Degradation of insulin and glucagon in developing rat kidney: immunolocalization of insulin-glucagon-specific protease and quantitative estimation.
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Animals↗
Biomedical subjects
A Rinne
Publications and source records attributed to A Rinne.
[Low-molecular cysteine protease inhibitors in the human palatal tonsil].
2 low-molecular cysteine-proteinase inhibitors were purified from human tonsillar tissues: an acid cysteine proteinase inhibitor (ACPI), and a neutral cysteine proteinase inhibitor (NCPI). Their biochemical and immunological characteristics appeared to be identical to those inhibitors which we have identified in other human tissues in previous studies (epidermis and spleen). An immunohistological analysis revealed in tonsillar squamous epithelium a strong and consistent immunoreactivity for both inhibitors. In the tonsillar lymphatic tissue, ACPI-immunoreactivity appeared to be a characteristic mainly of dendritic reticulum cells whereas a prominent NCPI-immunoreactivity was confined mostly for the histiocytic reticulum cells in lymphoid secondary follicles. We also compared the distribution of the 2 immunoreactive inhibitors with the immunohistology as revealed by antisera raised against keratin and muramidase. Limitations of the immunohistochemistry of cysteine proteinase inhibitors are discussed in the light of an extensive trial of various fixation procedures. We deem that proposal of Barrett (1984) for the nomenclature of cysteine proteinase inhibitors is appropriate. According to it the ACPI is the cystatin A, and the NCPI is the cystatin B.
Child↗
[Behavior of cysteine proteinase inhibitors in autologous epidermis transplanted into oral mucosa for relative elevation of the alveolar process].
The presence of cysteine proteinase inhibitors was investigated in skin autografts into the gingiva of denture carriers. Acid cysteine proteinase inhibitors was present both in the transplant and the surrounding gingival epithelium, while neutral cysteine proteinase inhibitors was seen only in the gingival epithelium. The results indicate that the normal expression of cysteine proteinase inhibitors is conserved during the adaptation of the skin autograft into the oral surroundings.
Alveolar Process↗
[Immunohistochemical detection of acid cysteine proteinase inhibitors in lymphatic infiltrates of the thyroid gland].
Thyroid tissues containing lymphoid secondary follicles were studied immunohistochemically for the presence of acid cysteine proteinase inhibitor (ACPI). Reticulum cells in the lymphoid secondary follicles, mainly dendritic reticulum cells, exhibited a positive reaction. In addition, in 2 cases a positive reaction could be detected in some of the thyroid epithelial cells, adjacent to the lymphoid secondary follicles. The possible function of ACPI generally and its role in the function of those cells containing it, is discussed.
Cysteine Proteinase Inhibitors↗
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↗
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↗
Dendritic reticulum cells in AIDS-related lymphadenopathy.
One of two cases of acquired immune deficiency syndrome-related persistent generalized lymphadenopathy revealed a profoundly altered pattern of dendritic reticulum cells as demonstrated by immunoreactive acid cysteine proteinase inhibitor. The alterations could be related to totally or partially destructed lymphoid secondary follicles.
Acquired Immunodeficiency Syndrome↗
Behaviour of dendritic reticulum cells possessing immunoreactive acid cysteine-proteinase inhibitor in human lymphoid secondary follicles and in follicular-centre cell lymphomas.
In our previous studies acid cysteine-proteinase inhibitor (ACPI) was shown to be a common characteristic of human squamous epithelia and dendritic reticulum cells (DRC) in lymphoid secondary follicles. In the present study, the behaviour of ACPI-immunoreactive DRC in reactive lymphoid secondary follicles and neoplastic follicles of follicular-centre cell (FCC) lymphomas was compared by the peroxidase-antiperoxidase method. The secondary follicles in reactive lymphoid tissues revealed a staining pattern characteristic of DRC comparable with the results of other studies. Contrary to this, the number of ACPI-positive DRC in the neoplastic lymphoid follicles was greatly reduced. This was occasionally accompanied by a weak reaction and in many cases the DRC were totally abolished. Moreover, morphological aberrations were observed in ACPI-positive DRC, especially diminution and shortening of dendritic processes. On occasion, ACPI-positive cell types were observed, which may represent intermediate forms between DRC and fibroblastic reticulum cells. Only one case--with a rather favourable clinical outcome (out of 41 follicular FCC lymphomas) exhibited an ACPI-positive DRC pattern comparable with that of reactive lymphoid follicles. Thus it seems that the ACPI-immunohistochemistry of DRC provides an additional tool for discerning the difference between reactive and neoplastic lymphoid follicles. This method is of particular value since it can be used with formalin-fixed, paraffin-embedded tissues. There was a tendency among the follicular FCC lymphoma patients towards a better survival rate for those with ACPI-positive DRC than for those lacking this cell type, although no statistically significant differences emerged from this limited material.
Aged↗
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↗
Production of acid and neutral cysteine-proteinase inhibitors by a cultured human skin epithelium cell line.
Human skin epithelial-like cells (NCTC-strain 2544) were grown in RPMI-1640 medium supplemented with foetal calf serum for up to 2 weeks. The culture medium and extracts made from the cells were subjected to gel-filtration chromatography in a Sephacryl S-200 column for fractionation of the proteins. The fractions were assayed for acid and neutral cysteine-proteinase inhibitor (ACPI, NCPI) using time-resolved fluoroimmunoassay and radioimmunoassay, and the cysteine-proteinase-inhibiting activities were assayed using papain. Free NCPI, i.e. a molecule with isoelectric variants at pHs 6.0 and 6.5, which has an Mr of around 12,000 and is capable of inhibiting papain, was detected both in the culture medium and in the cells. Immunodiffusion studies revealed its immunological identity with human spleen-derived NCPI. The amount of NCPI increased during the incubation period. ACPI--characterized as a molecule having an isoelectric point of 4.9, an Mr of about 12,000, papain-inhibiting capacity and antigenic reactivity with spleen-derived ACPI--was not detected in the culture medium. It was, however, detected in the cells after 2 weeks in culture. These data prove that ACPI and NCPI are synthesized by the NCTC-2544 cells under the present culture conditions.
Cells, Cultured↗
Occurrence of cysteine proteinase inhibitors in cells of the monocytic-histiocytic system. An immunohistochemical investigation.
Human tissues are known to contain two low molecular weight (MW about 12,000) cysteine proteinase inhibitors, i.e. an acid inhibitor (ACPI) with pI 4.7-5.0 and a neutral inhibitor (NCPI) with pI 6.0-6.5. ACPI is abundant in cornifying epithelial tissues and in the dendritic reticulum cells of germinal centres of the lymph nodes. NCPI is abundant in lymphatic tissue and is known to be synthesized and released by mononuclear phagocytes. In this report NCPI was localized immunohistochemically in the epitheloid cells of most sarcoidotic lymph nodes, in lymph node macrophages after lymphangiography and in alveolar macrophages, while no ACPI could be demonstrated in the same cells by similar methods. These inhibitors were not demonstrable in lymph node sinus histiocytosis. Peripheral blood monocytes did not exhibit any NCPI immunoreactivity. In occasional blood monocytes anti-ACPI serum gave a weak reaction, the specificity of which is questionable. These data suggest that studies on cysteine proteinase inhibitors reveal basic differences in the various histiomonocytic cells and possibly differences in their functional stages.
Cysteine Proteinase Inhibitors↗
Acid cysteine-proteinase inhibitor, a new characteristic of reticulum cells in human lymphoid secondary follicles.
Reactive lymph nodes, palatine tonsils and thyroid tissues infiltrated with reactive lymphatic tissue were studied for the presence of immunoreactive acid cysteine-proteinase inhibitor (ACPI). A positive reaction for ACPI was found in germinal centres in all the above tissue types. The morphology and distribution of the positive cells indicated immunoreactivity in the dendritic reticulum cells (DRC). A positive reaction was also found in starry sky cells when a strong starry sky reaction was present in germinal centres. ACPI-positive cells of dendritic appearance were also found outside the secondary follicles in tonsillar tissue from cases of chronic or recurrent tonsillitis, especially between the follicles and the crypt epithelium, in some lymph nodes exhibiting a strong follicular reactive hyperplasia and in thyroid tissue in one case of Hashimoto's thyroiditis. A close anatomical and morphological relationship is pointed out between ACPI reactive dendritic cells and epithelial tissue. This is especially true of the tonsillar crypt epithelium and adjacent lymphoid secondary follicles. The tonsillar crypt epithelium sometimes formed a loose, web-like structure with enmeshed lymphoid cells, even reminiscent of dendritic compartmentalization of lymphoid secondary follicles. The results suggest that ACPI-immunoreactivity of DRC could be a function of the outer membrane of dendritic processes, and thus could be in some way a parallel phenomenon to the morphological expression of the well-established function of DRC in capturing antigen and immune complexes.
Cysteine Proteinase Inhibitors↗
Distribution of cathepsin D immunoreactivity in the central nervous system of rat and selected brain regions of man.
The regional distribution and cellular localization of cathepsin D immunoreactivity was demonstrated at the light microscopic level in the CNS of rat and man by use of unlabelled immunoenzyme technique. A wide but uneven distribution was substantiated for the rat brain. Furthermore, we present evidence that antiserum produced against rat liver enzyme is capable of recognizing cathepsin D in human brain.
Animals↗
Atrial natriuretic factor. Immunohistochemical localization in the specific atrial granules of the rat heart.
Atrial natriuretic peptides (atrial natriuretic factor, ANF) were localized in rat heart atria using immunohistochemical methods. A large number of heavily stained granules were detected mainly in the vicinity of the nuclei of the atrial muscle cells, but some staining was also present in granules located near the sarcolemma. The results show that the specific atrial granules are loaded with atrial natriuretic peptides.
Animals↗
Serum cysteine proteinase inhibitors with special reference to kidney failure.
Serum levels of proteins reactive in radioimmunoassay with an antiserum prepared in rabbits against purified human spleen neutral cysteine proteinase inhibitor (NCPI) was determined in 70 healthy controls and from 80 patients suffering from suspected or proven kidney failure. The values varied from less than 0.2 mg/l in normal sera to levels over 2 mg/l in some patient sera. Serum level of NCPI was found to roughly correlate with serum creatinine values. However, there were sera with high NCPI levels which did not have increased serum creatinine values. In sera with high NCPI levels subjected to double radial immunodiffusion two precipitin lines, one completely and the other partially identical to NCPI were registered. After fractionating of serum proteins with gel chromatography on Sephadex G 100, two protein peaks of immunological similarity to purified NCPI were found: one low molecular weight (MW around 12,000) and one high molecular weight (MW around 100,000). The low molecular weight NCPI-like material appeared to inhibit human cathepsin B and papain and is thus free serum NCPI. alpha-Cysteine proteinase inhibitor did not increase with serum creatinine as did NCPI.
Blood Proteins↗
Localization of cholecystokinin immunoreactivity in the human brain with special reference to ontogeny.
The cellular localization and regional distribution of peptides of the gastrin/cholecystokinin family was investigated in human fetal, neonatal and adult brains by use of immunohistochemical techniques. It could be revealed that a cholecystokinin-like immunoreactivity is already present in human brain at the 11/12th gestational weeks. With the 19th week a strong increase in number of CCK reactive cells and the reaction intensity is obvious. The data are compared with the distribution pattern of the adult brain. Our data permit to conclude that gastrin/CCK-related material might play roles independent of neurotransmitter functions during early human brain development.
Aged↗
Immunocytochemical characterisation of human pituitary adenomas.
Immunohistochemical and histological investigations were undertaken on 24 surgically-removed pituitary adenomas. By histology (haemalu-eosin staining), 7 chromophobe, 12 acidophil and 5 basophil pituitary adenomas were revealed. For immunohistochemical purposes the peroxidase-antiperoxidase technique was applied. Primary antisera against 10 hormones were used. By immunohistochemistry, 7 prolactin-containing, 2 TSH-containing, 2 GH-containing and 1 beta-endorphin-containing pituitary adenomas were identified. Furthermore, 1 mixed thyrotropic-prolactin human pituitary adenoma was detected. A possible connection between histological and immunocytochemical findings is discussed.
Adenoma↗
Cysteine proteinase inhibitors produced by mononuclear phagocytes.
Monocytes were separated from human peripheral blood and allowed to attach to culture flasks, after which the content and production of a number of cysteine proteinase inhibitors was assayed. These were: a low molecular weight (MW 12000) acid cysteine proteinase inhibitor (ACPI); a low-molecular weight inhibitor of the same size with neutral pH (NCPI), and alpha-cysteine proteinase inhibitor with a molecular weight around 90 000 (alpha-CPI). Only NCPI was detectable in the cultures at the beginning of the incubation, and it was synthesized and released into the incubation mixture during the incubation, especially if the cells were stimulated with silica. The amount of NCPI contained in and released from the cells was drastically decreased by puromycin. Immunoblots after cell electrophoresis in polyacrylamide gel revealed only one molecular form of NCPI with a molecular weight of 12 000 both in the cells and in the culture medium. No ACPI or alpha-CPI could be detected.
Blood Proteins↗