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Biomedical subjects

A Rinne

Publications and source records attributed to A Rinne.

At least 73 records · Page 4Linked to original sources
PubMed1984

Occurrence of acid and neutral cysteine proteinase inhibitors in epidermal malignancies: immunohistochemical study.

Acid cysteine proteinase inhibitor ( ACPI ) and neutral cysteine proteinase inhibitor ( NCPI ) were localized in human epidermal malignancies by the unlabelled peroxidase-antiperoxidase complex method. Basaliomas did not contain ACPI or NCPI . In spinous, metatypic , and clear cell carcinomas of the epidermis, both inhibitors were located in the cytoplasm and sometimes on the cell membranes of the differentiated carcinoma cells. The inhibitors were not seen in the 1 or 2 most "basal" cells layers of the carcinoma islets. The locations of both inhibitors were similar, and the staining for ACPI was usually more intense than staining that NCPI .

Adenocarcinoma↗
PubMed1984

Acid and neutral cysteine proteinase inhibitor in normal uterine portio and in squamo-epithelial metaplasia, dysplasias and infiltrative carcinoma of the uterine portio.

Acid cysteine proteinase inhibitor (ACPI) and neutral cysteine proteinase inhibitor (NCPI) were localized in formalin-fixed normal human uterine portio as well as in the squamous cell carcinoma and dysplasias of the uterine portio. The peroxidase-antiperoxidase technique was used. In the squamous epithelium of normal uterine portio, ACPI and NCPI were localized in the cells of the upper and middle layers, mainly in the cytoplasm. In the precursors of cancer, immunoreactivity for ACPI and NCPI declined, and neither of the inhibitors was demonstrable immunohistochemically in the anaplastic squamo-epithelial carcinoma of the uterine portio. Our results suggest that ACPI and NCPI are associated with squamo-epithelial differentiation and that they may also be of significance for the regulation of cysteine proteinase activity in normal tissue and malignant growth.

Carcinoma, Squamous Cell↗
PubMed1984

Partial purification and some properties of a new papain inhibitor from psoriatic scales.

A new papain inhibitor was purified from psoriatic epidermal scales using gel chromatography and anion exchange chromatography. The purified protein inhibited papain and ficin but not cathepsin B, cathepsin H, trypsin, or chymotrypsin. Isoelectric focusing revealed 3 major inhibitor variants with pI's of 7.3, 6.9, and 6.5. A Mr of 38,000 was obtained by a gel chromatographic method for the crude inhibitor. After sodium dodecyl sulfate-polyacrylamide gel electrophoresis the Mr values of the isoelectric variants were: 43,000 for the variant pI 7.3, 43,000 and 35,000 for the variant pI 6.9, and 34,000-35,000 for the variant pI 6.5. An antiserum of the inhibitor was used to locate the inhibitor in the psoriatic and normal epidermis. In psoriatic epidermis, the inhibitor was found in the peripheral cytoplasm of spinous cells and in the scale. In normal epidermis, the staining was seen only in orifices of hair follicles. An inhibitor with similar size and antigenic properties to that isolated from the psoriatic scales was demonstrated in extracts made from the whole-thickness epidermis but not in extracts from the healthy epidermal scales, the dermis, the liver, the spleen, or the blood serum.

Cadaver↗
PubMed1984

Sound spectrographic cry analysis of infants with hydrocephalus.

Altogether 248 cries from 62 infants with hydrocephalus were analysed by sound spectrography: 92 cries from infants with congenital hydrocephalus and 52 cries from each of the groups with cerebral malformations, hydrocephalus as sequelae of meningitis, and after closure of a meningomyelocele. The cries were compared with 104 cries of normal healthy infants of corresponding age. The cry analysis showed that the most abnormal cries were seen in infants with congenital hydrocephalus and cerebral malformations. The pitch of the fundamental frequency did not differ from normal crying in cries of infants collected after recovery from meningitis and after closure of a meningomyelocele. The cries in hydrocephalus after meningitis showed more commonly flat melody types and the occurrence of bi-phonation.

Crying↗
PubMed1984

Brain gastrin/CCK immunoreactivity in sand rat (Psammomys obesus): decrease of number of positive neurons in diabetic animals.

Gastrin/CCK immunoreactivity appears to be widely distributed throughout the mammalian CNS, being most abundant in the cerebral cortex [Vanderhaeghen et al. 1975; Straus et al. 1977; Beinfeld et al. 1981]. Besides its putative role as a co-transmitter in dopaminergic neurotransmission [Hökfelt et al. 1980], cholecystokinin is apparently involved in the central regulation of appetite and satiety [Gibbs et al. 1973; Antin et al. 1975; Parret and Batt 1980; Smith 1980; Smith and Gibbs 1981] Furthermore, it has been shown that the brain concentration of the peptide is decreased in genetically obese mice as compared to non-obese animals [Strauss and Yalow 1979]. The sand rat (Psammomys obesus) is a desert rodent which tends to become diabetic when it is fed with normocaloric diet and restricted in movement [Haines et al. 1965; Hahn et al. 1971]. However, the usefulness of this animal as a paradigm of diabetes is now being revised, since because in its typical expression this metabolic dysfunction appears to be an obesity syndrome [Rice and Robertson 1980]. Therefore, it seems to be necessary to study the distribution of gastrin/CCK-immunoreactive nerve cells in the brain of normal and diabetic (obese) sand rats to get further information about mechanism underlying the development of this form of diabetes.

Animals↗
PubMed1984

[Immunoreactive insulin in the CNS of human fetuses and newborn infants of metabolically healthy and diabetic mothers--an immunohistochemical study].

The cellular localization and regional distribution of "insulin-like immunoreactivity" and "C-peptide immunoreactivity" were studied in brains of fetuses and newborns from normoglycaemic and diabetic mothers using immunohistochemical techniques. It is shown that "insulin-like material" and "C-peptide-like material" occur in the same nerve cells. No differences in regard to the localization of both polypeptides exist between abort material from normoglycaemic and diabetic mothers.

Brain Chemistry↗
PubMed1984

[Behavior of small molecular cysteine proteinase inhibitors in lung cancers and surrounding tissue].

In this work, we have studied the occurrence of acid and neutral cysteine proteinase inhibitors in 3 histologically different lung cancers. The acid cysteine proteinase inhibitor ( ACPI ) seems to be associated to squamous differentiation as our previous observations have shown. As a new observation we could show that the neutral cysteine proteinase inhibitor ( NCPI ) was localized in alveolar macrophages.

Adenocarcinoma↗
PubMed1983

Insulin- and glucagonlike peptides in the brain.

The cellular localization and regional distribution of insulin- and glucagonlike substance, C-peptide-like immunoreactivity, thiol:protein disulphide oxidoreductase, TPO (E.C.1.8.4.2.), and insulin/glucagon-specific proteinase, ISP (E.C.3.4.22.-), are studied in the CNS of man, adult and juvenile rats, mice, tortoises, and frogs by use of immunohistochemistry. Furthermore, the content of immunoreactive insulin, glucagon, and C-peptide was estimated in human cadaver brains by radioimmunoassay. It could be shown that insulinlike immunoreactive material is widely distributed in the human brain and the CNS of juvenile rats as well as in mice, whereas in the CNS of adult rats and nonmammalian animals (frogs, tortoises) the polypeptide is restricted to a few nerve cell populations. C-peptide immunoreactivity was demonstrated in human CNS in the same nerve cells as insulin. By use of two different glucagon-antisera it was revealed that gut-type glucagon occurs in many nerve cells of human and mouse brains, as well as in the CNS of juvenile rats. On the other hand, pancreas-type glucagon was less widely distributed in the human brain and nearly not detectable in the CNS of mice and rats. With the exception of neurosecretory nerve cells, there was a high degree of coincidence between the localization of insulin and TPO. The immunoreaction against the ISP antiserum was weak, but correlated well with the distribution of insulin-immunoreactivity. The occurrence of TPO and ISP in the brain demonstrates the ability of nervous tissue to degrade insulin and glucagon. By radioimmunoassay it was established that human brain contains insulin, glucagon and C-peptide at concentrations that exceed blood levels. We conclude from our data that, at least in part, cerebral insulin and glucagon are products of the brain itself.

Animals↗
PubMed1983

Cysteine proteinase inhibitors in psoriatic epidermis.

Human psoriatic epidermis and scales were demonstrated to contain two antigenically separate cysteine proteinase inhibitors, one acidic with an isoelectric point of 4.7-5.0 (ACPI) and one neutral with an isoelectric point of 6.0-6.5 (NCPI), while normal epidermis contains only ACPI. The total papain (cysteine proteinase) inhibiting activity of the psoriatic epidermis as calculated per mg protein was higher than that in normal epidermis. Both ACPI and NCPI were localized immunocytochemically, mainly in the highest spinous cell layers with less activity in the parakeratotic cells and lower layers of spinous cells. Basal cells were essentially negative.

Cysteine Proteinase Inhibitors↗
PubMed1983

Demonstration of immunoreactive acid cysteine-proteinase inhibitor in reticulum cells of lymph node germinal centres.

Seven human lymph nodes showing different types of reactive change, were examined for the presence of acid cysteine-proteinase inhibitor (ACPI) by the peroxidase-antiperoxidase method. A clear positive reaction was found in the germinal centres. The staining pattern indicated immunoreactivity of the dendritic reticulum cells, but the possibility that other cells, particularly histiocytic reticulum cells, may also react with antiserum raised against ACPI cannot be excluded.

Cysteine Proteinase Inhibitors↗
PubMed1983

Sound spectrographic analysis of pain cry in preterm infants.

Sound spectrographic cry analysis was performed on 302 cries of 48 preterm infants born at 30-37 gestational weeks. The cries were recorded during the first week of life and thereafter weekly until the infants were discharged. The control series comprised 54 cries from 27 fullterm healthy infants. The results showed that the cries of the smallest prematures compared with the controls were shorter, more high-pitched, and included bi-phonation and glide more often. The cry characteristics changed with increasing conceptual age and the older the child the more the cry pattern resembled that of the fullterm. The cries of the preterm infants when they had reached 38 conceptual weeks were similar to those of newly born fullterm infants. The results indicate that the gestational age should be taken into consideration in cry analysis.

Acoustics↗
PubMed1983

Localization of three inhibitors of cysteineproteinases in the human oral mucosa.

3 known human cysteineproteinase inhibitors--neutral cysteineproteinase inhibitor (NCPI), acid cysteineproteinase inhibitor (ACPI) and serum alpha-cysteineproteinase inhibitor (alpha-CPI)--were localized immunohistochemically in the squamous epithelium of the mouth by using the peroxidase-antiperoxidase complex method and formaldehyde-fixed paraffin-embedded tissue sections. Neither ACPI nor NCPI was found in the 2 to 3 most basal cell layers of the epithelium, but a strong cytoplasmic reaction was seen in the upper cell layers by using either anti-ACPI or anti-NCPI serum. In some cells the most dense stain precipitate was seen around or in the nucleus, and in the highest cell layers the staining was sometimes associated with the cell membrane. alpha-CPI was localized mainly in the epithelial stroma and in the intercellular space of the epithelium.

Cysteine Proteinase Inhibitors↗
PubMed1983

The glucagon/glucagon-like immunoreactivities in neurons of the human brain.

Using indirect immunofluorescence and Sternberger's PAP techniques on Bouin-fixed paraffin sections it was possible to show a glucagon/glucagon-like immunoreactivity in the following sites of the human brain: the Lamina V pyramidal cells of the Neocortex, the various neurons of the Hippocampus and Corpus amygdaloideum, the perikarya of neurons in the Nucleus ventromedialis and Nucleus infundibularis (arcuatus), the Nucleus ambiguus and the numerous granular cells of the cerebellar cortex. It was also possible with both techniques to find a similar distribution of the peptide hormones in the perikarya and the proximal parts of the neuronal extensions. Appropriate controls were used to confirm the results. Simultaneously, tissue specimens from the same brain regions were investigated for glucagon by radioimmunoassay. The glucagon content of nervous tissue was found to be much higher than the average glucagon concentration of blood plasma. The highest level of the polypeptide could be revealed for the Hypothalamus (up to 40 times higher than in blood plasma).

Brain Chemistry↗