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Biomedical subjects

M Rojkind

Publications and source records attributed to M Rojkind.

At least 109 records · Page 6Linked to original sources
PubMed1970

The relationship between the free pool of proline and collagen content in human liver cirrhosis.

The free proline, free glutamic acid, and total collagen contents of the livers of cirrhotic and noncirrhotic patients were determined. The amounts of free proline in the sera of the patients were also determined. The results indicated that certain metabolic changes occurred in cirrhotic livers of humans that were similar to the metabolic changes observed previously in CCl(4)-induced cirrhosis in the rat. The amount of free proline was coordinate with the increase in total collagen, and both were inversely related to the amount of free glutamic acid. The average proline concentration in sera of cirrhotic patients was not higher than that of non cirrhotic patients, suggesting that the metabolic alteration noted above is a local event in the liver related to fibrogenesis. These and other results suggest that the pool size of free proline may play a prime role in regulation of collagen biosynthesis in liver cirrhosis.

Autopsy↗
PubMedDate not supplied

A noncollagenous matrix for attachment of rat hepatocytes in culture.

Adult rat hepatocytes efficiently attach to intact connective tissue fibers prepared from normal rat liver; this material has been given the name of "biomatrix". The cells remain alive and differentiated for at least 4 months in culture. The liver biomatrix contains both collagen and noncollagenous glycoproteins. Heretofore, the functions of the different components of the biomatrix in facilitating cell adhesion and promoting survival and differentiation of rat hepatocytes have not been investigated. We now report on an aggregate of glycoproteins which were with dilute acetic acid from liver biomatrix and which facilitate hepatocyte adhesion to plastic dishes and collagen. One protein in the extract, with a molecular weight larger than 300,000, was selectively immunoprecipitated with an antibody prepared against the extract and immunoadsorbed to glutaraldehyde-cross-linked rat serum. The antibody did not cross-react with cold-insoluble globulin and selectively inhibited cell attachment. The protein of the molecular weight of 300,000 appears to be specific for liver, since similar extracts prepared from rat lung, kidney, and heart biomatrices did not cross-react with the antibody. Furthermore, the latter extracts did not facilitate cell attachment above values obtained with plain culture dishes. The results suggest that glycoproteins in the biomatrix, which are antigenically distinct from fibronectin, can mediate attachment of rat hepatocytes to plastic dishes and collagen.

Animals↗
PubMedDate not supplied

The nature of the collagen in hepatic fibrosis in advanced murine schistosomiasis.

Livers from CF 1 mice infected with Schistosoma mansoni, 50 cercariae each, were examined 8 weeks postinfection. The collagen content of the livers was increased about 18-fold over that for normal control animals. Quantitation of the collagen types in pepsin-solubilized collagen showed a change in the ratio of Type I to Type III from 2:1 in normal mice to 1:1 in the fibrotic animals. The change in ratio resulted from a very large accumulation of Type III collagen and, accordingly, may provide an important model for study of the possible reversibility of fibrotic lesion.

Amino Acids↗
PubMedDate not supplied

Abnormal matrix recognition by Morris hepatomas correlates with low glucagon binding capacity.

Liver biomatrix contains a group of connective tissue components needed for attachment, survival, and maintenance of liver-specific functions of adult rat hepatocytes in culture. An acidic extract of liver biomatrix that contains a group of glycoproteins can replace intact biomatrix in promoting attachment and survival of hepatocytes. However, except for albumin synthesis, liver-specific functions have not been tested. Acidic extracts of biomatrices prepared from heart, kidney, lung, and spleen (heterologous) contain a similar group of glycoproteins, but differ with respect to liver glycoproteins in their capacity to sustain hepatocyte binding. Normal hepatocytes attach poorly to heterologous glycoprotein extracts, although regenerating and tumoral hepatocytes attach to liver glycoproteins and adhere equally well or with greater efficiency to heterologous glycoprotein extracts. The increased efficiency of hepatocytes to attach to kidney biomatrix-derived glycoproteins showed a linear correlation with the decreased glucagon binding capacity of their isolated plasma membranes. An epithelioid cell-line derived from kidney (MDCK) attached with higher efficiency to kidney than to liver glycoproteins. These results suggest that biomatrices may contain specific glycoproteins needed for attachment and survival of their epithelial cells. This specificity is lost during the proliferative state of regenerating and tumoral hepatocytes and could be important in the general mechanism of tumor dissemination and metastases.

Animals↗
PubMedDate not supplied

Lack of glucagon receptors in Morris hepatoma 7800.

When compared to normal liver membranes, purified plasma membranes of regenerating liver and Morris hepatomas contain low but variable capacities to bind glucagon. This property is inversely related to the capacity of the isolated hepatocytes to bind to heterologous biomatrix glycoproteins. Since these parameters are characteristic of the proliferative state of the cells, it was important to further study the glucagon receptor protein and stimulation of adenylate cyclase activity. Our results show that 125I-iodinated plasma membranes obtained from normal liver contain three molecular species (117000, 98000, 86000 molecular weight) that can be eluted specifically with glucagon from a sepharose-glucagon affinity column. These proteins contain the putative glucagon receptor since binding of 125I- iodoglucagon is increased 150-fold as compared to unfractionated membranes. Plasma membranes obtained from Morris hepatoma (7800) and liver of chemically hepatectomized rats do not bind glucagon and lack these proteins. After inactivation with N-ethylmaleimide of the adenylate cyclase activity of the normal plasma membranes, they were fused with membrane of the hepatoma. The hybrid membranes showed 60% recovery of glucagon-stimulated cyclase activity. These results suggest that the plasma membranes of the proliferating liver cells do not contain receptor protein but have intact regulatory and catalytic subunits of the adenylate cyclase system.

Adenylyl Cyclases↗