Biomedical subjects

T Kumpulainen

Publications and source records attributed to T Kumpulainen.

27 records · Page 2Linked to original sources

PubMed1982

Immunohistochemical demonstration of extracellular carbonic anhydrase in epiphyseal growth cartilage.

The distribution of carbonic anhydrase isoenzymes C and B in the rate epiphyseal growth cartilage was demonstrated by an immunohistochemical method. The isoenzymes were found in different locations. Isoenzyme C was in the extracellular matrix of the hypertrophic and calcifying cartilage, and no reaction was observed in the chondrocytes. In contrast, the antiserum against isoenzyme B revealed only a weak cellular staining. This supports the hypothesis that carbonic anhydrase isoenzyme C, which is the high-activity form, changes the pH in the extracellular fluid of calcifying cartilage, favoring the deposition of calcium phosphate.

Animals↗

PubMed1982

Carbonic anhydrase in the type I skeletal muscle fibers of the rat. An immunohistochemical study.

The localization of carbonic anhydrase (CA) was studied in rat skeletal muscles with the use of immunohistochemical (peroxidase-antiperoxidase) method. CA was observed in all those fibers that also showed pH 4.3 stable actomyosin adenosine triphosphatase activity (type I fibers), but the reverse did not necessarily hold. More specifically, CA was apparently localized in I-bands, and a weak reaction was also observed in sarcolemma. The function of CA in muscle fibers is possibly connected with the greater demands on CO2 transport and buffer system in muscles adapted to long-lasting contractions.

Adenosine Triphosphatases↗

PubMed1982

Immunohistochemical localization of carbonic anhydrase isoenzyme C in the central and peripheral nervous system of the mouse.

The regional and cellular distribution of the high activity carbonic anhydrase isoenzyme (CA C or CA II) in the mouse nervous system was investigated by an indirect immunoperoxidase (peroxidase-antiperoxidase) method using cross-reactive antibodies prepared against human CA C. In the mature brain an overall strong CA C specific reactivity was revealed in the heavily myelinated nerve tracts, the main immunostaining originating from small, intensively reacting cells interpreted as oligodendrocytes and from the myelin sheaths. An obvious straining was also revealed in the choroid plexus cells, especially in their free borders, and in the erythrocytes of the blood vessels, while the glial cells of the retina similarly exhibited a strong reaction. In the developing brain, CA C was absent shortly after birth, but achieved almost the mature pattern of distribution within about 3 weeks. In the spinal cord most of the positive cells were found in the grey matter, their processes projecting towards the white matter. No reaction was obtained in the sciatic nerve fibers or in the neuronal or satellite cells of the coeliac ganglion.

Aging↗

PubMed1981

Immunohistochemical localization of carbonic anhydrase isoenzyme C in human brain.

Carbonic anhydrase isoenzymes of human brain were examined by the immunoperoxidase method. Only the catalytically highly active isoenzyme C was found in normal cerebral and cerebellar tissues, being located in a limited number of non-neuronal cells interpreted as oligodendrocytes and in myelinated nerve fibres. The enzyme was not evident in the glial cells of astrocytomas.

Brain↗

PubMed1981

Human carbonic anhydrase isoenzyme C. Effects of some fixatives on the antigenicity and improvements in the method of localization.

The effects of some alcohol and aldehyde containing fixatives on the antigenicity of human carbonic anhydrase isoenzyme C (HCA C) were tested in order to reveal the most suitable method for the immunohistochemical localization of this enzyme. The use of 2% and 4% paraformaldehyde or 2% glutaraldehyde solutions before immunoperoxidase (PAP) staining resulted in the loss of HCA C-specific reactivity in the surface epithelial cells of human appendicular and gastric mucosae, whereas the antigenic reactivity of HCA C was well retained in the parietal cells of gastric glands. In corresponding tissue sections fixed with one of the alcohol containing solutions (abs. methanol, methanol + chloroform 2:1 or Carnoy fluid) both the surface epithelial and parietal cells showed HCA C-specific immunostaining after the PAP procedure. In addition, the antigenicity of HCA C was found to be well preserved in some tubular cells of human kidney fixed in Carnoy fluid. The paraffin infiltration at relatively low temperature did not markedly affect the enzyme antigenicity. Fixation in Carnoy fluid coupled with paraffin embedding at 55-60 degrees C in vacuo was found to give the best preservation of the antigenicity of HCA C with good morphological integrity for light microscopical localization.

Alcohols↗

PubMed1981

Immunohistochemical localization of carbonic anhydrase isoenzymes in the human pancreas.

Carbonic anhydrase exists in two main forms (isoenzymes C and B) which differ from each other immunologically and in their level of activity, for instance. It is important to know the location of the enzyme in order to obtain a better understanding of its physiologic role. Since previous histochemical studies using metal salt methods for the demonstration of carbonic anhydrase activity have produced unsatisfactory results, the immunoperoxidase technique is applied here to investigate the location of the isoenzymes of carbonic anhydrase in the human pancreas. Isoenzyme C was localized specifically in the epithelium of the intra- and interlobular ducts, whereas the isoenzyme B was found only in the erythrocytes of the tissue. No carbonic anhydrase was found in the islets of Langerhans. The immunohistochemical results were confirmed by double immunodiffusion, in which the pancreatic tissue fluid from the thawed frozen sections generated a strong precipitation line with the rabbit antiserum against isoenzyme C and a very weak precipitation with the antiserum against the isoenzyme B.

Carbonic Anhydrases↗

PubMed1980

Carbonic anhydrase isoenzyme C in the human retina. An immunohistochemical study.

The occurrence of carbonic anhydrase isoenzymes C and B in the retina of the human eye was examined with specific antisera against these enzymes. Immunological analysis were carried out by the double diffusion method of Ouchterlony, and the localization of the enzymes was studied by an application of immunoperoxidase (PAP) technique. A large amount of isoenzyme C was detected in tissue sections from the human retina, whereas the isoenzyme B was totally absent. Isoenzyme C was considered to be located primarily in the glial elements of the retina, correlating with the earlier findings obtained by traditional metal salt methods.

Animals↗

PubMed1979

Immunohistochemical localization of human carbonic anhydrase isoenzyme C.

Methods for immunohistochemical localization of human carbonic anhydrase isoenzyme C (HCA C) with indirect fluorescent antibody and immunoperoxidase techniques are described. Both methods revealed large amounts of this "high activity" isoenzyme in the mucosae of human stomach and appendix. With the indirect immunofluorescent method the presence of the enzyme in human erythrocyte cytoplasm was also demonstrated. Correlations of present findings with those obtained with the traditional histochemical methods for demonstration of carbonic anhydrase activity are discussed.

Appendix↗

PubMed1978

Immunohistochemical demonstration of carbonic anhydrase.

Rabbits were immunized using human erythroxyte carbonic anhydrase B (HCA B) purified by the modified methods of Armstrong et al. (1966) and Bernstein and Schraer (1972). The globulin fraction was isolated by ammonium sulphate precipitation. The anti-HCA B globulin was specific, when judged using the double diffusion technique of Ouchterlony and immunoelectrophoresis. No cross reaction with human erythrocyte carbonic anhydrase C was found, but cross reactions with erythrocyte carbonic anhydrase from rat, mouse and guinea pig were observed. Flurorescein isothiocyanate conjugated goat anti-rabbit globulin was used for the localization of HCA B in tissue sections and erythrocytes on slides.

Animals↗