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Query: UMLS:C0020538 (hypertension)
 170,190 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Arteries and veins of hypertensive rabbits were examined 8 weeks after partially constricting the abdominal aorta above both kidneys, and compared with those from sham-operated animals. Structural and functional changes in blood vessels after 2 weeks, when the arterial pressure first attained a new elevated level, have been described previously, and are now compared with changes 6 weeks later. The increase in blood vessel mass could be correlated with an increase in deoxyribonucleic acid (DNA) content. In contrast to the status at 2 weeks postoperatively, there was no increased uptake of 3H-thymidine, 3H-proline, or 3H-lysine at 2 months. Furthermore, at this time cell nuclei labeled with 3H-thymidine were infrequent. Some vessels showed evidence of change in the physical characteristics of their wall. Only minimal changes were observed in those parameters of adrenergic nerve function measured -- neuronal 3H-norepinephrine uptake and vessel wall catecholamine content -- that had been markedly changed at 2 weeks. The results of this work, together with those of other studies of this model, suggest two phases of response of the arterial wall to pressure rise: an initial dynamic proliferative cellular response mainly of vascular smooth muscle associated with changes in adrenergic neuronal parameters, and a subsequent equilibrium phase characterized by an increased number of smooth muscle cells, some changes in the extracellular components, and minimal changes in the adrenergic innervation.
Hypertension
PMID:Transient and persistent changes in rabbit blood vessels associated with maintained elevation in arterial pressure. 644 27

A lot of over 60 atherosclerotics with clinical manifestations of senile depressive illness was studied comparatively with a lot of subjects of the same age with essential arterial hypertension (EAH). As concerns the behaviour of the catecholamine content in CSF and blood, the total catecholamines are approxiately equal in the two lots, but with a clear difference of the catecholamine fractions. The CSF catecholamines behaviour in old atherosclerotics is characterized by the presence of increased values of noradrenaline (NA) and of adrenaline (A), with increased statistical significance, but without modifications of the adrenaline percentage (A %) from the total catecholamines, comparatively to the values found in normal subjects. The serotonin (5-HT) content of the CSF in men with atherosclerotic senile depressive illness was lower even than in subjects with coronary atherosclerosis. In atherosclerosis protides modifications precede the histologic changes. In CSF, GLU, ALA, TYR increase in old subjects. In blood, GLU, ALA, TYR, HIS, LEU, SER increase in the same subjects. ARG decreases with age. THR is higher in men than in women. In the urine of all the men as well as of all the women of more than 60 years, GLN and ALA have increased values. LYS increases with age. GLN and ARG are higher in men than in women.
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PMID:Pattern of the cerebrospinal fluid (CSF) and blood biogenic amines and of the CSF, blood and urine amino acids as pathogenetic ground of the senile depressive illness. 677 91

In chloralose-anaesthetized dogs intravenous infection of lysine-vasopressin (0.01 to 100 mU/kg) induced a dose-dependent increase in blood pressure and a decrease in heart rate. The same dosis injected by central (intracisternal) route induced a constant decrease in blood pressure. These results suggest the involvement of vasopressin in central cardiovascular control and in pathogenesis of some varieties of arterial hypertension.
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PMID:[Demonstration of a central hypotensive action of lysine vasopressin in the dog]. 679 10

The influence of clonidine, guanethidine and furosemide on the development of arterial hypertension was studied in rats with hypertension induced by repeated administration of lysine vasopressin. It was found that these drugs administered during long time periods together with lysine vasopressin prevented the development of arterial hypertension. When any of these drugs was given in combination with vasopressin plasma renin activity failed to rise and the level and turnover of catecholamines in rat brain were unchanged.
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PMID:Effects of clonidine, guanethidine and furosemide on the development of vasopressin hypertension in rat. 700 88

1 The cardiovascular effects of intravenous and intracisternal administration of neurohypophysial peptides were compared in dogs anaesthetized with chloralose. 2 Intravenous lysine-vasopressin (0.1 to 100 mu/kg) induced a dose-dependent increase in blood pressure and a decrease in heart rate. In contrast, intracisternal lysine-vasopressin (0.01 to 10 mu/kg induced a dose-related decrease in blood pressure and did not change heart rate. 3 Intracisternal oxytocin (1 and 10 mu/kg) increased blood pressure and did not change heart rate, whereas the same doses injected intravenously were inactive. 4 Pretreatment with guanethidine (15 mg/kg i.v. 24 h beforehand) abolished the hypotensive responses to intracisternal vasopressin but not the pressor action of intravenous vasopressin. 5 The pressor responses to central injections of oxytocin were not modified by guanethidine. 6 Hypotension elicited by intracisternal vasopressin was probably due to a decrease in sympathetic tone whereas the hypertension induced by intracisternal oxytocin was independent of variations in sympathetic tone.
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PMID:Effects of lysine-vasopressin and oxytocin on central cardiovascular control. 712 97

After unilateral nephrectomy and bilateral adrenal enucleation at 5 weeks of age, salt-loaded rats developed hypertension (ARH) at 6 weeks. Fibrous vascular protein and in vivo incorporation of 3H-lysine into this protein fraction were measured at 15 weeks of age in these animals. This study demonstrates: (1) that incorporation rates of 3H-lysine into cardiac collagen and elastin in ARH rats were greater than in control rats (p less than 0.001, respectively), and (2) that administration of phenoxy-benzamine hydrochloride decreased the incorporation of tritiated lysine into cardiac collagen in ARH rats, concomitant with a reduction in blood pressure. Based on these findings, increased synthesis of cardiac collagen and elastin appears to play an important role in the development of hypertension in ARH.
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PMID:Enhanced protein synthesis of heart in adrenal-regeneration hypertension and its reduction following antihypertensive treatment. 716 78

A shortened and modified eledoisin-hexapeptide sequence (Lys-Phe-Ile-Gly-Leu-MetNH2) was tested for their action on avoidance learning and blood pressure of rats with spontaneous hypertension (SH-rats) and intact Wistar rats. Both groups were 10, 14, and 26 weeks of age. Disorders of avoidance learning and elevation of blood pressure were likely to aggravate along with growing age of SH-rat. The used eledoisin-hexapeptide sequence is related to the essential C-terminal pentapeptide sequence of Substance P (SP). After injection of the used hexapeptide at doses of 250 microgram/kg intraperitoneally disorders in avoidance learning were completely eliminated from ten-week SH-rats or conditionally for SH-rats aged 14 and 26 weeks. Elevated blood pressure in SH-rats aged 26 weeks was reduced by the hexapeptide from 220 Torr to approximately 190 Torr. Blood pressure in SH-rats aged 14 weeks, originally about 180 Torr, was almost unaffected by the hexapeptide. Blood pressure went up from about 150 Torr to 190 in ten-week-old Sh-rats. A hypothesis was made about the mode of action of Substance P and related peptides.
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PMID:Effects of a substance P-analogue on blood pressure and avoidance learning of rats with spontaneous hypertension. 728 83

11 beta-Hydroxysteroid dehydrogenase (11-HSD) catalyzes the interconversion of cortisol and cortisone. This activity is postulated to protect the type I (mineralocorticoid) receptor from excessive concentrations of cortisol, allowing aldosterone to function as a mineralocorticoid. An enzyme with 11-HSD activity was isolated from rat liver and the corresponding rat and human cDNA and genomic clones isolated. This enzyme is a member of the "short chain dehydrogenase" family. Using site-directed mutagenesis, it was demonstrated that two highly conserved residues, Tyr-179 and Lys-183, are required for enzymatic function. Elimination of the amino terminus or the two glycosylation sites also destroys enzymatic activity. This may be due to actual disruption of enzymatic function or to effects on intracellular localization or stability of the enzyme. Examination of patients with apparent mineralocorticoid excess, a syndrome of juvenile hypertension thought to represent 11-HSD deficiency, did not reveal any mutations in the gene for this enzyme. There is substantial evidence for a second 11-HSD isozyme with distinct kinetic properties that is expressed in the renal distal tubule and possibly other sites of mineralocorticoid action. Apparent mineralocorticoid excess may involve this enzyme.
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PMID:Functional studies of 11 beta-hydroxysteroid dehydrogenase. 779 18

The conversion of 11-deoxycorticosterone (DOC) to aldosterone is catalyzed by a single enzyme, termed P450c11AS, which has 11 beta-hydroxylase, 18-hydroxylase and 18-oxidase activities. The normotensive Dahl salt-resistant (R) rat has two mutation in P450c11AS that increase its aldosterone synthase activity. If such a mutation were to occur in human patients the predicted phenotype would be low-renin hypertension with elevated ratios of plasma aldosterone to plasma renin activity. Before searching for P450c11AS mutations in such patients we sought to determine if mutations in human P450c11AS could increase enzymatic activity in a fashion analogous to the Dahl R rat. We used site-directed mutagenesis of the human P450c11AS cDNA to create the mutants Glu 136-->Asp, Lys 251-->Arg and the combination of the two; these mutations correspond to those seen in the Dahl R rat. Cells transfected with these mutant human P450c11AS sequences could convert [14C]DOC to corticosterone, 18OH-corticosterone, and aldosterone. In particular the Lys 251-->Arg mutant produced 4 times as much 18OH-corticosterone and 50-80% more aldosterone than the wild type. These data show that mutations of human P450c11AS can increase enzymatic activity, suggesting that such mutations could, in theory, be the basis of some forms of human low-renin hypertension.
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PMID:Artificial mutations in P450c11AS (aldosterone synthase) can increase enzymatic activity: a model for low-renin hypertension? 788 20

The structure of the histidine-binding protein (HBP, M(r) = 26,100), involved solely in active transport, has been determined by the molecular replacement technique and refined to 1.89-A resolution and to an R-factor of 0.199. The structure is that of two protein molecules, each with a bound L-histidine, in the asymmetric unit. Replacement solution was achieved by using a model of the crystal structure of the ligand-free, open-cleft form of the lysine/arginine/ornithine-binding protein which was modified so that the two domains are close to each other by bending the hinge connecting the two domains. The bound histidine is held in place by 10 hydrogen bonds, 2 salt links, and about 60 van der Waals contacts. Elucidation of the HBP structure brings a total of eight different binding proteins structures determined in our laboratory, including those with specificities for monosaccharides, maltodextrins (linear and cyclic), aliphatic amino acids, and inorganic oxyanions. These structures comprise about a third of the entire family of periplasmic binding proteins which act as initial primary high-affinity receptors of active transport in Gram-negative bacteria. Two of the binding proteins with specificities for glucose/galactose and maltodextrins also serve in a similar capacity in chemotaxis. Though these proteins have different molecular weights (ranging from 26,000 to 40,000), amino acid sequences, and ligand specificities, their three-dimensional structures are similar overall. They are elongated (axial ratios of 2:1) and composed of two similar globular domains separated by a deep cleft wherein the ligand-binding site is located. These structures provide understanding of molecular recognition of a variety of ligands at the atomic level and functional roles of the binding proteins.
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PMID:Refined 1.89-A structure of the histidine-binding protein complexed with histidine and its relationship with many other active transport/chemosensory proteins. 816 36


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