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P Kloss

Publications and source records attributed to P Kloss.

16 recordsLinked to original sources

Ultrastructural study of cathepsin B immunoreactivity in rat brain neurons: lysosomal and extralysosomal localizations of the antigen.

Cathepsin B was localized in multiple neurons of the rat central nervous system by means of the peroxidase-antiperoxidase technique and immunogold labeling using a polyclonal antiserum produced in rabbits against rat liver enzyme. The main intracellular locus of cathepsin B antigenic sites was in lysosomes. In some cases, however, immunoreactive material was also detected outside lysosomes (i.e. at the membranes of the rough endoplasmic reticulum). The findings are discussed with respect to the proposed role of the enzyme in the general protein metabolism of the brain and the potency of the antiserum to label the proform of cathepsin B.

Animals

Cathepsin B immunoreactive neurons in rat brain. A combined light and electron microscopic study.

The regional distribution and cellular localization of the lysosomal proteinase cathepsin B was studied by use of monospecific antiserum. The application of the peroxidase-antiperoxidase technique at the light microscopic level revealed cathepsin B immunoreactive neurons in many brain areas. A strong immunoreaction was found in pyramidal cells of the cortex, large neurocytes of the septal region, some hippocampal neurons and magnocellular nerve cells of the hypothalamus. Immunogold labeling on ultrathin cryosections of rat neocortex revealed the enzyme protein to be associated with lysosomes.

Animals

Cathepsin B immunoreactivity is widely distributed in the rat brain.

The cellular localization and regional distribution of cathepsin B within rat CNS was revealed by immunohistochemistry using a monospecific antiserum. Cathepsin B protein was found to be widely but unevenly distributed throughout rat brain. Neurons were always cathepsin B immunoreactive. Glial elements were only occasionally immunostained. The distribution of the enzyme resembles largely that of cathepsin D.

Animals