Gastrointestinal stromal tumor of small intestine as the cause of massive gastrointestinal hemorrhage - case report

Wśród rzadkich przyczyn masywnego krwawienia do dolnego odcinka przewodu pokarmowego znajdują się guzy jelita typu GIST. Są to nowotwory wywodzące się z podścieliska przewodu pokarmowego, których patobiologia związana jest z mutacją przezbłonowego receptora KIT, zyskującego aktywność kinazy tyrozynowej. Podstawą rozpoznania jest badanie immunohistochemiczne na obecność antygenu CD117. W pracy przedstawiono przypadek 37-letniej pacjentki hospitalizowanej z powodu masywnego krwawienia do przewodu pokarmowego, u której rozpoznano i skutecznie usunięto guz jelita cienkiego typu GIST.Gastrointestinal stromal tumors (GIST) are amongst the rarest causes of massive gastrointestinal hemorrhage. These tumors are derived from the stromal tissue of the gastrointestinal tract and their pathobiology is related to the mutation of the KIT transmembrane receptor, which gains results in thyrosine kinase activity. A diagnosis is based on an immunohistochemical examination for the presence of the CD117 antigen. The case of a 37-year-old female, hospitalized for massive gastrointestinal hemorrhage due to a GIST-type tumor of the small intestine, is presented in this article. The tumor was successfully diagnosed and treated

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Abstract: Aldehyde dehydrogenase (ALDH) is known to be susceptible to oxidation, and its assays require stabilization of the enzyme by thiols. Application of the fluorimetric method to assay the ALDH activity in human saliva demonstrated significant differences between procedures utilizing glutathione (GSH) and dithiothreitol (DTT) as stabilizing agents. It has been recently shown that average aldehyde dehydrogenase (ALDH3A1) activity in cancerous (oral cavity cancer) patientsí tissues was higher than that found in the control group, what may indicate induction of tumor-specific ALDH

Excited-State Proton Transfer in 8-Azapurines I: A Kinetic Analysis of 8-Azaxanthine Fluorescence

A super-continuum white laser with a half-pulse width of ~75 ps was used to observe the kinetics of a postulated excited-state proton transfer in 8-azaxanthine and its 8-methyl derivative. Both compounds exhibited dual emissions in weakly acidified alcoholic media, but only one band was present in aqueous solutions, exhibiting an abnormal Stokes shift (>12,000 cm−1). It was shown that long-wavelength emissions were delayed relative to the excitation pulse within alcoholic media. The rise time was calculated to be 0.4–0.5 ns in both methanol and deuterated methanol. This is equal to the main component of the fluorescence decay in the short-wavelength band (340 nm). Time-resolved emission spectra (TRES) indicated a two-state photo-transformation model in both compounds. Global analysis of the time dependence revealed three exponential components in each compound, one of which had an identical rise-time, with the second attributed to a long-wavelength band decay (6.4 ns for aza-xanthine and 8.3 ns for its 8-methyl derivative). The origin of the third, intermediate decay time (1.41 ns for aza-xanthine and 0.87 ns for 8-methyl-azaxanthine) is uncertain, but decay-associated spectra (DAS) containing both bands suggest the participation of a contact ion pair. These results confirm the model of phototautomerism proposed earlier, but the question of the anomalous isotope effect remains unsolved

Enzymatic Synthesis of Highly Fluorescent 8-Azapurine Ribosides Using a Purine Nucleoside Phosphorylase Reverse Reaction: Variable Ribosylation Sites

Various forms of purine-nucleoside phosphorylase (PNP) were used as catalysts of enzymatic ribosylation of selected fluorescent 8-azapurines. It was found that the recombinant calf PNP catalyzes ribosylation of 2,6-diamino-8-azapurine in a phosphate-free medium, with ribose-1-phosphate as ribose donor, but the ribosylation site is predominantly N7 and N8, with the proportion of N8/N7 ribosylated products markedly dependent on the reaction conditions. Both products are fluorescent. Application of the E. coli PNP gave a mixture of N8 and N9-substituted ribosides. Fluorescence of the ribosylated 2,6-diamino-8-azapurine has been briefly characterized. The highest quantum yield, ~0.9, was obtained for N9-β-d-riboside (λmax 365 nm), while for N8-β-d-riboside, emitting at ~430 nm, the fluorescence quantum yield was found to be close to 0.4. Ribosylation of 8-azaguanine with calf PNP as a catalyst goes exclusively to N9. By contrast, the E. coli PNP ribosylates 8-azaGua predominantly at N9, with minor, but highly fluorescent products ribosylated at N8/N7

Pyrazolo[4,3-e][1,2,4]triazines: Purine Analogues with Electronic Absorption in the Visible Region

Synthesis of several pryrazolo[4,3-e][1,2,4]-triazines is described. Theabsorption spectrum of some 5-substituted derivatives was found to extend to the visibleregion. These compounds were found to inhibit some enzymes of purine metabolism, likexanthine oxidase or bacterial purine-nucleoside phosphorylase with Ki values in the 10-3 –10-5 M range

Site-Selective Ribosylation of Fluorescent Nucleobase Analogs Using Purine-Nucleoside Phosphorylase as a Catalyst: Effects of Point Mutations

Enzymatic ribosylation of fluorescent 8-azapurine derivatives, like 8-azaguanine and 2,6-diamino-8-azapurine, with purine-nucleoside phosphorylase (PNP) as a catalyst, leads to N9, N8, and N7-ribosides. The final proportion of the products may be modulated by point mutations in the enzyme active site. As an example, ribosylation of the latter substrate by wild-type calf PNP gives N7- and N8-ribosides, while the N243D mutant directs the ribosyl substitution at N9- and N7-positions. The same mutant allows synthesis of the fluorescent N7-β-d-ribosyl-8-azaguanine. The mutated form of the E. coli PNP, D204N, can be utilized to obtain non-typical ribosides of 8-azaadenine and 2,6-diamino-8-azapurine as well. The N7- and N8-ribosides of the 8-azapurines can be analytically useful, as illustrated by N7-β-d-ribosyl-2,6-diamino-8-azapurine, which is a good fluorogenic substrate for mammalian forms of PNP, including human blood PNP, while the N8-riboside is selective to the E. coli enzyme