Role of the putative PKC phosphorylation sites of the type IIc sodium-dependent phosphate transporter in parathyroid hormone regulation.

Animals Cell Line Female Kidney Tubules, Proximal / drug effects Male Mice, Knockout Opossums Parathyroid Hormone / pharmacology Peptide Fragments / pharmacology Phosphates / metabolism Phosphorylation Protein Kinase C / metabolism Protein Processing, Post-Translational / drug effects Protein Stability Renal Reabsorption / drug effects Sodium-Phosphate Cotransporter Proteins, Type IIa / deficiency Sodium-Phosphate Cotransporter Proteins, Type IIc / genetics Time Factors Xenopus
Opossum kidney cells Proximal tubule SLC34A3 Sodium-dependent Pi transport

Journal

Clinical and experimental nephrology
ISSN: 1437-7799
Titre abrégé: Clin Exp Nephrol
Pays: Japan
ID NLM: 9709923

Informations de publication

Date de publication:
Jul 2019
Historique:
received: 21 01 2019
accepted: 01 03 2019
pubmed: 22 3 2019
medline: 7 1 2020
entrez: 22 3 2019
Statut: ppublish

Résumé

Injection of parathyroid hormone (PTH) rapidly stimulates renal Pi excretion, in part by downregulating NaPi-IIa (Npt2a/SLC34A1) and NaPi-IIc (Npt2c/SLC34A3) transporters. The mechanisms underlying the effects of PTH on NaPi-IIc are not fully elucidated. We analyzed the effect of PTH on inorganic phosphate (Pi) reabsorption in Npt2a The Npt2a The present study suggests that acute regulation of NaPi-IIc protein by PTH is involved in the inactivation of Na

Sections du résumé

BACKGROUND BACKGROUND
Injection of parathyroid hormone (PTH) rapidly stimulates renal Pi excretion, in part by downregulating NaPi-IIa (Npt2a/SLC34A1) and NaPi-IIc (Npt2c/SLC34A3) transporters. The mechanisms underlying the effects of PTH on NaPi-IIc are not fully elucidated.
METHODS METHODS
We analyzed the effect of PTH on inorganic phosphate (Pi) reabsorption in Npt2a
RESULTS RESULTS
The Npt2a
CONCLUSIONS CONCLUSIONS
The present study suggests that acute regulation of NaPi-IIc protein by PTH is involved in the inactivation of Na

Identifiants

DOI: 10.1007/s10157-019-01725-6 PMID: 30895530
pubmed: 30895530
doi: 10.1007/s10157-019-01725-6
pii: 10.1007/s10157-019-01725-6
doi:

Substances chimiques

Parathyroid Hormone 0
Peptide Fragments 0
Phosphates 0
Slc34a1 protein, mouse 0
Slc34a3 protein, mouse 0
Sodium-Phosphate Cotransporter Proteins, Type IIa 0
Sodium-Phosphate Cotransporter Proteins, Type IIc 0
parathyroid hormone (1-34), bovine 12583-68-5
Protein Kinase C EC 2.7.11.13

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

898-907

Subventions

Organisme : Ministry of Education, Culture, Sports, Science, and Technology of Japan
ID : 23689045
Organisme : Ministry of Education, Culture, Sports, Science, and Technology of Japan
ID : 26293204

Références

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Auteurs

Toru Fujii (T)

Department of Molecular Nutrition, Institute of Biomedical Sciences, University of Tokushima Graduate School, 3-18-15 Kuramoto-cho, Tokushima, 770-8503, Japan.

Hiroko Segawa (H)

Department of Molecular Nutrition, Institute of Biomedical Sciences, University of Tokushima Graduate School, 3-18-15 Kuramoto-cho, Tokushima, 770-8503, Japan. segawa@tokushima-u.ac.jp.
ORCID: 0000-0002-0905-246X

Ai Hanazaki (A)

Department of Molecular Nutrition, Institute of Biomedical Sciences, University of Tokushima Graduate School, 3-18-15 Kuramoto-cho, Tokushima, 770-8503, Japan.

Shiori Nishiguchi (S)

Department of Molecular Nutrition, Institute of Biomedical Sciences, University of Tokushima Graduate School, 3-18-15 Kuramoto-cho, Tokushima, 770-8503, Japan.

Sakura Minoshima (S)

Department of Molecular Nutrition, Institute of Biomedical Sciences, University of Tokushima Graduate School, 3-18-15 Kuramoto-cho, Tokushima, 770-8503, Japan.

Akiko Ohi (A)

Department of Molecular Nutrition, Institute of Biomedical Sciences, University of Tokushima Graduate School, 3-18-15 Kuramoto-cho, Tokushima, 770-8503, Japan.

Rieko Tominaga (R)

Department of Molecular Nutrition, Institute of Biomedical Sciences, University of Tokushima Graduate School, 3-18-15 Kuramoto-cho, Tokushima, 770-8503, Japan.

Sumire Sasaki (S)

Department of Molecular Nutrition, Institute of Biomedical Sciences, University of Tokushima Graduate School, 3-18-15 Kuramoto-cho, Tokushima, 770-8503, Japan.

Kazuya Tanifuji (K)

Department of Molecular Nutrition, Institute of Biomedical Sciences, University of Tokushima Graduate School, 3-18-15 Kuramoto-cho, Tokushima, 770-8503, Japan.

Megumi Koike (M)

Department of Molecular Nutrition, Institute of Biomedical Sciences, University of Tokushima Graduate School, 3-18-15 Kuramoto-cho, Tokushima, 770-8503, Japan.

Yuki Arima (Y)

Department of Molecular Nutrition, Institute of Biomedical Sciences, University of Tokushima Graduate School, 3-18-15 Kuramoto-cho, Tokushima, 770-8503, Japan.

Yuji Shiozaki (Y)

Department of Molecular Nutrition, Institute of Biomedical Sciences, University of Tokushima Graduate School, 3-18-15 Kuramoto-cho, Tokushima, 770-8503, Japan.

Ichiro Kaneko (I)

Department of Molecular Nutrition, Institute of Biomedical Sciences, University of Tokushima Graduate School, 3-18-15 Kuramoto-cho, Tokushima, 770-8503, Japan.

Mikiko Ito (M)

Human Science and Environment, University of Hyogo Graduate School, Hyogo, Japan.

Sawako Tatsumi (S)

Department of Molecular Nutrition, Institute of Biomedical Sciences, University of Tokushima Graduate School, 3-18-15 Kuramoto-cho, Tokushima, 770-8503, Japan.

Ken-Ichi Miyamoto (KI)

Department of Molecular Nutrition, Institute of Biomedical Sciences, University of Tokushima Graduate School, 3-18-15 Kuramoto-cho, Tokushima, 770-8503, Japan. kmiyamoto@tokushima-u.ac.jp.

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Classifications MeSH

questionsmedicales.fr › Eucaryotes › Animaux › Role of the putative PKC phosphorylation sites...
questionsmedicales.fr › Cellules › Cellules cultivées › Lignée cellulaire › Role of the putative PKC phosphorylation sites...
questionsmedicales.fr › Appareil urogénital › Voies urinaires › Rein › Néphrons › Tubules rénaux › Tubules contournés proximaux › Role of the putative PKC phosphorylation sites...
questionsmedicales.fr › Eucaryotes › Animaux › Chordés › Vertébrés › Mammifères › Eutheria › Rodentia › Muridae › Murinae › Souris › Souris transgéniques › Souris knockout › Role of the putative PKC phosphorylation sites...
questionsmedicales.fr › Eucaryotes › Animaux › Chordés › Vertébrés › Mammifères › Marsupialia › Opossum › Role of the putative PKC phosphorylation sites...
questionsmedicales.fr › Acides aminés, peptides et protéines › Peptides › Hormones peptidiques › Hormone parathyroïdienne › Role of the putative PKC phosphorylation sites...
questionsmedicales.fr › Acides aminés, peptides et protéines › Peptides › Fragments peptidiques › Role of the putative PKC phosphorylation sites...
questionsmedicales.fr › Produits chimiques inorganiques › Composés du phosphore › Acides du phosphore › Acides phosphoriques › Phosphates › Role of the putative PKC phosphorylation sites...
questionsmedicales.fr › Métabolisme › Phosphorylation › Role of the putative PKC phosphorylation sites...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines et peptides de signalisation intracellulaire › Protein-Serine-Threonine Kinases › Protéine kinase C › Role of the putative PKC phosphorylation sites...
questionsmedicales.fr › Phénomènes génétiques › Régulation de l'expression des gènes › Modification traductionnelle des protéines › Maturation post-traductionnelle des protéines › Role of the putative PKC phosphorylation sites...
questionsmedicales.fr › Phénomènes chimiques › Phénomènes biochimiques › Stabilité protéique › Role of the putative PKC phosphorylation sites...
questionsmedicales.fr › Phénomènes physiologiques des appareils urinaire et reproducteur › Phénomènes physiologiques des voies urinaires › Capacité de concentration rénale › Réabsorption rénale › Role of the putative PKC phosphorylation sites...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines membranaires › Protéines de transport membranaire › Protéines transporteurs de solutés › Cotransporteurs sodium-phosphate de type II › Cotransporteurs sodium-phosphate de type IIa › Role of the putative PKC phosphorylation sites...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines membranaires › Protéines de transport membranaire › Protéines transporteurs de solutés › Cotransporteurs sodium-phosphate de type II › Cotransporteurs sodium-phosphate de type IIc › Role of the putative PKC phosphorylation sites...
questionsmedicales.fr › Phénomènes physiques › Temps › Facteurs temps › Role of the putative PKC phosphorylation sites...
questionsmedicales.fr › Eucaryotes › Animaux › Chordés › Vertébrés › Amphibiens › Anura › Pipidae › Xenopus › Role of the putative PKC phosphorylation sites...