Mechanisms Regulating Muscle Protein Synthesis in CKD.


Journal

Journal of the American Society of Nephrology : JASN
ISSN: 1533-3450
Titre abrégé: J Am Soc Nephrol
Pays: United States
ID NLM: 9013836

Informations de publication

Date de publication:
11 2020
Historique:
received: 10 12 2019
accepted: 21 06 2020
pubmed: 9 8 2020
medline: 10 3 2021
entrez: 9 8 2020
Statut: ppublish

Résumé

CKD induces loss of muscle proteins partly by suppressing muscle protein synthesis. Muscles of mice with CKD have increased expression of nucleolar protein 66 (NO66), as do muscle biopsy specimens from patients with CKD or those undergoing hemodialysis. Inflammation stimulates NO66 expression and changes in NF- Subtotal nephrectomy created a mouse model of CKD with BUN >80 mg/dl. Crossing NO66 Muscle-specific NO66 knockout in mice blocks CKD-induced loss of muscle mass and improves protein synthesis. NO66 suppression of ribosomal biogenesis CKD suppresses muscle protein synthesis

Sections du résumé

BACKGROUND
CKD induces loss of muscle proteins partly by suppressing muscle protein synthesis. Muscles of mice with CKD have increased expression of nucleolar protein 66 (NO66), as do muscle biopsy specimens from patients with CKD or those undergoing hemodialysis. Inflammation stimulates NO66 expression and changes in NF-
METHODS
Subtotal nephrectomy created a mouse model of CKD with BUN >80 mg/dl. Crossing NO66
RESULTS
Muscle-specific NO66 knockout in mice blocks CKD-induced loss of muscle mass and improves protein synthesis. NO66 suppression of ribosomal biogenesis
CONCLUSIONS
CKD suppresses muscle protein synthesis

Identifiants

pubmed: 32764136
pii: ASN.2019121277
doi: 10.1681/ASN.2019121277
pmc: PMC7608956
doi:

Substances chimiques

DNA, Ribosomal 0
Histones 0
IL6 protein, human 0
Interleukin-6 0
Muscle Proteins 0
NF-kappa B 0
RNA, Messenger 0
Tripartite Motif Proteins 0
Tumor Necrosis Factor-alpha 0
histone H3 trimethyl Lys4 0
Interferon-gamma 82115-62-6
Dioxygenases EC 1.13.11.-
Histone Demethylases EC 1.14.11.-
Jumonji Domain-Containing Histone Demethylases EC 1.14.11.-
nucleolar protein 66, mouse EC 1.14.11.-
RIOX1 protein, human EC 1.14.11.27
FBXO32 protein, human EC 2.3.2.27
SKP Cullin F-Box Protein Ligases EC 2.3.2.27
TRIM63 protein, human EC 2.3.2.27
Ubiquitin-Protein Ligases EC 2.3.2.27

Types de publication

Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

2573-2587

Subventions

Organisme : NIDDK NIH HHS
ID : R01 DK037175
Pays : United States
Organisme : NHLBI NIH HHS
ID : R01 HL147108
Pays : United States
Organisme : NIDDK NIH HHS
ID : P30 DK079638
Pays : United States

Commentaires et corrections

Type : CommentIn
Type : ErratumIn

Informations de copyright

Copyright © 2020 by the American Society of Nephrology.

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Auteurs

Liping Zhang (L)

Nephrology Division, Department of Medicine, Baylor College of Medicine, Houston, Texas lipingz@bcm.edu.

Qin Chen (Q)

Department of Epigenetics and Molecular Carcinogenesis, The University of Texas MD Anderson Cancer Center, Houston, Texas.

Zihong Chen (Z)

Nephrology Division, Department of Medicine, Baylor College of Medicine, Houston, Texas.

Ying Wang (Y)

Nephrology Division, Department of Medicine, Baylor College of Medicine, Houston, Texas.

Jorge L Gamboa (JL)

Department of Medicine, Vanderbilt University Medical Center, Nashville, Tennessee.

Talat Alp Ikizler (TA)

Department of Medicine, Vanderbilt University Medical Center, Nashville, Tennessee.

Giacomo Garibotto (G)

Nephrology Division, Department of Internal Medicine, Genoa University, Scientific Hospitalization and Treatment Institute Policlinico San Martino Hospital, Genoa, Italy.

William E Mitch (WE)

Nephrology Division, Department of Medicine, Baylor College of Medicine, Houston, Texas.

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Classifications MeSH