"Perilipin-1" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
A lipid droplet protein that is expressed primarily by ADIPOCYTES of WHITE ADIPOSE TISSUE and BROWN ADIPOSE TISSUE. It co-localizes with MACROPHAGES and FOAM CELLS of artherosclerotic lesions and stabilizes LIPID DROPLETS by inhibiting HORMONE SENSITIVE LIPASE. It may also protect TRIGLYCERIDES against hydrolysis within the PLASMA MEMBRANE and modulate CHOLESTEROL ESTER HYDROLASE activity.
Descriptor ID |
D000070778
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MeSH Number(s) |
D12.776.157.464.500.500
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Concept/Terms |
Perilipin-1- Perilipin-1
- Perilipin 1
- Perilipin A Protein
- Protein, Perilipin A
- PERI Protein
- Protein, PERI
- Perilipin
- Perilipin B Protein
- Protein, Perilipin B
- Perilipin Protein
- Protein, Perilipin
- Plin Protein
- Protein, Plin
|
Below are MeSH descriptors whose meaning is more general than "Perilipin-1".
Below are MeSH descriptors whose meaning is more specific than "Perilipin-1".
This graph shows the total number of publications written about "Perilipin-1" by people in this website by year, and whether "Perilipin-1" was a major or minor topic of these publications.
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Year | Major Topic | Minor Topic | Total |
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2006 | 0 | 1 | 1 |
2007 | 0 | 1 | 1 |
2009 | 0 | 1 | 1 |
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Below are the most recent publications written about "Perilipin-1" by people in Profiles.
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Variation in the perilipin gene (PLIN) affects glucose and lipid metabolism in non-Hispanic white women with and without polycystic ovary syndrome. Diabetes Res Clin Pract. 2009 Dec; 86(3):186-92.
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Role of adipocyte-derived apoE in modulating adipocyte size, lipid metabolism, and gene expression in vivo. Am J Physiol Endocrinol Metab. 2009 May; 296(5):E1110-9.
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Perilipin regulates the thermogenic actions of norepinephrine in brown adipose tissue. J Lipid Res. 2007 Jun; 48(6):1273-9.
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Perilipin promotes hormone-sensitive lipase-mediated adipocyte lipolysis via phosphorylation-dependent and -independent mechanisms. J Biol Chem. 2006 Jun 09; 281(23):15837-44.