Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0451641 (urolithiasis)
3,973 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A non-toxic, soluble polymeric preparation MAG with controlled period of gelation was synthetized for the extraction of stones from the pyelocalyceal system during surgery for urolithiasis. With respect to toughness the preparation proved superior to the fibrinogen-thrombin mixture, used in the so-called "fibrin pyelotomy" according to Dees. Its biologic testing in animals (rabbits, dogs and pigs) yielded excellent results.
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PMID:Polymeric pyelotomy (experimental studies). 53 76

The role of thrombin, fibrinogen, specific and unspecific immunological reactions in the pathogenesis of urolithiasis were evaluated. It was found in the urine of patients with urolithiasis and concomitant pyelonephritis that most bacteria, leucocytes and organic substances fixed on crystalloids contained on their surfaces immunoglobulins M, G and A. The mechanisms of the possible participation of immune reactions in the pathogenesis of urolithiasis are discussed.
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PMID:[The role of immunologic factors in the pathogenesis of urolithiasis]. 233 Jul 4

To evaluate the effect of a tissue adhesive agent (BI 0.022) on renal pelvic and ureteral surgery, the adhesive was applied for 44 patients with urolithiasis. The conventional suture method was performed in 87 patients as a control. The tissue adhesive is composed of fibrinogen, thrombin, factor XIII, aprotinin and CaCl2. The number of sutures for closure of the incision made on the rental pelvis and the ureter was significantly reduced by the use of the tissue adhesive (p less than 0.01). There was no tendency of increase in urinary leakage following the application of the method in comparison with the control. Furthermore, it was noteworthy that 10 in cases with less than a 1 cm ureteral incision were completely closed by the use of the adhesive agent. This tissue adhesive agent should be valuable for renal pelvic and ureteral surgery as a simple substitute for the conventional suture method.
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PMID:[The efficacy of a tissue adhesive agent (BI 0.022) in urinary tract surgery--application to pyelo- and ureterolithotomy]. 349 Jul 42

In recent years there has been great interest in the putative role of prothrombin and its activation peptides, especially the urinary form of prothrombin fragment 1, in the pathogenesis of calcium oxalate (CaOx) urolithiasis. Previously, we showed that prothrombin and its activation peptides inhibit CaOx crystallization in inorganic conditions in vitro. The aim of the present study was to determine if this inhibitory activity is retained in undiluted human urine and, therefore, whether it is likely to have any influence under physiological conditions. A secondary objective was to assess the relationship between the structures of the proteins and their inhibitory activities. Prothrombin was purified from Prothrombinex-HT, cleaved with thrombin and the resulting fragment 1 (F1) and fragment 2 (F2) were purified. The purity of each protein was confirmed by SDS/PAGE, and their effects on CaOx crystallization in undiluted ultrafiltered human urine were determined at a final concentration 80.65 nmol/l using Coulter Counter and [(14)C]oxalate analysis. The precipitated crystals were visualized using scanning electron microscopy. The Coulter Counter data revealed that, whereas prothrombin and its activation peptides did not affect the urinary metastable limit and the size of the precipitated particles, F1 did significantly reduce the latter. These findings were corroborated with scanning electron microscopy which also revealed that the reduction in particle size caused by F1 resulted from a decrease in the degree of crystal aggregation, rather than in the size of the individual crystals. The [(14)C]oxalate data showed that none of the proteins added significantly inhibited the mineral deposition. It was concluded that with the exception of F1, which does inhibit CaOx crystal aggregation, prothrombin and its activation peptides do not alter the deposition and aggregation of CaOx crystals in ultrafiltered human urine in vitro. Also, the gamma-carboxyglutamic acid domain of prothrombin and F1, which is absent from thrombin and F2, is the region of the molecules that determines their potent inhibitory effects. The superior potency of F1, compared with prothrombin, probably results from the molecule's greater charge-to-mass ratio.
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PMID:Effect of prothrombin and its activation fragments on calcium oxalate crystal growth and aggregation in undiluted human urine in vitro: relationship between protein structure and inhibitory activity. 1191 5