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Biomedical subjects

B Wiederanders

Publications and source records attributed to B Wiederanders.

At least 55 records · Page 3Linked to original sources
PubMed1989

Cell type-specific distribution of cathepsin B and D immunoreactivity within the rabbit retina.

The cellular localization of cathepsin B and D immunoreactivity was demonstrated at the light microscopic level in the retina of adult rabbits by use of the peroxidase-antiperoxidase technique. Antisera were raised against rat liver enzymes. Whereas cathepsin D immunoreactivity was confined to Müller (glial) cells, cathepsin B was demonstrated in some, but not all, neuronal cell types. It is proposed that the two enzymes might carry different functions within the neuronal versus glial compartment.

Animals↗
PubMed1989

Immunodetection of cathepsin D in neuritic plaques found in brains of patients with dementia of Alzheimer type.

The aspartic endopeptidase cathepsin D was immunolocalized in 21 human cadaver brains from patients with dementia and controls. Immunoreactive cathepsin D was found to be present in multiple neurons, neuritic plaques, some macroglial cells, and microvessels. It is suggested that the enzyme might be involved in certain posttranslational changes of cystoskeletal compounds that lead to the formation and/or further growth of neuritic plaques and neurofibrillary tangles.

Aged↗
PubMed1989

Isolation and some properties of a cathepsin E type proteinase from rat spleen.

Cathepsin E (EC 3.4.23.--) has been isolated from rat spleen. The procedure included autolysis at pH 4.2 which was probably the reason why we isolated a polypeptide of Mr 42 kDa instead of 90 kDa. The latter is reported in the literature to be the Mr of native cathepsin E. The enzyme dissociates under reducing conditions in two identical monomers. In our preparation a mechanism different from reduction must be active producing the 42 kDa polypeptide. This enzyme was hard to distinguish from cathepsin D (EC 3.4.23.5.) which shows similar properties such as size, substrate specificity, stability in 6 M urea, and dependence of the activity on pH. The clear distinction between the two enzymes was proven on the basis of immunochemical reactions. Antibodies to both cathepsins, D and E, did not show any crossreaction with the nonrelated antigen.

Animals↗
PubMed1988

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↗
PubMed1987

Lysosomal proteinases.

A characteristic of lysosomal cysteine proteinases is given by their kinetic constants with specific substrates, their sequence homology, and their reactivity with monospecific polyclonal antibodies.

Animals↗
PubMed1987

Immunohistochemical detection of cathepsin D in human neuroontogenesis.

An antiserum against rat liver cathepsin D, which was previously found to cross-react with human brain cathepsin(s) D, was used to immunolocalize the enzyme in developing CNS man. Cathepsin D protein was found in neurons as well as in glial cells. The aerliest occurrence of cathepsin D was observed in neuroblasts at the 12th gestational week. During pre-, peri-, and postnatal neuroontogenesis, there is a strong increase in the amount of immunoreactive material.

Brain↗
PubMed1986

Cathepsin S. The cysteine proteinase from bovine lymphoid tissue is distinct from cathepsin L (EC 3.4.22.15).

Cathepsin S was purified from bovine spleen by acid autolysis, (NH4)2SO4 fractionation and chromatography on CM-Sephadex C-50, CM-cellulose and activated-thiol-Sepharose. Cathepsin L was isolated from lysosomal fractions of rat liver, rat kidney and bovine liver. Generally, cathepsin L was bound tightly to CM-Sephadex C-50. Preparations of cathepsin L from rat liver, rat kidney and bovine liver were shown to have kinetic constants for the substrate benzyloxycarbonyl-Phe-Arg-7-(4-methyl)coumarylamide in the same range (Km 2-3 microM). Benzyloxycarbonyl-Phe-Phe-diazomethane proved to be a sensitive irreversible inhibitor of cathepsin L from different species. Cathepsin S differed in all these characteristics from cathepsin L. A polyclonal antibody to cathepsin L from rat reacted with bovine cathepsin L but not with bovine cathepsin S.

Animals↗
PubMed1986

Cathepsins B and D in rat brain glia during experimentally induced neuropathological defects. An immunocytochemical approach.

The lysosome-associated cathepsins B and D were localized by means of immunocytochemistry (peroxidase-antiperoxidase technique) in glial cells of rat brain. A specific reaction pattern of hippocampal neuroglia could be observed after intracerebroventricular application of the neurotoxin kainic acid. After the induction of a focal epilepsy in rats by the implantation of cobalt pellets there was a pronounced immunoreaction of glia near the primary focus as well as the mirror focus. It is concluded that both cathepsins are useful immunocytochemical markers to trace functionally activated glia.

Animals↗
PubMed1986

Are there species differences amongst the lysosomal cysteine proteinases?

Kinetic constants for the hydrolysis of synthetic substrates by cathepsin B, cathepsin L or cathepsin H show only small variations between various species. The species variants purified from human, beef and rabbit reacted with antisera raised against the enzymes from rat. With regard to these criteria we could show that cathepsin I from rabbit lung is a species variant of cathepsin H, whereas cathepsin S is a separate enzyme from cathepsin L.

Animals↗
PubMed1986

Immunohistochemical analysis of the distribution of cathepsin D throughout human nervous system with reference to developmental aspects.

The aspartic endopeptidase cathepsin D was demonstrated in post mortem human brain by means of the peroxidase-antiperoxidase technique. The enzyme protein was found to be present in multiple neurons as well as in some glial cells. In embryonic nervous tissue cathepsin D was detected as early as at the 12th gestational week. During neuroontogenesis there was a continuous increase in cathepsin D immunoreactivity.

Aged↗
PubMed1986

Demonstration of cathepsins H and L in rat tissues.

Using immunohistochemical techniques, cathepsins H and L were shown to be widely distributed in rat tissues. The intracellular location of the enzymes in the parenchymatous tissues was granular under light microscopy and was shown to be lysosomal by immunoelectron microscopy of the kidney proximal tubule epithelium. In the lymphatic tissue both cathepsins H and L were seen in the reticular cells and not in the lymphoid cells. The locations of the two enzymes differed from each other in some tissues suggesting that the enzymes may have specialized functions in those tissues.

Animals↗
PubMed1986

[A method for measuring oxalic acid absorption].

Increased oxalic acid absorption, hyperoxaluria and oxalatelithiasis are found in many gastroenterological diseases. All persons receive 370 kBq 14C-oxalic acid for the measurement of oxalic acid absorption. The absorbed and in the urine excreted 14C-activities are measured with a scintillation spectrophotometer and scintillator composed of 2,5-diphenyloxazole(POP), 1,4-bis-(4-methyl-5-phenyl-2-oxazolyl)benzene (dimethyl-POPOP), naphthalene, toluene and ethyleneglycol monomethylether. Normal values of oxalic acid absorption are means +/- S = 7.17 +/- 1.87%/24 h (n = 40).

Humans↗
PubMed1985

Localization of cathepsin H and its inhibitor in the skin and other stratified epithelia.

The rat-skin-derived cysteine proteinase, so-called BANA-hydrolase, which is capable of hydrolysing benzoylarginine naphthylamide and leucine naphthylamide was shown to be immunologically identical to cathepsin H purified from rat liver. The enzyme was immunocytochemically localized in the basal cell layer of rat epidermis. A natural inhibitor of cathepsin H with a molecular weight of about 13,000 was mainly localized in the keratinizing cell layers and showed only a weak reaction in the basal cells. Thus, cathepsin H appears to be a characteristic feature of the proliferating cell layer, whereas the cysteine-proteinase inhibitor is a characteristic feature of keratinizing cells.

Aminopeptidases↗