Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0033687 (proteinuria)
 24,015 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Normal mammals generally excrete only small amounts of protein in the urine, thus avoiding major leakage of proteins from the body. Proteinuria is the most commonly recognized abnormality in renal disease. However, healthy domestic cats ( Felis catus ) excrete proteins at high concentrations (about 0.5 mg/ml) in their urine. We investigated the possible cause of proteinuria in healthy cats, and discovered a 70 kDa glycoprotein, which was excreted as a major urinary protein in cat urine, irrespective of gender. To elucidate the biochemical functions and the excretion mechanism of this protein, we cloned the cDNA for this protein from a cat kidney cDNA library. The deduced amino acid sequence shared 47% identity with the rat liver carboxylesterase (EC 3.1.1.1), and both the serine hydrolase active site and the carboxylesterase-specific sequence were conserved. Therefore we named this protein cauxin (carboxylesterase-like urinary excreted protein). In contrast to the mammalian carboxylesterases, most of which are localized within the cells of various organs, cauxin was expressed specifically in the epithelial cells of the distal tubules, and was secreted efficiently into the urine, probably because it lacked the endoplasmic reticulum retention sequence (HDEL). Based on our finding that cauxin is not expressed in the immature cat kidney, we conclude that cauxin is involved in physiological functions that are specific for mature cats. Recently, cauxin-like cDNAs were found from human brain and teratocarcinoma cells. These data suggest that cauxin and cauxin-like human proteins are categorized as a novel group of carboxylesterase multigene family.
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PMID:Molecular cloning and characterization of a novel carboxylesterase-like protein that is physiologically present at high concentrations in the urine of domestic cats (Felis catus). 1240 Nov 31

Domestic cats exhibit physiological proteinuria due to the excretion of cauxin, a carboxylesterase, into the urine. In the present report, we demonstrate that cauxin is excreted in a species-, sex-, and age-dependent manner. Although the cauxin gene is conserved in mammals, including human, mouse, and dog, urinary cauxin was found only in member of the genus Felis and lynx (bobcat, and lynx) and not in other Felidae (genus: Panthera and puma) tested. In mature cats, cauxin excretion was higher in intact males than in castrated males or in intact or spayed females. Daily cauxin excretion decreased immediately after castration. Immunohistochemistry confirmed that cauxin expression in the kidney proximal straight tubules was higher in intact males than in castrated males. Urinary cauxin was detectable by Western blotting in cats older than about 3 months, and its excretion increased with age. In a zymographic esterase assay, urine contained a major cauxin band; by contrast, kidney homogenates contained three major bands, comprising two carboxylesterases and an unidentified esterase, and one minor cauxin band. These results suggest that 1. cauxin excretion is regulated by sex hormones, such as testosterone, 2. cauxin functions as an esterase in the urine rather than in kidney cells, and 3. the decomposition products by cauxin are excreted in a species-, sex-, and age-dependent manner, as is cauxin itself.
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PMID:Species-, sex-, and age-dependent urinary excretion of cauxin, a mammalian carboxylesterase. 1704 31

Removal of the major urinary protein, cauxin, a carboxylesterase, from cat urine is essential for distinguishing between physiological and abnormal proteinuria by a urine dipstick. We have previously developed a material for removing cauxin by using lens culinaris agglutinin (LCA) lectin which targets the N-linked oligosaccharides present in cauxin. To improve the affinity and specificity toward cauxin, we immobilized 1,1,1-trifluoro-3-(2-sulfanylethylsulfanyl) propane-2-one, an inhibitor of esterases, to a polymer chain grafted on to a porous hollow-fiber membrane by applying radiation-induced graft polymerization. Normal male urine was forced to permeate through the pores rimmed by the ligand-immobilized polymer chain. Cauxin could not be detected in the effluent from the membrane. The residence time of the urine across a membrane thickness of 1 mm was set at 7 s. The respective dynamic and equilibrium binding capacities of the membrane for cauxin were 2 and 3 mg/g. The developed cauxin-affinity membrane material was more effective for diagnosing cat kidney diseases than the LCA lectin tip.
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PMID:Immobilization of an esterase inhibitor on a porous hollow-fiber membrane by radiation-induced graft polymerization for developing a diagnostic tool for feline kidney diseases. 2409 69