Reymond I, Bitoun M, Levillain O, Tappaz M
Institut National de la Santé et de la Recherche Médicale, Unité INSERM 433, Faculté de Médecine RTH Laennec, Lyon, France.
J Histochem Cytochem. 2000 Nov;48(11):1461-8. doi: 10.1177/002215540004801103.
Cysteine sulfinate decarboxylase (CSD) is the rate-limiting biosynthetic enzyme of the pathway that forms taurine, a putative osmolyte in the kidney, which was previously localized in various segments of the nephron. Although CSD is known to be expressed in whole kidney extracts, no information on CSD mRNA regional expression and histological localization is yet available. Western blotting and Northern blotting were performed in four dissected regions of the kidney using an antiserum against recombinant CSD and a [(32)P]-dCTP-labeled CSD cDNA probe, respectively. In situ hybridization was carried out using a [(35)S]-CTP-labeled CSD RNA probe. A single protein (53 kD) and a single mRNA (2.5 kb) were detected, both of which appeared to be most enriched in the outer stripe of the outer medulla. In situ hybridization of CSD mRNA showed strong labeling of the thick tubules in the outer stripe of the outer medulla and in cortical medullary rays that corresponded to the proximal straight tubules. The significance of this restricted expression of CSD is discussed in relationship to the data previously reported on the location of taurine and the location of the taurine transporter along the nephron.
