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Biomedical subjects

A Rinne

Publications and source records attributed to A Rinne.

At least 91 records · Page 5Linked to original sources
PubMed1983

Insulin and C-peptide in human brain neurons (insulin/C-peptide/brain peptides/immunohistochemistry/radioimmunoassay).

The regional distribution and cellular localization of insulin and C-peptide immunoreactivities were studied in human cadaver brains using the indirect immunofluorescence method, the peroxidase-antiperoxidase technique, and radioimmunoassay. Products of the immune reactions to both polypeptides were observed in most nerve cells in all areas of the brain examined. Immunostaining was mainly restricted to the cell soma and proximal dendrites. Radioimmunoassay revealed that human brain contains insulin and C-peptide in concentrations much higher than the blood, the highest being in the hypothalamus. These findings support the hypothesis that the "brain insulin" is--at least in part--produced in the CNS.

Aged↗
PubMed1983

Separation of cysteine proteinase inhibitors from psoriatic scale.

Inhibitors of cysteine proteinases from extracts of psoriatic scales and from scrapings of normal skin surface were separated by using immunochemical, electrophoretic and chromatographic methods. The total inhibitory capacity of cysteine proteinases measured as inhibition of papain, was higher in the extracts from psoriatic scales than from normal skin surface scrapings. In normal skin samples only one inhibitor, acidic inhibitor, was identified while altogether three separate inhibitors were revealed in psoriatic extracts: an acid inhibitor (ACPI) with pI at 4 . 7-5 . 5, molecular weight around 12,000, a near-neutral inhibitor (NCPI) with pI at 6 . 0-6 . 5, molecular weight around 12,000, and a slightly alkaline inhibitor with pI around 7 . 0-7 . 5 and molecular weight 37,000. Two to three isoelectric variants were found in all these inhibitors. Quantitatively, the acid inhibitor is the most abundant one. The low molecular weight inhibitors (ACPI and NCPI) were localized with PAP method in the upper spinous cell layers in formalin-fixed skin sections. The slightly alkaline inhibitor with mol.wt 37,000 reacted in immunodiffusion with a commercial rabbit polyvalent antiserum. The abundance of cysteine proteinase inhibitors in the psoriatic lesion is considered as a local effort to compensate for the high cysteine proteinase activity.

Chromatography, Gel↗
PubMed1982

Human spleen cysteineproteinase inhibitor. Purification, fractionation into isoelectric variants and some properties of the variants.

The papain inhibitor from human spleen was purified by extraction in isotonic sucrose, acetone fractionation, papain-Sepharose affinity chromatography and gel filtration on Sephadex G-50. The purified inhibitor was fractionated by electrofocusing into four major isoelectric variants with pI values of 4.7, 5.0, 6.0 and 6.5. These variants can be classified into two groups: the acidic type, comprising the variants with pI 4.7 and 5.0, and the neutral type, comprising the variants with pI 6.0 and 6.5. The following properties distinguish the two types: 1. Immunological properties: antibodies raised against either of the neutral variants precipitated both of these, but not the acidic variants. The antiserum against the human epidermal cysteineproteinase inhibitor precipitated the acidic variants, but not the neutral variants. 2. Molecular size: two-dimensional electrophoresis of the purified inhibitor gave molecular weights of 11400 for the acidic variants and 12000 for the neutral variants. The pI 6.0 variant contained two compounds with molecular weights of 12000 and 12800. 3. Enzyme spectrum: human cathepsin B was inhibited by the acidic type, while the neutral type was a poor inhibitor. Both types inhibited cathepsin H, papain, ficin and bromelain, although the inhibition of bromelain did not exceed 70%. Human cathepsin D, bovine trypsin and chymotrypsin and porcine elastase were not inhibited by either type.

Aged↗
PubMed1982

Insulin-like immunoreactivity in the human brain- A preliminary report.

The localization and regional distribution of insulin-like immunoreactivity (IRI) was studied in human brain autopsy material using the indirect immunofluorescence technique. A positive reaction for IRI could be observed in many neurons of the hypothalamus, the hippocampus, corpus amygdaloideum, medulla oblongata (especially within the nuclei of cranial nerves IX, X and XII), and the cerebral cortex, whereas the cerebellar cortex was lacking in immunohistochemically detectable insulin-like material. No nerve fibres containing polypeptides could be revealed. Additionally, the insulin content of various brain regions was estimated by radioimmunoassay. Insulin concentrations in human nervous tissue were found to be elevated in comparison to blood plasma levels.

Aged↗
PubMed1982

C-peptide immunoreactive neurons in human brain.

C-peptide/C-peptide-like immunoreactivity was shown to be present in the cytoplasm of the soma and the proximal part of apical dendrites of some pyramidal cells in the Neocortex (Gyrus precentralis) and Hippocampus of man. C-peptide (connecting peptide) is a metabolic product in insulin biosynthesis and its localization in neurons is a proof for extrapancreatic insulin production.

Brain Chemistry↗
PubMed1982

Colonoscopic appearance of the remnant of the appendix after total inversion.

In a series of 395 total colonoscopies, an oblong smooth tumor was seen in the cecum of six patients corresponding to the remnant of the totally inverted appendix. All the patients had undergone a laparotomy during which the appendix was inverted. The histological examination demonstrated a uniform finding without any signs of polyp or malignancy. Our findings stress that the appendix fails to undergo necrosis after total inversion in some cases, in which the changes in the cecum can be readily identified by total colonoscopy.

Adult↗
PubMed1981

Immunoreactive glucagon in neurons of various parts of the human brain. Demonstration by immunofluorescence technique.

The presence of glucagon-like immunoreactivity in nerve cells of different parts of the human brain was demonstrated by the indirect immunofluorescence technique. A bright fluorescent reaction was observed in the pyramidal cells of lamina V of the Neocortex. Less prominent concentrations of the glucagon-like material were detected in a few pyramidal cells of the Hippo-campus and in some neurons of the Presubiculum and Subiculum. Within the Corpus amygdaloideum, only a few magnocellular neurons showed a positive reaction. The Hypothalamus was evidenced by a moderate, but widely distributed, reaction in magnocellular and medium-sized nerve cells in different nuclei (especially Nuc. ventromedialis and Nuc. arcuatus). A strong immunofluorescence was localized to some neurocytes in the Nuc. amibigus, and Nuc. n. hypoglassi. The Purkinje cells of the cerebellar cortex were free from immunoreactive material, but fluorescence occurred in some very small nerve cells of the Cerebellum (probably granular cells). A dependence of the strength of immunofluorescence of the time delay between autopsy and death is shown.

Amygdala↗
PubMed1981

Intracellular immunoglobulins in plasma cells of nasal biopsies taken from vanadium-exposed workers. A retrospective case control study by the peroxidase-antiperoxidase (PAP) method.

The amount and classes of immunoglobulins were determined in plasma cells of nasal biopsies taken from vanadium-exposed workers, by peroxidase-antiperoxidase (PAP) method. Antiserum 1: 100 dilution proved better than 1: 1000 dilution in demonstrating the immunoglobulins in the formalin-fixed paraffin-embedded nasal biopsies stored four years. The number of plasma cells of the exposed was found to be increased, but no reliable conclusions could be drawn from the amounts of immunoglobulins in this survey. The number of positive cells had decreased probably due to storage and perhaps to fixation method, too (10% formalin). However, these findings seem to support our previous suggestion that vanadium does not cause an allergic nasal inflammation.

Humans↗
PubMed1980

[Demonstration of an epidermal SH-protease inhibitor in normal epithelium and in some human neoplasms--an immunological study (author's transl)].

Using a specific antiserum, it was possible to demonstrate (with the Ouchterlony-test, immunofluorescence and peroxidase-antiperoxidase reaction) that the epidermal thiolprotease inhibitor was present in all the squamous epithelia tested by us, e.g. oesophagus, vagina and portio. Immunological methods further showed that epidermoid carcinoma of the skin, squamoepithelial carcinomas of the portion and oesophagus, and squamoepithelial carcinoma of the lung contained an immunoreactive protein reminiscent of the epidermal protease. The immunoreactive protein typical of squamous epithelium was also visible in part of the anaplastic lung carcinomas, which means that the determination of the inhibitor may be of significance in the classification of lung tumors.

Carcinoma, Squamous Cell↗
PubMed1979

Localization of the rat epidermal SH-protease inhibitor in proventricular and vaginal squamous epithelium. An immunofluorescence study.

The rat epidermal SH-protease inhibitor was localized with the indirect immunofluorescence method in the rat proventricle and vagina fixed in cold phosphate-buffered formalin. Bright fluorescence was seen in the cytoplasms of the superficial layers of these squamous epithelia only when a highly specific antiinhibitor serum was used. The fluorescence diminished when normal rabbit serum or a rabbit antiserum againts bovine serum albumin was used instead of the anti-inhibitor serum. When the anti-inhibitor serum was neutralized with the purified epidermal inhibitor, the fluorescence was again markedly weakened. The results confirm our previous observations showing that the epidermal SH-protease inhibitor also occurs in other squamous epithelia, especially in the cytoplasms of the cells in their upper layers.

Animals↗
PubMed1979

Localization of the rat epidermal SH-protease inhibitor in the proventricular squamous epithelium using the peroxidase-antiperoxidase (PAP) method.

The rat epidermal SH-protease inhibitor was localized by the PAP method in the squamous epithelium of rat proventricle. Brown accumulation due to the peroxidase reaction was seen in the superficial and middle layers of squamous epithelia. The localization of the inhibitor in squamous epithelium is the same as we have demonstrated with immunofluorescence staining.

Animals↗
PubMed1979

Effects of vanadium on the upper respiratory tract of workers in a vanadium factory. A macroscopic and microscopic study.

An epidemiologic cross-sectional case-history study on the injurious effects of vanadium was carried out among the workers of a vanadium factory. The upper respiratory tract of 63 male workers exposed to vanadium dust was examined macroscopically and microscopically, and the findings were compared with those of a reference group of workers who were exposed to inert dust only. The groups compared were of similar ages and had similar smoking habits. Nasal smears and sputum cells were studied microscopically, and biopsies for histological study were taken from the nasal mucosa. The biopsies from the vanadium workers showed a significant increase in the number of plasma and round cells, and the histological picture was almost characteristic. There were no increased numbers of secretion eosinophils or other signs indicative of allergic inflammation.

Age Factors↗
PubMed1978

A protein reminiscent of the epidermal SH-protease inhibitor occurs in squamous epithelia of man and rat.

The occurence of the human and rat epidermal SH-protease inhibitors in various human and rat tissues was studied by double radial immunodiffusion against specific antisera to the inhibitors. An immunoreactive protein was found in the extracts prepared from human and rat epidermis and from eosophageal and vaginal squamous epithelia, and from rat pro-ventricular squamous epithelium. No immunoreactive protein was found in man or rat in any other of their tissues, studied by us. The results strongly suggest that a protein reminiscent of the human or rat epidermal SH-protease inhibitor is present in squamous epithelia but not in other tissues. The identity of the epidermal inhibitor and the immunoreactive protein in the other squamous epithelia was confirmed by immunodiffusion, immunoelectrophoresis and gel chromatography, and by immunoinhibition of the papain inhibiting activity of the human epidermal and oesophageal inhibitors by gammaglobulins separated from antiserum to the human epidermal inhibitor.

Animals↗
PubMed1978

Localization of the human SH-protease inhibitor in the epidermis. Immunofluorescent studies.

Human epidermis contains a low molecular weight SH-protease inhibitor (Human Epidermal Inhibitor = HEI), whose epidermal localization was performed with the indirect immunofluorescence method. The fluorescence was most intensive in the cytoplasms of epidermal cells, often occurring perinuclearly. The fluorescent material in the frozen sections was often finely granular and occasionally extended outside the cytoplasm, while the fluorescence in fixed sections was more uniform, but weaker. Stratum basale generally stained poorly or not at all, as did also stratum lucidum. Stratum corneum stained fairly intensively throughout. In addition to fixation, the outcome of staining was also affected by the thickness of the epidermis, particularly stratum corneum. The significance of this inhibitor for the differentiation of epidermal cells and the keratinization of epidermis has therefore been discussed, and the authors assume it to be of considerable significance in these processes.

Cytoplasm↗