In this report, we first cloned a cDNA for a protein that is highly expressed in mouse kidney and then isolated its counterparts in human, rat hamster, and guinea pig by polymerase chain reaction-based cloning. The cDNAs of the five species encoded polypeptides of 244 amino acids, which shared more than 85% identity with each other and showed high identity with a human sperm 34-kDa protein, P34H, as well as a murine lung-specific carbonyl reductase of the short-chain dehydrogenase/reductase superfamily. In particular, the human protein is identical to P34H, except for one amino acid substitution. The purified recombinant proteins of the five species were about 100-kDa homotetramers with NADPH-linked reductase activity for alpha-dicarbonyl compounds, catalyzed the oxidoreduction between xylitol and l-xylulose, and were inhibited competitively by n-butyric acid. Therefore, the proteins are designated as dicarbonyl/l-xylulose reductases (DCXRs). The substrate specificity and kinetic constants of DCXRs for dicarbonyl compounds and sugars are similar to those of mammalian diacetyl reductase and l-xylulose reductase, respectively, and the identity of the DCXRs with these two enzymes was demonstrated by their co-purification from hamster and guinea pig livers and by protein sequencing of the hepatic enzymes. Both DCXR and its mRNA are highly expressed in kidney and liver of human and rodent tissues, and the protein was localized primarily to the inner membranes of the proximal renal tubules in murine kidneys. The results imply that P34H and diacetyl reductase (EC ) are identical to l-xylulose reductase (EC ), which is involved in the uronate cycle of glucose metabolism, and the unique localization of the enzyme in kidney suggests that it has a role other than in general carbohydrate metabolism.
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http://dx.doi.org/10.1074/jbc.M110703200 | DOI Listing |
Angiogenesis
January 2025
Department of Pharmacology & Toxicology, Indiana University School of Medicine, Indianapolis, IN, USA.
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January 2025
School of Medicine, Nankai University, Tianjin, 300071, China.
Cholangiocarcinoma (CCA), a highly aggressive form of cancer, is known for its high mortality rate. A Disintegrin and Metalloprotease Domain-like Protein Decysin-1 (ADAMDEC1) can promote the development and metastasis in various tumors by degrading the extracellular matrix. However, its regulatory mechanism in CCA remains unclear.
View Article and Find Full Text PDFPreserving a large number of essential yet highly unstable ribosomal DNA (rDNA) repeats is critical for the germline to perpetuate the genome through generations. Spontaneous rDNA loss must be countered by rDNA copy number (CN) expansion. Germline rDNA CN expansion is best understood in Drosophila melanogaster, which relies on unequal sister chromatid exchange (USCE) initiated by DNA breaks at rDNA.
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Lunenfeld-Tanenbaum Research Institute, Sinai Health System, Toronto, ON, Canada.
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January 2025
Department of Urology, The First Affiliated Hospital of Soochow University, No. 899 Pinghai Road, Suzhou, 215006, People's Republic of China.
CXCL14 is a highly conserved chemokine expressed in various cell types, playing crucial roles in both physiological and pathological processes, including immune regulation and tumorigenesis. Recently, the role of CXCL14 in tumors has attracted considerable attention. However, previous pan-cancer studies have reported inconsistencies regarding the effects of CXCL14 on tumors, particularly concerning its expression levels in tumor tissues and its influence on various phenotypes of cancer cells.
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