Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0020538 (hypertension)
 170,190 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The abundant heme-binding protein of the liver, probably identical with Z-protein or liver fatty acid-binding protein, has an apparent molecular weight of 14,000 Da and is presumably involved in the intracellular transport of a variety of compounds. The cellular and subcellular distribution of HBP in the liver was studied in adult male and female rats by postembedding immunocytochemistry using the protein A-gold technique. By light microscopic examination heme-binding protein is present exclusively in parenchymal cells and not found in the sinusoidal lining cells or other cells in portal tracts. Immunoreactivity for heme-binding protein is uniformly strong throughout the liver lobule in female rats but is markedly reduced in the pericentral region in male animals. By immunoelectron microscopy heme-binding protein immunoreactivity is localized in cytoplasm and nuclear matrix. The mitochondria and peroxisomes and the secretory apparatus are free of the label. In nuclei, gold labeling is confined to the interchromatin region (euchromatin) and nucleoli; condensed chromatin (heterochromatin) and nucleolus-associated chromatin are negative. The subcellular localization was substantiated by radioimmunoassay and immunoblotting of nuclear and cytosolic fractions. Immunoblotting shows that the heme-binding protein-like immunoreactive protein in the nucleus has a slightly larger molecular weight than that in the cytoplasm.
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PMID:Localization of the heme-binding protein in the cytoplasm and of a heme-binding protein-like immunoreactive protein in the nucleus of rat liver parenchymal cells: immunocytochemical evidence of the subcellular distribution corroborated by radioimmunoassay and immunoblotting. 234 57

We examined the photodynamic effects of porphyrins, known photosensitizers, on proteins of cytosol and plasma that bind them and are implicated in their transport. Their susceptibility to photodecomposition by porphyrins was found to be higher than that of proteins with low or no affinity for tetrapyrroles. Inhibition of porphyrin binding by the addition of equimolar amounts of heme had no effect, indicating that protein photodecomposition may be induced, in part, by free or nonspecifically bound porphyrins. HBP, a heme-binding Z protein of liver cytosol, exhibited the highest susceptibility of all proteins tested, including glutathione S-transferases, albumin, hemopexin, and apotransferrin. HBP was extensively photo-oxidized, as evidenced by a decrease in its antigenicity and electrophoretic mobility, and it was cross-linked by naturally occurring porphyrins as well as by the synthetic tin-protoporphyrin and hematoporphyrin derivative. The water-soluble singlet oxygen scavengers L-histidine (50 mmol/L) and sodium azide (100 mmol/L) completely prevented the photodynamic effects of uroporphyrin (100 mumol/L) on HBP. Hydroxyl radical scavengers such as manitol and benzoate were partially effective, whereas water-insoluble singlet oxygen scavengers such as beta-carotene were totally ineffective. Preferential inhibition of cross-linking over other photodynamic effects of uroporphyrin was consistent with previous reports that cross-linking occurs subsequently to amino acid oxidation.
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PMID:Effects of porphyrins on proteins of cytosol and plasma. In vitro photo-oxidation and cross-linking of proteins by naturally occurring and synthetic porphyrins. 244 89

The hexameric sequence ACGTCA functions in transcriptional regulation of wheat histone genes. The cauliflower mosaic virus (CaMV) 35S RNA promoter has the same hexameric sequence, and mutation analyses confirmed that the hexamer contributed greatly to transcription from the 35S promoter when a test gene with this promoter was introduced into sunflower cells. Electrophoretic mobility shift assays revealed the existence of a nuclear protein(s) in sunflower cells which is homologous to the HBP-1b that has been identified as binding to the 35S promoter in wheat. These results provide evidence of the involvement of the hexameric sequence and the HBP-1b-like DNA binding protein(s) in transcription from the 35S promoter.
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PMID:Function of the hexameric sequence in the cauliflower mosaic virus 35S RNA promoter region. 247 31

In a baseline survey of 4,936 school children aged 6-16 years, 199 children with systolic blood pressure (SBP) values equal or greater than the 95-th percentiles for age and sex were chosen as the hypertensive group (HBP), and were matched for age and sex with 197 children with SBP from the 5-th through the 50-th percentiles as the control (normotensive) group (NBP). For both groups the intra-RBC and plasma sodium and potassium contents, 8-hour night urinary sodium, potassium and creatinine excretions for three days, and an oral saline-water load test were performed. The results show that (1) intra-RBC potassium level in the HBP was lower than that in NBP. The level in those with positive hypertension family history (FH+) was lower than that with negatives (FH-). The intra-RBC potassium contents correlated inversely with diastolic BP. No correlation between intra-RBC sodium and BP was found; (2) Plasma sodium concentration in HBP was much lower than that in NBP. No difference was found between the FH+ and FH- in the plasma sodium concentrations; (3) Mean 8-hour night urinary potassium excretion expressed as mmol/g creatinine, was lower in HBP than in NBP; (4) After the saline load test the 4-hour urinary sodium excretion was significantly higher in HBP. Of those children with FH- the 4-hour sodium excretion in HBP was higher than that in NBP, but no significant difference was found between HBP and NBP of the FH+ children in the 4-hour urinary sodium excretions.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Sodium and potassium levels in hypertensive children. 251 56

To study the effects of myocardial hypertrophy resulting from chronic pressure overload on excitation-contraction coupling, the cardiac transmembrane L-type calcium current (ICa) was investigated in the Goldblatt renovascular hypertensive (HBP) rat. ICa was measured in single myocytes enzymatically isolated from control (CTRL) and HBP rat hearts using the whole-cell, patch-clamp method. The peak ICa and ICa density (obtained by normalizing ICa to the average cell capacitative surface area) were larger in HBP cells (n = 15) than in CTRL cells (n = 10) at membrane potentials of -20 to 50 mV (p less than 0.01). The maximal peak ICa increased from 0.9 +/- 0.5 nA (mean +/- SD) in CTRL cells to 2.8 +/- 1.0 nA in HBP cells (p less than 0.001). The corresponding ICa density increased from 5.3 +/- 2.7 to 16.2 +/- 6.0 microA/cm2 (p less than 0.001). There was no shift in the current-voltage relation between CTRL and HBP cells. The time course of decay of HBP ICa in response to clamp steps to the plateau range of the action potential (membrane potential, Vm = -10 to 30 mV) was delayed when compared with that of CTRL ICa. The inactivation time constants (biexponential) for the maximal ICa were 6.9 +/- 1.9 and 36.0 +/- 9.3 msec for CTRL cells and 6.7 +/- 1.4 and 49.5 +/- 12.9 msec for HBP cells (p less than 0.05 for the slower component of the maximal ICa). There was no difference in the steady-state inactivation of ICa (f infinity) for the CTRL and HBP cells. From the maximal peak ICa, cytoplasmic free Ca2+ was estimated to reach a pCa of 6.95 +/- 0.07 for CTRL cells and 6.64 +/- 0.13 for HBP cells. It is concluded that ICa is increased with myocardial hypertrophy. The lengthening of the action potential in hypertrophied rat myocardium is due to an increase in peak current density and to the slower inactivation of the maximal ICa. The increased transmembrane flux of Ca2+ via ICa in HBP cells is inadequate to achieve a myoplasmic free Ca2+ level sufficient for direct partial activation of the contractile myofilaments. However, in the scheme of the calcium-triggered calcium release hypothesis such an increase could provide an increased amount of activator calcium and/or serve to amplify the release of Ca2+ from sarcoplasmic reticulum, thereby contributing to preserved peak developed tension in hypertrophied rat myocardium.
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PMID:Calcium current is increased in isolated adult myocytes from hypertrophied rat myocardium. 252 34

HBP-1 is a sequence-specific DNA-binding protein that interacts with the hexameric sequence ACGTCA, the putative cis-acting element of the wheat histone H3 gene. Gel mobility shift and DNase I footprint analyses showed that this protein interacts with homologous sequences in the regulatory regions for the transcription of the cauliflower mosaic virus (CaMV) 35S RNA and nopaline synthase (NOS) genes, evidence that HBP-1 may bind to hexameric sequences in the regulatory regions of various genes. An HBP-1-like protein, indistinguishable from wheat HBP-1 in its the DNA-binding specificity, is present in sunflower nuclear extract, an indication that HBP-1-like DNA-binding proteins also exist in dicots.
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PMID:Wheat nuclear protein HBP-1 binds to the hexameric sequence in the promoter of various plant genes. 260 42

Monoclonal antibodies (MAbs) were obtained from hybridoma clones established by cell fusion between P3X63Ag8.653 mouse myeloma cells and spleen cells of mice or rats hyperimmunized against human bladder cancer tissue or BC47 rat bladder cancer cells. RBS-31 and RBS-85 mouse MAbs and RBA-1 rat MAb were raised against BC47 cells and HBP-1 MAb was raised against human bladder cancer tissues. Urinary antigens detected by these MAbs were quantitatively assayed by means of ELISA using 50 microliters of 1:2 diluted urine samples. The cut-off value of the assay was set up as the mean + 4 X SD of the mean using data from the healthy individual urine samples. The reactivity of all healthy control urine samples were under the cut-off value (negative). By contrast, urine from bladder cancer patients reacted positively with the RBS-31 MAb at 72%, with the RBS-85 MAb at 63%, with the RBA-1 MAb at 51% and with the HBP-1 MAb at 35%. The urine samples from some patients with renal calculi, acute cystitis or complicated urinary tract infections showed only a weak reactivity with our MAbs. As for extra-bladder cancers, some patients with renal, renal pelvis, prostate or ureter cancer, but no patients with esophageal, gastric, colon or liver cancer or leukemia, had reactive urinary antigens.
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PMID:Increase in murine monoclonal-antibody-defined urinary antigens in patients with bladder cancer and benign urogenital disease. 267 68

A novel DNA-binding protein that specifically interacts with the hexameric sequence ACGTCA in the regulatory region of the wheat histone H3 gene has been identified in wheat nuclear extract and designated HBP-1a. The nuclear protein HBP-1 previously identified as a DNA-binding protein that interacts with hexameric sequences in the H3, cauliflower mosaic virus (CaMV) 35 S RNA, and nopaline synthase (NOS) promoter regions therefore has been renamed HBP-1b. The flanking sequences that surround the hexameric sequence may account for the difference in the binding properties of HBP-1a and HBP-1b.
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PMID:Multiplicity of the DNA-binding protein HBP-1 specific to the conserved hexameric sequence ACGTCA in various plant gene promoters. 268 Jun 1

A galactose-specific lectin, recently described by our laboratory, is immunologically demonstrable on the surface of neoplastic cells derived from patients with Hodgkin's disease. This Hodgkin's lectin is shown to be functionally and antigenically related to the galactose-N-acetylgalactosamine-specific lectin of the hepatocyte (HBP). Poly- and monoclonal antibodies against either the cytoplasmic tail or the cell-surface binding site of HBP recognize the Hodgkin's lectin as a 55 Kd protein. Expression of the 55 Kd antigen appears to be restricted to Hodgkin's disease involved tissues and cells of the monocyte/macrophage lineage. The putative identification of the Hodgkin's lectin as an ectosialyltransferase unique to Hodgkin's cells is supported by inhibition of enzymatic activity by anti-HBP antibodies. Cultured Hodgkin's cells, in analogy to purified HBP, agglutinate T-lymphocytes mediated by the Hodgkin's lectin. This cell-to-cell interaction results in the incorporation of sialic acid into lymphocyte surface asialoglycans as well as in the stimulation of lymphocyte proliferation. The function of the Hodgkin's lectin as lymphocyte agglutinant in vitro suggests its role as an immunomodulator contributing to the immunodeficiencies associated with Hodgkin's disease.
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PMID:A marker and putative pathoantigen of Hodgkin's cells. 269 Feb 34

The purpose of this research was to evaluate the effectiveness of hypertension (HBP) education within a population of sixth grade students (n = 1204) and their parents (n = 1446). The "3Rs and HBP" curriculum attempts to diffuse the HBP information from teachers, to pupils and then to parents using the sixth grade son/daughter as a "health messenger." This curriculum was tested with and without a home blood pressure measurement component versus controls in 21 schools randomly assigned to the three conditions. Postintervention data were collected from students at school and from their parents at home interviews. Students were compared for knowledge, blood pressure measurement skill, and home diffusion activities. Parents were compared for knowledge, risk factor reduction, blood pressure, care-seeking, and compliance behaviors. Student self-esteem and family interactions were investigated as possible intervening variables in the diffusion process. Student knowledge, BP measurement skills, and diffusion to parents was increased by the 3Rs and HBP curriculum with the home component. Parental effects beyond the diffusion process were limited to knowledge improvement in certain groups. Family interaction (level and style) was found to be a significant intervening variable in the diffusion process.
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PMID:Evaluation of a diffusion strategy for school-based hypertension education. 273 67


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