Evidence map›Paper›PMID 28548960›Full record

ArticleOncotarget2017

Severe hypertriglyceridemia due to two novel loss-of-function lipoprotein lipase gene mutations (C310R/E396V) in a Chinese family associated with recurrent acute pancreatitis.

Yu Lun, Xiaofang Sun, Ping Wang, Jingwei Chi, Xu Hou, Yangang Wang

Open access · diamondAbstract readCase Reports
In one paragraph

Article in Oncotarget, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.7field-weighted citation impact, top 27% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

8 citing papers in PubMed, 14 citations in OpenAlex.

  1. Review
  2. Loss-of-Function Homozygous Variant inKidney international reports · 2023
    Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 1 country.

Yu LunDepartment of Endocrinology and Metabolic Diseases, The Affiliated Hospital of Qingdao University, Qingdao, China.
Xiaofang SunDepartment of Endocrinology and Metabolic Diseases, The Affiliated Hospital of Qingdao University, Qingdao, China.
Ping WangDepartment of Endocrinology and Metabolic Diseases, The Affiliated Hospital of Qingdao University, Qingdao, China.
Jingwei ChiDepartment of Endocrinology and Metabolic Diseases, The Affiliated Hospital of Qingdao University, Qingdao, China.
Xu HouDepartment of Endocrinology and Metabolic Diseases, The Affiliated Hospital of Qingdao University, Qingdao, China.
Yangang WangDepartment of Endocrinology and Metabolic Diseases, The Affiliated Hospital of Qingdao University, Qingdao, China.
Affiliated Hospital of Qingdao University · CNQingdao University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lipoprotein lipase (LPL) is widely expressed in skeletal muscles, cardiac muscles as well as adipose tissue and involved in the catabolism of triglyceride. Herein we have systematically characterized two novel loss-of-function mutations in LPL from a Chinese family in which afflicted members were manifested by severe hypertriglyceridemia and recurrent pancreatitis. DNA sequencing revealed that the proband was a heterozygote carrying a novel c.T928C (p.C310R) mutation in exon 6 of the LPL gene. Another member of the family was detected to be a compound heterozygote who along with the c.T928C mutation also carried a novel missense mutation c.A1187T (p.E396V) in exon 8 of the LPL gene. Furthermore, COS-1 cells were transfected with lentiviruses containing the mutant LPL genes. While C310R markedly reduced the overall LPL protein level, COS-1 cells carrying E396V or double mutations contained similar overall LPL protein levels to the wild-type. The specific activity of the LPL mutants remained at comparable magnitude to the wild-type. However, few LPL were detected in the culture medium for the mutants, suggesting that both mutations caused aberrant triglyceride catabolism. More specifically, E396V and double mutations dampened the transport of LPL to the cell surface, while for the C310R mutation, reducing LPL protein level might be involved. By characterizing these two novel LPL mutations, this study has expanded our understanding on the pathogenesis of familial hypertriglyceridemia (FHTG).

Indexed as

Amino Acid SubstitutionLoss of Function MutationAcute DiseaseAnimalsAsian PeopleChinaChlorocebus aethiopsCOS CellsDNA Mutational AnalysisFamilyFemaleHumansHypertriglyceridemiaLipidsLipoprotein LipaseMaleLipidsLipoprotein Lipaseacute pancreatitiscompound heterozygosityhypertriglyceridemialipoprotein lipasemutation

Identifiers

PMID28548960
PMCPMC5564601
OpenAlexW2613023673

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.