Clinical value of the guanase screening test in donor blood for prevention of posttransfusional non-A, non-B hepatitis

Ito, Susumu; Tsuji, Yasuhiro; Kitagawa, Naoyuki; Ishihara, Akihiko; Syundo, Jyoji; Tamura, Yoshiyuki; Kishi, Seiichiro; Mori, Hiromu

doi:10.1002/hep.1840080233

Cited by 20 publications

(9 citation statements)

References 8 publications

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“…Thus a high serum guanase level is considered to be a specific indicator of hepatocellular damage (4,6,16,18). Moreover, Yamasaki et al (20), Mihara et al (17) and Ito et al (11) reported that the incidence of posttransfusional non-A, non-B hepatitis (PTH) was significantly higher in recipients of blood with high guanase activity, and that PTH could be prevented by avoiding use of donor bloods with high guanase activities (12).…”

Section: Humanmentioning

confidence: 99%

Histochemical and biochemical studies on guanase in the human and rat kidney.

Ito

Maeda

Iwasaki

et al. 1991

Acta Histochem. Cytochem

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A specific antibody against purified human liver guanase was raised in rabbits. The antiserum formed a single precipitin line with human liver extracts, and completely inhibited the activity of the enzyme derived from human liver and kidney. Immunoblotting showed that the antibody bound only to the one protein band of liver and kidney guanase activity. In immunohistochemical studies, the DAB (3, 3'-diaminobenzidine tetrahydrochloride)-reaction with this antibody was positive in the same locations as the histochemical guanase reaction. Moreover, biochemical data of enzymic activity in nephron segments of the rat indicated that guanase activity was located in the proximal tubules. Thus, the DAB reaction appeared to show the location of guanase itself. This immunohistochemical procedure for detection of guanase should useful in clinical studies on this enzyme.

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Section: Humanmentioning

confidence: 99%

Histochemical and biochemical studies on guanase in the human and rat kidney.

Ito

Maeda

Iwasaki

et al. 1991

Acta Histochem. Cytochem

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“…4 A variety of pathogens are dependent upon the host’s purine salvage pathway for the nucleotides necessary for their survival, as they do not possess a de novo purine biosynthesis mechanism. 5–8 It was demonstrated that inhibition of GDA could be caused selectively in pathogens without affecting the mammalian biosynthesis of nucleic acids. 9 Therefore, a new chemotherapeutic strategy lies in the search for drugs that selectively block the parasite from the pathway that is required for its survival.…”

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confidence: 99%

“…Reaction of 5 with acetic anhydride afforded the N 5 -acetyl derivative 6 in 81% yield. Compound 6 was alkylated at N 5 position with 1,1-diethoxy-2-iodoethane 31 employing potassium carbonate in DMF and 18- crown-6 to provide 7 in 66% yield. 29 The N 5 -acetyl group was then removed by treatment with sodium ethoxide in ethanol to obtain 8 in 84% yield.…”

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confidence: 99%

“…Compound 6 was alkylated at N 5 position with 1,1-diethoxy-2-iodoethane 31 employing potassium carbonate in DMF and 18- crown-6 to provide 7 in 66% yield. 29 The N 5 -acetyl group was then removed by treatment with sodium ethoxide in ethanol to obtain 8 in 84% yield. The silyl protecting groups of the sugar were removed by tetra- n -butylammonium fluoride to obtain 9 in 70% yield, 32 followed by hydrolysis and ring-closure with 1N aqueous HCl to obtain a mixture of diastereomeric nucleosides 2 and 3 in 90% yield.…”

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Investigations into specificity of azepinomycin for inhibition of guanase: Discrimination between the natural heterocyclic inhibitor and its synthetic nucleoside analogues

Chakraborty

Shah

Fishbein

et al. 2012

Bioorganic & Medicinal Chemistry Letters

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In our long and broad program to explore structure-activity relationships of the natural product azepinomycin and its analogues for inhibition of guanase, an important enzyme of purine salvage pathway of nucleic acid metabolism, it became necessary to investigate if the nucleoside analogues of the heterocycle azepinomycin, which are likely to be formed in vivo, would be more or less potent than the parent heterocycle. To this end, we have resynthesized both azepinomycin (1) and its two diastereomeric nucleoside analogues (2 and 3), employing a modified, more efficient procedure, and have biochemically screened all three compounds against a mammalian guanase. Our results indicate that the natural product is at least 200 times more potent toward inhibition of guanase as compared with its nucleoside analogues, with the observed Ki of azepinomycin (1) against the rabbit liver guanase = 2.5 (± 0.6) × 10−6 M, while Ki of Compound 2 =1.19 (± 0.02) × 10−4 M and that of Compound 3 = 1.29 (± 0.03) × 10−4 M. It is also to be noted that while IC50 value of azepinomycin against guanase in cell culture has long been reported, no inhibition studies nor Ki against a pure mammalian enzyme have ever been documented. In addition, we have, for the first time, determined the absolute stereochemistry of the 6-OH group of 2 and 3 using conformational analysis coupled with 2-D 1H NMR NOESY

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“…Most cases of posttransfusion hepatitis are now consid ered to be of the non-A, non-B variety [1,4,5], This form is thought to progress to a chronic condition [6][7][8][9], and the possibly gives rise to hepatocellular carcinoma [10,11], The risk factors of posttransfusion hepatitis have been investigated in regard to age and sex of recipients [6.12], serum alanine aminotransferase (ALT) [13], anti-HBc [14], anti-HBs [15] and guanase activity [16] of donated blood, and the volume of transfusion. To assess the risk of development of this disease.…”

Section: Introductionmentioning

confidence: 99%

Posttransfusion Hepatitis in Japan

Takano¹,

Omata²,

Ohto³

et al. 1992

Vox Sanguinis

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The incidence of posttransfusion hepatitis and the rate of chronicity were investigated in a program devised at our hospital in December, 1982. Out of 2,596 blood recipients between January, 1982, and December, 1987, 451 (22.7%) developed posttransfusion hepatitis. Seventy-seven patients out of 217 (35.3%) whose course was closely followed progressed to chronicity. The incidence of posttransfusion hepatitis increased with the volume of transfused blood without any evident limitation. Recipients of elevated-ALT donor blood (>26 Karmen units) were found to be more susceptible to posttransfusion hepatitis than those who had received only normal-ALT donor blood. Packed red blood cells, whole blood and fresh whole blood were high-risk components, and fresh frozen plasma a low-risk component of blood. The carrier rate of non-A, non-B hepatitis agents in Japanese healthy blood donors was determined to be 1.2% using the Frost-Reed model of infectious diseases. Anti-hepatitis C virus was detected in 62% of the cases of posttransfusion hepatitis 1 year after transfusion.

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Clinical value of the guanase screening test in donor blood for prevention of posttransfusional non-A, non-B hepatitis

Cited by 20 publications

References 8 publications

Histochemical and biochemical studies on guanase in the human and rat kidney.

Histochemical and biochemical studies on guanase in the human and rat kidney.

Investigations into specificity of azepinomycin for inhibition of guanase: Discrimination between the natural heterocyclic inhibitor and its synthetic nucleoside analogues

Posttransfusion Hepatitis in Japan

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