Human fibrinogen gel formed by the action of a cell surface polysaccharide obtained from a Staphylococcus

Usui, Yukio; Ohtomo, Toshichika; Yoshida, Kenichi

doi:10.1016/0304-4165(82)90244-6

Cited by 5 publications

(6 citation statements)

References 13 publications

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“…This CCFAS, which is an alkali-stable polysaccharide, was also studied to clarify its specific bonding to fibrinogen Ohtomo et al 1985). This substance also differs from coagulase and CF and appears to convert fibrinogen and fibrin degradation products (FDP) directly into fibrin, a process resembling PC (Yoshida et al 1980;Usui et al 1982). In view of the fact that coagulase and CF produced by S. aureus are made-up proteins, as previously described, any structural multiplicity demonstrated by this CCFAS of polysaccharide is significant in clarifying the mechanism by which it is bonded to fibrinogen.…”

Section: Discussionmentioning

confidence: 85%

“…We reported that CCFAS isolated from an unencapsulated strain of S. aureus, which forms compact colonies in serum-containing SSA, shows PC to cause direct conversion from fibrinogen to fibrin (Yoshida et al 1977(Yoshida et al , 1978Ohtomo et al 1980a;Usui et al 1982). This CCFAS, which is an alkali-stable polysaccharide, was also studied to clarify its specific bonding to fibrinogen Ohtomo et al 1985).…”

Section: Discussionmentioning

confidence: 89%

“…We have previously shown an alkali-dependent polysaccharide (substance 1), composed of galactose and 2-amino-2-deoxy-D-galacturonic acid, isolated from staphylococci cell surfaces to be involved in compact colony formation in SSA and paracoagulation (PC) with fibrinogen (Yoshida et al 1975(Yoshida et al , 1977(Yoshida et al , 1978Usui et al 1982;Ohtomo et al 1985). It was, therefore, also assumed that adsorption of the converting activity (change of diffuse to compact growth) in SSA of serum and fibrinogen could be interpreted as polymerization of fibrinogen, FDP and/or soluble fibrin monomer and that the relative compact colony-forming activity of the S. aureus strain would correlate with the relative activity of fibrinogen clotting by the compact colony-forming active substance (CCFAS) (Ohtomo and Yoshida 1981;Usui et al 1982).…”

Section: Introductionmentioning

confidence: 96%

“…It was, therefore, also assumed that adsorption of the converting activity (change of diffuse to compact growth) in SSA of serum and fibrinogen could be interpreted as polymerization of fibrinogen, FDP and/or soluble fibrin monomer and that the relative compact colony-forming activity of the S. aureus strain would correlate with the relative activity of fibrinogen clotting by the compact colony-forming active substance (CCFAS) (Ohtomo and Yoshida 1981;Usui et al 1982). In another study, CCFAS produced by S. aureus and S. epidermidis was shown to be heterogeneous both biochemically and serologically (Usui et al 1979).…”

Section: Introductionmentioning

confidence: 99%

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Comparison of compact colony-forming activity and paracoagulation activity of strains ofStaphylococcus aureus in serum and plasmas of various animals

Ohtomo

Hata

Yoshida

1988

Med Microbiol Immunol

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Using 20 strains of Staphylococcus aureus isolated from clinical specimens, the compact colony-forming activity (CCFA) in serum-soft agar (SSA) in sera from various animals and the paracoagulation (PC) activity of the compact colony-forming active substance (CCFAS) extracted from these strains were investigated. The results of this comparative study revealed that the CCFA and PC of S. aureus for sera from various animals in SSA were different, not only among different strains but also in the same strains. In addition, the effect of galactose and calcium ions on the PC activity of these strains in experiments employing human fibrinogen permitted the recognition of these groups of S. aureus strains. In one group, PC activity was decreased by galactose but unaffected by calcium ions, in the second group PC activity was unaffected by galactose but increased by calcium ions, while in the third group it was unaffected by both. These results suggest the possibility of heterogeneity of CCFA among different strains of S. aureus.

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Section: Discussionmentioning

confidence: 85%

Section: Discussionmentioning

confidence: 89%

Section: Introductionmentioning

confidence: 96%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Comparison of compact colony-forming activity and paracoagulation activity of strains ofStaphylococcus aureus in serum and plasmas of various animals

Ohtomo

Hata

Yoshida

1988

Med Microbiol Immunol

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“…In the past, Yoshida and Minegishi (10) and Yoshida et al (11) regarded alkaline dependent polysaccharide substance as a cellular factor reacting with fibrin monomer, fibrinogen degradation products, and fibronectin (7) involved in serum for the compact-colony formation in SSA. Highly purified CCFAS clots plasmas by paracoagulation (4,6). Comparison of the relative activities of coagulase, clumping factor, and CCFAS in the coagulation of plasma showed that they were independent (14).…”

Section: Duferences In Chemical Composition Of the Highly Purified CCmentioning

confidence: 99%

Isolation of a Serologically Different Compact‐Colony‐Forming Active Substance from Strains of Staphylococcus aureus

Yoshida

Ohtomo

Suganuma

1990

Microbiology and Immunology

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To observe the possible serological heterogeneity of compact-colonyforming active substance (CCFAS), heat-killed vaccines were prepared by two strains of Staphylococcus aureus, strains SMU 1-46 and SMU 7931, cultured in 0.03 M trishydrochloride-buffered brain heart infusion, pH 8.4. After immunization with the vaccine in rabbits, antibody responses were observed during a period of six weeks after the immunization either by homologous and heterologous organisms using alkaline serum-soft agar technique.The results showed that remarkable antibody production was shown only against homologous strain, but not against heterologous strain. The antibodies were absorbed out only with highly purified preparation of CCFAS extracted from homologous strain and not with heterologous CCFAS. Differences of the major chemical composition of the substances showed that highly purified CCFAS extracted from strain SMU 7931 contained 2.84 and 2.04 times higher amounts of galactose and 2-amino-2-deoxy-D-galacturonic acid than those of CCFAS obtained from strain SMU 1-46.

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Purification and Characterization of a Vasoactive Intestinal Polypeptide-degrading Endoprotease from Porcine Antral Mucosal Membranes

Jeohn

Takahashi

1995

Journal of Biological Chemistry

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A neutral endoprotease was isolated from porcine antral mucosa and purified to homogeneity as examined by SDS-polyacrylamide gel electrophoresis (PAGE). Throughout the purification, t-butyloxycarbonyl-Arg-Val-Arg-Arg-4- methylcoumaryl-7-amide (MCA) was used as a substrate, which was found to be hydrolyzed specifically by the enzyme at the Arg-Arg bond. Unexpectedly, however, the enzyme was also found to hydrolyze vasoactive intestinal polypeptide (VIP) fairly specifically and more efficiently when various neuropeptides and related peptides were examined as substrates. It could degrade VIP by cleaving three peptide bonds not containing an arginine residue(s) with Km = 7.7 x 10(-6) M and kcat/Km = 7.4 x 10(6) M-1 s-1 (at pH 7.6 in the presence of 0.1% Lubrol PX), whereas only secretin, substance P, and a few others were hydrolyzed at much slower rates among the various peptides examined. Both activities toward the MCA substrate and VIP behaved in parallel throughout the purification procedures and showed essentially the same pH optimum and susceptibility toward various inhibitors and detergents. Therefore, both activities are thought to be due to the same enzyme. This endoprotease required 0.001% or a higher concentration of a detergent such as Lubrol PX or Triton X-100 for its maximal activity. Its optimum pH was about 7.5 and the molecular weight was estimated to be approximately 37,000 by SDS-PAGE. This enzyme was strongly inhibited by serine protease inhibitors such as diisopropyl-fluorophosphate and phenylmethanesulfonyl fluoride. It was also inhibited by p-chloromercuribenzoic acid, but not by some other cysteine protease inhibitors. Therefore, the enzyme appears to be most likely a kind of serine protease although its possibility as a cysteine protease cannot be completely excluded. Analysis of its cleavage specificity toward various oligopeptides indicated the possibility that the protease might recognize a specific amino acid sequence(s) and/or conformation in the vicinity of the cleavage site of the target peptide. Various characteristics of the endoprotease suggest that it is a novel membrane-bound neuropeptide-degrading endoprotease fairly specific for VIP.

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Human fibrinogen gel formed by the action of a cell surface polysaccharide obtained from a Staphylococcus

Cited by 5 publications

References 13 publications

Comparison of compact colony-forming activity and paracoagulation activity of strains ofStaphylococcus aureus in serum and plasmas of various animals

Comparison of compact colony-forming activity and paracoagulation activity of strains ofStaphylococcus aureus in serum and plasmas of various animals

Isolation of a Serologically Different Compact‐Colony‐Forming Active Substance from Strains of Staphylococcus aureus

Purification and Characterization of a Vasoactive Intestinal Polypeptide-degrading Endoprotease from Porcine Antral Mucosal Membranes

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