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Biomedical subjects

A Rinne

Publications and source records attributed to A Rinne.

At least 37 records · Page 2Linked to original sources

Cathepsin S from bovine spleen. Purification, distribution, intracellular localization and action on proteins.

Cathepsin S was detected in bovine kidney, spleen, lymph nodes and lung by immunochemical methods. The immunostaining of cathepsin S in kidney was concentrated to the cells of the proximal tubule, where the enzyme was present in cytoplasmic granules. The purification method for cathepsin S from bovine spleen involved (NH4)2SO4 fractionation, chromatography on CM-Sephadex C-50, gel filtration on Sephacryl S-200 and chromatofocusing (pH 8.0-6.0). The enzyme was partially destroyed by autolysis of the homogenate at pH 4.2. The isoelectric point of cathepsin S was 7.0. Cathepsin S was found to hydrolyse proteins at a similar rate to cathepsin L below pH 7.0. At pH values of 7.0-7.5 cathepsin S retained most of its activity, whereas cathepsin L was completely inactive.

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↗

The 43 kDa papain inhibitor in normal and diseased skin.

The presence of 43 kDa papain inhibitor in 43 different skin diseases was immunohistochemically studied by using both poly- and monoclonal antibodies. Psoriasis and various eczematoid reactions as well as viral infections showed the most pronounced staining in the squamous cells of the epidermis. The antigen was also present in benign tumours or precancerous lesions which showed keratinization. Cells of poorly differentiated squamous cell carcinomas, basal cell carcinomas and melanocytic tumours were negative. The antigen seems to be related to disturbed keratinization and benign proliferation in non-neoplastic dermatoses and it is also present in differentiating squamous neoplasms.

Antibodies↗

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↗

Human cystatins in normal and diseased tissues--a review.

Immunohistochemica and quantitative immunochemical methods were used to demonstrate the presence of two cysteine proteinase inhibitors, cystatins A and B, in normal and diseased tissues. Cystatin A is expressed in squamous epithelia, neutrophil granulocytes, and dendritic reticulum cells of the lymphatic tissues. Its concentration is increased in inflammatory skin diseases and decreases after the malignization of squamous epithelia. Cystatin B is seen in wet squamous epithelia, and in the cells of monocyte-macrophage series, where its concentration varies depending on the activation state of the cells. In the malignant keratinocytes cystatin B follows the behaviour of cystatin A.

Cystatin B↗

The 43 kDa inhibitor of human skin and other epithelia.

We have used immunohistochemical and quantitative immunochemical techniques to study the tissue distribution of the 43 kDa papain inhibiting protein, originally isolated from psoriatic scale. High amounts of the inhibitor were found in the epidermis only in several skin diseases where the epidermal cell proliferation was increased (psoriasis, various eczemas). The inhibitor was also found in the basal cells of the bronchial epithelium and in the squamous epithelia of mouth and oesophagus, and the Hassal's corpuscles of the thymus. Sera of patients suffering from several skin diseases did not contain the inhibitor, but antibodies against it were found in the sera of two patients suffering from leg ulceration. The inhibitor was immunologically unrelated to filaggrin, involucrin, or keratins.

Electrophoresis, Polyacrylamide Gel↗

Detection of low molecular weight cysteine proteinase inhibitors by time-resolved fluoroimmunoassay.

A time-resolved fluoroimmunoassay was developed for the detection of 3 human low molecular weight cysteine proteinase inhibitors, ACPI (cystatin A), NCPI (cystatin B), and gamma-trace (cystatin C). Polystyrene tubes or polystyrene microtitration strips were used as solid phase. The rabbit anti-inhibitor immunoglobulins were used as the capture antibody, and, when labelled with europium, also as the detector antibody. The threshold sensitivity of the tests was 0.1 ng/ml for NCPI and 1 ng/ml for the others. All the 3 cysteine proteinase inhibitors, ACPI, NCPI, and gamma-trace, were detected in pooled serum samples of patients with kidney failure. gamma-Trace seemed to be quantitatively the major and ACPI the minor inhibitor. No other low molecular mass cysteine proteinase inhibitor was detected after isoelectric focusing of the 12 kDa area of gel filtered human serum.

Antibody Specificity↗

A 43-kDa papain inhibitor produced by a cultured human epidermal cell line.

Epidermis-derived cells (NCTC 2544) were cultured and the proteins of the culture medium, as well as of the cells, were fractionated by gel-chromatography. The fractions were analyzed for their papain-inhibitory capacity and for the presence of so-called 43-kDa papain inhibitor. A papain inhibitor was identified with molecular weight and immunological characteristics similar to the original 43-kDa inhibitor that was isolated from psoriatic scales. The result proves that NCTC-2544 cells can produce the so-called psoriasis inhibitor under culture conditions.

Cell Line↗

Immunocytochemical detection of peptides in the guinea pig cochlea.

The cochleae of juvenile guinea pigs were investigated for the presence of several neuropeptides. Glucagon, insulin, CCK and beta-endorphin immunoreactive neurons and nerve fibers as well as hair cells were demonstrated by the peroxidase antiperoxidase technique. Small amounts of substance P were also found in different sites in the inner ear. In contrast, prolactin-like material could not be found at all. These findings have significance with regard to the putative role of neuropeptides in neuromodulation.

Animals↗

Damage to secondary lymphoid follicles in AIDS-related persistent generalized lymphadenopathy, as revealed by the behaviour of dendritic reticulum cells possessing immunoreactive acid cysteine-proteinase inhibitor.

It has been shown previously that dendritic reticulum cells (DRC) in human secondary lymphoid follicles possess an immunoreactive acid cysteine-proteinase inhibitor (ACPI). In the present study, lymph nodes from 12 patients with AIDS-related persistent generalized lymphadenopathy (PGL) were investigated in order to detect whether or not any alterations occur in ACPI-immunoreactive DRC in this disorder. In the majority of PGL cases, profound alterations were found, the main characteristics of which were erosion, partial or total disruption of lymphoid follicles. However, similar though much less marked alterations were also found in some control cases. It is concluded that this type of follicular damage is a common and characteristic feature in PGL. It is not specific to PGL, however, but represents rather a special type of reaction in lymphatic tissue. The advantage of ACPI immunohistology for demonstrating the DRC pattern is that it can be performed on routinely fixed and paraffin-embedded tissues.

Acquired Immunodeficiency Syndrome↗

Atrial natriuretic polypeptides in the specific atrial granules of the rat heart: immunohistochemical and immunoelectron microscopical localization and radioimmunological quantification.

Atria of several mammalian species contain atrial natriuretic polypeptides (ANP) with natriuretic, diuretic, and vasodilating activity. In the present studies ANP were localized and quantitated in different parts of the heart by immunocytochemical and radioimmunological methods. The concentration of immunoreactive ANP as determined by quantitative radioimmunoassay in rat heart atria was a follows (ng/mg, mean +/- SD, n = 5): right auricle (688 +/- 156), left auricle (556 +/- 156), right atrium (334 +/- 60), and left atrium (93 +/- 36). The staining intensities in immunohistochemical localizations were consistent with the quantitative data. The location of the peptides was sarcoplasmic and granular. The highest concentration of ANP was found in the perinuclear area of the atrial myocyte sarcoplasm, but some staining was also seen in the periphery of the cells. The indirect immunoelectron microscopical gold method showed that ANP are located in the specific atrial granules supporting previous findings.

Animals↗

Neuropeptides in macula utriculi and macula sacculi of guinea pig labyrinth. An immunohistochemical study.

The neuropeptides Substance P, beta-Endorphin, Prolactin, Cholecystokinin, and Glucagon were investigated by means of Sternbergers PAP technique in the neuroepithelium of the Maculae utriculi and sacculi of the labyrinth of newborn guinea pigs. This brief report will show the localization of some neuropeptides in the neuroepithelium of the Maculae utriculi and sacculi. We could not find information about similar studies on this topic in the literature. In connection with investigations of the sensory apparatus of the inner ear we have recently presented neuropeptides evidence for the presence of certain peptides in the Ggl. spirale and the hair cells of the organ of Corti. With this paper we continue to report on neuropeptides in the labyrinth of the juvenile guinea pig as revealed by immunohistochemistry (Nowak et al., in press).

Acoustic Maculae↗

Immunoelectron microscopical location of the acid cysteine proteinase inhibitor in the lymphatic tissue of the tonsils.

Previous studies have shown the acid cysteine proteinase inhibitor (ACPI) to be a common characteristic of human squamous epithelial cells and dendritic reticulum cells (DRC) in lymphoid secondary follicles. In the present study, we used the PAP-preembedding technique for the immunoelectron microscopic identification of ACPI in DRC in palatine tonsillar tissue. ACPI appeared to be located in the cytoplasm of perikaryon and of dendritic processes of DRC on the membranes of the endoplasmic reticulum and the outer membrane of mitochondria. Further more, the tonofilaments and the desmosomal membranes exhibited a strong ACPI reactivity.

Adolescent↗

Natural cysteine proteinase inhibitors reduce lectin induced lymphocyte stimulation.

Lymphocyte stimulation by lectins can be inhibited by several synthetic inhibitors of proteolytic enzymes, notably those of cysteine proteinases. The effects of naturally occurring enzyme inhibitors are less well known. The effect of the neutral low-molecular weight cysteine proteinase inhibitor (NCPI) recently purified from lymph nodes and spleen was therefore investigated. Cultured peripheral blood lymphocytes were stimulated by PHA or ConA in the presence or absence of NCPI and the incorporation of 3H-thymidine was measured. NCPI was found to inhibit these lymphocyte responses in these circumstances.

Cells, Cultured↗