acid-phosphatase and Hypertension

Topics: Acetylglucosaminidase; Acid Phosphatase; Animals; Arteries; Arteriosclerosis; Diabetes Mellitus; Endocytosis; Humans; Hypertension; Lipid Metabolism; Lysosomes; Rabbits

To evaluate the effects of the lercanidipine on bone healing (BH) and bone density (BD) in the tibiae of spontaneously hypertensive rats (SHR), using histometric and tartrate-resistant acid phosphatase (TRAP) expression analyses.. Wistar and SHR were assigned to one of the following groups: normotensive rats (NTR) (n = 15), untreated SHR (n = 15), and lercanidipine-treated SHR (n = 15). The latter group was treated daily with lercanidipine for 6 weeks. Two weeks after the beginning of drug administration, a critical-sized surgical defect was created in the right tibia of all groups, whereas the contralateral tibia remained without defect. The animals were killed 30 days after the creation of the bone defect.. There were no significant differences among the groups for BH, trabecular BD, and the number of TRAP+ cells in the newly formed cortical bone (P > 0.05). SHR presented significantly lower cortical BD and increased cortical levels of TRAP+ cells, when compared with NTR and lercanidipine-treated SHR (P < 0.05).. SHR presented a lower cortical BD and increased levels of TRAP+ cells. In addition, the treatment of SHR with lercanidipine during 6 weeks was able to revert the deleterious effects of hypertension on cortical BD and on the number of TRAP+ cells in the tibia of SHR.

Topics: Acid Phosphatase; Animals; Antihypertensive Agents; Biomarkers; Bone Density; Bone Diseases; Bone Regeneration; Calcium Channel Blockers; Dihydropyridines; Hypertension; Image Processing, Computer-Assisted; Isoenzymes; Male; Rats; Rats, Inbred SHR; Rats, Wistar; Tartrate-Resistant Acid Phosphatase; Tibia; Wound Healing

This study evaluates the ligature-induced bone loss (BL) and quality of tooth-supporting alveolar bone in spontaneously hypertensive rats (SHRs) by histometric, histochemical, and immunohistochemical analyses and assesses the effects of lercanidipine on these parameters.. Wistar rats and SHRs were assigned to one of the following groups: normotensive rats (n = 15), untreated SHRs (n = 15), and treated SHRs (n = 15). The latter group was treated daily with lercanidipine for 45 days. Two weeks after the beginning of drug administration, the first right mandibular molar received a cotton ligature, whereas the contralateral tooth was left unligated. The following parameters were analyzed in the furcation area of decalcified histologic sections: BL, bone density (BD), number of positive cells for tartrate-resistant acid phosphatase (TRAP+), and expression of receptor activator of nuclear factor-kappa B ligand (RANKL) and osteoprotegerin (OPG).. In ligated teeth, no significant differences among groups were found regarding BL, TRAP+ cells, and the ratio of RANKL/OPG+ cells (P >0.05), although the expression of RANKL was decreased in the treated SHR group (P <0.05). Increased BL and decreased BD were observed around unligated teeth of the untreated and treated SHR groups (P <0.05). In the furcation area of the unligated teeth, the untreated SHR group presented a higher number of TRAP+ cells and higher ratio of RANKL/OPG+ cells compared to the other groups.. SHRs present harmful alterations in the quality of tooth-supporting bone, independently of inflammation. In addition, the administration of lercanidipine for 45 days decreased the expression of bone-resorption markers.

Topics: Acid Phosphatase; Alveolar Bone Loss; Alveolar Process; Animals; Antihypertensive Agents; Biomarkers; Bone Density; Dihydropyridines; Hypertension; Immunohistochemistry; Isoenzymes; Male; Molar; Osteoprotegerin; RANK Ligand; Rats; Rats, Inbred SHR; Rats, Wistar; Tartrate-Resistant Acid Phosphatase; Tooth Root

Genetic and environmental factors may contribute to the pathogenesis of essential hypertension. To facilitate genetic studies of hypertension and renal disorders, we sought to clone novel genes from a modified, equalized kidney (MEK) cDNA library of a spontaneously hypertensive rat (SHR).. A kidney cDNA library of an SHR was synthesized using the modified equalization method. Inserts of 350 random clones were amplified by polymerase chain reaction (PCR) and sequenced, of which 246 were presumably unknown after being compared against a nonredundant database in the GenBank. The cDNA ends of clone 38S were obtained by rapid amplification of cDNA ends, sequenced, and then analyzed with Translate, Prosite, Profile, SignalP, and TMpred programs.. The full-length cDNA was 938 bp, and translated into a 182-amino acid protein. The deduced protein had a metallophosphoesterase domain, a signal peptide at its amino end, a protein kinase C phosphorylation site, and a transmembrane domain. Northern blot analysis revealed that this gene was expressed in the heart, brain, spleen, lungs, liver, skeletal muscles, kidneys and testes of Sprague-Dawley rats. A putative protein of Arabidopsis thaliana shares 62% homology with protein 38S, but the two proteins differ in terms of function and structure.. Our results support that protein 38S is a novel membrane metallophosphoesterase, although its function in the kidneys remains to be elucidated. This study also demonstrates the feasibility of using PCR to clone novel genes from our MEK cDNA library.

Topics: Acid Phosphatase; Amino Acid Sequence; Animals; Base Sequence; Blotting, Northern; Cloning, Molecular; Gene Library; Hypertension; Kidney; Male; Molecular Sequence Data; Phosphoric Diester Hydrolases; Rats; Rats, Inbred SHR; Sphingomyelin Phosphodiesterase

In order to clarify the role of lysosomal enzymes in the developmental mechanisms of cerebral lesions under chronic hypertensive conditions, we histochemically and biochemically investigated acid phosphatase, N-acetyl-beta-glucosaminidase, and cathepsin B in the cerebral cortex and subcortical white matter in stroke-prone spontaneously hypertensive rats (SHRSP). Histochemical investigation showed that SHRSP had an increased number of cells with positive reaction to these enzymes in the edematous cortex and degenerated subcortical white matter. The cells with positive reaction were made up of reactive astrocytes and microglias. The activities of all enzymes in the aged SHRSP were higher than those in normotensive rats, the differences being significant at 24 weeks of age. The present study suggests that chronic hypertension or chronic edema causes increased activities of lysosomal enzymes in the cerebral cortex and subcortical white matter, and that the activated lysosomal enzymes take part in the developmental mechanisms of cystic formation as well as the diffuse degeneration of the white matter.

Topics: Acetylglucosaminidase; Acid Phosphatase; Animals; Astrocytes; Brain; Brain Edema; Cathepsin B; Cerebral Cortex; Cerebrovascular Disorders; Enzyme Activation; Hypertension; Male; Nerve Degeneration; Neurons; Rats; Rats, Inbred SHR; Rats, Inbred WKY

In an attempt to clarify the role of lysosomal enzymes in the developmental mechanisms of cerebral lesions under chronic hypertensive conditions, we biochemically investigated the activities of acid phosphatase (AcPase), N-acetyl beta-glucosaminidase (NAGase) and cathepsin B (CathB) in the cerebral cortex and subcortical white matter in stroke-prone spontaneously hypertensive rats (SHRSPs). We also investigated enzyme-histochemically the activities of AcPase and NAGase, and immunohistochemically the distribution of CathB. The activities of all enzymes tended to increase with advancing age. The enzyme activities in the aged SHRSPs were in general higher than those in normotensive rats, the differences being significant at 24 weeks of age. Histochemical investigation showed that SHRSPs had an increased number of cells with positive reaction to these enzymes in the edematous cortex with and without vascular changes, and degenerated subcortical white matter. These cells with positive reaction were made up of reactively increased astrocytes and microglia. Neurons in the edematous area also showed slightly intensified enzyme activities. The present studies suggest that chronic hypertension or chronic edema due to hypertension causes increased activities of lysosomal enzymes in the cerebral cortex and subcortical white matter and, thus, that activated lysosomal enzymes may take part in the developmental mechanisms of cystic formation as well as the diffuse degeneration of the white matter.

Topics: Acetylglucosaminidase; Acid Phosphatase; Animals; Blood Pressure; Body Weight; Brain; Cathepsin B; Cerebral Cortex; DNA; Histocytochemistry; Hypertension; Lysosomes; Male; Rats; Rats, Inbred SHR; Rats, Inbred WKY

Cytochemistry of peripheral blood lymphocyte enzymes was studied in 58 patients with State II essential hypertension (36 of these were treated with traditional hypotensive therapy and 22 with plasmapheresis + drug therapy). alpha-GPDH, LDH, and acid phosphatase activities were found reduced in these patients. The degree of the enzymic activity reduction (SDH included) depended on the disease standing and family history of patients. Plasmapheresis elevated the activities of energy enzymes and reduced arterial pressure, i.e. these parameters were in inverse correlation. In the patients treated by routine hypotensive therapy energy enzymes' activity was unchanged, despite the clinical effect.

Topics: Acid Phosphatase; Adult; Aged; Antihypertensive Agents; Combined Modality Therapy; Female; Glycerolphosphate Dehydrogenase; Humans; Hypertension; L-Lactate Dehydrogenase; Lymphocytes; Male; Middle Aged; Plasmapheresis

In order to obtain information about the changes in lysosomal enzyme activities in arterial endothelial cells under hypertensive conditions, a biochemical study was performed on 5 lysosomal enzymes, acid phosphatase, N-acetyl-beta-glucosaminidase (NAGase), cathepsin B, cathepsin D and beta-glucuronidase, in endothelial cells isolated by an enzymatic technique from the aorta of spontaneously and renal hypertensive rats, and normotensive control rats. The aortic endothelial cells in the old spontaneously and the renal hypertensive rats showed increased activities of enzymes examined in comparison with those in the age-matched control rats. Endothelial cells in young spontaneously hypertensive rats did not show any elevated enzyme activities compared with those in the controls, and the enzyme activities tended to increase with aging. From this, it is deduced that hypertension activates lysosomal enzyme activities in aortic endothelial cells. The differences in the activities of NAGase, cathepsin B and cathepsin D between hypertensive and control animals increased markedly with advancing age. These activated lysosomal enzymes seem to be involved in the developmental mechanism of arterial endothelial cell injury in hypertension and in further development of hypertensive vascular changes.

Topics: Acetylglucosaminidase; Acid Phosphatase; Animals; Aorta; Cathepsin B; Cathepsin D; Cell Separation; Endothelium, Vascular; Glucuronidase; Hypertension; Lysosomes; Male; Rats; Rats, Inbred SHR; Rats, Inbred WKY

In an attempt to clarify the role of lysosomal enzymes in the developmental mechanisms of the changes of cerebral microvessels under hypertensive conditions, the activities of acid phosphatase, N-acetyl-beta-glucosaminidase, and beta-glucuronidase in the isolated microvessels from the cerebral cortex of spontaneously and renal hypertensive rats were biochemically studied. The activities of all the enzymes were higher than those in normotensive control animals, although there was a variation in intensity according to the age and kind of enzymes. The enzyme activities in spontaneously hypertensive rats showed a tendency to increase with advancing age. Hypertension seems to increase activities of lysosomal enzymes in cerebral microvessels, and this activation may in turn play a role in the development of further hypertensive cerebrovascular and cerebral changes.

Topics: Acetylglucosaminidase; Acid Phosphatase; Animals; Blood Pressure; Body Weight; Cerebral Cortex; Glucuronidase; Hypertension; Hypertension, Renal; Lysosomes; Male; Microcirculation; Rats; Rats, Inbred SHR; Rats, Inbred WKY

Low-density lipoprotein (LDL) is essential for the regulation of cellular cholesterol homeostasis. Intracellular LDL cholesterol metabolism is achieved by the action of lysosomal enzymes. The hydrolytic cleavage of cholesterol is apparently suppressed in the smooth muscle of arterial vessels of hypertensive animal models, contributing to atherosclerosis. The change in the hydrolytic activity of the enzymes can be reversed by Ca2+ antagonists which also lower increased blood pressure. Thus, a blood pressure lowering effect of calcium antagonists may explain the antiatherosclerotic action of these agents. Preliminary data, using platelets as a model for studies on LDL action, suggest that LDL induces rapid cellular activation via phosphatidylinositol turnover.

Topics: Acetylglucosaminidase; Acid Phosphatase; Animals; Arteriosclerosis; Blood Platelets; Calcium Channel Blockers; Humans; Hyperlipidemias; Hypertension; Lipoproteins, LDL; Muscle, Smooth, Vascular; Rats; Rats, Inbred SHR; Risk Factors; Sterol Esterase

Electron microscopically the role of acid phosphatase (acid P) positive lysosomes in the pathogenesis of intramyocardial coronary artery lesions of hypertensive rats with bilaterally constricted renal arteries was studied. At 3 postoperative weeks, acid P positive lysosomes were increased in endothelial cells of the coronary arteries, but at 5 weeks and thereafter, they were decreased in number. In the intima, intimal smooth muscle cells with acid P positive lysosomes appeared at 3 postoperative weeks, but their number remained small as late as 9 postoperative weeks. The internal elastic lamina was fragmented into amorphous masses from 3 postoperative weeks, at 5 weeks and thereafter the fragmentation and disruption became severer, and at 9 weeks the lamina disappeared because of marked disruption. At 3 postoperative weeks, acid P positive extracellular lysosomes were observed in the gaps of the fragmented internal elastic lamina. At 5 weeks and thereafter, extracellular lysosomes and attenuated processes of medial smooth muscle cells with lysosomes were seen extending through the gaps of the fragmented internal elastic lamina. Necrosis of these extending cell processes and lysosomes remaining after the necrosis were observed. The findings suggested that the fragmentation and lytic change of the internal elastic lamina observed in hypertensive rat intramyocardial coronary arteries might be induced by extracellular lysosomes discharged not only from endothelial cells and intimal smooth muscle cells but also from the extending processes of medial smooth muscle cells into the gaps of the internal elastic lamina.

Topics: Acid Phosphatase; Animals; Coronary Vessels; Hypertension; Lysosomes; Male; Microscopy, Electron; Muscle, Smooth, Vascular; Rats; Rats, Inbred Strains

Some metabolic consequences of experimental hypertension on rat brain capillaries and kidney glomeruli have been studied in rats made hypertensive by a combination of deoxycorticosterone acetate injection and elevated salt intake (DOCA-salt hypertension) and isoproterenol injection. Enzyme activities were studied in vitro to ascertain directly or indirectly any changes in the metabolism of catecholamines and prostaglandins, and lysosomal integrity under conditions of experimental hypertension. Experimental hypertension was accompanied by an elevation in the activities of aromatic L-aminoacid decarboxylase, dopamine beta-hydroxylase, and malondialdehyde concentration, both in the brain capillaries and kidney glomeruli of rats. On the other hand, monoamine oxidase activity increased in brain capillaries but decreased in kidney glomeruli. Acid phosphatase activity increased marginally in kidney glomeruli but decreased significantly in brain capillaries. The catecholamine-synthesizing potential appears to have been augmented in both the tissue capillaries with a compensatory increase in the degrading enzyme activity in the brain capillaries of hypertensive rats. The absence of such an increase and an actual decrease in the monoamine oxidase activity in the kidney glomeruli may be responsible for the sustained maintenance of the hypertensive state. Increased malondialdehyde concentration may be due to the stimulation of the prostaglandin metabolism by the augmented catecholamine metabolism.

Topics: Acid Phosphatase; Animals; Aromatic-L-Amino-Acid Decarboxylases; Brain; Capillaries; Desoxycorticosterone; Dopamine beta-Hydroxylase; Female; Hypertension; Isoproterenol; Kidney Glomerulus; Male; Malondialdehyde; Monoamine Oxidase; Rats

Using electron microscopy and cytochemical techniques we investigated structures which are associated with long-term hypertension and ageing in the myocardial cell of the rat. Lysosomes, demonstrated by acid phosphatase and aryl sulfatase activities, were found mainly in the perinuclear region in young rats. With age these organelles appeared with increasing frequency in other regions of the cell. Spontaneously hypertensive rats (SHR) showed an earlier apparent migration of lysosomes than did normotensive rats (WKY). Our observations indicate that lysosomes were closely associated with autophagic vacuoles, membrane swirls , translucent mitochondria, myelin figures and other structures linked with degenerative events. In the oldest SHR lysosomes, autolysosomes (autophagic vacuoles with lysosomal activity), and degenerative structures were observed in various regions of the myocardial cell. Peroxisomes, as demonstrated by catalase activity, did not seem to be affected by hypertension or age. A number of dense osmophilic structures did not react for any of the enzymes studied; these included myelin figures, mitochondrial inclusions and diffuse dense bodies. Our observations implicate both ageing and hypertension in the enhancement of lysosomes and their end products.

Topics: Acid Phosphatase; Animals; Arylsulfatases; Autophagy; Cardiomegaly; Catalase; Histocytochemistry; Hypertension; Lysosomes; Microbodies; Microscopy, Electron; Myocardium; Rats; Rats, Inbred Strains; Sulfatases

In order to obtain information about changes in lysosomal enzyme activities in the aortic endothelial cells under hypertensive conditions, semiquantitative histochemical investigations of acid phosphatase (Ac-Pase) and N-acetyl-beta-glucosaminidase (NAGase) activities in the aorta of spontaneously hypertensive rats (SHR) were performed on 'Häutchen' monolayer preparations. The aortic endothelial cells in SHR showed increased Ac-Pase and NAGase activities as compared with those in control normotensive rats, and the activities tended to increase with advancing age. The degenerating process of endothelial cells expressed by lysosomal enzyme activity seems to be accelerated by hypertension. The increased lysosomal enzymes may participate in the further development of hypertensive vascular changes.

Topics: Acetylglucosaminidase; Acid Phosphatase; Animals; Aorta, Thoracic; Endothelium; Histocytochemistry; Hypertension; Lysosomes; Male; Rats; Rats, Inbred Strains

Topics: Acid Phosphatase; Aging; Animals; Carotid Arteries; Hemodynamics; Hypertension; Intracranial Aneurysm; Ligation; Male; Rats; Rats, Inbred Strains

In spontaneously hypertensive rats, prolonged hypertension caused a decrease in aortic cholesterol esterase activity with N-acetyl-beta-D-glucosaminidase activity increased and acid phosphatase activity unchanged [3]. The present study was undertaken to compare these changes with those caused by other experimentally induced types of hypertension. Treatment with DOCA-salt for one month significantly elevated both aortic cholesterol esterase and acid phosphatase activities. In contrast, to spontaneous hypertension, venous changes were also observed. An intake of 1% NaCl ad libitum produced results similar to those with the DOCA-salt treatment, despite the fact that blood pressure did not increase. This suggested that humoral factors were the main cause of the elevated enzyme activities in DOCA-salt hypertension. In rats made hypertensive by unilateral renal arterial constriction with contralateral nephrectomy (one clip--one kidney hypertension) or without contralateral nephrectomy (one clip--two kidney hypertension), aortic cholesterol esterase activities were unchanged, while aortic N-acetyl-beta-D-glucosaminidase, and aortic and venous acid phosphatase activities were increased. These results show distinct differences in the response of lysosomal enzymes during the three hypertensive states.

Topics: Acetylglucosaminidase; Acid Phosphatase; Animals; Aorta; Carboxylic Ester Hydrolases; Desoxycorticosterone; Hypertension; Hypertension, Renal; Lysosomes; Male; Rats; Sodium Chloride; Sterol Esterase

In an attempt to obtain information about the arterial lysosomal enzymes in hypertension, we biochemically investigated acid phosphatase (Ac-Pase) activity in the aorta of spontaneously hypertensive rats (SHR) and the effects of various antihypertensive drugs. Ac-Pase activity in SHR was always higher than that in age-matched control rats. The enzyme activity tended to increase progressively with advancing age, a tendency which was more pronounced in SHR than in control rats. The aging process expressed by the Ac-Pase activity seems to be accelerated under hypertensive conditions. Antihypertensive drugs such as reserpine, hydrochlorothiazide, hydralazine and propranolol significantly suppressed the rise of blood pressure and decreased the aortic Ac-Pase activity in SHR. In particular reserpine and propranolol lowered Ac-Pase activity more effectively than it did blood pressure. Hypertension as well as catecholamine seem to be involved in the increase in the aortic lysosomal enzyme activity in SHR.

Topics: Acid Phosphatase; Animals; Antihypertensive Agents; Aorta; Blood Pressure; Body Weight; Hypertension; Male; Rats; Rats, Inbred Strains

Acid phosphatase activity in the cerebral arterial system in spontaneously hypertensive rats (SHR) was cytochemically investigated. In the endothelial and medial smooth muscle cells, endoplasmic reticulums and Golgi complex revealed an intense acid phosphatase activity and primary lysosomes containing the high enzyme activity were found to be augmented in number. The enzyme activity was demonstrated in the vacuolated secondary lysosomes and in the intercellular spaces of the arterial walls. Lytic changes of the arterial mural cells and vessel matrix due to lysosomal enzymes were also evident. Causes of the lysosomal enzyme induction and roles of the enzyme in the developmental mechanism of hypertensive cerebrovascular changes in the SHR brain are discussed.

Topics: Acid Phosphatase; Age Factors; Animals; Cerebral Arteries; Endothelium; Enzyme Induction; Histocytochemistry; Hypertension; Inclusion Bodies; Lysosomes; Male; Muscle, Smooth, Vascular; Rats

Spontaneously hypertensive rats (SHRSP and SHR) and normotensive WKR were treated with hypotensive drugs, and arterial and venous enzyme activities were compared between treated and nontreated hypertensive groups. With the 4 month experiment, cholesterol esterase activity in the aorta from hypertensive SHRSP and SHR was significantly lower than that in the respective treated groups, whereas venous activity did not differ. By contrast, aortic NAGA activity was significantly higher in the hypertensive groups without any changes in venous activity. Acid phosphatase activity was unaltered. No effects of treatment were observed in the normotensive WKR. Accompanying a decrease in aortic cholesterol esterase, there was a marked increase in aortic cholesteryl esters accompanying hypertension. Aortic phosphodiesterase activity was significantly elevated in the hypertensive SHRSP and SHR compared with the respective treated groups. These results suggest that hypertension of long duration specifically decreased aortic cholesterol esterase activity with a consequent accumulation of cholesteryl esters in the aorta, and that this hemodynamic effect seemed to be partly mediated by cyclic AMP with an effect on the lysosomal membrane. These results could provide the biochemical bases for the relationship between hypertension and atherosclerosis.

Topics: 3',5'-Cyclic-AMP Phosphodiesterases; Acetylglucosaminidase; Acid Phosphatase; Animals; Aorta, Abdominal; Blood Pressure; Carboxylic Ester Hydrolases; Cholesterol Esters; Hexosaminidases; Hypertension; Male; Methyclothiazide; Rats; Reserpine; Sterol Esterase

Changes in aortic lipolytic enzyme activities (cholesterol esterase and lipoprotein lipase) and acid phosphatase activity during aging were investigated in three strains of rats with different blood pressures; stroke prone spontaneously hypertensive rats (SHRSP), spontaneously hypertensive rats (SHR) and normotensive Wistar Kyoto (WKR). The blood pressures of male, 7 month old animals, was 234 (SHRSP), 173 (SHR) and 128 (WKR) mmHg. The cholesterol esterase activity markedly decreased with age in the aortas of SHRSP, SHR and normotensive WKR rats, while acid phosphatase activity decreased only slightly, if at all, and lipoprotein lipase activity remained unchanged. This effect was enhanced by increasing blood pressure in SHRSP, SHR and WKR. The total aortic cholesterol content increased significantly with hypertension in a inverse relation with cholesterol esterase activity. These results suggest that cholesterol deposition in aged arteries is, at least partialy, ascribable to an age-related decrease in cholesterol esterase, and that hypertension aggravates the deposition of arterial cholesterol by accelerating the age-related decrease in aortic cholesterol esterase activity.

Topics: Acid Phosphatase; Aging; Animals; Aorta; Blood Pressure; Body Weight; Carboxylic Ester Hydrolases; Cerebrovascular Disorders; Cholesterol; Female; Hypertension; Male; Phospholipids; Rats; Sterol Esterase; Triglycerides

Vascular smooth muscle (VSM) cells from hypertensive and normotensive rat aortae and caudal arteries were isolated by enzymatic techniques, homogenized, and fractionated by differential pelleting. By these techniques, only mitochondria could be enriched more than fivefold in any one fraction. The other organelles were distributed heterogeneously in almost all fractions. Hypertensive smooth muscle enzyme distribution patterns were different from the normotensive, suggesting that changes in sedimentation characteristics had occurred. Activity of the enzyme 5'-nucleotidase increased in whole tissue homogenates and in the 'microsomal' fraction of aortic and caudal artery of hypertensive VSM. The lysosomal protease, cathepsin D, of hypertensive animals decreased in activity for both vascular smooth muscles while N-acetyl-beta-glucosaminidase and pNPPase (acid phosphatase) increased. The possibility of a functional deficiency in protein degradation causing lysosomal overloading is discussed.

Topics: Acetylglucosaminidase; Acid Phosphatase; Animals; Aorta; Arteries; Catalase; Cathepsins; Cell Membrane; Electron Transport Complex IV; Hypertension; Lysosomes; Mitochondria, Muscle; Muscle Proteins; Muscle, Smooth; Nucleotidases; Organoids; Rats

Samples of aortae and caudal arteries from normotensive and hypertensive rats were studied for cytochemical and biochemical determinations of acid and alkaline phosphatase activities. Cytochemical examination revealed an increased amount of acid phosphatase reaction product in hypertensive samples, with extensive localization to the extracellular matrix. Alkaline phosphatase activity was localized to the plasma membrane of fibroblasts and vascular smooth muscle cells and to the extracellular matrix. Biochemical assays of enzyme activities supported the cytochemical findings, showing increased activity in aortae from hypertensive rats.

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Aorta, Thoracic; Blood Pressure; Desoxycorticosterone; Hypertension; Male; Muscle, Smooth; Rats; Tail

Topics: Acid Phosphatase; Animals; Female; Glucuronidase; Hydrolases; Hypertension; Kidney; Lysosomes; Proteins; Rats; Renin

Changes in acid phosphatase activity in the cerebrovascular system and brain parenchyma in SHR were investigated histochemically. An increased activity of the enzyme was demonstrated in the SHR endothelial and medial smooth muscle cells of the cerebral arterial system as compared to the control. The pericytes of intraparenchymal blood vessels also showed an intensified enzyme activity. The enzyme activity increased with advancing age. In SHR brain parenchyma, the enzyme activity was decreased in the cortical nerve cells. Glial cells with the enzyme activity were increased in number and showed an intensified activity. Causative factors of changes in acid phosphatase activity in SHR cerebral arteries and parenchyma were discussed.

Topics: Acid Phosphatase; Aging; Animals; Brain; Cerebral Cortex; Chemical Phenomena; Chemistry; Hypertension; Male; Rats; Time Factors

Topics: Acid Phosphatase; Animals; Cathepsins; Centrifugation, Isopycnic; Glucuronidase; Hydrolases; Hypertension; Kidney Cortex; Lysosomes; Proteins; Rats; Renin; Tissue Distribution

Topics: Acid Phosphatase; Adenosine Triphosphatases; Alkaline Phosphatase; Animals; Cerebral Arteries; Histocytochemistry; Humans; Hypertension; Intracranial Arteriosclerosis; L-Lactate Dehydrogenase; Rats; Succinate Dehydrogenase

Topics: Acetylglucosaminidase; Acid Phosphatase; Animals; Antihypertensive Agents; Aorta; Arteries; Body Weight; Collagen; Desoxycorticosterone; Elastin; Glucose-6-Phosphatase; Hexosaminidases; Hypertension; Male; Nucleotidases; Organ Size; Rats; Rats, Inbred Strains

Topics: 4-Nitrophenylphosphatase; Acid Phosphatase; Alkaline Phosphatase; Animals; Cerebrovascular Disorders; Hypertension; Kidney; L-Lactate Dehydrogenase; Male; Rats; Succinate Dehydrogenase

The activity of succinate dehydrogenase, alpha-glycerophosphate dehydrogenase and acid phosphatase in the lymphocytes of peripheral blood was studied in 28 patients with hypertensive disease and vasorenal hypertension (the diagnosis was made on the basis of the findings of angiographic examination) by the method of quantitative cytochemical analysis suggested by R.P. Nartsissov. It was revealed that alpha-glycerophosphate dehydrogenase activity was significantly lower in vasorenal hypertension than in hypertensive disease. The calculation of the difference between the value of succinate dehydrogenase activity and that of alpha-glycerophosphate dehydrogenase activity in these groups was also significant. It is concluded that a complex of cytochemical analysis may be used in differential diagnosis of vasorenal hypertension and hypertensive disease.

Topics: Acid Phosphatase; Adolescent; Adult; Clinical Enzyme Tests; Diagnosis, Differential; Female; Glycerolphosphate Dehydrogenase; Humans; Hypertension; Hypertension, Renal; Hypertension, Renovascular; Lymphocytes; Male; Middle Aged; Oxidoreductases; Succinate Dehydrogenase

The functional abnormalities of the cells in the cardiovascular system in SHR were revealed by enzyme histo-cytochemical study. The enzymatic activity was usually increased in the area where the arteries branched and in proliferating cells in the thickened wall. Such was more remarkable in the distorted arteries with aging. Functional roles of these 4 enzymes were discussed.

Topics: Acid Phosphatase; Adenosine Triphosphate; Alkaline Phosphatase; Animals; Cardiovascular System; Hypertension; Male; Nucleotidases; Rats

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Aorta; Azides; Calcium; Desoxycorticosterone; Hypertension; Male; Microsomes; Mitochondria, Heart; Muscle, Smooth; Rats; Subcellular Fractions

Topics: Acetylglucosaminidase; Acid Phosphatase; Animals; Body Weight; Cardiomegaly; Cathepsins; Creatine Kinase; Desoxycorticosterone; Hexosaminidases; Hypertension; Lysosomes; Male; Myocardium; Organ Size; Rats; Sodium Chloride

Metabolic intermediate levels, glycolytic and Krebs cycle enzyme activities and lysosomal acid hydrolase activities were measured in aortas of spontaneously hypertensive (SHR) versus normotensive (WKY) rats. In the hypertensive aortas the level of lactate, the ratio of lactate to glucose and of lactate to malate was higher in the SHR than WKY aortas. In the hypertensive aortas the obvious shift of metabolism toward higher rate of glycolysis was associated with decreased activity of malate dehydrogenase and espically of lipoamide dehydrogenase. The latter is an essential compoenent of the alpha-ketoglutarate and pyruvate dehydrogenase enzyme complexes and it appears that these complexes are among the sites of arterialmetavolism which are primarily altered by the elevated blood pressure, resulting in increased production of lactate. The activity of the marker lysosomal enzyme N-acetyl-beta-glucosaminidase was unequivocally elevated in the hypertensive aortas. The activity of beta-glucuronidase exhibited incogruous differences between the SHR and WKY aortas and the activity of aortic acid phosphatase did not differ in the two rat strains. The results are discussed in relation to arterial injury, permeability, and atherogenesis.

Topics: Acetylglucosaminidase; Acid Phosphatase; Animals; Aorta; Dihydrolipoamide Dehydrogenase; Glucose; Hypertension; Lactates; Lysosomes; Malates; Male; Rats

Topics: Acid Phosphatase; Animals; Cathepsins; Choroid; Glucuronidase; Hypertension; Lysosomes; Pigment Epithelium of Eye; Rats; Retina; Retinal Degeneration

Topics: Acid Phosphatase; Adult; Aged; Alkaline Phosphatase; Brain; Brain Chemistry; Cerebrovascular Disorders; DNA; Female; Glycosaminoglycans; Humans; Hypertension; Intracranial Arteriosclerosis; Male; Middle Aged; RNA

The cellular events that occur in the vessel wall consequent to changes in endothelial permeability result in the progression of vascular disease, particularly atherosclerosis. Female rhesus monkeys were fed an atherogenic diet or were made hypertensive for 6-8 months; and their vessels were then compared with vessels from control monkeys. Length-defined segments of coronary vessels, the thoracic aorta, and the abdominal aorta showed significant increases in total connective tissue in the atherosclerotic and hypertensive groups; pulmonary vessels did not. The diseased aortic segments had increased levels of two lysosomal enzymes, acid phosphatase and beta-N-acetylglucosaminidase; pulmonary vessels were not diseased and did not show these changes. Coronary vessels from the atherosclerotic and hypertensive groups did not show an increase in enzyme levels on biochemical measurements, but focal accumulations of lysosomes were identified by cytochemical techniques. In atherosclerotic lesions, a doubling of cholesterol and more than a tenfold increase in cholesterol ester were found. These connective tissue and lysosomal changes are early features of primate vascular disease and may result from the accumulation of excessive substrate (cholesterol ester) in the lysosomes of vascular smooth muscle cells.

Topics: Acid Phosphatase; Animals; Aorta, Abdominal; Aorta, Thoracic; Arteries; Arteriosclerosis; Blood Vessels; Cholesterol; Connective Tissue; Coronary Vessels; Diet, Atherogenic; DNA; Female; Hexosaminidases; Hypertension; Lung; Lysosomes; Macaca mulatta

Esterase and Acid phosphatase isozymes were examined in a number of organs, glands and tissues from Spontaneously Hypertensive Rats (SHR) and kidney and liver from DOCA hypertensive rats at various stages in comparison with those of normotensive rats (CR). In SHR, the abnormalities in the patterns of esterase isozyme were demonstrated in endocrine glands and respiratory tracts as well as in the kidney, liver and digestive tracts throughout the whole life span, and abnormalities in the patterns of acid phosphatase isozyme was also demonstrated in the liver after seven days of age. Moreover, in DOCA hypertensive Rats, minute alterations in esterase isozyme were demonstrated in the kidney and liver after seventh month of the duration of hypertension.

Topics: Acid Phosphatase; Aging; Animals; Desoxycorticosterone; Digestive System; Embryo, Nonmammalian; Endocrine Glands; Esterases; Exocrine Glands; Female; Hypertension; Isoenzymes; Kidney; Lung; Male; Myocardium; Placenta; Pregnancy; Pregnancy Complications, Cardiovascular; Rats

Topics: Acid Phosphatase; Animals; Anti-Inflammatory Agents; Aorta, Thoracic; Aspirin; Connective Tissue; DNA; Elastin; Estradiol; Hexosaminidases; Hypertension; Lysosomes; Male; Methylprednisolone; Muscle, Smooth; Proteins; Rats; Vitamin D

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Aorta; Blood Pressure; Glucosephosphate Dehydrogenase; Hypertension; Isoenzymes; Kidney; L-Lactate Dehydrogenase; Liver; Malate Dehydrogenase; Male; Mesenteric Arteries; Mice; Mice, Inbred Strains; Myocardium; Rats

Topics: Acid Phosphatase; Aged; Cardiovascular Diseases; Humans; Hypertension; Male; Middle Aged; Prolactin; Prostate; Prostatic Neoplasms; Protein Binding; Reserpine; Testosterone

Topics: Acid Phosphatase; Adrenal Glands; Amino Acids; Animals; Blood Pressure; Brain Stem; Carboxy-Lyases; Coronary Vessels; Esterases; Hypertension; Isoenzymes; Kidney; Male; Organ Size; Pituitary Gland; Rats; Rats, Inbred Strains; Thyroid Gland

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Blood Pressure; Body Weight; Cholesterol; Diet; Esterases; Hypertension; Isoenzymes; Kidney; Liver; Organ Size; Pedigree; Rats; Rats, Inbred Strains; Rodent Diseases; Thyroid Gland

Topics: Acid Phosphatase; Angiotensin II; Animals; Blood Cell Count; Female; Fluoroscopy; Histocytochemistry; Hypertension; Lymph Nodes; Lymphocytes; Lysosomes; Mesenteric Arteries; Monocytes

Topics: Acid Phosphatase; Alkaline Phosphatase; Capillaries; Coronary Disease; Coronary Vessels; Dihydrolipoamide Dehydrogenase; Electron Transport Complex IV; Esterases; Glycogen; Heart Conduction System; Heart Neoplasms; Histocytochemistry; Humans; Hypertension; Lipase; Methods; Myocardial Infarction; NAD; NADP; Regional Blood Flow; Succinate Dehydrogenase

Topics: Acetylcholinesterase; Acid Phosphatase; Acute Disease; Animals; Blood Pressure; Body Weight; Chronic Disease; Desoxycorticosterone; Ganglia, Autonomic; Histocytochemistry; Hypertension; Hypertension, Renal; Male; Microscopy, Electron; Monoamine Oxidase; Neck; Neurons; Organ Size; Rats; Renal Artery

Topics: Acid Phosphatase; Adenosine Triphosphatases; Adult; Alkaline Phosphatase; Angina Pectoris; Animals; Aortic Diseases; Blood Proteins; Chromatography; Chromatography, Gel; Diabetes Mellitus; Dogs; Electrocardiography; Electrophoresis; Female; Heart Failure; Humans; Hypertension; Isoenzymes; Kidney; Kidney Diseases; Liver; Liver Diseases; Lysosomes; Male; Mesenteric Arteries; Middle Aged; Mitochondria; Muscles; Myocardium; Potassium; Radionuclide Imaging; Rats; Sodium; Transaminases

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Chlorides; Electron Transport Complex IV; Esterases; Female; Glucose-6-Phosphatase; Glucuronidase; Glycogen; Histocytochemistry; Hypertension; Methacholine Compounds; Microscopy, Electron; Monoamine Oxidase; Potassium; Rats; Sodium; Succinate Dehydrogenase; Sweat Glands; Sweating; Uremia

Topics: Acid Phosphatase; Animals; Blood Pressure; Body Weight; Cell Nucleus; Desoxycorticosterone; Dihydrolipoamide Dehydrogenase; Female; Glucosephosphate Dehydrogenase; Histocytochemistry; Hypertension; Hypothalamo-Hypophyseal System; Male; NAD; Neurosecretion; Rats; Renal Artery

Topics: Acetates; Acid Phosphatase; Animals; Autoradiography; Blood Vessels; Cats; Cell Nucleus; Constriction; Cortisone; Desoxycorticosterone; Dilatation; DNA; Dogs; Esterases; Estrone; Hemodynamics; Humans; Hypertension; Infant, Newborn; Karyometry; Methods; Muscle, Smooth; Progesterone; Rats; Succinate Dehydrogenase; Testosterone

Topics: Acid Phosphatase; Adenosine Triphosphatases; Adrenal Glands; Alcohol Oxidoreductases; Alkaline Phosphatase; Aminopeptidases; Animals; Arteries; Histocytochemistry; Hypertension; Kidney; Liver; Male; Mesentery; Myocardium; Oxidoreductases; Pancreas; Rats

Topics: Acid Phosphatase; Adenosine Triphosphatases; Adrenal Cortex Hormones; Adrenocortical Hyperfunction; Alkaline Phosphatase; Animals; Aorta, Thoracic; Arteries; Biological Transport, Active; Blood Pressure; Calcium; Coronary Vessels; Esterases; Histocytochemistry; Hyperplasia; Hypertension; Hypertrophy; Ischemic Attack, Transient; Kidney; Malate Dehydrogenase; Male; Mesenteric Arteries; Methods; Organ Size; Potassium; Rabbits; Sodium; Succinate Dehydrogenase

Topics: Acid Phosphatase; Alkaline Phosphatase; Female; Glucose-6-Phosphatase; Glucosephosphate Dehydrogenase; Glycerolphosphate Dehydrogenase; Histocytochemistry; Humans; Hypertension; L-Lactate Dehydrogenase; Leucyl Aminopeptidase; Malate Dehydrogenase; Oxidoreductases; Placenta; Pre-Eclampsia; Pregnancy; Succinate Dehydrogenase

Topics: Acid Phosphatase; Adenosine Triphosphatases; Adrenal Glands; Animals; Aorta; Calcium; Histocytochemistry; Hypertension; Juxtaglomerular Apparatus; Kidney; Malate Dehydrogenase; Methods; Myocardium; NAD; NADP; Potassium; Rats; Sodium; Sodium Chloride; Succinate Dehydrogenase; Water-Electrolyte Balance

Topics: Acetylcholinesterase; Acid Phosphatase; Animals; Blood Pressure; Body Weight; Cervical Plexus; Ganglia, Autonomic; Histocytochemistry; Hypertension; Male; Monoamine Oxidase; Rats

Topics: Acid Phosphatase; Adenosine Triphosphatases; Alkaline Phosphatase; Animals; Aortic Diseases; Edema; Enzymes; Esterases; Glucosephosphate Dehydrogenase; Glycosaminoglycans; Histocytochemistry; Hypertension; Lipase; Nucleotidases; Rabbits; Sulfatases

Topics: Acid Phosphatase; Adenosine Triphosphatases; Adenosine Triphosphate; Adult; Aged; Alkaline Phosphatase; Bilirubin; Female; Heart Failure; Humans; Hydrogen-Ion Concentration; Hypertension; Liver Diseases; Male; Middle Aged; Phenolphthaleins; Phosphoric Monoester Hydrolases; Temperature; Transaminases

Topics: Acetylcholinesterase; Acid Phosphatase; Adrenalectomy; Adrenocorticotropic Hormone; Animals; Body Weight; Cortisone; Dihydrolipoamide Dehydrogenase; Histocytochemistry; Hypertension; Hypothalamus; Iodine Isotopes; Male; Methylthiouracil; Monoamine Oxidase; NAD; Organ Size; Rats; Thyroid Hormones; Thyroidectomy

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Arteries; Arteritis; Coronary Vessels; Diet; Dihydrolipoamide Dehydrogenase; Hypertension; Mesenteric Arteries; Oxidoreductases; Phosphoric Monoester Hydrolases; Rats; Sodium Chloride

Topics: Acid Phosphatase; Adrenal Cortex Hormones; Adrenal Glands; Alkaline Phosphatase; Histocytochemistry; Hyperplasia; Hypertension; Hypertrophy; Norepinephrine; Pathology; Physiology

Topics: Acid Phosphatase; Adenosine Triphosphatases; Alanine Transaminase; Alkaline Phosphatase; Aspartate Aminotransferases; Biomedical Research; Bronchial Spasm; D-Alanine Transaminase; Humans; Hypertension; Hypertension, Renal; Kidney; Nephritis; Phosphorus Metabolism Disorders

Topics: Acid Phosphatase; Adrenalectomy; Alkaline Phosphatase; Aorta; Humans; Hypertension; Hypertension, Renal; Hypophysectomy; Kidney; Male; Nephrectomy; Phosphoric Monoester Hydrolases; Rats; Research; Testis

Topics: 5'-Nucleotidase; Acid Phosphatase; Animals; DNA; Hypertension; Islets of Langerhans; Pancreas; Protein Tyrosine Phosphatases; Rats; RNA

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Aorta; Aorta, Abdominal; Aortic Diseases; Constriction; Disease; Electron Transport Complex II; Hypertension; Kidney; Phosphoric Monoester Hydrolases; Rats; Succinate Dehydrogenase