Hypocomplementemic urticarial vasculitis with Jaccoud's arthropathy and valvular heart disease: case report and review of the literature.

We describe a female Japanese patient with concomitant hypocomplementemic urticarial vasculitis, Jaccoud's arthropathy and valvular heart disease. In 1996, she developed arthritis with swelling of both proximal interphalangeal joints and urticarial vasculitis on both arms that was resolved by administration of glucocorticoid (prednisolone 30 mg/day). Tests for antineutrophil cytoplasmic antibodies, antinuclear antibody and rheumatoid factor gave negative results. The findings of a skin biopsy examination were consistent with 'leukocytoclastic vasculitis'. During 10 years of observation, the patient manifested polyarthritis leading to progressive deformity of the joints of the hands and feet (without loss of cartilage or erosion of bone), persistent urticaria exacerbated by cold and accompanied by hypocomplementemia and progressive cardiac valvular disease with mitral valve regurgitation. There are only three reports described previously documenting five patients with this rare combination of manifestations.

[Estimation of antibacterial activity of various antibiotics against Pseudomonas aeruginosa by score method].

Antibacterial activity of various antibiotics against Pseudomonas aeruginosa isolated from each hospitals depends on the variety or amount of antibiotics used in each hospital. The antibiotic, which is effective to P. aeruginosa in a certain hospital is not always effective to that in other hospital. The excellent antibiotics in antibacterial activity have low MIC and hard to progress in resistance, and such antibiotics may be effective against P. aeruginosa isolated from any hospitals. Therefore we thought that the antibiotic, which was progress to resistance, would show a great difference in MIC among hospitals, and we investigated MIC and difference of MIC of various antibiotics against P. aeruginosa isolated from six hospitals. Furthermore, we converted the data of MICs and difference of MIC among six hospitals into the score, and tried to estimate antibacterial activity of various antibiotics by using those scores. From the results of analysis in this report, we think the antibiotics actually surpass in antibacterial activity may be imipenem, cefozopran, cefsulodin and amikacin. New analytical method proposed in this report will become one of potential methods to estimate antibacterial activity of antibiotics against bacteria isolated from inpatient with bacterial infections.

[Evaluation of antibacterial activities of various antibiotics against glucose non-fermentative gram-negative rods other than Pseudomonas aeruginosa].

MICs of piperacillin, sulbactam/cefoperazone, minocycline (MINO), gentamicin, amikacin, flomoxef, ceftazidime, cefozopran, cefsulodin and imipenem were determined, against 189 clinical isolated strains of glucose non-fermentative Gram-negative Rods (NFGNR; Acinetobacter baumannii (44), Alcaligenes faecalis (5), Alcaligenes xylosoxidans (25), Burkholderia cepacia (12), Chryseobacterium indologenes (23), Chryseobacterium meningosepticum (9), Pseudomonas fluorescens (8), Pseudomonas putida (12), Stenotrophomonas maltophilia (51). Most species of these NFGNR show resistance to many antibiotics tested. Among the antibiotics used in this study, the only antibiotic effective against all species of NFGNR tested is MINO. The spectrums of antibacterial activities of various antibiotics determined by MICs may be useful in preliminary test for identification of these NFGNR.

Cloning and characterization of the Pichia pastoris PRC1 gene encoding carboxypeptidase Y.

We purified a 58 kDa serine protease from culture-supernatant of Pichia pastoris and found that the NH2-terminal amino acid sequence of this protease is closely homologous to that of mature protein of Saccharomyces cerevisiae carboxypeptidase Y (CPY), which is encoded by the PRC1 gene. Using the S. cerevisiae PRC1 gene as a hybridization probe, a cross-hybridizing fragment of P. pastoris genomic DNA was identified and the gene, PRC1, encoding CPY, was cloned. The open reading frame of the P. pastoris PRC1 gene consists of 1569 bp encoding a protein of 523 amino acids. The molecular mass of the protein is calculated to be 59.44 kDa without sugar chains. The protein comprises 20 amino acids of pre (signal)-peptide, 87 amino acids of pro-peptide and 416 amino acids of mature peptide, and has four N-glycosylation sites. The NH2-terminal amino acid sequence of mature peptide is completely identical with that of the protease purified from the culture-supernatant. There is 61% identity between the amino acid sequences of P. pastoris Prc1p and S. cerevisiae Prc1p. Chromosomal disruption of the PRC1 gene resulted in the loss of CPY activity. Over-expression of the PRC1 gene under regulation of the P. pastoris AOX1 promoter resulted in accumulation of a large amount of active CPY in the intracellular fraction, and secretion of a slightly larger molecule that is thought to be pro-CPY. The nucleotide sequence data reported in this paper will appear in the EMBL Nucleotide Sequence Databases under the Accession Number X87987.

[N-acetyl-beta-D-glucosaminidase].

N-acetyl-beta-D-glucosaminidase (NAG), one of the glycolytic enzymes, is distributed in various tissue cells. Among them, the lysosome in the renal proximal tubular cells contains high amount of NAG. NAG is secreted in urine when kidney is damaged. Urinary NAG, therefore, is used as a marker which can detect the extent of the renal damage. Electrophoresis divides urinary NAG into three isozymes, pre A, A, and B forms. In normal males, the percentages of three isozymes are 12.3 +/- 5.56%, 73.15 +/- 4.77%, and 14.81 +/- 2.90%, respectively. In normal females, they are 12.87 +/- 4.70%, 65.47 +/- 4.61%, and 21.70 +/- 5.03%, respectively. The measurement of urinary NAG isozymes is useful to determine the type and severity of renal disease, especially renal tubular disease.

Observation of tissue prokallikrein activation by some serine proteases, arginine esterases in rat submandibular gland.

Two serine proteases, arginine esterases (esterases I and II) which showed the activity of tissue prokallikrein activation were identified in rat submandibular gland. These enzymes were separated from the homogenate of rat submandibular gland by two successive DEAE-cellulose chromatographies and were further purified and characterized. Esterases I and II were found to be identical with tonin and esterase B-like enzyme, respectively. Both enzymes activated rat urinary prokallikrein at near neutral pH. Esterase B-like enzyme activated rat urinary prokallikrein better than tonin.

Re-evaluation of normal human urinary proteins fractionated by one-dimensional sodium dodecyl sulphate-polyacrylamide gel electrophoresis.

Proteins in normal human urine were clearly fractionated into 26 bands with molecular weights from 14,000 to 230,000 by means of one-dimensional sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) coupled with silver staining. The main band contained uromucoid, and the second main band had albumin. However, when urine samples from healthy persons were electrophoresed in the absence of SDS using polyacrylamide gel or agarose gel, or a cellulose acetate membrane, albumin but not uromucoid, frequently formed the main protein band. It is suggested that this is due to the complexing of uromucoid subunits to form a large molecule which cannot penetrate into the gel. In order to correctly fractionate all the proteins contained in normal human urine, it was concluded that it was best to treat a urine sample with SDS with pre-condensation, fractionate it by SDS-PAGE and stain fractionated proteins by a highly sensitive method such as silver staining.