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Biomedical subjects

J Shoji

Publications and source records attributed to J Shoji.

At least 19 recordsLinked to original sources
PubMed1995

[Histological study of allergic conjunctivitis--1. Study on the adhesion molecules to allergic conjunctivitis].

We performed an immunohistochemical study on the relationship between inflammatory cells and adhesion molecules to investigate inflammatory reaction in allergic conjunctivitis. Guinea pigs were sensitized with an intraperitoneal injection of ovalbumin with hydroxyalminium. Ovalbumin was applied topically to the conjunctiva 3 weeks after the initial treatment. Then the cornea, conjunctiva and lacrymal gland were taken and processed for frozen sections. The specimens were stained with acid Giemsa for inflammatory cells and enzyme-labelled antibody for ICAM-1 and VCAM-1. Neutrophils were dominantly observed 6 hours after the challenge with the antigen, eosinophils at 12 hours, and eosinophils and lymphocytes at 24 hours, respectively. ICAM-1 and VCAM-1 were detected at 6 and 24 hours in the vascular tissue in the subconjunctival tissue and lacrymal gland. There results suggest that adhesion molecules play a role in the infiltration of inflammatory cells in allergic conjunctivitis.

Animals↗
PubMed1992

Six new triterpenoidal glycosides including two new sapogenols from Albizziae Cortex. V.

Six new triterpenoid glycosides called julibrosides A1-A4, B1 and C1 were isolated from Albizziae Cortex, the dried stem bark of Albizzia julibrissin Durazz. Their structures were determined based on spectral and chemical evidence. Julibrosides B1 and C1 had new sapogenols, designated julibrogenin B and C, respectively, while julibrosides A3 included N-acetyl-D-glucosamine as a sugar component.

Carbohydrate Sequence↗
PubMed1992

Isolation and characterization of new peptide antibiotics, plusbacins A1-A4 and B1-B4.

New antibiotics, plusbacins A1-A4 and B1-B4, were isolated from the culture broth of a strain of Pseudomonas sp. These antibiotics were isolated as a complex by column chromatographies on Diaion HP-20 and silica gel, and then separated by HPLC. They are amphoteric in nature. The hydrochlorides are obtained as colorless powders, soluble in methanol and alkaline water. From their physico-chemical properties, these antibiotics are presumed to be acyloctapeptides containing a lactone linkage, and their differences occur in amino acid and fatty acid residues. The antibiotics are active against Gram-positive bacteria in vitro and in vivo.

Amino Acids↗
PubMed1992

Structures of new peptide antibiotics, plusbacins A1-A4 and B1-B4.

The constituent amino acids of plusbacins A1-A4 were determined to be two moles of L-trans-3-hydroxyproline and one mole each of D-threo-beta-hydroxyaspartic acid, L-threo-beta-hydroxyaspartic acid, D-allo-threonine, D-serine, D-alanine and L-arginine. In plusbacins B1-B4, one mole of L-trans-3-hydroxyproline is replaced by L-proline. The fatty acid residue of A1 and B1 was determined to be 3-hydroxy-tetradecanoic acid, for A2 and B2 to be 3-hydroxy-isopentadecanoic acid, for A3 and B3 to be 3-hydroxy-isohexadecanoic acid, and for A4 and B4 to be 3-hydroxy-hexadecanoic acid. A lactone linkage was suggested to reside between L-threo-beta-hydroxyaspartic acid and 3-hydroxy-fatty acid residues by degradation experiments. The amino acid sequences of plusbacins A2 and B2 were confirmed by Edman degradation of their deacylated products, and supported by mass spectrometric studies. From the above, structures of all components of plusbacins were concluded.

Amino Acid Sequence↗
PubMed1992

[The local immune system of ocular surface].

Local immunity on the ocular surface was observed in guinea pigs immunized with horseradish peroxidase (HRP) by determining the activity of a specific antibody in local sites of the conjunctiva by the enzyme-antigen method, which enables a specific antibody to be stained. In addition, immunohistochemical study of the localization of IgA was performed by the enzyme-labelled antibody method. The enzyme-antigen method revealed a number of positive cells in the subconjunctival tissue and the parafollicular area of conjunctival-associated lymphoid tissue. These cells were identified as plasma cells by electron microscopy. The mirror section technique revealed that the cells positive for the enzyme-antigen method were consistent with anti-IgA-positive cells at many sites. Thus the distribution of plasma cells secreting IgA-specific antibody responsible for local immunity on the ocular surface was observed immunohistochemically. The results suggest that immunocytes in the conjunctival-associated lymphoid tissue differentiate and mature into specific antibody-producing plasma cells.

Animals↗
PubMed1992

[Immunoresponses to the external antigen in conjunctival-associated lymphoid tissue].

The local immunity of the ocular surface is governed by conjunctival-associated lymphoid tissue (CALT), secretory IgA and immunocytes. The authors performed a histological investigation of the time-course changes in CALT caused by invasion of antigen to the ocular surface through the instillation of horseradish peroxidase (HRP) into the guinea pig eye. We used PAS staining, peroxidase staining, alkaline phosphatase staining. The lymphoepithelial cells of CALT phagocytized HRP 30-60 min after the instillation, and formed intraepithelial pockets 24 hours after instillation. The follicular area of CALT was strongly positive for alkaline phosphatase 2 weeks after instillation. These changes were considered to be the first step in the manifestation of local immunity on the ocular surface. Each staining technique revealed differences between the lymphoepithelium and conjunctival epithelium, suggesting that lymphoepithelium has characteristics different from those of conjunctival epithelium.

Animals↗
PubMed1990

Revised structure of the peptide lactone antibiotic, TL-119 and/or A-3302-B.

The peptide lactone antibiotic TL-119 and/or A-3302-B was chemically synthesized in order to confirm the proposed structure. The synthetic compound was different from both natural TL-119 and A-3302-B in their physicochemical properties and in biological activity. Re-examination of the configuration of the constituent amino acid residues in natural TL-119 and/or A-3302-B indicated that natural TL-119 and A-3302-B contains D-aThr instead of the original L-Thr. We tentatively propose a revised structure for TL-119 and/or A-3302-B.

Amino Acid Sequence↗
PubMed1990

Structures of agglomerins.

Structures of a series of new antibiotics, agglomerins A, B, C and D, which are active against a variety of anaerobic bacteria, were determined to be 1-acyl-2,3-dihydroxy-1,3-butadiene-1-carboxylic acid, (1----3)-gamma-lactones, i.e., 2-acyl-4-ylidenetetronic acids with different hydrocarbon chains in the acyl group. Their common chromophore exhibited tautomerism in solution. The relationship of their structure to the activity against anaerobes is discussed.

4-Butyrolactone↗
PubMed1990

Isolation, characterization and structures of PA-46101 A and B.

New antibiotics, PA-46101 A and B, were isolated from the culture broth of a Streptomycete. The molecular formulae of A and B were determined to be C52H70O18 and C61H86O22, respectively, by elemental analyses, NMR and mass spectrometry. Their structures were elucidated by X-ray crystallography and NMR spectroscopy. These antibiotics are active in vitro against anaerobic Gram-positive and Gram-negative bacteria and also against a limited number of aerobic Gram-positive bacteria.

Aminoglycosides↗
PubMed1990

Isolation of cepafungins I, II and III from Pseudomonas species.

New acylpeptide antibiotics named cepafungins I, II and III were isolated from the culture broth of a strain identified as Pseudomonas sp. These antibiotics are neutral substances, soluble in aqueous alcohols and dimethyl sulfoxide, and show UV maxima at 260.5 nm. The IR spectra indicated these to be peptides. Molecular formulas C28H46N4O6, C27H44N4O6 and C26H42N4O6 for cepafungins I, II and III were indicated by elemental analysis and SI-MS. Cepafungins exhibited inhibitory activity against yeast and fungi, and antitumor activity against P388 leukemia in mice.

Animals↗
PubMed1990

Structures of cepafungins I, II and III.

Structures of interesting acylpeptide antibiotics cepafungins I, II and III were elucidated by NMR spectroscopic studies and some degradation experiments. The antibiotics contain a common peptide part that consists of threonine and two unusual amino acid residues, gamma-hydroxylysine and 4-amino-2-pentenoic acid. The unusual amino acid residues compose an interesting 12-membered ring with an exocyclic N-terminus to which the threonine is connected. Different fatty acyl groups connected to the N-terminus of the threonine distinguish the three cepafungins. The major component I and minor component III are new substance, but the minor component II has a structure identical with that of the recently reported antibiotic glidobactin A.

Amino Acids↗
PubMed1989

Isolation and characterization of hypeptin from Pseudomonas sp.

An antibiotic, named hypeptin, was isolated from the culture broth of a strain of Pseudomonas sp. The antibiotic was extracted with butanol and purified by chromatography on a Sephadex LH-20 column. The antibiotic is basic in nature. The dihydrochloride is soluble in aqueous alcohols and positive to ninhydrin and Sakaguchi's reaction. A molecular formula, C44H71N13O15.2HCl was indicated by microanalysis and secondary ion MS. The IR spectrum and acid hydrolysis indicated it to be a peptide antibiotic. The stereochemistries of the amino acids produced by hydrolysis were clarified by HPLC using a chiral column. The antibiotic is active in vitro against a wide variety of anaerobic bacteria and aerobic Gram-positive bacteria.

Anti-Bacterial Agents↗
PubMed1989

Isolation and characterization of thioxamycin.

A new peptide antibiotic named thioxamycin which contained thiazole and oxazole rings was isolated from the culture broth of Streptomyces sp. The antibiotic is acidic and lipophilic in nature. A molecular formula, C52H48N16O15S4, was indicated by elemental analysis and MS. One mol of threonine and three unusual amino acids were detected by amino acid analysis of the acid hydrolysate. The antibiotic is active in vitro against anaerobic Gram-positive and Gram-negative bacteria and also aerobic Gram-positive bacteria.

Animals↗
PubMed1989

Isolation and characterization of agglomerins A, B, C and D.

New antibiotics, agglomerins A, B, C and D, were isolated from the culture broth of a bacterial strain identified as Enterobacter agglomerans. These antibiotics are acidic in nature and their sodium salts are obtained as colorless crystalline powders, soluble in lower alcohols. All the antibiotics shows characteristic UV maxima at 248 and 298 nm. Molecular formulas: A, C15H21O4Na; B, C17H23O4Na; C, C17H25O4Na and D, C19H27O4Na; were indicated by elemental analysis and MS. These antibiotics are active against a wide variety of anaerobic bacteria and weakly against aerobic Gram-positive bacteria in vitro.

4-Butyrolactone↗
PubMed1989

New antibiotics, resorcinomycins A and B: antibacterial activity of resorcinomycin A against mycobacteria in vitro.

Resorcinomycin A, N-[(S)-alpha-guanidino-3,5-dihydroxy-4-isopropylphenylacetyl]glyci ne, S-RSM-A, a new antibiotic produced by Streptoverticillium roseoverticillatum, has an antibacterial spectrum directed towards mycobacterial species. It is not active against Gram-negative and Gram-positive bacteria, except mycobacteria and weakly active against mycoplasmas. In vitro activities of the S-, R- and S,R-isomers of RSM-A against atypical mycobacterial strains were compared with those of streptomycin (SM) and kanamycin (KM) by 2-fold agar dilution methods using Middlebrook 7H10 agar medium. Although R-RSM-A and S,R-RSM-A were comparable or inferior to both antibiotics, the antimycobacterial activity of S-RSM-A was superior to that of SM and KM.

Anti-Bacterial Agents↗
PubMed1989

Isolation of CB-25-I, an antifungal antibiotic, from Serratia plymuthica.

A new antifungal antibiotic, CB-25-I, was isolated from the culture broth of a strain of Serratia plymuthica. The antibiotic, a water-soluble dipeptide, is structurally related to Sch 37137 and A 19009, both produced by strains of Actinomycetales. The antibiotic exhibits inhibitory activity against Candida albicans in YNB medium (a synthetic medium), but the activity is significantly reduced in Sabouroud dextrose medium.

Amino Acids↗
PubMed1988

Isolation of a new phenazine antibiotic, DOB-41, from Pseudomonas species.

A new phenazine antibiotic, DOB-41, was isolated from the culture broth of a Pseudomonas strain. The antibiotic obtained as yellow crystals showed UV maxima at 255 nm and 370 nm. A molecular formula, C19H18N2O6, was indicated by elemental analysis and mass spectrometry. The structure was elucidated by X-ray diffraction analysis. The antibiotic exhibited inhibitory activity against Gram-positive bacteria, and antitumor effect against leukemia P388 in mice.

Animals↗