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Biomedical subjects

R H Hinton

Publications and source records attributed to R H Hinton.

At least 55 records · Page 3Linked to original sources
PubMed1979

Secretory component as the receptor for polymeric IgA on rat hepatocytes.

Rat hepatocytes in short-term monolayer cultures bound radiolabeled polymeric rat IgA but not IgG. The binding of 125I-IgA was inhibited equally well by unlabeled polymeric IgA and by antiserum to rat secretory component (SC). The antibody to SC, after specific purification and radiolabeling, was bound to hepatocytes as effectively as the IgA. These results indicate that SC acts as the receptor for polymeric IgA on rat hepatocytes as it does on human gut epithelia, and that the transport of IgA from blood to bile in rats across the liver is analogous to that of IgA across human enterocytes.

Animals↗
PubMed1979

Endocytic vesicles in liver carry polymeric IgA from serum to bile.

The distributions both of endogenous IgA and of injected 125I-labelled IgA were determined amongst the components of a liver homogenate. Rate zonal sedimentation, under conditions where separation was principally determined by particle size, showed that IgA was tightly bound to material which sedimented in the size range of the larger endoplasmic reticulum fragments. Further fractionation of the components within this size range according to their densities, by isopycnic centrifugation, showed that the IgA was associated with small vesicles with a density range of 1.12--1.17 g/ml, quite distinct from endoplasmic reticulum fragments. We therefore conclude that the IgA is present in liver cells in a distinct class of vesicles, which are, presumably, responsible for the transport of IgA from blood to bile.

Animals↗
PubMed1979

Reflux of billiary components into blood in experimental intrahepatic cholestasis induced in rats by treatment with alpha-naphthylisothiocyanate.

The sera of rats treated with alpha-naphthylisothiocyanate, an agent reported to cause intrahepatic cholestasis, and of rats treated with carbon tetrachloride, are examined for evidence of leakage of bile into blood. The levels of the four bile components assayed, namely IgA, free IgA secretory component, the biliary isoenzyme of 5'-nucleotidase and of direct reacting (conjugated) bilirubin, were all elevated in the sera of rats treated with alpha-naphthylisothiocyanate. No change in any of these components was found in rats treated with carbon tetrachloride, indicating that their appearance in serum is not an inevitable consequence of damage to hepatocytes. As the bile components assayed reach bile by three different routes. their rapid appearance in the sera of rats treated with alpha-naphthylisothiocyanate indicates reflux of bile into blood, presumably as a result of mechanical obstruction of intraheptic bile ducts.

1-Naphthylisothiocyanate↗
PubMed1979

Apparent heterogeneity of hepatic lysosomes due to membrane-bound acid phosphatase.

Hepatic lysosomes have been fractionated by rate sedimentation and by isopycnic banding. In all experiments, the distribution of acid phosphatase differed from that of the other lysosomal enzymes. Evidence is presented that this difference is due not to the separation of lysosomes from different cell types, but simply reflects the membrane location of a part of the acid phosphatase.

Acid Phosphatase↗
PubMed1978

Sources of the proteins of rat bile.

The protein composition of rat bile has been studied systematically using two-dimensional agarose-polyacrylamide gel electrophoresis, with or without prior absorption by immobilised antisera, and by crossed immunoelectrophoresis. Sixteen bile proteins were distinguished. Of these, thirteen are immunologically identical to proteins present in rat serum and only one is identical to a protein present in rat liver plasma membrane but not in rat serum. Of the remaining two proteins, one is bile lipoprotein and the other has many of the properties of immunoglobulin A secretory component. The serum-related proteins in rat bile fall into two distinct groups. In the first group are immunoglobulin A and an alpha2-globulin. These proteins are major constituents of bile but only minor constituents of serum. In the second group are albumin and some other major serum proteins which are found in bile at concentrations less than 1% of their concentrations in serum. The relative proportions of these proteins in bile appear to differ from their proportions in serum. It therefore appears that, although the majority of bile proteins are derived from serum, there cannot be direct leakage of serum into bile. Examination of the proteins contained within liver lysosomes indicates that, although discharge of lysosomal contents at the bile canalicular face of the hepatocyte may contribute to the bile proteins, an additional mechanism, with a considerable degree of selectivity, must also be involved in the transport of proteins from serum to bile.

Animals↗
PubMed1978

Changes in rat serum lipoproteins following ligation of the bile duct.

Lipoproteins in the serum of normal and of cholestatic rats have been studied by crossed immunoelectrophoresis coupled with separations by rate and isopycnic density gradient centrifugation and by gel exclusion chromatography. Normal rat serum contained distinct lipoprotein species closely analogous to human VLDL, LDL, HDL2 and HDL3. Three days after ligation of the common bile duct, there were major changes in the lipoproteins of rat serum. The amounts of VLDL, LDL and of a minor HDL component were elevated and several novel types of lipoprotein were detected. Three of these could be identified as the characteristic lipoprotein of cholestasis, LP-X, as an enlarged and modified HDL and as a lipoprotein of density 1.055 g/ml intermediate in size between LDL and VLDL. Some unusually small VLDL particles were also detected. It is concluded that the changes in rat serum lipoproteins following ligation of the common bile duct are very similar to the changes observed in cholestatic disease in human patients.

Animals↗
PubMed1977

Bile 5'-nucleotidase in the serum of jaundiced rats.

Rat serum 5'-nucleotidase, L-leucyl-beta-naphthylamidase and beta-glycerophosphatase activities are increased whilst alkaline p-nitrophenylphosphatase and alkaline phosphodiesterase activities are unchanged or decreased three days after bile duct ligation. Affinity chromatography on an immobilised antiserum raised against highly purified liver plasma membranes showed that although 5'-nucleotidase in normal serum is unrelated to the 5'-nucleotidase of liver plasma membrane, the 5'-nucleotidase of bile and much of the 5'-nucleotidase in the jaundiced serum are closely related to the plasma membrane enzyme. Since bile is rich in 5'-nucleotidase, the changes in level of this enzyme after bile duct ligation are most simply explained by leakage of bile into the blood; changes in the patterns of the other enzymes are shown to be consistent with this explanation. The jaundiced serum was examined by gel exclusion chromatography and flotation in sucrose gradients for the presence of small fragments of plasma membrane as reported in human jaundiced sera, but no such fragments could be detected three days after bile-duct ligation.

Animals↗
PubMed1977

Bile proteins in the serum of jaundiced rats.

The major bile proteins can be detected by two-dimensional electrophoresis in the serum of cholestatic rats, three days after ligation of the common bile duct. The novel electrophoresis system used agarose gel electrophoresis in the first dimension followed by equilibrium electrophoresis in a polyacrylamide gel gradient.

Animals↗
PubMed1976

Differences between newly formed and recycled free small ribosome subunits in liver cytoplasm.

Heterogeneity among the free small ribosomal subunits of rat liver was studied. Newly made free small subunits differ from the bulk of the free subunits in the following ways. (1) The newly made free small subunits sediment slightly faster than most free small subunits and form a band at slightly lower densities. (2) Mature free small subunits, prepared under conditions which minimize the amount of loosely bound protein, readily dimerize in solutions of low ionic strength. Little dimerization is found with newly formed subunits. This permits the separation of fractions enriched in newly formed subunits. (3) The fraction enriched in newly formed subunits contains a distinctive additional protein as compared the most of the free small subunits.

Animals↗
PubMed1975

Determination of the amount of small messenger ribonucleic acid-containing particles free in liver cytoplasm.

To assess the contribution made by mRNA-containing particles to the heterogeneity previously observed among rat liver 40S ribonucleoprotein particles, the amount of poly(A)-containing RNA in subribosomal particles was determined. RNA was labelled with orotate in vivo for 24h and then for 50min. Poly(A)-containing RNA was trapped on filters impregnated with poly(U). Very little poly(A)-containing RNA was found in conventionally prepared ribonucleoprotein particles after fractionation in sucrose. However, after preparation of ribonucleoprotein particles by sedimentation through 1 M-sucrose in the presence of 0.15M-KCl or by precipitation with Mg2+ as described by Leitin & Lerman [(1969) Biokhimiya 34, 839-849], amounts of poly(A)-containing RNA were similar to amounts of mRNA found by other workers in total ribonucleoprotein particles. Even in such preparations, less than 5% of the total rapidly labelled RNA in native subribosomal-particle fractions was mRNA. It seems that mRNA-containing particles make up only a very small part of the population of subribosomal particles in liver.

Animals↗