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A Amano

Publications and source records attributed to A Amano.

At least 91 records · Page 5Linked to original sources
PubMed1994

Salivary receptors for recombinant fimbrillin of Porphyromonas gingivalis.

Fimbriae are considered important in the adherence and colonization of Porphyromonas gingivalis in the oral cavity. It has been demonstrated that purified fimbriae bind to whole human saliva adsorbed to hydroxyapatite (HAP) beads, and the binding appears to be mediated by specific protein-protein interactions. Recently, we expressed the recombinant fimbrillin protein (r-Fim) of P. gingivalis corresponding to amino acid residues 10 to 337 of the native fimbrillin (A. Sharma, H.T. Sojar, J.-Y. Lee, and R.J. Genco, Infect. Immun. 61:3570-3573, 1993). We examined the ability of individual salivary components to promote the direct attachment of r-Fim to HAP beads. Purified r-Fim was radiolabeled with 125I and incubated with HAP beads which were coated with saliva or purified individual salivary components. Whole, parotid, and submandibular-sublingual salivas increased the binding of 125I-r-Fim to HAP beads. Submandibular-sublingual saliva was most effective in increasing the binding of 125I-r-Fim to HAP beads (1.8 times greater than that to uncoated HAP beads). The binding of 125I-r-Fim to HAP beads coated with acidic proline-rich protein 1 (PRP1) or statherin was four and two times greater, respectively, than that to uncoated HAP beads. PRP1 and statherin molecules were also found to bind 125I-r-Fim in an overlay assay. The binding of intact P. gingivalis cells to HAP beads coated with PRP1 or statherin was also enhanced, by 5.4 and 4.3 times, respectively, over that to uncoated HAP beads. The interactions of PRP1 and statherin with 125I-r-Fim were not inhibited by the addition of carbohydrates or amino acids. PRP1 and statherin in solution did not show inhibitory activity on 125I-r-Fim binding to HAP beads coated with PRP1 or statherin. These results suggest that P. gingivalis fimbriae bind strongly through protein-protein interactions to acidic proline-rich protein and statherin molecules which coat surfaces.

Adult↗
PubMed1994

Left main coronary artery patch plasty with internal mammary artery.

Isolated stenosis of the left main coronary artery was surgically enlarged by patch angioplasty using a distal flap of the left internal mammary artery. The remaining proximal mammary artery pedicle was anastomosed to the anterior descending coronary artery as an in situ graft for security. The patient's recovery was uneventful, and postoperative angiography at 2 weeks showed good patency of both the left main trunk and the internal mammary artery graft.

Aged↗
PubMed1994

Characterization of coaggregation and fibrinogen-binding by Porphyromonas gingivalis.

We have examined whether the adhesin of Porphyromonas gingivalis which aggregates Streptococcus oralis contributes to its fibrinogen-binding. Various properties of coaggregation between P. gingivalis and S. oralis were compared with those of fibrinogen-binding to P. gingivalis cells. The coaggregation activity was measured by a turbidimetric method and the fibrinogen-binding activity was determined by using 125I-fibrinogen. Both the activities showed maximum values in the pH range from 5.0 to 6.0 and they were inhibited by arginine and lysine. Heating treatment of P. gingivalis 381 cells at 75 degrees C abrogated the activities. However, treatment of P. gingivalis 381 cells with proteinase K considerably reduced the fibrinogen-binding activity but not the coaggregation activity. Metal ions such as Zn2+ and Cu2+ inhibited the coaggregation activity but enhanced the fibrinogen-binding activity. The results also indicated that P. gingivalis strains 381, ATCC 33277 and SU-3 showed relatively higher activities both in coaggregation and fibrinogen-binding, whereas P. gingivalis strains W83, 51 and 165 showing lower fibrinogen-binding activity than P. gingivalis 381 did not coaggregate with S. oralis ATCC 9811. These findings suggest that coadhesin of P. gingivalis with S. oralis is not be associated with its fibrinogen-binding.

Adhesins, Bacterial↗
PubMed1994

[A case report of coronary artery bypass graft surgery and subsequent chemotherapy for the patient with unstable angina and small cell lung cancer].

A 74 year old female with lung cancer had undergone coronary artery bypass graft surgery (CABGS) and survived for 9 months after subsequent chemotherapy. She had been suffering from severe chest pain since 2 years before that time, and deteriorated intractably. At the same time, lung cancer was suggested radiologically, and revealed as small cell lung cancer by bronchial biopsy. Coronary angiogram study was done to verify the coronary artery disease and severe triple artery disease was shown. CABGS was done to relieve her condition to start chemotherapy. Post-operative course was fine and CODE therapy [cisplatin, oncovin (vincristine), doxorubicin (adriamycin), etoposide] was done subsequently to CABGS. Cancer focus and swollen lymph node were vanished in radiographic examination. She had discharged and spent at home for a while. However, multiple metastatic lesions emerged later, and deceased finally 9 mouths after CABGS. We conclude, CABGS done for her was a reasonable therapy to relief her condition and was successful to carry out chemotherapy.

Aged↗
PubMed1993

Inhibition of coaggregation between Porphyromonas gingivalis and Streptococcus oralis by fibrinogen fragments.

The localization of regions of fibrinogen that inhibit coaggregation between Porphyromonas gingivalis and Streptococcus oralis was investigated. The coaggregation was inhibited by A alpha and gamma chains, but not by B beta chain. The inhibitory activity of fragment D was more potent than that of fragment E. Some cyanogen bromide-treated fragments isolated from A alpha and gamma chains including the NH2-terminal 148-207 amino acid residues of A alpha chain (A alpha 148-207) and gamma 1-78 showed inhibitory activities. A alpha 148-207 was further digested with lysyl endopeptidase. A alpha 158-176 and A alpha 192-206 which contained four and two arginine residues, respectively, retained the inhibitory activities. When the arginine residues of these two peptides were modified by phenylglyoxal, the inhibitory activities were much reduced. These findings suggest that the arginine residues of some specific regions of fibrinogen may play an important role in the inhibition of the coaggregation.

Amino Acid Sequence↗
PubMed1993

[Allergic granulomatosis and angiitis associated with intestinal perforation and eye movement disorder].

A perforation in the small intestine and one and a half syndrome were observed in 45-year-old male with allergic granulomatosis and angiitis (AGA). The patient was first admitted to our hospital in 1988 with complaints of bronchial asthma and an abnormal density on his chest X ray. The diagnosis of PIE syndrome was made based on marked peripheral blood eosinophilia. He was successfully treated with prednisolone and had been well on the maintenance therapy of small doses of it. In May 1990, peripheral neuropathy occurred in his bilateral lower legs and it was followed by nausea and vomiting. The laboratory findings on admission showed leukocytosis (19,300/mm3) with 43% eosinophilia and elevated blood level of IgE (3000 IU/ml). On the tenth day of admission, ileus symptom and subsequently a perforation of the small intestine were observed. The mesenterial specimens obtained during the emergency operation showed the findings compatible with AGA. Remission of AGA was induced by the treatment with 60 mg prednisolone and 100 mg cyclophosphamide per day following methylprednisolone pulse therapy. He was well on maintenance prednisolone until June 1991, when he suddenly developed one and a half syndrome. Although cranial CT scan and MRI showed no abnormal findings, cyclophosphamide therapy was resumed and prednisolone was increased because microangiopathy due to AGA was thought to be the cause of this central nervous system symptom. The one and a half syndrome improved with this therapy. This case suggests that the long term treatment with prednisolone and cyclophosphamide would be indicated in the severe AGA with close monitoring of the symptoms and peripheral blood eosinophilia.

Churg-Strauss Syndrome↗
PubMed1992

Identity of amino acid sequences of superoxide dismutase purified from both anaerobically maintained and aerated Porphyromonas gingivalis.

Superoxide dismutase (SOD) from anaerobically maintained Porphyromonas gingivalis (anaero-SOD) has the characteristic of Fe-SOD, whereas SOD from aerated cells (aero-SOD) has that of Mn-SOD. However, both types of apoSOD can bind either Fe or Mn. To elucidate the structure relationship between anaero- and aero-SOD, we examined the amino acid sequence of aero-SOD by direct protein analysis. The amino acid sequence of aero-SOD was shown to be identical with that of anaero-SOD determined previously. Our findings support the hypothesis that cambialistic SOD is formed from a single apoprotein in bacterial cells.

Aerobiosis↗
PubMed1992

Role of superoxide dismutase in resistance of Porphyromonas gingivalis to killing by polymorphonuclear leukocytes.

Porphyromonas gingivalis in which the synthesis of superoxide dismutase (SOD) was induced by nitrate or by aeration was rendered resistant to killing by polymorphonuclear leukocytes. SOD purified from either anaerobically maintained or aerated cells also inhibited bacterial killing when added exogenously, and no difference between the effects of the two SODs was observed. These results suggest that SOD may form part of a defense mechanism that helps protect P. gingivalis against killing by polymorphonuclear leukocytes.

Blood Bactericidal Activity↗
PubMed1992

Changes in oxygen consumption in dog gingiva during induction of experimental periodontitis.

The purpose of this study was to examine changes in oxygen consumption in dog gingiva during induction of experimental periodontitis. The disease was induced in adult mongrel dogs during a 16-week period by placement of silk ligatures around selected teeth. The oxygen consumption rate of gingival tissue was determined in vivo by a non-invasive technique, tissue reflectance spectrophotometry. Changes in such clinical parameters as gingival index, plaque index, pocket depth, attachment level, and gingival crevicular fluid flow indicated acute inflammatory responses during the first three weeks after ligation, followed by the appearance of chronic inflammation during the remaining 13 weeks. The oxygen consumption rate increased during the first seven days after ligation and stayed near the maximum level for 2-7 weeks; this was followed by a gradual decrease during the final nine weeks. These results suggest that gingival oxygen consumption increases rapidly with the increase of acute inflammation responses and then decreases slightly with the gradual development of chronic inflammation. Positive correlations were observed between the oxygen consumption rate and other clinical indices. Thus, the tissue reflectance spectrophotometry is a new, useful method for objective, quantitative, and non-invasive assessment of gingival oxygen consumption.

Animals↗
PubMed1991

Purification and properties of neuraminidase from the culture medium of Bacteroides loescheii.

Neuraminidase was purified from the culture medium of Bacteroides loescheii ATCC 15930 by ultrafiltration followed by a DEAE-Sephacel anion exchange chromatography, fast-protein liquid chromatography using Mono P column and high-performance liquid chromatography using a Shim-pack Diol-300 column. The molecular weight of the purified enzyme was measured to be approximately 87 kDa and the optimal pH was at 4.8. Although the enzyme was able to hydrolyze the substrates with alpha,2-3, alpha,2-6, and alpha,2-8 linkages of N-acetylneuraminic acid, the rate of hydrolysis of N-acetylneuraminosyl-alpha,2-3-lactose was greater than that of the alpha,2-6-isomer.

Bacteroides↗
PubMed1991

Inhibitory effects of human salivary histatins and lysozyme on coaggregation between Porphyromonas gingivalis and Streptococcus mitis.

The effects of histatins on coaggregation between Porphyromonas gingivalis 381 and Streptococcus mitis ATCC 9811 were investigated by using a turbidimetric assay. The coaggregation activity was significantly inhibited by histatins 5 and 8 and strongly by lysozyme. Tritium-labeled histatin 8 bound to P. gingivalis cells but not to S. mitis cells.

Amino Acid Sequence↗
PubMed1991

Effect of transferrin on the growth of Porphyromonas gingivalis.

This study describes the effect of transferrin as an iron source on the growth of Porphyromonas (formally Bacteroides) gingivalis. Bacterial growth was monitored spectrophotometrically. All strains of P. gingivalis tested grew well in medium containing transferrin. The growth of P. gingivalis depended not only on the concentration of transferrin, but also on the iron saturation level of the protein. However, growth was not stimulated with either the ferrous or ferric iron salts tested. The addition of dipyridyl to the medium containing transferrin suppressed the growth of P. gingivalis, which also did not show species-specificity for human transferrin. Transferrin-binding activity was found in P. gingivalis by solid-phase assay with peroxidase-conjugated human transferrin. These results suggest that P. gingivalis may be capable of utilizing transferrin as an iron source for growth in vivo.

2,2'-Dipyridyl↗
PubMed1991

[A case of coronary artery bypass utilizing natural bifurcation of the right internal mammary artery].

A Forty five year old male with unstable angina due to multiple coronary artery stenosis underwent successful complete coronary revascularization utilizing the natural bifurcation of the right internal mammary artery. As this procedure has not been reported in detail previously in the literature and since the use of the natural bifurcation of the internal mammary artery was considered to be useful for the treatment of multiple coronary stenosis, this case was presented. Pre and post operative angiography is included.

Angina, Unstable↗
PubMed1990

The primary structure of superoxide dismutase purified from anaerobically maintained Bacteroides gingivalis.

The superoxide dismutase (SOD) of Bacteroides gingivalis can use either iron or manganese as a cofactor in its catalytic activity. In this study, the complete amino acid sequence of this SOD purified from anaerobically maintained B. gingivalis cells was determined. The proteins consisted of 191 amino acid residues and had a molecular mass of 21,500. The sequence of B. gingivalis SOD showed 44-51% homology with those for iron-specific SODs (Fe-SODs) and 40-45% homology with manganese-specific SODs (Mn-SODs) from several bacteria. However, this sequence homology was considerably less than that seen among the Fe-SOD (65-74%) or Mn-SOD family (42-60%). This indicates that B. gingivalis SOD, which accepts either iron or manganese as metal cofactor, is a structural intermediate between the Fe-SOD and Mn-SOD families.

Amino Acid Sequence↗
PubMed1990

Purification and characterization from human parotid secretion of a peptide which inhibits hemagglutination of Bacteroides gingivalis 381.

A peptide from human parotid secretion which inhibited hemagglutination of Bacteroides gingivalis 381 was purified by ultrafiltration followed by DEAE-Sephadex A-25 column chromatography and by gel filtration on Sephadex G-25, and then by reversed-phase HPLC. The complete amino acid sequence of the peptide, determined by automated Edman degradation was as follows; Lys-Phe-His-Glu-Lys-His-His-Ser-His-Arg-Gly-Tyr. The peptide contained 12 residues and the charged amino acids predominated with 4 histidine, 2 lysine, 1 arginine and 1 glutamic acid residues, thus being a histidine-rich peptide. The peptide was an active inhibitor of the hemagglutinating activity of B. gingivalis. Specific binding of tritium-labeled peptide to B. gingivalis cells was demonstrated. These results suggest that the histidine-rich peptide may function as a binding domain for the hemagglutinins of B. gingivalis during agglutination.

Amino Acid Sequence↗
PubMed1990

Characterization of superoxide dismutases purified from either anaerobically maintained or aerated Bacteroides gingivalis.

Superoxide dismutases (SODs) were purified from extracts of either anaerobically maintained or aerated Bacteroides gingivalis. Each purified enzyme (molecular weight, 46,000) was a dimer composed of two subunits of equal sizes. SOD from anaerobically maintained cells (anaero-SOD) contained 1.79 g-atom of Fe and 0.28 g-atom of Mn, and SOD from aerated cells (aero-SOD) contained 1.08 g-atom of Mn and 0.36 g-atom of Fe. Spectral analysis showed that anaero-SOD had the characteristic of Fe-SOD and that aero-SOD had that of Mn-SOD. Both enzyme preparations contained three isozymes with identical isoelectric points. On the basis of inactivation of SOD by H2O2, it was found that aero-SOD consisted of one Mn-SOD and a small quantity of two Fe-SODs, whereas anaero-SOD contained only Fe-SOD. However, each apoprotein from anaero-SOD and aero-SOD, prepared by dialysis in guanidinium chloride plus 8-hydroxyquinoline, showed only one protein band each with the same isoelectric point on an isoelectric focusing gel. Subsequent dialysis of both apoenzymes with either MnCl2 or Fe(NH4)2(SO4)2 restored the activity. These reconstituted SODs showed only one protein band with SOD activity on native polyacrylamide gel electrophoresis. Furthermore, the two enzymes had similar amino acid compositions, and their amino-terminal sequences were identical through the first 12 amino acids. These results suggest that the three isozymes of anaero-SOD and aero-SOD in B. gingivalis are formed from a single apoprotein.

Aerobiosis↗
PubMed1990

[Purification, characterization and induction by oxygen of superoxide dismutase from Bacteroides gingivalis 381].

Several strains of Bacteroides gingivalis had strong activities of superoxide dismutase (SOD) and were markedly tolerant in the presence of oxygen in 13 strains of black-pigmented Bacteroides species tested. Thus, the strains were maintained and incubated in the either anaerobic or aerobic system. It was found that the SOD activity was significantly induced by oxygen, especially in B. gingivalis 381. The SODs, anaero-SOD and aero-SOD from the extracts of B. gingivalis 381 cells, each was purified by hydrophobic chromatography followed by anion exchange chromatography, and then by gel filtration, respectively. Both the purified enzymes having molecular weight of about 46,000 consisted of two subunits of equal sizes. Spectral analysis revealed that anaero-SOD had the characteristic A350 of Fe-SOD, but aero-SOD exhibited A475 of Mn-SOD. Both samples contained three isozymes with identical isoelectric points of 5.25, 5.10 and 5.00. On the basis of inactivation of SOD by H2O2, it was shown that aero-SOD consisted of one Mn-SOD and a small quantity of two Fe-SODs, whereas anaero-SOD contained only Fe-SOD. To ascertain whether or not the apoprotein of aero-SOD is the same as that of anaero-SOD, each apoprotein was prepared by dialysis in guanidinium chloride plus 8-hydroxyquinoline. Only one protein band with the same isoelectric point of 5.30 on an isoelectric focusing gel was obtained in each purified SOD sample. Subsequent reconstitution of both apoenzymes with either Fe (NH4)2 (SO4)2 or MnCl2 significantly restored their activity. These reconstituted SODs showed only one protein band with SOD activity on Native-PAGE. The complete amino acid sequence of anaero-SOD was determined by automated Edman degradation of the protein, Achrombacter protease I, endoproteinase Asp-N and tryptic digestion. The sequence consisted of 191 residues corresponding to a molecular weight of 21,500 per subunit. Furthermore, the first 36 amino acid sequence of aero-SOD was determined following N-terminal analysis. The two enzymes had similar amino acid compositions, and their amino-terminal sequences were identical through the first 36 amino acids in which methionine residue was present at N-terminal. These results suggest the three isozymes of either anaero-SOD or aero-SOD in B. gingivalis 381 may be formed from the same apoprotein.

Amino Acid Sequence↗