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C C Tisher

Publications and source records attributed to C C Tisher.

At least 37 records · Page 2Linked to original sources
PubMed1994

Angiotensin II regulates H(+)-ATPase activity in rat cortical collecting duct.

Angiotensin II (ANG II) plays an important role in the regulation of solute transport in the kidney, and its effect on proximal tubule sodium and fluid transport has been studied extensively. Although there is evidence that ANG II receptors are present also in the distal nephron and collecting duct, little is known about the physiological role of ANG II in these segments of the renal tubule. Preliminary studies in our laboratory suggest that ANG II may have both structural and functional effects on intercalated cells in the cortical collecting duct (CCD). Therefore, the present study examines the effect of ANG II on H(+)-adenosinetriphosphatase (H(+)-ATPase) and H(+)-K(+)-ATPase activity in individual CCD segments microdissected from collagenase-treated rat kidneys. The H(+)-ATPase was measured as bafilomycin-sensitive ATPase activity, and H(+)-K(+)-ATPase was measured as Sch-28080-sensitive ATPase activity, by a fluorometric microassay. Preincubation of CCD segments with ANG II, 10(-10)-10(-5) M, caused a dose-dependent decrease in H(+)-ATPase activity with maximum inhibition at 10(-8) M of ANG II. The inhibitory effect of ANG II was abolished when tubules were incubated with ANG II in the presence of 10(-6) M losartan, indicating that the inhibition was mediated via specific AT1 receptors. The AT2-receptor antagonist, PD-123319, had no effect on the ANG II-mediated inhibition of H(+)-ATPase activity. Preincubation of CCD segments with 10(-10) or 10(-7) M ANG II had no effect on H(+)-K(+)-ATPase activity.(ABSTRACT TRUNCATED AT 250 WORDS)

Adenosine Diphosphate↗
PubMed1994

Immunocytochemical localization of distinct isoforms of nitric oxide synthase in the juxtaglomerular apparatus of normal rat kidney.

Nitric oxide (NO) is a messenger molecule that functions as a vasodilator and accounts for the biologic activity of endothelium-derived relaxing factor (EDRF). The enzyme responsible for NO production, NO synthase (NOS), exists in different isoforms. Some are expressed constitutively in various tissues, whereas others require induction by endotoxin and cytokines. There is evidence that NO plays an important role in the regulation of basal renal vascular resistance and in the tubuloglomerular feedback response. Specific antibodies to a constitutive NOS isolated from rat brain (B-NOS) and an inducible NOS isolated from rat aortic smooth muscle (VSM-NOS) were used to establish the cellular and subcellular distribution of NOS in the kidney. Kidneys from normal rats were preserved and processed for light and electron microscopic immunohistochemical studies using both a preembedding and a postembedding horseradish peroxidase technique. By light microscopy, strong immunostaining for B-NOS was observed in the juxtaglomerular apparatus, where it was located in cells of the macula densa. In contrast, immunostaining for VSM-NOS was specifically located in the terminal afferent arteriole and occasionally also in the initial efferent arteriole in the juxtaglomerular apparatus. In addition, faint immunostaining was present in the entire distal tubule. There was no labeling of arcuate or interlobular arteries. The injection of lipopolysaccharide was associated with increased immunostaining for VSM-NOS in the afferent arteriole but had no effect on B-NOS staining. By electron microscopy, B-NOS immunostaining was present throughout the cytoplasm of the macula densa cells, where it appeared to be associated mainly with small vesicles. Immunostaining for VSM-NOS in the afferent arteriole exhibited a patchy distribution in some cells, whereas other cells were stained throughout the cytoplasm. These results indicate that two distinct isoforms of NOS are present in the juxtaglomerular apparatus and support the hypothesis that NOS is involved in the regulation of tubuloglomerular feedback and glomerular capillary pressure.

Amino Acid Oxidoreductases↗
PubMed1994

Ultrastructural localization of H+ATPase in rabbit cortical collecting duct.

In contrast to results obtained in the rat kidney, studies of H+ATPase localization in the rabbit kidney have failed to demonstrate basolateral plasma membrane H+ATPase immunoreactivity in intercalated cells in the cortical collecting duct (CCD). Previous studies have relied on light microscopic immunofluorescence techniques, which have limited resolution. Therefore, the immunogold procedure was used to localize H+ATPase in rabbit collecting ducts at the ultrastructural level. Rabbit kidneys were preserved in vivo with periodate-lysine-paraformaldehyde or glutaraldehyde solutions, and samples of cortex were embedded in Lowicryl K4M. Thin sections were labeled for H+ATPase by the immunogold procedure with a rabbit polyclonal antibody against the 70-kd subunit of bovine brain H+ATPase. Three patterns of localization of H+ATPase were observed. The majority of intercalated cells in the CCD exhibited label over cytoplasmic vesicles only. In these cells, no label was associated with either the apical or basolateral plasma membranes. In a second group of cells, label for H+ATPase was observed along the basolateral plasma membrane and over cytoplasmic vesicles throughout the cell. Rarely, intercalated cells with H+ATPase label along the apical plasma membrane and over the apical cytoplasmic vesicles were observed in the CCD. In the initial collecting tubule and connecting segment, intercalated cells with either pronounced apical or basolateral plasma membrane label prevailed, whereas few cells exhibited label restricted to the cytoplasmic vesicles. In summary, in the rabbit CCD, three patterns of H+ATPase distribution exist in intercalated cells, two of which conform to published models of type A and type B intercalated cells.

Animals↗
PubMed1993

Immunohistochemical mapping of cellular and subcellular distribution of 5-HT1A receptors in rat and human kidneys.

Northern blotting studies have demonstrated mRNA for the serotonin 5-HT1A receptor in human neonatal kidney (B. K. Kobilka, T. Frielle, S. Collins, T. Yang-Feng, T. S. Kobilka, U. Francke, R. J. Lefkowitz, and M. G. Caron. Nature Lond. 329: 75-79, 1987). To confirm expression of receptor protein in kidney, we raised antibodies to two peptides derived from the third intracellular loop of the human 5-HT1A receptor. Specific immunoglobulin G (IgG) was purified sequentially on protein A-Sepharose and peptide-Affigel 10 columns. Each IgG was able to: 1) quantitatively immunoprecipitate [3H]8-OH-2-(di-n-propylamino)1,2,3,4-tetrahydronaphthalene ([3H]8-OH-DPAT)-labeled human and rat receptors; 2) immunoblot a new protein in cells transfected with human 5-HT1A receptor DNA; and 3) immunoautoradiographically label areas of rat brain (frontal cortex, hippocampus, and lateral septum) in a highly characteristic pattern similar to that labeled by 125I-Bolton-Hunter-8-methoxy-2-(N-propyl-N-propylamino)Tetralin, a specific 5-HT1A receptor autoradiography ligand. By use of a light microscopic immunoperoxidase labeling technique, incubation of each IgG antibody with sections of rat and human kidney demonstrated an identical pattern of immunoreactivity. Specific labeling of basolateral plasma membranes was detected throughout medullary and cortical thick ascending limbs (TAL), in distal convoluted tubules (DCT), in connecting tubule cells of the connecting tubule, and in principal cells of the initial collecting tubule. There was no labeling in the inner medulla, glomeruli, or blood vessels. The labeling was blocked by preincubation with the corresponding peptide, but not with noncorresponding peptide or carrier protein. There was no labeling with preimmune IgG. Electron microscopic immunoperoxidase labeling confirmed the specific localization of the IgG antibody along the basolateral plasma membrane in all positively staining cells in rat kidney. Radioligand binding studies with the specific 5-HT1A receptor ligand [3H]8-OH-DPAT confirmed the presence of 5-HT1A receptor binding sites in bulk-isolated rat medullary TAL. These studies provide the first evidence that the 5-HT1A receptor is expressed on the basolateral surface of TAL and DCT cells of human and rat kidney. The specific localization to these cells suggests a possible role for the 5-HT1A receptor in the regulation of salt and water transport in mammalian kidney.

Amino Acid Sequence↗
PubMed1993

Differential expression and cellular distribution of mRNAs encoding alpha- and beta-isoforms of Na(+)-K(+)-ATPase in rat kidney.

We have used in situ hybridization histochemistry with isoform-specific, digoxigenin-labeled cRNA probes to characterize systematically the cellular distribution of mRNAs encoding alpha- and beta-subunit isoforms of the Na(+)-K(+)-adenosinetriphosphatase (Na(+)-K(+)-ATPase) in the normal rat kidney. Transcripts encoding the alpha 1-, alpha 2-, alpha 3-, beta 1-, and beta 2-subunits were detected in virtually all of the nephron segments, with prominent hybridization signal in the S3 segment of the proximal tubule, the cortical and medullary thick ascending limb of Henle's loop, the distal convoluted tubule, the cortical collecting duct along its entire length, and the renal pelvic epithelium. Several differences in the cell-specific pattern of expression of the various isoforms were observed. Among the alpha-isoforms, the alpha 3-subunit appeared to be preferentially expressed in the glomerular podocytes and mesangial cells, papillary interstitial cells, and renal pelvic epithelium. The beta-isoforms also differed in their distribution pattern, with the beta 1-subunit expressed to a greater degree in the glomerulus and renal pelvic epithelium and the beta 2-subunit preferentially expressed in the papillary interstitial cells and papillary surface epithelium. The detection and expression pattern of alpha- and beta-subunit mRNAs in structures throughout the kidney is compatible with the possibility of six structurally unique Na(+)-K(+)-ATPase isozymes and suggests a potentially greater role for isozymes comprised of the alpha 2-, alpha 3-, and beta 2-subunits in renal sodium and potassium transport.

Animals↗
PubMed1992

Immunocytochemical response of type A and type B intercalated cells to increased sodium chloride delivery.

Two populations of intercalated cells, type A and type B, are present in the rat cortical collecting duct (CCD). Type A cells are involved in proton secretion and contain an apical H(+)-adenosinetriphosphatase (ATPase) and a basolateral Cl(-)-HCO3- exchanger. Type B cells are believed to be involved in HCO3- secretion, which is mediated by a Cl(-)-HCO3- exchange process and is Cl- dependent. The aim of this study was to examine the morphological and immunocytochemical response of type B intercalated cells in the rat to increased delivery of Cl- to the CCD. This was accomplished by chronic infusion of a loop diuretic, bumetanide (30 mg.kg body wt-1.day-1), via an osmotic minipump, and simultaneous administration of 0.9% sodium chloride in the drinking water for 6 days. The kidneys were preserved by in vivo perfusion with a periodate-lysine-paraformaldehyde fixative and processed for horseradish peroxidase and protein A gold immunocytochemistry, using rabbit polyclonal antibodies against carbonic anhydrase II, proton ATPase, and band 3 protein. Chronic infusion of bumetanide in combination with a high salt intake was associated with significant changes in the intercalated cells. Type B cells were increased in size and exhibited numerous apical microvilli, increased basolateral membrane area, and marked cytoplasmic and basolateral labeling for H(+)-ATPase. In contrast, type A cells were small and had sparse apical microprojections. H(+)-ATPase immunolabeling was observed primarily over apical tubulovesicles, and there was decreased basolateral immunolabeling for band 3 protein and occasional labeling for band 3 in lysosome-like structures. These observations support the hypothesis that increased delivery of Cl- to the CCD is associated with stimulation of type B intercalated cells to secrete HCO3-. The observations in type A cells are consistent with the cells being in a resting or inactivated state.

Adenosine Triphosphatases↗
PubMed1992

Response of intercalated cells to chloride depletion metabolic alkalosis.

We examined the effect of Cl- depletion metabolic alkalosis (CDA) on H(+)-ATPase and band 3 protein localization in intercalated cells (IC) of the rat cortical collecting duct (CCD) and the outer medullary collecting duct (OMCD). After 30 min of peritoneal dialysis against 0.15 M NaHCO3 to produce CDA, or Ringer bicarbonate to serve as controls (CON), both groups were infused intravenously with an 80 mM Cl- solution for 90 min. For CDA vs. CON, physiological parameters were as follows: plasma total CO2, 38.0 +/- 1.1 vs. 27.8 +/- 0.6 meq/l (P less than 0.001); urinary total CO2 excretion, 141 +/- 89 vs. 20 +/- 3 neq.min-1.100 g body wt-1; and urinary Cl- excretion, 20 +/- 10 vs. 486 +/- 144 neq.min-1.100 g body wt-1 (P less than 0.001). H(+)-ATPase was localized in thin sections using a rabbit polyclonal antibody against the 70-kDa subunit of bovine brain H(+)-ATPase. Band 3 protein was localized using a polyclonal antibody against the 43-kDa subunit of the cytoplasmic domain of human erythrocyte band 3 protein. In CON rats, H(+)-ATPase localized along the apical plasma membrane and over the apical cytoplasmic vesicles of type A ICs in the CCD and ICs of the OMCD. H(+)-ATPase was observed along the basolateral plasma membrane and over cytoplasmic vesicles throughout type B ICs. In CDA rats, H(+)-ATPase was only observed over apical cytoplasmic vesicles in type A ICs and in the majority of OMCD ICs. In type B ICs, H(+)-ATPase staining was intensified along the basal plasma membrane in CDA. Band 3 protein was consistently localized in the basolateral plasma membrane of all type A cells in the CCD and ICs of the OMCD in both CON and CDA. In summary, stimulation of HCO3- secretion in rats caused withdrawal of H(+)-ATPase from the apical plasma membrane and storage in apical cytoplasmic vesicles of ICs of the OMCD and type A ICs of the CCD. H(+)-ATPase appeared to be inserted into the basal plasma membrane of type B ICs. These findings suggest that, during correction of CDA, proton secretion by type A and OMCD ICs is suppressed and proton transport across the basolateral plasma membrane of type B ICs is stimulated.

Adenosine Triphosphatases↗
PubMed1992

Intracellular band 3 immunostaining in type A intercalated cells of rabbit kidney.

Intercalated cells (ICs) in the collecting duct and the connecting tubule (CNT) are involved in H+ secretion and HCO3- reabsorption. H+ secretion is mediated by an H(+)-adenosinetriphosphatase in the apical plasma membrane, whereas a band 3-like Cl(-)-HCO3- exchanger in the basolateral membrane is responsible for HCO3- reabsorption. Recent studies have reported that a band 3-like protein is also present in mitochondria in rabbit ICs. The purpose of this study was to establish the subcellular location of the band 3-like Cl(-)-HCO3- exchanger in rabbit ICs by electron microscopic immunocytochemistry using a monoclonal antibody, IVF12, against erythrocyte band 3 protein. Rabbit kidneys were preserved by in vivo perfusion with a paraformaldehyde-lysine-periodate solution and processed for immunocytochemistry using a horseradish peroxidase preembedding technique. Band 3 immunostaining was observed on the basolateral plasma membrane of ICs in the outer medullary collecting duct and type A cells in the cortical collecting duct (CCD) and CNT. In addition, distinct staining for band 3 was present in numerous small vesicles and in multivesicular bodies in type A ICs in the CCD and CNT. However, there was no evidence of band 3 immunostaining of mitochondria or of the apical plasma membrane in any cells of the collecting duct. These observations suggest that basolateral Cl(-)-HCO3- exchangers in type A ICs in the rabbit kidney are stored in intracellular vesicles and possibly degraded in the vascular-lysosomal system when these cells are in a resting state. The previously reported band 3 immunolabeling of mitochondria could not be confirmed.

Animals↗
PubMed1991

Successful pregnancy in a patient receiving hemodialysis.

Pregnancy is an unusual occurrence in women with ESRD. We report a successful pregnancy in a patient with ESRD who was receiving hemodialysis; she gave birth to a healthy female infant at 34 weeks' gestational age. We discuss possible physiologic causes of gonadal dysfunction in patients with ESRD.

Adult↗
PubMed1991

Acute anuric renal failure after pigmy rattlesnake bite.

Acute renal failure has been known to follow viper bites in up to 30% of patients, but we believe we have reported the first case in which anuric renal failure developed after the bite of a pigmy rattlesnake. Our patient's renal failure is thought to have been due to a combination of rhabdomyolysis and intrarenal thrombosis caused by DIC. Prompt surgical debridement should be offered to the victim of a bite by any poisonous snake, and antivenin should be administered to any patient with signs of systemic envenomation, with close monitoring for signs of allergic reactions.

Acute Kidney Injury↗
PubMed1991

Effects of glucose on receptor-mediated phosphoinositide hydrolysis and second messenger generation in rat glomerular mesangial cells.

The phosphoinositide system plays a critical role in mesangial cell contraction. myo-Inositol depletion occurs in glomeruli from diabetic animals and may result in mesangial cell dysfunction. The hypothesis that mesangial cell exposure to high concentrations of glucose could lead to abnormalities in phosphoinositide metabolism and receptor-mediated inositol phosphate release was tested. When compared with controls (5 mM glucose), inositol phosphate release in mesangial cells exposed to 28 mM glucose was decreased by 27% after maximal stimulation with angiotensin II, by 41% after arginine vasopressin, and by 63% after the thromboxane A2 analog, U46619. Increasing the concentration of glucose to 50 mM caused a further reduction (from 27 to 54%) in maximal angiotensin II stimulation of inositol phosphate release. High glucose decreased incorporation of myo-inositol into phospholipids but did not change phosphoinositide mass. High glucose also resulted in increased de novo synthesis of diacylglycerol which was associated with membrane translocation of protein kinase C. myo-inositol supplementation prevented the reduction in phosphoinositide hydrolysis whereas sorbinil did not. It was concluded that high concentrations of glucose cause abnormalities in myo-inositol metabolism in mesangial cells which lead to reduced receptor-mediated phosphoinositide hydrolysis. These abnormalities appear to be related to desensitization of receptor-mediated phosphoinositide responses due to negative feedback by protein kinase C which becomes activated as a result of enhanced de novo diacylglycerol formation from glucose. These changes are unrelated to the polyol pathway and can be prevented by myo-inositol supplementation.

Animals↗
PubMed1990

H-K-ATPase immunoreactivity in cortical and outer medullary collecting duct.

Biochemical and physiologic studies in individual segments of the cortical collecting duct (CCD) and outer medullary collecting duct (OMCD) have provided evidence for the presence of an H-K-ATPase which is involved in the reabsorption of potassium in exchange for protons. The present study was designed to determine the cellular distribution of H-K-ATPase immunoreactivity in the CCD and OMCD of the rat and rabbit using mouse monoclonal antibodies against hog gastric H-K-ATPase. Kidneys of normal rats and rabbits were preserved for light microscopic immunohistochemistry and embedded in paraffin. Sections were incubated with the primary antibody followed by the avidin-biotin-horseradish peroxidase procedure. Sections incubated without primary antibody or with a non-specific mouse Ig served as controls. Light microscopy revealed diffuse cytoplasmic staining indicating H-K-ATPase immunoreactivity in intercalated cells in the CCD and OMCD in both rat and rabbit. In all segments studied except the rat CCD, the percentage of H-K-ATPase immunoreactive cells corresponded to the percentage of intercalated cells. In the rat CCD only 23% of the cells were reactive with H-K-ATPase antibodies, which is less than the percentage of intercalated cells in this region. It is possible that only type A intercalated cells possess H-K-ATPase immunoreactivity or that some intercalated cells did not have sufficient activity to be detected by our method. These results demonstrate H-K-ATPase immunoreactivity in the intercalated cells of the CCD and OMCD of rat and rabbit, suggesting that these cells are involved in potassium reabsorption in exchange for proton secretion in the mammalian collecting duct.

Adenosine Triphosphatases↗
PubMed1990

Effect of low molecular weight proteins and dextran on renal cathepsin B and L activity.

Renal extraction of low molecular weight proteins (LMWP) accounts for 30% to 80% of their total metabolic clearance. Extraction includes glomerular filtration, proximal tubular uptake, and intralysosomal proteolysis. To characterize the anatomic sites and enzymes involved in digestion of reabsorbed LMWP, the lysosomal proteases, cathepsin B and L, were measured by ultramicroassay in isolated S1, S2 and S3 segments of the proximal tubule of proteinuric rats. Increased glomerular filtration and tubular uptake of LMWP were induced by i.v. and i.p. injections of myoglobin and cationic and anionic lysozyme. Both cationic lysozyme and myoglobin increased cathepsin B and L activities in the proximal tubule, while anionic lysozyme had no effect. Morphologic examination of kidney tissue suggested that proximal tubular uptake of anionic lysozyme was negligible in comparison with the cationic form. Hence, only LMWP absorbed by the proximal tubule cells stimulated cathepsin B and L activities. Proximal tubular uptake of cationic lysozyme was determined by measurement of lysozyme activities in S1, S2, and S3. S1 segments contained the highest lysozyme activity, while S2 and S3 had much lower activities, and cathepsin B and L activity following cationic lysozyme injection was stimulated only in S1 segments. These results suggest that cathepsin B and L participate in lysosomal digestion of certain LMWP. Furthermore, the activities of cathepsin B and L adapt to increased uptake of LMWP. To gain additional insight into the mechanism of cathepsin adaptation, the cathepsin B and L activities were measured following injection of dextran with a similar low molecular weight.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1990

Gallium scan in the diagnosis and treatment of renal malacoplakia.

A middle-aged female was admitted with a presumptive diagnosis of pyelonephritis that failed to respond to conventional antibiotic therapy. Multiple investigations to define the etiology of the persistent fever and accompanying acute renal failure were negative. A gallium scan revealed intense uptake in the renal parenchyma. Percutaneous renal biopsy revealed malacoplakia. Six weeks of therapy with ciprofloxacin resulted in resolution of fever, improvement in the follow-up gallium scan, and reversal of the acute renal failure.

Ciprofloxacin↗