which corresponds to 130,000 +/- 20,000 sites/cell. The molecular characteristics of ANF binding sites were examined by affinity cross-linking of 125I-ANF to intact cells with disuccinimidyl suberate. ANF specifically labelled two sites with molecular sizes of 66 and 130 kDa, which we have identified in other cultured cells. ANF and sodium nitroprusside produced a time- and concentration-dependent increase in intracellular cyclic GMP. An increase in cyclic GMP by ANF was detected at 1 nM, and at 100 nM an approx. 100-fold increase in cyclic GMP was observed. Nitroprusside stimulated cyclic GMP at 10 nM and at 1 mM a 500-600-fold increase in cyclic GMP occurred. The simultaneous addition of 100 nM-ANF and 10 microM-nitroprusside to cells resulted in cyclic GMP levels that were additive. ANF increased the activity of particulate guanylate cyclase by about 10-fold, but had no effect on soluble guanylate cyclase. In contrast, nitroprusside did not alter the activity of particulate guanylate cyclase, but increased the activity of soluble guanylate cyclase by 17-fold. These results demonstrate that rat lung fibroblasts contain ANF receptors and suggest that the ANF-induced stimulation of cyclic GMP is mediated entirely by particulate guanylate cyclase.

Sign in / Sign up

Export Citation Format

Share Document