scholarly journals Review of data on the role of cortisol at the final stages of spawning migration and the reproductive cycle in sturgeons (Acipenseridae)

2019 ◽  
Vol 323 (4) ◽  
pp. 412-428
Author(s):  
L.V. Bayunova
Keyword(s):  
Reproductive Cycle ◽  
Coelomic Fluid ◽  
Enzyme Linked Immunosorbent Assay ◽  
Hormonal Stimulation ◽  
Acipenser Gueldenstaedtii ◽  
Anadromous Migration ◽  
Interrenal Gland ◽  
Acipenser Stellatus ◽  
Stimulation Of

This review presents data on the role of cortisol (F) at the final stages of the reproductive cycle in migratory sturgeons (Acipenseridae) of the Volga-Caspian region: Russian sturgeon (Acipenser gueldenstaedtii Brandt et Ratzeburg, 1833), stellate sturgeon (Acipenser stellatus Pallas, 1771) and beluga (Huso huso (Linnaeus, 1758) obtained using a special variant of enzyme-linked immunosorbent assay (ELISA), which allowed us to compare the indicators of different years. The dynamics of F level in blood serum (BS) and the state of the interrenal gland (IG) in sturgeons were studied during feeding in the sea and at the beginning of the anadromous migration, as well as at the reproduction in the conditions of hatcheries. Higher levels of F in BS and high functional activity of IG are characteristic of sturgeon migrants when entering the river compared with data for fish during feeding in the sea. Reservation of sturgeon breeders at the hatchery led to decrease of the F serum level; and hormonal stimulation of maturation caused an increase in this indicator. Data on the F content in oocytes and abdominal (coelomic) fluid during maturation of female sturgeon are also presented. The F “profiles” were evaluated in sturgeon breeders under stress impacts that are unavoidable at the conditions of hatchery enterprises, as well as under experimentally simulated stress impacts. Peculiarities of the interaction of the hypothalamic-pituitary-gonadal and hypothalamic-pituitary-interrenal axes in sturgeons during reservation at hatcheries and during hormonal stimulation of fish maturation are discussed. Particular attention is paid to the compilation of data contained in the works performed in the late 90s – early 2000s under the guidance of Dr. Sc., prof. I.A. Barannikova (1926–2017), to whose memory the review is dedicated.

Regulation of total mitochondrial Ca2+ in perfused liver is independent of the permeability transition pore

1999 ◽  
Vol 276 (6) ◽  
pp. C1297-C1302 ◽  
Author(s):  
Ove Eriksson ◽  
Piero Pollesello ◽  
Erika Geimonen
Keyword(s):  
Permeability Transition Pore ◽  
Permeability Transition ◽  
Mitochondrial Content ◽  
Hormonal Stimulation ◽  
Intact Cells ◽  
Mitochondrial Energy Metabolism ◽  
Isolated Mitochondria ◽  
Rat Livers ◽  
Stimulation Of

Triggering of the permeability transition pore (PTP) in isolated mitochondria causes release of matrix Ca2+, ions, and metabolites, and it has been proposed that the PTP mediates mitochondrial Ca2+ release in intact cells. To study the role of the PTP in mitochondrial energy metabolism, the mitochondrial content of Ca2+, Mg2+, ATP, and ADP was determined in hormonally stimulated rat livers perfused with cyclosporin A (CsA). Stimulation of livers perfused in the absence of CsA with glucagon and phenylephrine induced an extensive uptake of Ca2+, Mg2+, and ATP plus ADP by the mitochondria, followed by a release on omission of hormones. In the presence of CsA, the PTP was fully inhibited, but neither the hormone-induced uptake of Ca2+, ATP, or ADP by mitochondria nor their release after washout of hormones was significantly changed. We conclude that the regulation of sustained changes in mitochondrial Ca2+content induced by hormonal stimulation is independent of the PTP.

scholarly journals Hormonal stimulation of mitochondrial glutaminase. Effects of vasopressin, angiotensin II, adrenaline and glucagon

1983 ◽  
Vol 210 (3) ◽  
pp. 957-960 ◽  
Author(s):  
S Corvera ◽  
J A García-Sáinz
Keyword(s):  
Angiotensin Ii ◽  
Hormonal Stimulation ◽  
Hormonal Modulation ◽  
Glutaminase Activity ◽  
Stimulation Of

Adrenaline (through alpha 1-adrenoceptors), vasopressin and angiotensin II stimulate mitochondrial glutaminase activity. This stimulation probably contributes to the ureogenic effect of these hormones. The activity of the enzyme is sensitive to Ca2+ depletion. A role of Ca2+ in hormonal modulation of glutaminase activity is suggested.

scholarly journals The role of cytosolic Ca2+, protein kinase C, and protein kinase A in hormonal stimulation of phospholipase D in rat hepatocytes.

1994 ◽  
Vol 269 (2) ◽  
pp. 849-859
Author(s):  
L. Gustavsson ◽  
G. Moehren ◽  
M.E. Torres-Marquez ◽  
C. Benistant ◽  
R. Rubin ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Protein Kinase A ◽  
Phospholipase D ◽  
Rat Hepatocytes ◽  
Hormonal Stimulation ◽  
Kinase C ◽  
Kinase A ◽  
Stimulation Of

Stimulation of Ca(2+)-dependent exocytosis of the sperm acrosome by cAMP acting downstream of phospholipase A2

Reproduction ◽  
2000 ◽  
pp. 57-68 ◽  
Author(s):  
J Garde ◽  
ER Roldan
Keyword(s):  
Arachidonic Acid ◽  
Phospholipase A2 ◽  
Phospholipase C ◽  
Phosphodiesterase Inhibitors ◽  
Dibutyryl Camp ◽  
Camp Phosphodiesterase ◽  
Ram Sperm ◽  
Camp Formation ◽  
Stimulation Of

Spermatozoa undergo exocytosis in response to agonists that induce Ca2+ influx and, in turn, activation of phosphoinositidase C, phospholipase C, phospholipase A2, and cAMP formation. Since the role of cAMP downstream of Ca2+ influx is unknown, this study investigated whether cAMP modulates phospholipase C or phospholipase A2 using a ram sperm model stimulated with A23187 and Ca2+. Exposure to dibutyryl-cAMP, phosphodiesterase inhibitors or forskolin resulted in enhancement of exocytosis. However, the effect was not due to stimulation of phospholipase C or phospholipase A2: in spermatozoa prelabelled with [3H]palmitic acid or [14C]arachidonic acid, these reagents did not enhance [3H]diacylglycerol formation or [14C]arachidonic acid release. Spermatozoa were treated with the phospholipase A2 inhibitor aristolochic acid, and dibutyryl-cAMP to test whether cAMP acts downstream of phospholipase A2. Under these conditions, exocytosis did not occur in response to A23187 and Ca2+. However, inclusion of dibutyryl-cAMP and the phospholipase A2 metabolite lysophosphatidylcholine did result in exocytosis (at an extent similar to that seen when cells were treated with A23187/Ca2+ and without the inhibitor). Inclusion of lysophosphatidylcholine alone, without dibutyryl-cAMP, enhanced exocytosis to a lesser extent, demonstrating that cAMP requires a phospholipase A2 metabolite to stimulate the final stages of exocytosis. These results indicate that cAMP may act downstream of phospholipase A2, exerting a regulatory role in the exocytosis triggered by physiological agonists.

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