Papers - YOKOTA Shinichi

Transcriptional activation of mouse cytosolic chaperonin CCT subunit genes by heat shock factors HSF1 and HSF2

H Kubota, S Matsumoto, S Yokota, H Yanagi, T Yura

FEBS LETTERS   461 ( 1-2 ) 125 - 129  1999.11  [Refereed]

DOI PubMed CiNii

Structures and co-regulated expression of the genes encoding mouse cytosolic chaperonin CCT subunits

H Kubota, S Yokota, H Yanagi, T Yura

EUROPEAN JOURNAL OF BIOCHEMISTRY   262 ( 2 ) 492 - 500  1999.06  [Refereed]

DOI PubMed CiNii

Effect of Helicobacter pylori lipopolysaccharides on human polymorphonuclear neutrophils and endotherial cells

Isogai E, Isogai H, Amano K, Yokota S, Hayashi S, Hirose K, Oguma K, Hirai Y, Asaka M, Sugiyama T

Bioscience and Microflora ( JAPAN BIFIDUS FOUNDATION )  18 ( 2 ) 119 - 124  1999  [Refereed]

　View Summary

We have examined the responses of polymorphonuclear neutrophils (PMNs) and human umbilical vein endothelial cells (HUVEC) to Helicobacter pylori lipopolysaccharides (LPSs). High-antigenicity-polysaccharide-carrying smooth LPS and rough LPS from H. pylori were used for the experiments. PMN activation was determined by chemiluminescence response (CLR). The priming effect of patient's serum or IL-8 on the CLR was also examined. After stimulation of HUVEC with the LPSs, the supernatant was tested for IL-6, IL-8 and RANTES by ELISA. Direct induction of CLR was observed after the stimulation of H. pylori LPSs. Though the response was weak, enhancement occurred in response to high-antigenicity-polysaccharide-carrying smooth LPS by patient's serum against the LPS. IL-8 priming was also effective to enhance CLR, which was induced by H. pylori LPS. Following exposure to H. pylori LPSs, HUVEC secreted IL-6 and IL-8 but not RANTES. The enhanced secretion of both IL-6 and IL-8 occurred in a time-dependent manner. However, the cytokine-inducing ability of H. pylori LPSs is significantly lower than that of other Gram-negative bacteria such as Escherichia coli and Campylobacter jejuni. Structurally similar LPS from Porphyromonas gingivalis also showed weak potency. These results suggest that the ability of H. pylori LPSs is not directly effected to induce inflammation. However, an indirect effect of these LPSs, or continuous stimulation with these LPSs to endothelial cells, may relate to persistent infection.

DOI CiNii

Human antibody response to Helicobacter pylori lipopolysaccharide: Presence of an immunodominant epitope in the polysaccharide chain of lipopolysaccharide

SI Yokota, KI Amano, S Hayashi, T Kubota, N Fujii, T Yokochi

INFECTION AND IMMUNITY   66 ( 6 ) 3006 - 3011  1998.06  [Refereed]

Utilization of proteinase K-Treated cells as lipopolysaccharide antigens for the serodiagnosis of Helicobacter pylori infections

K Amano, S Yokota, T Ishioka, S Hayashi, T Kubota, N Fujii

MICROBIOLOGY AND IMMUNOLOGY   42 ( 7 ) 509 - 514  1998  [Refereed]

Low antigenicity of the polysaccharide region of Helicobacter pylori lipopolysaccharides derived from tumors of patients with gastric cancer

SI Yokota, KI Amano, S Hayashi, N Fujii

INFECTION AND IMMUNITY   65 ( 9 ) 3509 - 3512  1997.09  [Refereed]

Reactivities of Lewis antigen monoclonal antibodies with the lipopolysaccharides of Helicobacter pylori strains isolated from patients with gastroduodenal diseases in Japan

K Amano, S Hayashi, T Kubota, N Fujii, S Yokota

CLINICAL AND DIAGNOSTIC LABORATORY IMMUNOLOGY   4 ( 5 ) 540 - 544  1997.09  [Refereed]

Reduction of rat myocardial ischemia and reperfusion injury by sialyl Lewis x oligosaccharide and anti-rat P-selectin antibodies

SJ Tojo, S Yokota, H Koike, J Schultz, Y Hamazume, E Misugi, K Yamada, M Hayashi, JC Paulson, S Morooka

GLYCOBIOLOGY   6 ( 4 ) 463 - 469  1996.06  [Refereed]

DOI PubMed CiNii

A polyreactive human anti-lipid A monoclonal antibody having cross reactivity to polysaccharide portions of Pseudomonas aeruginosa lipopolysaccharides

S Yokota, H Ohtsuka, T Kohzuki, H Noguchi

FEMS IMMUNOLOGY AND MEDICAL MICROBIOLOGY   14 ( 1 ) 31 - 38  1996.05  [Refereed]  [International journal]

DOI PubMed

Intracellular interaction of collagen-specific stress protein HSP47 with newly synthesized procollagen

Mamoru Satoh, Kazunori Hirayoshi, Shin-Ichi Yokota, Nobuko Hosokawa, Kazuhiro Nagata

Journal of Cell Biology   133 ( 2 ) 469 - 483  1996.04  [Refereed]

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Heat shock protein 47 (HSP47), a collagen-specific stress protein, has been postulated to be a collagen-specific molecular chaperone localized in the ER. We previously demonstrated that HSP47 transiently associated with newly synthesized procollagen in the ER (Nakai, A., M. Satoh, K. Hirayoshi, and K. Nagata. 1992. J. Cell Biol. 117:903-914). In the present work, we examined the location where HSP47 binds to and dissociates from newly synthesized procollagen within the cells, and whether HSP47 associates with nascent single procollagen polypeptide chains and/or with mature triple- helix procollagen. This was accomplished by biochemical coprecipitation with anti-HSP47 and anticollagen antibodies, combined with pulse-label and chase experiments in the presence or absence of various inhibitors for protein secretion, as well as by confocal laser microscopic observation of the cells double stained with both antibodies. We further examined whether the RDEL (Arg-Asp-Glu-Leu) sequence at the COOH terminus of HSP47 can act as an ER- retention signal, as the KDEL sequence does. When the secretion of procollagen was inhibited by the presence of α, α'-dipyridyl, an iron chelator that inhibits procollagen triple-helix formation, or by the presence of brefeldin A, which inhibits protein transport between the ER and the Golgi apparatus, procollagen was found to be bound to HSP47 during the chase period in the intermediate compartment. In contrast, the dissociation of procollagen chains from HSP47 was not inhibited when procollagen secretion was inhibited by monensin or bafilomycin A1, both of which are known to be inhibitors of post-cis-Golgi transport. These findings suggest that HSP47 and procollagen dissociated between the post-ER and the cis-Golgi compartments. HSP47 was shown to bind to nascent, single-polypeptide chains of newly synthesized procollagen, as well as to the mature triple-helix form of procollagen. HSP47 with the RDEL sequence deleted was secreted out of the cells, which suggests that the RDEL sequence actually acts as an ER-retention signal, as the KDEL sequence does. This secreted HSP47 did not acquire endogycosidase H resistance. The biological significance of the interaction between HSP47 and procollagen in the central secretory pathway, as well as possible mechanisms for this pathway, will be discussed.

DOI PubMed

Novel O-polysaccharide expression, as a lipid A core-free form, in a lipopolysaccharide-core-defective mutant of Pseudomonas aeruginosa

S Yokota

MICROBIOLOGY-UK   142 ( 2 ) 289 - 297  1996.02  [Refereed]  [International journal]

DOI PubMed

Cross-linking of the ninth consensus repeat domain of P-selectin (GMP-140, CD62P) with a monoclonal antibody enhanced leukocyte adhesive activity

S Yokota, MF Nunn, S Morooka

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS   218 ( 3 ) 709 - 713  1996.01  [Refereed]

DOI PubMed CiNii

IDENTIFICATION OF OUTER-MEMBRANE PROTEINS AS TARGET ANTIGENS OF PSEUDOMONAS-AERUGINOSA HOMMA SEROTYPE-M

S YOKOTA

CLINICAL AND DIAGNOSTIC LABORATORY IMMUNOLOGY   2 ( 6 ) 747 - 752  1995.11  [Refereed]  [International journal]

PubMed

ROLE OF LPS LENGTH IN CLEARANCE RATE OF BACTERIA FROM THE BLOOD-STREAM IN MICE

A OHNO, Y ISII, K TATEDA, T MATUMOTO, S MIYAZAKI, S YOKOTA, K YAMAGUCHI

MICROBIOLOGY-UK   141 ( 10 ) 2749 - 2756  1995.10  [Refereed]  [International journal]

PubMed

CYTOTOXIN-CONVERTING PHAGES, PHI-CTX AND PS21, ARE R-PYOCIN-RELATED PHAGES

T HAYASHI, H MATSUMOTO, M OHNISHI, S YOKOTA, T SHINOMIYA, M KAGEYAMA, Y TERAWAKI

FEMS MICROBIOLOGY LETTERS   122 ( 3 ) 239 - 244  1994.10  [Refereed]  [International journal]

DOI PubMed CiNii

IDENTIFICATION OF THE LIPOPOLYSACCHARIDE CORE REGION AS THE RECEPTOR-SITE FOR A CYTOTOXIN-CONVERTING PHAGE, PHI-CTX, OF PSEUDOMONAS-AERUGINOSA

S YOKOTA, T HAYASHI, H MATSUMOTO

JOURNAL OF BACTERIOLOGY   176 ( 17 ) 5262 - 5269  1994.09  [Refereed]  [International journal]

PubMed

EPITOPES FOR HUMAN MONOCLONAL-ANTIBODIES AND SEROTYPING ANTISERA AGAINST THE O-SPECIFIC POLYSACCHARIDE OF PSEUDOMONAS-AERUGINOSA O-11

S YOKOTA, H NOGUCHI

CARBOHYDRATE RESEARCH   261 ( 1 ) 57 - 66  1994.08  [Refereed]  [International journal]

DOI PubMed CiNii

STUDIES OF THE STRUCTURE OF THE LIPOPOLY SACCHARIDE OF VIBRIO-ANGUILLARUM V-123 .2. STRUCTURE OF THE O-POLYSACCHARIDE CHAIN OF THE LIPOPOLYSACCHARIDE OF VIBRIO-ANGUILLARUM V-123

H EGUCHI, S KAYA, Y ARAKI, N KOJIMA, S YOKOTA

CARBOHYDRATE RESEARCH   231   159 - 169  1992.07  [Refereed]

MONOCLONAL-ANTIBODIES AGAINST PSEUDOMONAS-AERUGINOSA ELASTASE - A NEUTRALIZING ANTIBODY WHICH RECOGNIZES A CONFORMATIONAL EPITOPE RELATED TO AN ACTIVE-SITE OF ELASTASE

SI YOKOTA, H OHTSUKA, H NOGUCHI

EUROPEAN JOURNAL OF BIOCHEMISTRY   206 ( 2 ) 587 - 593  1992.06  [Refereed]  [International journal]

DOI PubMed CiNii

BINDING OF MONOCLONAL-ANTIBODY SPECIFIC FOR DOMAIN-IA/II OF PSEUDOMONAS-AERUGINOSA EXOTOXIN-A AT PH-4 STRONGLY NEUTRALIZES EXOTOXIN-A-INDUCED CYTOTOXICITY IN CELL-CULTURE AND INVIVO

H OHTSUKA, K HORIGOME, A HIGUCHI, N NOMURA, H OCHI, S YOKOTA, T KOHZUKI, H NOGUCHI

INFECTION AND IMMUNITY   60 ( 3 ) 1061 - 1068  1992.03  [Refereed]  [International journal]

PubMed