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[Effect of the preliminary action of angiotensin on the sensitivity of the adrenal cortex of dogs to this peptide].

Experiments on dogs demonstrated that an increase of aldosterone secretion depended not only on the angiotensin II level in the blood, but also on the character of the changes in the peptide concentration: reaction of the glomerular zone of the adrenal cortex to this octapeptide increased after a preliminary angiotensin stimulation of the adrenal glands. The effect revealed was independent of the sum total dose of the preparation administered and was not accompanied by any increase in the glucocorticosteroid level in the plasma. This effect permitted the renin-aldosterone system to change under definite conditions to increased functional level without any marked rise of renin secretion and angiotensin II formation.

11-Hydroxycorticosteroids↗
PubMed1986

Acute stimulation of steroidogenesis in corpus luteum and adrenal cortex by peptide hormones. Rapid induction of a similar protein in both tissues.

Two-dimensional electrophoresis was used to detect a protein (ic) synthesized in rat corpus luteum cells in response to acute stimulation by human chorionic gonadotropin or dibutyryl cyclic AMP. This induced protein ic is isoelectric at pH 6.5 (isoelectric focusing) and has an apparent molecular weight of 28,000 (sodium dodecyl sulfate electrophoresis). The human chorionic gonadotropin or dibutyryl cyclic AMP dose response and time course of synthesis of the protein parallel those of progesterone synthesis in stimulated luteal cells. Additionally, cycloheximide, which inhibits the increase in progesterone formation caused by human chorionic gonadotropin or cAMP, also inhibits the synthesis of ic. Proteolytic polypeptide mapping suggests that ic has a very similar primary structure to another protein (pc), which has the same molecular weight as ic, differs from ic in pI, and is synthesized only in unstimulated cells. These polypeptide maps also demonstrate the close similarity of pc and ic to two proteins p and i, synthesized in control and in adrenocorticotropic hormone-stimulated rat adrenal cortex cells, respectively (Krueger, R. J. and Orme-Johnson, N. R. (1983) J. Biol. Chem. 258, 10159-10167). In both adrenal cortex and corpus luteum, binding of a tissue-specific polypeptide hormone acts via cAMP to cause increased steroidogenesis and induction of the synthesis of protein i (ic), with the same time course and hormone dose dependence. Also in both tissues, inhibition of protein synthesis at the level of translation (e.g. by cycloheximide addition) causes inhibition of i (ic) synthesis and of stimulated steroid production. This close correlation between the two different tissues in conditions which cause induction of the synthesis of these proteins suggests that the proteins may be common intermediaries in the control by polypeptide hormones of steroidogenesis in endocrine tissues.

Adipose Tissue↗
PubMed1990

Distinctive properties of adrenal cortex mitochondria.

The mitochondria in cells that synthesize steroid hormones not only have enzymes not present in mitochondria of non-steroidogenic cells but also have unique mechanisms for regulating the steroid substrate availability for certain of these enzymes. We have considered in detail the cytochrome P-450scc system that is located in the inner mitochondrial membrane and that catalyzes the initial and rate-determining step in the steroid hormone biosynthetic pathway. The flux through this pathway is regulated both by the levels of these catalysts themselves and by the availability of the substrate cholesterol for conversion to pregnenolone. These two levels of regulation occur in different time frames but are both controlled externally by the action of tissue-specific peptide hormone. We have used the adrenal cortex fasciculata cells as our paradigmatic cell type. The overall picture seems closely similar for mitochondria in other such steroidogenic cells when analogous data are available. Thus, in adrenal cortex fasciculata cells ACTH triggers several long-term (trophic) and short-term (acute) effects upon and within mitochondria that influence the initial and rate-determining step in the steroid hormone biosynthetic pathway. The only second messenger for both effects characterized thus far is cAMP. An increase in membrane-associated cAMP rapidly activates cAMP-dependent protein kinase, which in turn phosphorylates several cellular proteins, e.g., cholesterol ester hydrolase (vide supra). The trophic action, i.e., that produced by exposure of the cells to increased levels of ACTH or cAMP for a prolonged period (minutes to hours), increases the amounts of the steroid hormone synthesizing proteins in the mitochondria by increasing the transcription of the relevant nuclear genes. This latter process is not needed for the acute increase in the rate of steroid hormone biosynthesis. Whether induction of steroidogenic enzymes requires activation of a kinase has not been determined. However, the postulated SHIP proteins provide a mechanism by which cAMP levels and protein synthesis itself may regulate this induction. Mitochondria in steroidogenic tissues exert control over this process by their ability to recognize, import and process correctly the nuclear encoded precursors of the steroidogenic enzymes. Whether control at this level is ultimately dictated by nuclear or mitochondrial gene products or by an interplay between them is still unknown.(ABSTRACT TRUNCATED AT 400 WORDS)

Adrenal Cortex↗
PubMed1985

Pitfalls in the interpretation of whole-body autoradiograms: long-time retention in brain and adrenal cortex caused by metabolic incorporation of 14C from various labelled xenobiotics.

The long-time retention of radioactivity in mice was studied by whole-body autoradiography after administration of 1-14C-alkanes (C12 and C16), 1-14C-polychlorododecanes (56 and 68% Cl w/w), U-14C-polychlorohexadecane (23% Cl w/w), ethyl-14C-phenacetin and ring-3H-phenacetin. All the labelled xenobiotics, except the high-chlorinated (68% Cl) polychloroalkane and the ring-3H-phenacetin, gave rise to long-time (12-60 days) retention of radioactivity in the central nervous system and in the adrenal cortex; the distribution of radioactivity within the brain corresponded to the stain intensity of myelin stained sections. Administration of 1-14C-fatty acids (C12 and C16) and 1-14C-acetylcoenzyme A gave a similar distribution pattern. The lipophilic radioactivity in brain and adrenal tissue was extracted and separated with thin-layer chromatography. In the adrenal extracts, the label co-chromatography mainly with cholesteryl ester, and in the brain extracts with cholesterol and with more polar lipids (mainly phosphatidyl-choline and -ethanolamine). The brain homogenate contained a non-extracted, probably proteinaceous, residue, with comparably high radioactivity. The results show that several 14C-labelled xenobiotics which give long time retention of radioactivity in the adrenal cortex and brain, are degraded to intermediates with the possibility to become incorporated into endogenous substances. The high-chlorinated alkane (1) and ring-3H-phenacetin (2) did not give such long time retention due to its persistance towards degradation (1), and lack of labelling of the degradable part of the molecule (2). It is concluded that erroneous interpretations can be drawn from distribution studies if the routes of degradation and positions of label of the 14C-labelled compounds are not considered.

Adrenal Cortex↗
PubMed1987

[Reactions of the adrenal cortex and thyroid gland of hypophysectomized rats to hypothermia].

Male Wistar rats were hypophysectomized 7 days (group 1) and 4-7 weeks (group II) before exposure to hypothermia (4 degrees C for 1 1/2 h). The hypophysectomized rats from group I were devoid of both the posterior lobe and the adenohypophysis, while the rats from group II had the posterior hypophysis but not the adenohypophysis regenerated. A decreased arginine-vasopressin (AVP) blood level in group I (32%) and a very high level of AVP in group II (311%, P less than 0.05) was determined by RIA. The exposure to hypothermia did not influence the AVP plasma level. The thyroid hypofunction was revealed morphometrically in both hypophysectomized groups. Nevertheless, cooling stimulated the thyroid glands in rats of both experimental groups, like it was in the control. Thus, there is no evidence that thyroid gland reaction to hypothermia is affected by AVP. Cooling caused an increase of corticosteroid blood and adrenal cortex content in nonoperated control rats as well as in group II, but not in group I of experimental animals. Hence, it may be assumed that when the adenohypophysis is ablated, a high AVP blood level is necessary to realize the adrenal cortex response to hypothermia.

11-Hydroxycorticosteroids↗