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  • 1
    Electronic Resource
    Electronic Resource
    Mitochondrial Carbonic Anhydrase in the Nervous System (2000)
    Oxford UK : Blackwell Science Ltd.
    Journal of neurochemistry 75 (2000), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Carbonic anhydrase (CA) V is a mitochondrial enzyme that has been reported in several tissues of the gastrointestinal tract. In liver, it participates in ureagenesis and gluconeogenesis by providing bicarbonate ions for two other mitochondrial enzymes: carbamyl phosphate synthetase I and pyruvate carboxylase. This study presents evidence of immunohistochemical localization of CA V in the rodent nervous tissue. Polyclonal rabbit antisera against a polypeptide of 17 C-terminal amino acids of rat CA V and against purified recombinant mouse isozyme were used in western blotting and immunoperoxidase stainings. Immunohistochemistry showed that CA V is expressed in astrocytes and neurons but not in oligodendrocytes, which are rich in CA II, or capillary endothelial cells, which express CA IV on their plasma face. The specificity of the immunohistochemical results was confirmed by western blotting, which identified a major 30-kDa polypeptide band of CA V in mouse cerebral cortex, hippocampus, cerebellum, spinal cord, and sciatic nerve. The expression of CA V in astrocytes and neurons suggests that this isozyme has a cell-specific, physiological role in the nervous system. In astrocytes, CA V may play an important role in gluconeogenesis by providing bicarbonate ions for the pyruvate carboxylase. The neuronal CA V could be involved in the regulation of the intramitochondrial calcium level, thus contributing to the stability of the intracellular calcium concentration. CA V may also participate in bicarbonate ion-induced GABA responses by regulating the bicarbonate homeostasis in neurons, and its inhibition could be the basis of some neurotropic effects of carbonic anhydrase inhibitors.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1471-4159.2000.0752212.x
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  • 2
    Electronic Resource
    Electronic Resource
    Alcoholic macrocytosis–is there a role for acetaldehyde and adducts? (2004)
    Oxford, UK : Blackwell Publishing Ltd
    Addiction biology 9 (2004), S. 0 
    Details
    ISSN: 1369-1600
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Although alcohol abuse is known to cause a wide array of adverse effects on blood cell formation, the molecular mechanisms by which alcohol exerts its toxic actions have remained poorly defined. Elevated mean corpuscular volume (MCV), macrocytosis, is the most typical morphological abnormality induced by excessive ethanol consumption. This paper reviews recent data indicating that acetaldehyde, the first metabolite of ethanol, may play a role in the haematological derangements in peripheral blood cells and in bone marrow of alcoholic patients. Studies in experimental animals and in human alcoholics have shown that acetaldehyde can bind to proteins and cellular constituents forming stable adducts. Elevated adduct levels have been found from the erythrocytes of alcohol abusers, which may also be associated with ethanol-induced effects in haematopoiesis and adverse consequences in cellular functions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1080/13556210410001674031
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  • 3
    Electronic Resource
    Electronic Resource
    Carbonic anhydrase isoenzymes II and I are present in the zona glomerulosa cells of the human adrenal gland (1993)
    Springer
    Histochemistry and cell biology 99 (1993), S. 37-41 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Human carbonic anhydrase isoenzymes I and II (HCA I and II) were purified from human erythrocytes by inhibitor affinity chromatography and ion-exchange chromatography. These isoenzymes were then located in the human adrenal gland using specific polyclonal antisera raised in rabbits and specific detection by immunohistochemical techniques. Both HCA II and I were located in the zona glomerulosa cells, although the staining for HCA I was faint. The cells of the zona fasciculata and the zona reticularis failed to stain with either antiserum. Control stainings with preimmune or anti-HCA VI sera were negative. The presence of HCA II and I in the zona glomerulosa cells may be linked to regulation of the biosynthesis or secretion of mineralocorticoids.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00268018
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  • 4
    Electronic Resource
    Electronic Resource
    Expression of transmembrane carbonic anhydrase isoenzymes IX and XII in normal human pancreas and pancreatic tumours (2000)
    Springer
    Histochemistry and cell biology 114 (2000), S. 197-204 
    Details
    ISSN: 1432-119X
    Keywords: Adenoma Cancer Carbonic anhydrase Gastrointestinal Human Immunohistochemistry Pancreas Plasma membrane
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. Carbonic anhydrase (CA) IX and XII are transmembrane isoenzymes which are expressed in several epithelia and overexpressed in some carcinomas. They have recently been linked to von Hippel-Lindau gene-mediated carcinogenesis in that both isoenzymes are downregulated by the product of the wild-type von Hippel-Lindau tumour suppressor gene. This paper describes the localisation of CA IX and XII in the normal human pancreas and pancreatic tumours. Both isoenzymes showed positive reaction in the basolateral plasma membrane of the normal acinar and ductal epithelia. The hyperplastic ductal epithelium in tumour specimens generally showed an increased staining for CA IX. Of 29 malignant tumours of exocrine pancreas, 10 showed moderate or strong immunoreaction for CA IX. The signal for CA XII remained weak in most malignant lesions. The present results show that both CA IX and XII are unevenly expressed in the ductal and acinar compartments of the human pancreas. The expression of these isoenzymes in a relatively low number of malignant tumour specimens suggests that they have a limited value in diagnostic evaluation of pancreatic carcinoma. However, the increased expression of CA IX in hyperplastic ductal epithelium may contribute to the pancreatic tumourigenesis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004180000181
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  • 5
    Electronic Resource
    Electronic Resource
    Detection of cervical metastases of thyroid medullary carcinoma by MoAb anti-CEA scintigraphy and immunohistochemistry (1995)
    Springer
    European journal of nuclear medicine 22 (1995), S. 1064-1068 
    Details
    ISSN: 1619-7089
    Keywords: Anti-carcinoembryonic antigen scintigraphy ; Medullary thyroid carcinoma ; Single-photon emission tomography ; Immunohistochemistry
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Four patients with medullary thyroid carcinoma (MTC) were examined using anti-carcinoembryonic antigen (CEA) scintigraphy. Two patients had positive and two normal scintigraphic findings, although all the patients had elevated blood test markers (calcitonin or CEA). One patient with clinical suspicion of MTC metastases had only a faintly positive anti-CEA image, although single-photon emission tomographic scanning was used to increase the sensitivity and resolution of the method. Therefore, digital image processing of the planar images was performed to obtain more detailed information. The analysis revealed distinct accumulation of the activity at the right side of the neck at 20 h post administration. The specificity of the antibody binding in the malignant cells was confirmed after surgery by immunohistochemical staining of the tumour specimens for CEA. Both conventional and confocal laser scanning microscopy revealed distinct positive staining, indicating that the results obtained from the anti-CEA scanning showed specific binding of the labelled antibody in the neoplastic tissue.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00808419
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  • 6
    Electronic Resource
    Electronic Resource
    Immunohistochemical demonstration of human carbonic anhydrase isoenzyme II in brain tumours (1995)
    Springer
    Journal of molecular histology 27 (1995), S. 974-982 
    Details
    ISSN: 1573-6865
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Carbonic anhydrase (CA) is a functionally important enzyme in the central nervous system (CNS), where it is involved in the control of the acid-base balance and regulates the production of cerebrospinal fluid (CSF). Isoenzyme II (CA II) is the most widely distributed CA in the CNS, being present in at least myelin, oligodendrocytes, astrocytes and the choroid plexus. This study was undertaken to examine the presence of CA II in different brain tumours from 31 patients. Specific antibodies recognizing CA II were used in immunoperoxidase staining of tumour specimens. Anti-CA I and VI sera and normal rabbit serum were used as controls. CA II-positive staining was observed in all the astrocytic tumours (n = 9), oligodendrogliomas (n = 3) and medulloblastomas (n = 3). The most malignant tumours exhibited the strongest staining. In addition, four acoustic neurinomas, one plexiform neurofibroma, one choroid plexus papilloma, one ependymoblastoma and one subependymoma expressed the enzyme. Meningiomas (n = 4) and neuronal tumours (N = 4), including one dysplastic gangliocytoma of the cerebellum (Lhermitte-Duclos), were negative. Anti-CA I, VI and normal rabbit sera showed no specific staining in tumour cells. The presence of CA II in the astrocytomas was confirmed by Western blotting, which revealed a distinct 29 kDa polypeptide band corresponding the CA II. Anti-CA I serum showed similarly a single 29 kDa band, recognizing the enzyme which is abundantly present in the erythrocytes. The present results demonstrate that despite the malignant transformation of the cells, the expression of CA II is sustained in astrocytic tumours, oligodendrogliomas, ependymal and choroid plexus tumours and tumours of nerve sheath cell origin. Our results suggest that some tumours contain abundant CA II, which might leak into the CSF.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02389687
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  • 7
    Electronic Resource
    Electronic Resource
    Immunohistochemical demonstration of the carbonic anhydrase isoenzymes I and II in pancreatic tumours (1995)
    Springer
    Journal of molecular histology 27 (1995), S. 133-138 
    Details
    ISSN: 1573-6865
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The location of carbonic anhydrase (CA) isoenzymes I, II and VI in normal and neoplastic pancreatic tissue was studied using polyclonal antisera and the immunoperoxidase technique. Samples were obtained from patients with well-differentiated (n = 4), moderately differentiated (n = 1) and poorly differentiated (n = 4) ductal adenocarcinomas, cystadenocarcinoma (n = 2), adenosquamous carcinoma (n = 1), acinar adenocarcinoma (n = 1), gastrinoma (n = 3), insulinoma (n = 3) and glucagonoma (n = 1). The control specimens were from a patient with traumatic laceration of the pancreas. The normal and malignant endocrine tissue showed intense positive staining for CA I localized in the cells expressing glucagon. In the exocrine pancreatic tissue, CA II was detected in the normal and neoplastic ductal epithelium. No specific staining was detected with anti-CA VI serum in either normal or malignant tissue.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00243908
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  • 8
    Electronic Resource
    Electronic Resource
    Immunohistochemical demonstration of human carbonic anhydrase isoenzyme II in brain tumours (1995)
    Springer
    Journal of molecular histology 27 (1995), S. 974-982 
    Details
    ISSN: 1573-6865
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Carbonic anhydrase (CA) is a functionally important enzyme in the central nervous system (CNS), where it is involved in the control of the acid-base balance and regulates the production of cerebrospinal fluid (CSF). Isoenzyme II (CA II) is the most widely distributed CA in the CNS, being present in at least myelin, oligodendrocytes, astrocytes and the choroid plexus. This study was undertaken to examine the presence of CA II in different brain tumours from 31 patients. Specific antibodies recognizing CA II were used in immunoperoxidase staining of tumour specimens. Anti-CA I and VI sera and normal rabbit serum were used as controls. CA II-positive staining was observed in all the astrocytic tumours (n = 9), oligodendrogliomas (n = 3) and medulloblastomas (n = 3). The most malignant tumours exhibited the strongest staining. In addition, four acoustic neurinomas, one plexiform neurofibroma, one choroid plexus papilloma, one ependymoblastoma and one subependymoma expressed the enzyme. Meningiomas (n = 4) and neuronal tumours (N = 4), including one dysplastic gangliocytoma of the cerebellum (Lhermitte-Duclos), were negative. Anti-CA I, VI and normal rabbit sera showed no specific staining in tumour cells. The presence of CA II in the astrocytomas was confirmed by Western blotting, which revealed a distinct 29 kDa polypeptide band corresponding the CA II. Anti-CA I serum showed similarly a single 29 kDa band, recognizing the enzyme which is abundantly present in the erythrocytes. The present results demonstrate that despite the malignant transformation of the cells, the expression of CA II is sustained in astrocytic tumours, oligodendrogliomas, ependymal and choroid plexus tumours and tumours of nerve sheath cell origin. Our results suggest that some tumours contain abundant CA II, which might leak into the CSF.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00175572
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  • 9
    Electronic Resource
    Electronic Resource
    Salivary Carbonic Anhydrase Protects Gastroesophageal Mucosa from Acid Injury (1997)
    Springer
    Digestive diseases and sciences 42 (1997), S. 1013-1019 
    Details
    ISSN: 1573-2568
    Keywords: CARBONIC ANHYDRASE ; ESOPHAGITIS ; GASTRIC ACID ; PEPTIC ULCER ; SALIVA
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Saliva contains several factors that protect thealimentary canal mucosa against acidity. We measured thesecretory carbonic anhydrase (CA VI) levels in thesaliva of patients with gastrointestinal disorders using a time-resolved immunofluorometric assay.The mean enzyme concentrations were found to be lower inpatients with verified esophagitis, gastric ulcer, orduodenal ulcer than in control patients with nonacid peptic diseases. The biochemical datafrom the enzyme activity assays and western blots of thehuman gastric mucosa and gastric juice samples indicatedthat the swallowed CA VI probably retains its activity in the harsh environment of thegastric lumen. In the upper alimentary canal, CA VI mayneutralize the acid by catalyzing the formation ofcarbon dioxide and water. The present findings suggest that drugs supplemented with CA VI may provebeneficial in treating acid-peptic diseases.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1018889120034
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  • 10
    Electronic Resource
    Electronic Resource
    Expression of Testosterone-Dependent Enzyme, Carbonic Anhydrase III, and Oxidative Stress in Experimental Alcoholic Liver Disease (1999)
    Springer
    Digestive diseases and sciences 44 (1999), S. 2205-2213 
    Details
    ISSN: 1573-2568
    Keywords: ALCOHOLIC LIVER DISEASE ; OXIDANT STRESS ; IMMUNOHISTOCHEMISTRY ; LIPID PEROXIDATION
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract We studied the sequential immunohistochemicalappearance of androgen-dependent carbonic anhydrase (CAIII) during the development of ethanol-induced liverinjury using liver samples from castrated andnoncastrated male micropigs. In castrated micropigs, thebaseline expression of CA III was either low or absent,while distinct positive immunoreactions were found inzone 3 hepatocytes at 5 and 12 months after the initiation of the ethanol diet. The CA IIIenzyme and protein adducts of lipid peroxidation-derivedaldehydic products, malondialdehyde and4-hydroxynonenal, appeared together in the perivenousregion, suggesting that the enzyme functions in anoxidative environment. The positive staining became moreabundant and widespread during the progression ofalcoholic liver disease. After 12 months, CA III was significantly more abundant in both theethanol-fed noncastrated and castrated micropigs than inthe control animals (P 〈 0.001, P 〈 0.05,respectively). CA III content was strikingly high in the ethanol-fed noncastrated animals, consistentwith a potential role of androgens in the regulation ofethanol-induced CA III expression. The strongly positiveCA III immunoreactions in the ethanol-fed noncastrated micropigs were associated with scant evidenceof aldehydic protein adducts and minimal histopathology.Thus, enhanced expression of CA III during ethanolconsumption may also account in part for gender differences in the susceptibility foralcohol-induced liver injury.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1026640317233
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