Chemistry and function of ferritin and hemosiderin.
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Biomedical subjects
Publications and source records attributed to K Shimada.
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Statistical studies on 1,893 outpatients, 538 inpatients and 554 operative procedures at our department in 1984 revealed the following. The most frequent diseases among the outpatients were urogenital infections followed by anomalies, tumors and stones. The major diseases among the inpatients were hypospadias, vesicoureteral reflux, benign prostatic hypertrophy, bladder tumor and congenital urethral stenosis. A total of 554 operations were performed on 534 patients, and five major operations were hypospadias repair (68), ureterocystoneostomy (57), optic internal urethrotomy (50), TUR-P (42) and TUR-Bt (33).
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A case of combined anomalies of the urinary tract, horseshoe kidney, retrocaval ureter and pelviureteric stenosis, is presented. Routine urological examination of a three-year-old girl who complained of recurrent cystitis, showed horseshoe kidney and right hydronephrosis. Surgical exploration revealed the retrocaval ureter, and the isthmus of the horseshoe kidney lying between the aorta and the inferior vena cava. The pelviureteric junction itself was also stenotic and compressed from behind by the aberrant vessels. In addition to the dismembered pyeloplasty in front of the vena cava, isthmotomy was performed. The literatures on such combined anomalies were reviewed.
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The inhibitory effect of methylprednisolone 21-succinate ester (MPS) on the activities of complement components in human serum was studied by incubating human serum with various concentrations of MPS at 37 degrees C for 30 min and then measuring the residual activity of each component in human serum. The formation of EAC1 and EAC14 by C1 and C4 respectively, were only weakly inhibited by MPS at a final concentration of 10 mg/ml. In contrast, the same concentration of MPS completely inhibited the capacity of C2, C3, C5 and C6-9 to induce respective succeeding intermediates. On the basis of these findings a simplified method was devised for the preparation of EAC14 intermediates using human serum pretreated with MPS.
Thirty-three phage clones carrying DNAs homologous to human mitochondrial DNA (mtDNA) were isolated from two independently constructed human gene libraries, and the region and extent of homology of mtDNA-like sequences carried by these clones were examined in hybridization experiments. Each phage clone contained DNA sequences homologous to various parts of the mtDNA and the extent of homology differed from clone to clone. From the efficiency of the library screening, it was estimated that human nuclear DNA contains at least several hundred copies of mtDNA-like fragments. Four clones carrying nuclear DNA sequences homologous to the mitochondrial Unidentified Reading Frame (URF) 4 and URF5 regions were chosen for further studies, and their structures were analyzed by DNA sequencing. Comparison of these mtDNA-like sequences with that of mtDNAs of several mammalian species revealed conservation of a part of the structures present in direct ancestral mtDNAs. The mtDNA fragments seem to have been continuously integrated into mammalian nuclear DNA during evolution.
Using cloned human prealbumin cDNA as a probe, Southern blot hybridization of human genomic DNA revealed that the prealbumin gene consists of an unique, single-copy DNA. The nucleotide sequences of the entire human prealbumin gene, including both 581 base pairs of the 5'- and 95 base pairs of the 3'-flanking sequences, were determined. The gene spans about 7.0 kilobase pairs and consists of four exons and three introns. As in most eukaryotic genes, the consensus TATA and CAAT sequences are found 30 and 101 nucleotides, respectively, upstream from the putative cap site, and a polyadenylation signal sequence AA-TAAA is found in the 3'-untranslated region. Unexpectedly, two independent open reading frames provided with respective regulatory sequences were found within the gene: one in the first intron and the other in the third intron.
Anticoagulant heparan sulfate proteoglycans have been shown to be released from cultured endothelial cells. The effect of thrombin on their release was investigated. Thrombin at more than one unit/ml accelerated the release of [35S] sulfate-labeled glycosaminoglycans from cultured porcine aortic endothelial cells. The effect of thrombin reached a maximum after one hour of incubation, and was dependent on the enzyme concentration. 10 unit/ml of thrombin released approximately twice as much amount of 35S-glycosaminoglycans as did Hanks' balanced salt solution alone. When the active site of thrombin was blocked by either diisopropylfluorophosphate or hirudin, the enzyme effect was completely abolished. Released glycosaminoglycans were resistant to chondroitin ABC lyase digestions, but degraded by either heparitinase or nitrous acid treatments. Released 35S-materials were precipitated with trichloroacetic acid and shown to be degraded into smaller molecules after alkali treatment on Sepharose CL-6B gel filtration chromatography. On the other hand, thrombin treatment of 51Cr-labeled cells did not cause the release of radioactivity. These results indicate that thrombin potentiates the release of heparan sulfate proteoglycans from cultured aortic endothelial cells without causing an appreciable damage to the cells. The effect of thrombin is active site-dependent and requires a relatively high enzyme concentration.
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Glycosaminoglycans isolated from culture medium conditioned by human endothelial cells showed heparin-like anti-thrombin III cofactor activity measured by Xa inhibition. Their activity was relatively weak, 0.1% of the potency of heparin, but was approximately 5-fold more potent than that of glycosaminoglycans derived from vascular smooth muscle cells.