Search PubMed⌕ Search

Biomedical subjects

M Torii

Publications and source records attributed to M Torii.

At least 145 records · Page 8Linked to original sources
PubMed1983

Liver cell membrane antibody detected by protein A and isolated rabbit liver plasma membrane in sera of patients with chronic liver diseases.

Using the plasma membrane fraction isolated from rabbit liver (RLPM), we detected non-species specific IgG antibody against liver cell surface membrane in the sera from the patients with chronic liver diseases. The sea were treated with dithiothreitol and iodoacetamide, and absorbed with sufficient amount of actin isolated from rabbit striated muscles. The antibody was detected by incubation of RLPM with the treated and absorbed sera and subsequent determination of IgG bound to RLPM by 125I-staphylococcal protein A. It was found mainly in the patients with autoimmune hepatitis (12 of 28) and liver cirrhosis (eight of 24). It occurred more frequently in HBsAg negative liver cirrhosis than in HBsAg positive forms (six of 13 vs two of 11). The frequency of the antibody was low in chronic hepatitis except autoimmune hepatitis, and primary biliary cirrhosis. Thus the antibody against RLPM was an immunological marker of autoimmune hepatitis and HBsAg negative liver cirrhosis. The occurrence did not correlate with those of anti-smooth muscle antibody, anti-nuclear antibody and anti-mitochondrial antibody. In two cases of autoimmune hepatitis, the antibody against RLPM decreased with clinical improvement induced by corticosteroids.

Adrenal Cortex Hormones↗
PubMed1982

Enhancement of murine immune responses to orally administered haptenated Streptococcus mutans.

The induction of immune responses to orally administered trinitrophenyl (TNP)-haptenated Streptococcus mutans and its enhancement with muramyldipeptide (MDP), peptidoglycan (PG), and concanavalin A (Con A) were investigated in lipopolysaccharide (LPS)-non-responsive C3H/HeJ mice and the syngeneic, LPS-responsive C3H/HeN strain. Both mouse strains manifested similar immune responses, primarily of the IgM isotype, after a single gastric intubation (GI) with TNP-S. mutans. However, when groups of animals were first carrier-primed by GI with S. mutans for 2 consecutive days, followed by a single GI with TNP-S. mutans 1 week later, C3H/HeJ mice gave a significantly higher (P less than or equal to 0.01) splenic IgA anti-TNP plaque-forming cell (PFC) response than identically treated C3H/HeN mice. Furthermore, saliva, urine and serum from these C3H/HeJ mice possessed high levels of IgA anti-TNP antibodies as determined by the enzyme-linked immunosorbent assay, whereas C3H/HeN mice exhibited low antibody levels. Oral administration of Con A (either 250 micrograms or 500 micrograms/mouse) or purified PG (1 mg/mouse) at the time of TNP-S. mutans immunization resulted in significantly (P less than or equal to 0.01) enhanced splenic IgA anti-TNP PFC responses, especially in C3H/HeJ mice. On the other hand, MDP promoted IgA anti-TNP PFC responses in LPS-responsive C3H/HeN mice but did not augment responses in C3H/HeJ animals. A similar immune response pattern was seen when antibody levels were measured in serum, saliva, and urine of both mouse strains. These results demonstrate that haptenated S. mutans is a good antigen for the induction of high IgA responses in orally immunized C3H/HeJ mice and that this high response can be enhanced with the adjuvants Con A and PG. However, MDP is ineffective in C3H/HeJ mice but enhances IgA responses in normal LPS-responsive C3H/HeN animals.

Acetylmuramyl-Alanyl-Isoglutamine↗
PubMed1981

Immunochemical studies on dextrans. Cross-reaction of synthetic linear dextrans with rabbit anti-N4 dextran.

Alpha (1 Leads to 6) specific anti-dextran antibody was raised in rabbits by injecting N4 dextran-concanavalin A conjugate, and the interactions of five synthetic linear dextrans (alpha(1 Leads to 6)-D-glucopyranans) with rabbit anti-N4 dextran were studied. The ability of glucans to precipitate antibody depended on their average molecular weight, samples with higher molecular weight precipitating more antibody nitrogen under the same conditions. This phenomenon was shown to be due to solubility of the antigen-antibody complex. Oligosaccharide inhibition assay indicated that the maximum size of the alpha(1 Leads to 6)-specific antibody combining site corresponded to isomaltopentaose. The precipitated antibody class was shown to be IgG immunoglobulin, and it was mostly directed to linear non-terminal glucosidic linkages. Determination of antibody nitrogen and glucan in the precipitates indicated that the ratio of antibody molecule to numbers of glucose residues was 1:16 in the extreme antibody excess region.

Animals↗
PubMed1981

Adherence of Streptococcus sanguis clinical isolates to smooth surfaces and interactions of the isolates with Streptococcus mutans glucosyltransferase.

Streptococcus sanguis isolated from human dental plaque were grown in Todd-Hewitt broth. Cells were collected by centrifugation and lyophilized after extensive washing with water. The cell-associated glucosyltransferase (GTase) activities of S. sanguis strains were assayed with [14C]sucrose. Strain differences in GTase activity were significant within the same serotype or biotype or both. The ability of S. sanguis cells to adhere to smooth glass surfaces was generally weak, irrespective of significant cell-associated GTase activity synthesizing water-insoluble, gel-like glucans. Resting cells of most S. sanguis strains bound extracellular GTase from Streptococcus mutans strain B13 (serotype d), resulting in the strong adherence of the S. sanguis cells to smooth glass surfaces in the presence of sucrose. Conversely, S. mutans B13 cells also could bind extracellular GTase from some strains of S. sanguis examined. The sucrose-dependent adherence of S. mutans cells was not altered, although S. sanguis strains from which the extracellular GTases were obtained did not produce significant adherence in the presence of sucrose. In view of these findings, it was suggested that S. mutans GTase could affect the adherence of S. sanguis to smooth tooth surfaces in the oral cavity.

Binding Sites↗
PubMed1981

Lymphoid cell responses to bacterial cell wall components: mitogenic responses of murine B cells to Streptococcus mutans carbohydrate antigens.

The mitogenic activity of various purified serotype carbohydrate and cell wall lysate fractions of Streptococcus mutans for murine lymphocytes has been determined. The highest mitogenic responses occurred after 48 hr of stimulation with these carbohydrate preparations when tested on splenic cultures derived from C3H/HeJ and BALB/c mice. The response pattern obtained with optimum concentrations of these preparations was very similar to that seen with the B cell mitogen, LPS. A purified serotype g carbohydrate (M1 g) prepared by mutanolysin enzyme treatment of S. mutans 6715 cell walls stimulated good mitogenic responses in BALB/c nude and nu/+ splenic cultures, suggesting an effect on mouse B cells. This was further substantiated by studies showing that this antigen also induced responses in cultures of B cells purified by nylon wool fractionation, whereas purified T cells did not respond. Mitogenic responses were due to the carbohydrate moiety and not to possible LPS contamination, since alkaline treatment or mixture with polymyxin B greatly reduced responses to LPS; however, no alteration of mitogenic responses to M1 g occurred. Further, LPS nonresponsive C3H/HeJ spleen cells yielded good mitogenic responses to M1 g. On the other hand, periodate treatment, which is known to decompose carbohydrate moieties completely abrogated the mitogenic activity of M1 g antigen. Additional studies with serotypes c and e carbohydrate, which also induced mitogenic responses, suggested that this activity for lymphoid cells may be a common property of S. mutans cell wall carbohydrate.

Animals↗
PubMed1981

Presence and location of an O-acetyl group in O4-antigen of Vibrio parahaemolyticus.

A polysaccharide moiety (PS) released from O4-LPS of Vibrio parahaemolyticus was purified. The constituent sugars of the purified PS were glucose, galactose, arabinose, fucose, heptose, N-acetyl galactosamine and an unknown N-acetyl amino sugar. The unknown amino sugar was deduced to be a terminal deoxy amino sugar from its NMR spectrum. PNMR spectroscopy at 200 MHz, periodate oxidation and treatment with alpha-L-fucosidase of the purified PS sample before and after alcoholic sodium methoxide-treatment suggested that PS contained an O-acetyl and alpha-linked non-reducing terminal L-fucose and that the O-acetyl group was located at the C-2 or C-4 position of the non-reducing terminal fucose. The contribution of the O-acetyl group located in L-fucose to the O4-antigenic determinant seemed to be small, judging from immunochemical experiments.

Acetylation↗
PubMed1980

Electron microscopic studies on hepatic alkaline phosphatase in experimentally induced biliary obstruction of the rat.

The alterations of the alkaline phosphatase (ALP) activity in the rat liver following bile duct ligation were investigated by electron microscopical techniques. Serum ALP activity reached the maximum at 24 hours after ligation and two isozymes of ALP, high molecular and low molecular one, appeared in the serum. Bile canaliculi became dilated at 48 hours after ligation and the microvilli were destructed and diminished in number. ALP activity was observed almost only on the bile canalicular membrane of the liver cells in the control. On the other hand, in the bile duct-ligated rat, the ALP activity on the canalicular membrane was markedly increased initially, then it appeared on the lateral membrane, and finally on the sinusoidal membrane also. It was not stainable on the canalicular membranes which lacked microvilli. The proposed pathway through which hepatic ALP enters the blood stream in bile duct-ligated rats is as follows: ALP, being synthesized in the microsomes of hepatocytes, is initially transferred to the bile canalicular membrane and diffused to lateral membrane through tight junction, reaches to sinusoidal membrane then released into the blood stream.

Alkaline Phosphatase↗
PubMed1980

Immunochemical studies on dextrans. Two distinct alpha 1 linked to 3 specificities of rabbit anti-dextran B1355.

Rabbit anti-dextran B1355 sera prepared by injecting rabbits with Leuconostoc mesenteroides NRRL B1355 were separated on a Sephadex G75 column into two fractions, one binding and the other not binding to the column. Oligosaccharide inhibition of precipitation of the two fractions with dextran B1355 indicated that both fractions had alpha 1 linked to 3 specificity. However, antibodies in the non-binding fraction were shown to be directed against O-alpha-D-glucopyranosyl-(1 linked to 3)-O-alpha-D-glucopyranosyl-(1 linked to 6)-D-glucose, while those in the binding fraction were directed against O-alpha-D-glucopyranosyl-(1 linked to 6)-O-alpha-D-glucopyranosyl-(1 linked to 3)-D-glucose. These results are consistent with the proposal of Bhoopalam et al. (Proc. Soc. Exp. Biol. Med. (1979(=) 161, 430-434) that there are different epitopic groups on this dextran.

Animals↗