ArticleJournal of molecular and cellular cardiology2010
Natriuretic peptide pharmacogenetics: membrane metallo-endopeptidase (MME): common gene sequence variation, functional characterization and degradation.
Article in Journal of molecular and cellular cardiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
18 citing papers in PubMed, 27 citations in OpenAlex.
- Circulating Neprilysin in Patients With Heart Failure and Preserved Ejection Fraction.JACC. Heart failure · 2020Trial
- Circulating atrial natriuretic peptide genetic association study identifies a novel gene cluster associated with stroke in whites.Circulation. Cardiovascular genetics · 2015Trial
- Maltol Improves Peripheral Nerve Function by Inhibiting Schwann Cell Apoptosis via the PERK/eIF2α/CHOP Pathway and MME Upregulation in Diabetic Peripheral Neuropathy.Pharmaceuticals (Basel, Switzerland) · 2024Article
- Functional mutation, splice, distribution, and divergence analysis of impactful genes associated with heart failure and other cardiovascular diseases.Scientific reports · 2023Article
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- Association between soluble neprilysin and diabetes: Findings from a prospective longitudinal study.Frontiers in endocrinology · 2023Article
- Effects of intramuscular fat on meat quality and its regulation mechanism in Tan sheep.Frontiers in nutrition · 2022Article
- Soluble Neprilysin in the General Population: Clinical Determinants and Its Relationship to Cardiovascular Disease.Journal of the American Heart Association · 2019Article
- Beneficial effects of sacubitril/valsartan in heart failure with reduced ejection fraction: pas à cause du BNP?European journal of heart failure · 2019Article
- Pharmacogenomic Next-Generation DNA Sequencing: Lessons from the Identification and Functional Characterization of Variants of Unknown Significance inDrug metabolism and disposition: the biological fate of chemicals · 2019Article
- Pharmacogenomics of the Natriuretic Peptide System in Heart Failure.Current heart failure reports · 2017Review
- Chronic heart failure as a state of reduced effectiveness of the natriuretic peptide system: implications for therapy.European journal of heart failure · 2017Review
- Practical Pharmacogenomic Approaches to Heart Failure Therapeutics.Current treatment options in cardiovascular medicine · 2016Review
- Rare Variants Association Analysis in Large-Scale Sequencing Studies at the Single Locus Level.PLoS computational biology · 2016Article
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- Article
- Natriuretic peptide receptor-3 gene (NPR3): nonsynonymous polymorphism results in significant reduction in protein expression because of accelerated degradation.Circulation. Cardiovascular genetics · 2013Article
Corrections and comments
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Authors and funding
9 authors at 4 institutions in 2 countries.
Funding
Abstract
Membrane metallo-endopeptidase (MME), also known as neutral endopeptidase 24.11 (EC 3.4.24.11), is involved in the metabolism of natriuretic peptides that play a key role in modulating cardiac structure and function. Common genetic variation in MME has not been addressed by resequencing the gene using DNA from different ethnic populations. We set out to identify and functionally characterize common genetic variation in MME in three ethnic groups. DNA samples from 96 European-American, 96 African-American, and 96 Han Chinese-American healthy subjects were used to resequence MME. Ninety polymorphisms, 65 novel, were identified, including 8 nonsynonymous single nucleotide polymorphisms (nsSNPs). Expression constructs for the nsSNPs were created and COS-1 cells were transfected with constructs for wild type (WT) and variant allozymes. Recombinant proteins were analyzed by quantitative Western blot analysis and by a one-step fluorometric assay. A significant reduction in enzyme activity (21% of WT) and immunoreactive protein (29% of WT) for the Val73 variant allozyme was observed. Proteasome-mediated degradation and autophagy participated in the degradation of this variant allozyme. The chaperone proteins, BiP and GRP94, were upregulated after transfection with Val73 MME, suggesting protein misfolding, compatible with conclusions based on the MME X-ray crystal structure. Multiple novel polymorphisms of MME were identified in three ethnic groups. The Val73 variant allozyme displayed a significant decrease in MME protein quantity and activity, with degradation mediated by both proteasome and autophagy pathways. This polymorphism could have a significant effect on the metabolism of natriuretic peptides.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.