Yuka Shiraiwa

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Serine palmitoyltransferase (SPT) belongs to the fold type I family of the pyridoxal 5'-phosphate (PLP)-dependent enzyme and forms 3-ketodihydrosphingosine (KDS) from l-serine and palmitoyl-CoA. Like other alpha-oxamine synthase subfamily enzymes, SPT is different from most of the fold type I enzymes in that its re face of the PLP-Lys aldimine is occupied(More)
Serine palmitoyltransferase (SPT) is a key enzyme of sphingolipid biosynthesis and catalyzes the pyridoxal 5'-phosphate (PLP)-dependent decarboxylative condensation reaction of l-serine with palmitoyl-CoA to generate 3-ketodihydrosphingosine. The binding of l-serine alone to SPT leads to the formation of the external aldimine but does not produce a(More)
OBJECTIVE To examine whether the changes in endolymphatic ion concentrations were involved in hair cells degeneration in claudin-14 knockout (KO) mice (Cldn14-/-), we measured the endocochlear potential (EP) along with concentrations of K+, Na+, H+, or Ca2+ ([K]e, [Na]e, pHe, [Ca]e) in Cldn14-/-, in which hair cells were selectively damaged, and compared(More)
In 187 dogs we cut through certain branches of the nerves innervating the urinary bladder and we determined the changes caused thereby from a cytometrical and a biochemical point of view. We thus observed that the section of the corresponding ventral and dorsal sacral nerves accompanied by the removal of the sacral ganglions brought about the same changes(More)
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