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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

HMG-box transcription factor 1

HBP1, GPIHBP1
Dietary fats are packaged by intestine into triglyceride-rich lipoproteins called chylomicrons. The triglycerides in chylomicrons are hydrolyzed by lipoprotein lipase (LPL: MIM 609708) along the luminal surface of capillaries, mainly in heart, skeletal muscle, and adipose tissue. GPIHBP1 is a capillary endothelial cell protein that provides a platform for LPL-mediated processing of chylomicrons (Beigneux et al., 2007 [PubMed 17403372]).[supplied by OMIM, Apr 2009] (from NCBI)
Top mentioned proteins: Lipoprotein Lipase, HAD, ACID, CAN, APOA5
Papers on HBP1
Absence of AMPKα2 accelerates cellular senescence via p16 induction in mouse embryonic fibroblasts.
New
Song et al., Atlanta, United States. In Int J Biochem Cell Biol, Feb 2016
Interestingly, knockdown of HMG box-containing protein 1 (HBP1) partially blocked the cellular senescence of AMPKα2-deleted MEFs via the reduction of p16.
MicroRNA-155 enhances the activation of Wnt/β-catenin signaling in colorectal carcinoma by suppressing HMG-box transcription factor 1.
New
Zhang et al., Changchun, China. In Mol Med Report, Feb 2016
HMG‑box transcription factor 1 (HBP1) was identified as a novel target of miR‑155, which mediated its effect on CRC via the Wnt/β‑catenin pathway.
The acidic domain of the endothelial membrane protein GPIHBP1 stabilizes lipoprotein lipase activity by preventing unfolding of its catalytic domain.
New
Ploug et al., Copenhagen, Denmark. In Elife, Feb 2016
UNASSIGNED: GPIHBP1 is a glycolipid-anchored membrane protein of capillary endothelial cells that binds lipoprotein lipase (LPL) within the interstitial space and shuttles it to the capillary lumen.
A novel APOC2 gene mutation identified in a Chinese patient with severe hypertriglyceridemia and recurrent pancreatitis.
New
Gao et al., Shanghai, China. In Lipids Health Dis, Dec 2015
The coding regions of 5 candidate genes (namely LPL, APOC2, APOA5, LMF1, and GPIHBP1) were sequenced using genomic DNA from peripheral leucocytes.
Update on the molecular biology of dyslipidemias.
Review
New
Ramasamy, Worcester, United Kingdom. In Clin Chim Acta, Dec 2015
Monogenic hypertriglyceridemia is the result of mutations in genes that regulate the metabolism of triglyceride rich lipoproteins (eg LPL, APOC2, APOA5, LMF1, GPIHBP1).
A complex phenotype in a child with familial HDL deficiency due to a novel frameshift mutation in APOA1 gene (apoA-IGuastalla).
New
Bertolini et al., Genova, Italy. In J Clin Lipidol, Nov 2015
We sequenced the candidate genes for HTG (LPL, APOC2, APOA5, GPIHBP1, LMF1) and HDL deficiency (LCAT, ABCA1 and APOA1), analyzed HDL subpopulations, measured cholesterol efflux capacity (CEC) of sera and constructed a model of the mutant apoA-I.
Intrinsic and extrinsic regulation of cardiac lipoprotein lipase following diabetes.
Review
New
Rodrigues et al., Vancouver, Canada. In Biochim Biophys Acta, Feb 2015
Diabetes also increased the expression of glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1 (GPIHBP1) in EC, which mediates the transport of LPL across EC.
MYC through miR-17-92 suppresses specific target genes to maintain survival, autonomous proliferation, and a neoplastic state.
Impact
Felsher et al., Stanford, United States. In Cancer Cell, 2014
Here we report that MYC via miR-17-92 maintains a neoplastic state through the suppression of chromatin regulatory genes Sin3b, Hbp1, Suv420h1, and Btg1, as well as the apoptosis regulator Bim.
Physiological regulation of lipoprotein lipase.
Review
Kersten, Wageningen, Netherlands. In Biochim Biophys Acta, 2014
Upon production by the underlying parenchymal cells, LPL is transported and attached to the capillary endothelium by the protein GPIHBP1.
The GPIHBP1-LPL complex is responsible for the margination of triglyceride-rich lipoproteins in capillaries.
Impact
Fong et al., Los Angeles, United States. In Cell Metab, 2014
Triglyceride-rich lipoproteins (TRLs) undergo lipolysis by lipoprotein lipase (LPL), an enzyme that is transported to the capillary lumen by an endothelial cell protein, GPIHBP1.
[Research advances in the effects of excise and diet on LPL and its mechanism].
Review
Wang et al., In Sheng Li Ke Xue Jin Zhan, 2014
The expression and activity of LPL are regulated by multiple factors, such as hormones, nutrition, exercise, PPARgamma, apolipoproteins, glycosylphosphatidylinositol-anchored high-density lipoprotein-binding protein 1 (GPIHBP1) and angiopoietin-like proteins (ANGPTL).
[Primary hyperchylomicronemia].
Review
Yamashita, Ōsaka, Japan. In Nihon Rinsho, 2013
More recently, patients with primary hyperchylomicronemia caused by mutations in the gene for glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1(GPIHBP1) or lipase maturation factor 1(LMF1).
Mutations in LPL, APOC2, APOA5, GPIHBP1 and LMF1 in patients with severe hypertriglyceridaemia.
GeneRIF
Dallinga-Thie et al., Amsterdam, Netherlands. In J Intern Med, 2012
Mutations in GPIHBP1 are rare but the associated clinical phenotype of hypertriglyceridaemia is severe.
Deletion of GPIHBP1 causing severe chylomicronemia.
GeneRIF
Hobbs et al., Dallas, United States. In J Inherit Metab Dis, 2012
analysis of a neonate with complete GPIHBP1 deficiency due to homozygosity for a deletion of GPIHBP1 [case report]
Effects of hyperinsulinemia on lipoprotein lipase, angiopoietin-like protein 4, and glycosylphosphatidylinositol-anchored high-density lipoprotein binding protein 1 in subjects with and without type 2 diabetes mellitus.
GeneRIF
Eriksson et al., Umeå, Sweden. In Metabolism, 2012
Expression of glycosylphosphatidylinositol-anchored high-density lipoprotein binding protein 1 tended to be higher in young healthy subjects than in subjects with type 2 diabetes mellitus or Colder control subjects
GPIHBP1, an endothelial cell transporter for lipoprotein lipase.
Review
GeneRIF
Beigneux et al., Los Angeles, United States. In J Lipid Res, 2011
function and genetics of GPIHBP1 in lipoprotein lipase transport
GPIHBP1 C89F neomutation and hydrophobic C-terminal domain G175R mutation in two pedigrees with severe hyperchylomicronemia.
GeneRIF
Marçais et al., Bron, France. In J Clin Endocrinol Metab, 2011
we first report a mutation of the hydrophobic C-terminal domain that impairs GPIHBP1 membrane targeting
GPIHBP1 is responsible for the entry of lipoprotein lipase into capillaries.
Impact
GeneRIF
Fong et al., Los Angeles, United States. In Cell Metab, 2010
GPIHBP1 is located at the basolateral surface of capillary endothelial cells and actively transports LPL across endothelial cells.
GPIHBP1: lipoprotein lipase's ticket to ride.
Impact
Fisher, New York City, United States. In Cell Metab, 2010
In this issue, Davies et al. (2010) report that GPIHBP1 is required for LPL transcytosis from the basolateral to apical capillary endothelial surface.
Glycosylphosphatidylinositol-anchored high-density lipoprotein-binding protein 1 plays a critical role in the lipolytic processing of chylomicrons.
Impact
GeneRIF
Young et al., Oakland, United States. In Cell Metab, 2007
GPIHBP1 is an important platform for the LpL-mediated processing of chylomicrons in capillaries.
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