ArticleBiochemical and biophysical research communications2014
Purification, cellular levels, and functional domains of lipase maturation factor 1.
Article in Biochemical and biophysical research communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 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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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.
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Who cites it
7 citing papers in PubMed, 10 citations in OpenAlex.
- LMF1 frameshift deletion in Franches-Montagnes horses with hypertriglyceridemia-induced pancreatitis.Scientific reports · 2025Article
- Genome-wide association studies of egg production traits by whole genome sequencing of Laiwu Black chicken.Poultry science · 2024Article
- The role of lipase maturation factor 1 in hypertriglyceridaemia and atherosclerosis: An update.SAGE open medicine · 2024Review
- Assessment of Zinc- alpha2 glycoprotein (ZAG) and Lipase Maturation Factor 1 (LMF1) concentration in children with chronic kidney disease.Physiological research · 2021Article
- Endoplasmic reticulum quality control in lipoprotein metabolism.Molecular and cellular endocrinology · 2019Review
- A Compound Heterozygous Mutation of Lipase Maturation Factor 1 is Responsible for Hypertriglyceridemia of a Patient.Journal of atherosclerosis and thrombosis · 2019Article
- Lipase maturation factor 1 affects redox homeostasis in the endoplasmic reticulum.The EMBO journal · 2018Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Over a third of the US adult population has hypertriglyceridemia, resulting in an increased risk of atherosclerosis, pancreatitis, and metabolic syndrome. Lipoprotein lipase (LPL), a dimeric enzyme, is the main lipase responsible for TG clearance from the blood after food intake. LPL requires an endoplasmic reticulum (ER)-resident, transmembrane protein known as lipase maturation factor 1 (LMF1) for secretion and enzymatic activity. LMF1 is believed to act as a client specific chaperone for dimeric lipases, but the precise mechanism by which LMF1 functions is not understood. Here, we examine which domains of LMF1 contribute to dimeric lipase maturation by assessing the function of truncation variants. N-terminal truncations of LMF1 show that all the domains are necessary for LPL maturation. Fluorescence microscopy and protease protection assays confirmed that these variants were properly oriented in the ER. We measured cellular levels of LMF1 and found that it is expressed at low levels and each molecule of LMF1 promotes the maturation of 50 or more molecules of LPL. Thus we provide evidence for the critical role of the N-terminus of LMF1 for the maturation of LPL and relevant ratio of chaperone to substrate.
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Registered trials
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