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Biomedical subjects

A V Tennov

Publications and source records attributed to A V Tennov.

8 recordsLinked to original sources
PubMed1989

[A decrease in the content of immunoreactive alpha- and gamma-endorphins in the blood and the suppression of their hypersecretion under the influence of dexamethasone in emotional stress in monkeys].

Daily administration of 12 mg of dexamethasone to monkeys during 10 days resulted in decrease of the levels of alpha- and gamma-endorphins and cortisol 7 days after the first injection. The titers of these peptides in plasma of monkeys. exposed to two hours of immobilization stress were elevated twice above basal levels. The maximum elevation took place 6 hours after the beginning of immobilization. This effect wasn't detected in monkeys, which received 12 mg of dexamethasone during 10 days.

Acute Disease↗
PubMed1986

[Detection of the pro-opiomelanocortin peptide fragments--beta-endorphin and ACTH--in the adrenals of rats and mice by immunohistochemistry].

Independent peptide fragments of pro-opiomelanocortin molecule, beta-endorphin and ACTH, have been detected immunohistochemically in the adrenal glands of rats and mice. Immunoreactive beta-endorphin and ACTH have been revealed in the adrenal medulla and reticular zone of the adrenal cortex. beta-endorphin and ACTH distribution patterns in adrenal sections were identical, which is indicative of the linked synthesis of these peptides in the adrenal gland. The data obtained suggest the existence of pituitary-independent mechanisms regulating corticosteroidogenesis in the adrenal gland, involving adrenal pro-opiomelanocortin fragments.

Adrenal Glands↗
PubMed1985

[Distribution of alpha-, beta- and gamma-endorphins in the forebrain and diencephalon of the rat brain (immunohistochemical study)].

The investigation performed by means of specific rabbit antisera is one of the stages for mapping peptides. This is necessary for revealing functional role of the endorphins in the CNS. The indirect method of Coons is applied in parallel series of frontal paraffin slices of the brain 10 mcm thick. Neurons containing alpha-, beta- and gamma-endorphins are localized in the same brain areas. These are structures of the palaeocortex (the prepiriform cortex and the diagonal area) and those of the hypothalamus (the supraoptic, arcuate, ventromedial, mammillary nuclei, anterior and posterior fields). Endorphinergic neural fibers run within composition of various conducting cerebral systems, such as the corpus collosum, fornix, internal and external capsules.

Animals↗
PubMed1985

[Identification of pro-opiomelanocortin and the secretion of its peptide fragments in the adrenals of the bull].

Immunoreactive alpha-, beta- and gamma-endorphins and beta-lipotropin--C-terminal peptide fragments of pro-opiomelanocortin (POMC)--were discovered and measured by RIA in the bovine adrenal medulla and cortex. These peptides were also discovered in perfusates of the adrenal gland. POMC proper and some intermediate forms of its processing not differing in electrophoretic mobility from the respective molecular forms of hypophyseal POMC were identified in the medulla and cortex of the adrenals by the immunoblotting technique with the use of antiserum to beta-lipoprotein. It is concluded that POMC gene is expressed in the adrenal medulla and cortex and that as a result of POMC processing a noticeable amount of its peptide fragments is formed and secreted in adrenal cells. The authors thus suggest the presence of existence of the pituitary-unrelated mechanisms of adrenal function control with participation of POMC peptides synthesized in the adrenals.

Adrenal Glands↗
PubMedDate not supplied

[Radioimmunological assay of plasma levels of alpha-gamma-endorphins in healthy donors and patients with endogenous depression].

Radioimmunological procedure enabled to estimate alpha- and gamma-endorphins in human blood plasma without pre-extraction. Basal level of these neuropeptides in peripheric blood plasma of 18 healthy donors constituted: C alpha = 392 +/- 244 pg/ml and C gamma = 20.6 +/- 9.1 pg/ml. Content of these endorphins in blood plasma did not depend on age and sex. Concentration of alpha- and gamma-endorphins were shown to correlate in peripheric blood (r = 0.88); this suggests the overall mechanisms for regulation of their synthesis, secretion and degradation. At the same time, distinct differences in concentrations of alpha- and gamma-endorphins in blood plasma were not found in groups of healthy donors and of patients with endogenous psychoses and pronounced depressive symptoms.

Adolescent↗
PubMedDate not supplied

Dimensions of homo- and heteropolymeric sections of DNA synthesized by reverse transcription from globin mRNA matrices.

The lengths of globin messenger RNAs, isolated from rabbit and pigeon reticulocytes, and single-stranded complementary DNAs, synthesized from mRNA in presence of RNA-directed DNA-polymerase and oligo(dt) have been investigated by polyacrylamide gel electrophoresis under denaturing conditions. The cDNA preparations contained a fraction which corresponded in length to the alpha and beta chains of the mRNA used as a matrix. The lengthwise distribution of poly(A) sequences, isolated from globin mRNAs, corresponded to a statistical distribution, with a maximum at 75-80 nucleotides and with a maximum length of approximately 150 nucleotides. The lengthwise distribution of poly(dt) sequences, isolated from cDNA, corresponded to the poly(A) sequence distribution. It was concluded that: 1) cDNA is heterogeneous with respect to the length of poly(dt) sequences located at the 5' end of the molecule; 2) there was no selective use as primer of only that oligo(dt) which was located within the complex formed with the 5' end of the mRNA poly(A) sequence; 3) the heterogeneity of poly(DT) corresponded qualitatively to two models of template-primer interaction: selective use as a true primer of the oligonucleotide located in the complex formed with the 3' end of mRNA, and a statistical distribution of primer along the poly(A) sequence; and 4) the heterogeneity of the homopolymeric section of the cDNA may affect the kinetics of hybridization with mRNA, which possibly explains the previously observed [1] anomalous dependence of the hybridization rate on time.

Animals↗