Carbonic anhydrase III in liver and muscle of male rats purification and properties.

Cytosolic carbonic anhydrases CAI, CAII, and CAIII from liver, and CAII, and CAIII from muscle of adult male Sprague-Dawley rats were purified to homogeneity. CAIII from liver and muscle had the same amino acid composition and were immunochemically similar. Their kinetic properties at 0 degrees C were also similar.

Mechanism and clinical significance of prostaglandin-induced iris pigmentation.

The new glaucoma drugs latanoprost, isopropyl unoprostone, travoprost, and bimatoprost cause increased pigmentation of the iris in some patients. The purpose of the present article is to survey the available preclinical and clinical data on prostaglandin-induced iris pigmentation and to assess the phenomenon from a clinical perspective. Most of the data have been obtained with latanoprost, and it appears that there is a predisposition to latanoprost-induced iris pigmentation in individuals with hazel or heterochromic eye color.

Localization of a protein inhibitor of carbonic anhydrase in pig tissues.

The protein inhibitor of carbonic anhydrase (CA), pICA, was localized in pig tissues by an immunohistochemical technique, using rabbit antipICA IgG. Staining for pICA was found in liver sinusoids and kidney glomeruli, where phagocytic cells are located, i.e.

Inhibition of carbonic anhydrase in the lens does not induce myopia in cynomolgus monkeys.

Refraction was measured in eyes of cynomolgus (Macaca irus) monkeys, before and during continuous intravenous infusion of large doses of the carbonic anhydrase (CA) inhibitors acetazolamide and ethoxzolamide. No changes of refraction were seen. Therefore, inhibition of CA in lens, cornea and retina does not appear to be the cause of the transient myopia and associated symptoms, occasionally observed in patients treated with CA inhibitors.

Androgen-linked control of carbonic anhydrase III expression occurs in rat perivenous hepatocytes; an immunocytochemical study.

Carbonic anhydrase (CA) isozymes CAII and CAIII were assayed by a radioimmunosorbent technique in liver cytosolic fractions and in isolated hepatocytes of adult male and female rats. Male livers contained 0.16 mg of CAII and 57 mg of CAIII per g cytosolic protein.

Biochemical, histological, and inhibitor studies of membrane carbonic anhydrase in frog gastric acid secretion.

Gastric acid secretion is dependent on carbonic anhydrase (CA). To define the role of membrane-bound CA, we used biochemical, histochemical, and pharmacological approaches in the frog (Rana pipiens). CA activity and inhibition by membrane-permeant and -impermeant agents were studied in stomach homogenates and microsomal fractions.

Membrane-associated carbonic anhydrase activity in the brain of CA II-deficient mice.

Membrane-associated carbonic anhydrase (CA) activity is of importance for transepithelial transport of ions and fluid. Histochemical studies have indicated its presence in the brain, but the data are difficult to evaluate because of interference from cytoplasmic CA isozymes, of which CA II is the predominant one. CA II-deficient mice offer a possibility to study the location of membrane-associated CA-activity, without interference from CA II.

Human lens carbonic anhydrases. Purification and properties.

Purpose: To isolate and characterize carbonic anhydrase (CA) isozymes of human lenses.

Methods: Affinity chromatography was used to separate CA isozymes, as monitored by an immunosorbent assay. Amino acid analysis was done on the antigenic CAII.

Carbonic anhydrase IV activity is localized on the exterior surface of human erythrocytes.

Carbonic anhydrase (CA) cytoplasmic isozymes CA I and CA II were found in human erythrocyte membrane ghosts, when prepared at pH 5.4 and pH 7.4, but not in ghosts prepared at pH 8.

The incidence and time-course of latanoprost-induced iridial pigmentation as a function of eye color.

Latanoprost, a phenyl-substituted analogue of prostaglandin F2 alpha administered as eye drops, induces increased melanogenesis in the iridial melanocytes of monkeys. Similar effects were seen in 12, 23 and 11% of patients in the USA, United Kingdom (UK) and Scandinavia, respectively, during one year of treatment. The highest incidence of induced pigmentation was seen in green-brown, yellow-brown and blue/grey-brown eyes, in that order.

Colour vision and side-effects during treatment with methazolamide.

The retina contains Na+K(+)-ATPase and carbonic anhydrase (CA), enzymes that regulate ion fluxes across cell membranes of photoreceptors. Since inhibition of retinal Na+K(+)-ATPase by digitalis impairs colour vision, we wanted to find out whether this also occurs after inhibition of CA. In a double-masked cross-over study with placebo, 14 male volunteers were given 50 mg q.

Renal handling and plasma elimination kinetics of carbonic anhydrase isoenzymes I, II and III in the rat.

Using a radio-immunosorbent technique, the levels of the carbonic anhydrase (CA) isoenzymes CA I, II and III in plasma (1-3 micrograms ml-1), lymph (0.5-1.6 micrograms ml-1) and urine (0.

Membrane-associated CA activity in the eye of the CA II-deficient mouse.

Purpose: Membrane-associated carbonic anhydrase (CA) activity is probably of great importance for transepithelial transport of ions and fluid. Histochemical studies have indicated its presence in the eye, but such histochemical data are difficult to evaluate because of interference from cytoplasmic CA isozymes, of which CA II is predominant. CA II-deficient mice offered the possibility to study the localization of membrane-associated CA activity, without influence from CA II:

Methods: The localization of CA in the eyes of CA II-deficient mice and of normal mice was studied by the cobalt-phosphate histochemical method.

Chemical properties of carbonic anhydrase IV, the membrane-bound enzyme.

The carbonic anhydrase (CA) isozyme (IV) in microsomes is thought to have a dominant role in secretory processes. Using microsomes from bovine kidney and lung (which had the same activity), we have measured the Km and kcat for CO2 hydration and compared these numbers with those for CA I (red blood cells and gut), CA II (red blood cells and secretory cells), and CA III (muscle). For kidney CA IV, Km is 10 mM and kcat is 170,000 sec-1 at 0 degree, approaching the rate for CA II but much greater than those for CA I or III.

Membrane-associated carbonic anhydrase activity in the kidney of CA II-deficient mice.

Carbonic anhydrase II-deficient mice offer a possibility to study the localization along the nephron of membrane-associated carbonic anhydrase (CA) activity without interference from the cytoplasmic enzyme. We studied the localization of CA in kidneys from CA II-deficient and control mice by immunocytochemistry (CA II) and histochemistry. Cytoplasmic staining was found in convoluted proximal tubule, thick limb of Henle, and principal and intercalated cells of collecting duct in the control animals but was absent in the CA II-deficient mice.

Leakage of carbonic anhydrase III from normal and denervated rat skeletal muscle following contractile activity.

Skeletal muscle extracellular carbonic anhydrase III was investigated in anesthetized rats by a microdialysis technique. A small dialysis probe was inserted into the tibialis anterior (TA) muscle and perfused continuously. Perfusates were collected before and during muscle contraction, induced by electrical stimulation of the muscle or of the sciatic nerve.

Muscle ATP and lactate and the release of myoglobin and carbanhydrase III in acute lower-limb ischaemia.

Serum-myoglobin and carbanhydrase III (S-CAIII), a specific muscle enzyme, were measured on admission, during surgery and in the postoperative period in 23 patients with acute lower-limb ischaemia and in 21 patients with chronic limb ischaemia in order to evaluate these molecules as possible markers of the degree of clinical ischaemia. The muscle contents of ATP and lactate were determined in muscle biopsies from patients with acute ischaemia on admission. Unlike S-myoglobin and S-CAIII they discriminated between cases which required subsequent amputation from those which did not.

Membrane-bound carbonic anhydrase CA IV in the human kidney.

The distribution of membrane-bound carbonic anhydrase, CA IV, was studied in human kidneys by an indirect immunoperoxidase method using a rabbit polyclonal antibody directed against human kidney CA IV. Clear staining of CA IV was found in the apical cell borders of some cells in the cortical and medullary segments of the collecting ducts, presumably the A type of intercalated cells. Weak staining for CA IV was located in the interior of a number of collecting duct cells and in the basolateral regions of the proximal convoluted tubules.

The excretion of carbonic anhydrase isozymes CA I and CA II in the urine of apparently healthy subjects and in patients with kidney disease.

Carbonic anhydrase isozymes CA I and CA II were assayed by a radio-immunosorbent technique in the plasma and urine of apparently healthy subjects and of patients with renal disease. The concentrations (mean +/- SD, n = 8) of CA I and CA II in the plasma of healthy subjects were 2.3 +/- 2.

Membrane specific carbonic anhydrase (CAIV) expression in human tissues.

Membrane-bound carbonic anhydrase IV (CAIV) expression has been evaluated in a range of fetal and adult human tissues and in cell culture. All tissues tested showed expression of CAIV, assessed by Western blotting, with a single immunodetected band at 55 kDa. The levels varied in fetal lung and liver during development and in various zones of the fetal brain.

Coupling of 22Na and 36Cl uptake in cultured pigmented ciliary epithelial cells: a proposed role for the isoenzymes of carbonic anhydrase.

Uptake studies with 22Na and 36Cl were performed in cultured bovine pigmented ciliary epithelial cells (PE) to investigate interdependence of Na+ and Cl- transport. (1) 22Na uptake into NaCl depleted cells was stimulated by Cl-. This stimulation was abolished by the simultaneous application of amiloride (1 mM) and bumetanide (0.