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Biomedical subjects

H M Tinberg

Publications and source records attributed to H M Tinberg.

At least 19 recordsLinked to original sources
PubMed1983

Alcoholic hepatitis: granulocyte chemotactic factor from Mallory body-stimulated human peripheral blood mononuclear cells.

The characteristic histopathological features of acute alcoholic hepatitis include hyaline degeneration of hepatic parenchymal cells (Mallory bodies), hepatocellular necrosis, and granulocyte infiltration of the liver. The chemotactic response of neutrophils to highly purified Mallory bodies was studied. Mallory bodies, per se, were not chemotactic for granulocytes, nor did they generate chemotactic factors when incubated with serum. However, a factor(s) chemotactic for both granulocytes and mononuclear cells was generated when Mallory bodies were incubated with mononuclear cells, both from patients with alcoholic hepatitis or from normal controls. It was concluded that Mallory bodies stimulate peripheral blood mononuclear cells to release a factor chemotactic for granulocytes and mononuclear cells. This factor may be important in the etiology of the cellular infiltration in the livers of patients with alcoholic hepatitis.

Acute Disease↗
PubMed1982

Immunocytochemical identity of hepatocellular hyalin in alcoholic and non-alcoholic liver diseases.

Intracellular, eosinophilic, hyaline inclusions (alcoholic hyalin, Mallory bodies) are found in livers of patients with a number of hepatic disorders, although they are most common in alcoholic liver disease. Tissues from patients with primary biliary cirrhosis, jejunoileal bypass, hepatocellular carcinoma, Wilson's disease, and Indian childhood cirrhosis were all positive for hyalin by hematoxylin and eosin staining. Immunocytochemical labeling, using guinea-pig antiserum specific for alcoholic hyalin, was utilized to determine the extent of crossreactivity between hepatocellular hyalin in these various conditions. This antiserum bound to hyalin in fixed paraffin-embedded sections of all liver tissues studied as detected by indirect immunoperoxidase labeling. Binding to normal human liver, however, was restricted to light staining at the surface of hepatocytes. Preimmune guinea-pig serum did not bind to either normal liver or to the test tissues. Our results suggest that hyalin found found in a diverse group of liver conditions represents an immunologically related structure and that its formation may involve a common mechanism.

Adolescent↗
PubMed1981

Identification of Mallory bodies with rhodamine B fluorescence and other stains for keratin.

Rhodamine B staining in conjunction with fluorescence microscopy is shown to demonstrate Mallory bodies. Mallory body morphology, localization, and distribution in hepatocytes from griseofulvin-fed mice, human hepatoma, and human alcoholics were similar to those observed in the same tissues after conventional staining methods for Mallory bodies. The presence of these inclusions was further confirmed by specific cytochemical localization with indirect immunoperoxidase labeling, horseradish peroxidase labeling, and electron microscopy. Other tinctorial or histochemical procedures previously used for keratin or prekeratin (modified Mallory stain, Kreyberg method, Pauly method for histidine) also stained Mallory bodies for study with white light microscopy but with decreasing sensitivity respectively. Mallory bodies from mouse and human liver both appear to contain a keratin-like moiety. This entity may be simply, rapidly, and permanently stained with rhodamine B, and selectively and reproducibly demonstrated with fluorescence microscopy.

Animals↗
PubMed1979

Mallory bodies. Horseradish peroxidase: specific cytochemical and biochemical marker for alcoholic hyalin.

Horseradish peroxidase (HRP), a glycoprotein enzyme, bound specifically to Mallory bodies (MBs) in cryostat sections of autopsy liver and liver biopsies. In contrast, HRP did not bind to cryostat sections of normal liver. The specificity of HRP binding was also observed using light and electron microscopy in autopsy liver-derived subcell fractions prepared by the MB isolation procedure. In order to quantitate HRP binding, a solid phase colorimetric assay was developed. This assay involves immobilizing purified MBs or homogenized tissue fractions in glass tubes, incubating with HRP, and measuring the enzymatic activity of bound HRP. A linear relationship between MB concentration and HRP binding was observed. The assay was capable of detecting as little as 1 microgram of MB protein. The specificity of HRP binding was also investigated using the solid phase assay. The specific activity (HRP bound per milligram of protein) of purified MBs was 10 to 15 times that of a glass wool-filtered liver homogenate suggesting that the solid phase assay may be of use in monitoring the purification of MBs. HRP did not bind to normal liver homogenate even when large loads were assayed. The results of this study indicate that HRP binding, employed cytochemically, represents a rapid and facile procedure for ascertaining the presence of MBs in tissue. In some cases, those structures may not be easily visualized by conventional staining procedures. Furthermore, quantitation of MBs in tissue may be possible by using a solid phase enzyme-linked assay.

Colorimetry↗
PubMed1978

Mallory bodies: isolation of hepatocellular hyalin and electrophoretic resolution of polypeptide components.

Mallory bodies (MBs) were obtained in purified form from human liver obtained at autopsy using a new procedure consisting of sedimentation through a Ficoll viscosity barrier. Preparations from six livers ranged in purity from 95 to 99 per cent. MB preparations were autofluorescent. MBs were strongly agglutinated by Concanavalin A. The presence of carbohydrate was also indicated by the fact that MBs bound fluorescently labeled Concanavalin A; no binding was observed in the presence of appropriate inhibitor monosaccharides. Direct analysis indicated that MBs contained variable amounts of neutral hexose (0.65 to 2.4 mumoles of glucose-equivalents per milligram of protein) but no sialic acid. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis indicated that purified MBs contain five major polypeptides possessing apparent molecular weights of 56,000, 48,500 to 45,000 (triplet), and 32,500. Periodic acid-Schiff-positive components were not detected. Scanning electron microscopy of isolated MBs revealed the presence of a rough, fibrous surface, whereas conventional transmission electron microscopy indicated the filamentous nature of MBs.

Concanavalin A↗
PubMed1975

Effect of crosslinking on mitochondrial structure and function.

Rat liver mitochondria were treated with ethylacetimidate and methylbutyrimidate, monofunctional imidates, and with dimethylsuberimidate, a bifunctional imidate, and the effects on structure and function studied. Mitochondria treated with 5 mM dimethylsuberimidate or greater did not respond osmotically when placed in deionized water. Sodium dodecylsulfate-polyacrylamide gel electrophoresis revealed that at concentrations greater than 5 mM dimethylsuberimidate nearly all mitochondrial polypeptides failed to enter 6% gels, indicating crosslinking of both membrane and soluble proteins. Extensive amidination by ethylacetimidate and methylbutyrimidate had little effect on ascorbate-tetramethylphenylenediamine oxidase while extensive inhibition resulted from dimethylsuberimidate treatment. The possible involvement of molecular motion in electron transport is discussed.

Alkylating Agents↗