000117706 001__ 117706
000117706 005__ 20240319081016.0
000117706 0247_ $$2doi$$a10.1152/AJPCELL.00404.2021
000117706 0248_ $$2sideral$$a128817
000117706 037__ $$aART-2022-128817
000117706 041__ $$aeng
000117706 100__ $$0(orcid)0000-0002-1273-9967$$aLucea, Susana
000117706 245__ $$aInhibition of phosphate transport by NAD+/NADH in brush border membrane vesicles
000117706 260__ $$c2022
000117706 5060_ $$aAccess copy available to the general public$$fUnrestricted
000117706 5203_ $$aNicotinamide is an important regulator of Pi homeostasis after conversion into NAD+/NADH. In this work, we have studied the classical inhibition of Pi transport by these compounds in the brush border membrane vesicles (BBMV) of rat kidney and rat intestine, and we examined the effects in opossum kidney (OK) cells and in phosphate transporter-expressing Xenopus laevis oocytes. In BBMV, NAD+ required preincubation at either room temperature or on ice to inhibit Pi uptake in BBMV. However, no effects were observed in the known Slc34 or Slc20 Pi transporters expressed in Xenopus oocytes, in OK cells, or in isolated rat cortical nephron segments. In BBMV from jejunum or kidney cortex, the inhibition of Pi transport was specific, dose-related, and followed a competitive inhibition pattern, as shown by linear transformation and nonlinear regression analyses. A Ki value of 538 mM NAD+ in kidney BBMV was obtained. Ribosylation inhibitors and ribosylation assays revealed no evidence that this reaction was responsible for inhibiting Pi transport. An analysis of the persistence of NAD+/NADH revealed a half-life of just 2 min during preincubation. Out of several metabolites of NAD degradation, only ADP-ribose was able to inhibit Pi uptake. Pi concentration also increased during 30 min of preincubation, up to 0.67 mM, most likely as a metabolic end product. In conclusion, the classical inhibition of Pi transport by NAD+/NADH in BBMV seems to be caused by the degradation metabolites of these compounds during the preincubation time. Copyright © 2022 the American Physiological Society.
000117706 536__ $$9info:eu-repo/grantAgreement/ES/DGA-IIU/1-2017$$9info:eu-repo/grantAgreement/ES/MINECO-FEDER/PGC2018-098635-B-I00
000117706 540__ $$9info:eu-repo/semantics/openAccess$$aAll rights reserved$$uhttp://www.europeana.eu/rights/rr-f/
000117706 590__ $$a5.5$$b2022
000117706 592__ $$a1.468$$b2022
000117706 591__ $$aPHYSIOLOGY$$b10 / 79 = 0.127$$c2022$$dQ1$$eT1
000117706 593__ $$aPhysiology$$c2022$$dQ1
000117706 591__ $$aCELL BIOLOGY$$b66 / 191 = 0.346$$c2022$$dQ2$$eT2
000117706 593__ $$aCell Biology$$c2022$$dQ1
000117706 594__ $$a8.3$$b2022
000117706 655_4 $$ainfo:eu-repo/semantics/article$$vinfo:eu-repo/semantics/acceptedVersion
000117706 700__ $$0(orcid)0000-0001-6627-298X$$aGuillén, Natalia$$uUniversidad de Zaragoza
000117706 700__ $$0(orcid)0000-0003-2907-0427$$aSosa, Cecilia$$uUniversidad de Zaragoza
000117706 700__ $$0(orcid)0000-0003-3457-323X$$aSorribas, Víctor$$uUniversidad de Zaragoza
000117706 7102_ $$11002$$2807$$aUniversidad de Zaragoza$$bDpto. Bioq.Biolog.Mol. Celular$$cÁrea Toxicología
000117706 773__ $$g322, 5 (2022), C803-C813$$pAm. j. physiol., Cell physiol.$$tAmerican Journal of Physiology - Cell Physiology$$x0363-6143
000117706 8564_ $$s4671701$$uhttps://zaguan.unizar.es/record/117706/files/texto_completo.pdf$$yPostprint
000117706 8564_ $$s696570$$uhttps://zaguan.unizar.es/record/117706/files/texto_completo.jpg?subformat=icon$$xicon$$yPostprint
000117706 909CO $$ooai:zaguan.unizar.es:117706$$particulos$$pdriver
000117706 951__ $$a2024-03-18-15:40:13
000117706 980__ $$aARTICLE