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    Gpihbp1 GPI-anchored HDL-binding protein 1 [ Mus musculus (house mouse) ]

    Gene ID: 68453, updated on 9-Dec-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    AAV-mediated hepatic LPL expression ameliorates severe hypertriglyceridemia and acute pancreatitis in Gpihbp1 deficient mice and rats.

    AAV-mediated hepatic LPL expression ameliorates severe hypertriglyceridemia and acute pancreatitis in Gpihbp1 deficient mice and rats.
    Yuan C, Xu Y, Lu G, Hu Y, Mao W, Ke L, Tong Z, Xia Y, Ma S, Dong X, Xian X, Wu X, Liu G, Li B, Li W.,

    01/11/2024
    Severe hypertriglyceridemia caused by Gpihbp1 deficiency facilitates vascular remodeling through increasing endothelial activation and oxidative stress.

    Severe hypertriglyceridemia caused by Gpihbp1 deficiency facilitates vascular remodeling through increasing endothelial activation and oxidative stress.
    Fan R, An X, Wang Y, Zhang J, Liu S, Bai J, Li J, Lin Q, Xie Y, Xia Y, Liao J.

    06/1/2023
    GPIHBP1, a partner protein for lipoprotein lipase, is expressed only in capillary endothelial cells.

    GPIHBP1, a partner protein for lipoprotein lipase, is expressed only in capillary endothelial cells.
    Meng X, Zeng W, Young SG, Fong LG., Free PMC Article

    07/24/2021
    The reduced expression of GPIHBP1 was insufficient to prevent LPL from reaching the capillary lumen, and it did not lead to hypertriglyceridemia-even when mice were fed a high-fat diet.

    An upstream enhancer regulates Gpihbp1 expression in a tissue-specific manner.
    Allan CM, Heizer PJ, Tu Y, Sandoval NP, Jung RS, Morales JE, Sajti E, Troutman TD, Saunders TL, Cusanovich DA, Beigneux AP, Romanoski CE, Fong LG, Young SG., Free PMC Article

    07/4/2020
    Gpihbp1 deficiency accelerates the development of atherosclerosis in the aorta, and the instability of plaques in Ldlr knockout mice and diabetes promotes these pathologic processes with coronary atherosclerosis

    Gpihbp1 deficiency accelerates atherosclerosis and plaque instability in diabetic Ldlr(-/-) mice.
    Liu X, Li J, Liao J, Wang H, Huang X, Dong Z, Shen Q, Zhang L, Wang Y, Kong W, Liu G, Huang W.

    05/16/2020
    GPIHBP1 expression in gliomas facilitates triglyceride-rich lipoproteins processing and provides a source of lipid nutrients for glioma cells.

    GPIHBP1 expression in gliomas promotes utilization of lipoprotein-derived nutrients.
    Hu X, Matsumoto K, Jung RS, Weston TA, Heizer PJ, He C, Sandoval NP, Allan CM, Tu Y, Vinters HV, Liau LM, Ellison RM, Morales JE, Baufeld LJ, Bayley NA, He L, Betsholtz C, Beigneux AP, Nathanson DA, Gerhardt H, Young SG, Fong LG, Jiang H., Free PMC Article

    02/22/2020
    GPIHBP1-independent pathway for clearance of plasma TGs in Angptl4(-/-)Gpihbp1(-/-) mice

    Novel GPIHBP1-independent pathway for clearance of plasma TGs in Angptl4(-/-)Gpihbp1(-/-) mice.
    Cushing EM, Sylvers KL, Chi X, Shetty SK, Davies BSJ., Free PMC Article

    08/24/2019
    we assessed visceral adipose tissue GPIHBP1 protein expression in type 2 diabetes Lepr db/db mouse model as well as in subjects with ranging levels of insulin resistance. We report that insulin reduces the expression of GPIHBP1 protein in HMVECs. Furthermore, GPIHBP1 protein expression in visceral adipose tissue in Lepr db/db mice is significantly reduced as is the active monomeric form of GPIHBP1 as compared to Leprdb/m

    Decreased GPIHBP1 protein levels in visceral adipose tissue partly underlie the hypertriglyceridemic phenotype in insulin resistance.
    Surendran RP, Udayyapan SD, Clemente-Postigo M, Havik SR, Schimmel AWM, Tinahones F, Nieuwdorp M, Dallinga-Thie GM., Free PMC Article

    04/6/2019
    the negatively charged IDR of GPIHBP1 traverses a vast space, facilitating capture of LPL by capillary endothelial cells and simultaneously contributing to GPIHBP1's ability to preserve LPL structure and activity.

    A disordered acidic domain in GPIHBP1 harboring a sulfated tyrosine regulates lipoprotein lipase.
    Kristensen KK, Midtgaard SR, Mysling S, Kovrov O, Hansen LB, Skar-Gislinge N, Beigneux AP, Kragelund BB, Olivecrona G, Young SG, Jørgensen TJD, Fong LG, Ploug M., Free PMC Article

    09/8/2018
    mutation of a conserved cysteine in GPIHBP1 abolishes the ability of GPIHBP1 to bind LPL

    Mutating a conserved cysteine in GPIHBP1 reduces amounts of GPIHBP1 in capillaries and abolishes LPL binding.
    Allan CM, Jung CJ, Larsson M, Heizer PJ, Tu Y, Sandoval NP, Dang TLP, Jung RS, Beigneux AP, de Jong PJ, Fong LG, Young SG., Free PMC Article

    03/10/2018
    LPL moved quickly from heparan sulfate proteoglycans (HSPGs) on adipocytes to GPIHBP1-coated beads, thereby depleting LPL stores on the surface of adipocytes. We conclude that HSPG-bound LPL in the interstitial spaces of tissues is mobile, allowing the LPL to move to GPIHBP1 on endothelial cells

    Mobility of "HSPG-bound" LPL explains how LPL is able to reach GPIHBP1 on capillaries.
    Allan CM, Larsson M, Jung RS, Ploug M, Bensadoun A, Beigneux AP, Fong LG, Young SG., Free PMC Article

    08/26/2017
    An LPL structural model suggests that the LPL S447X truncation exposes residues implicated in LPL binding to lipoprotein binding uptake receptors, such as GPIHBP1.

    Biochemical Analysis of the Lipoprotein Lipase Truncation Variant, LPL(S447X), Reveals Increased Lipoprotein Uptake.
    Hayne CK, Lafferty MJ, Eglinger BJ, Kane JP, Neher SB., Free PMC Article

    05/20/2017
    Laminin regulates PDGFRbeta cell differentiation, fate determination, cell stemness and muscle development via gpihbp1.

    Laminin regulates PDGFRβ(+) cell stemness and muscle development.
    Yao Y, Norris EH, Mason CE, Strickland S., Free PMC Article

    09/10/2016
    the two domains of GPIHBP1 interact independently with LPL and the functionality of LPL depends on its localization on GPIHBP1

    Evidence for Two Distinct Binding Sites for Lipoprotein Lipase on Glycosylphosphatidylinositol-anchored High Density Lipoprotein-binding Protein 1 (GPIHBP1).
    Reimund M, Larsson M, Kovrov O, Kasvandik S, Olivecrona G, Lookene A., Free PMC Article

    08/22/2015
    TRL margination depends on LPL bound to GPIHBP1.

    The GPIHBP1-LPL complex is responsible for the margination of triglyceride-rich lipoproteins in capillaries.
    Goulbourne CN, Gin P, Tatar A, Nobumori C, Hoenger A, Jiang H, Grovenor CR, Adeyo O, Esko JD, Goldberg IJ, Reue K, Tontonoz P, Bensadoun A, Beigneux AP, Young SG, Fong LG., Free PMC Article

    01/3/2015
    In adipose tissue, Gpihbp1 levels increases rapidly during fasting, when lipoprotein lipase activity decreases.

    Linking nutritional regulation of Angptl4, Gpihbp1, and Lmf1 to lipoprotein lipase activity in rodent adipose tissue.
    Kroupa O, Vorrsjö E, Stienstra R, Mattijssen F, Nilsson SK, Sukonina V, Kersten S, Olivecrona G, Olivecrona T., Free PMC Article

    10/26/2013
    Neither a high fat diet nor fasting/re-feeding markedly altered the distribution pattern of LPL or GPIHBP1 in mouse pancreas.

    Localization of lipoprotein lipase and GPIHBP1 in mouse pancreas: effects of diet and leptin deficiency.
    Nyrén R, Chang CL, Lindström P, Barmina A, Vorrsjö E, Ali Y, Juntti-Berggren L, Bensadoun A, Young SG, Olivecrona T, Olivecrona G., Free PMC Article

    07/6/2013
    The GPIHBP1 and LPL move bidirectionally across endothelial cells in vesicles and that transport is efficient even when caveolin-1 is absent.

    Assessing mechanisms of GPIHBP1 and lipoprotein lipase movement across endothelial cells.
    Davies BS, Goulbourne CN, Barnes RH 2nd, Turlo KA, Gin P, Vaughan S, Vaux DJ, Bensadoun A, Beigneux AP, Fong LG, Young SG., Free PMC Article

    04/27/2013
    analysis of glycosylphosphatidylinositol-anchored HDL-binding protein 1 (GPIHBP1) expression in mouse tissues revealed by positron emission tomography scanning

    Unexpected expression pattern for glycosylphosphatidylinositol-anchored HDL-binding protein 1 (GPIHBP1) in mouse tissues revealed by positron emission tomography scanning.
    Olafsen T, Young SG, Davies BS, Beigneux AP, Kenanova VE, Voss C, Young G, Wong KP, Barnes RH 2nd, Tu Y, Weinstein MM, Nobumori C, Huang SC, Goldberg IJ, Bensadoun A, Wu AM, Fong LG., Free PMC Article

    01/15/2011
    Intravenously injected apoA-V rHDL significantly lowers plasma TG in an apoA-V deficient mouse model and requires gpihbp1.

    Intravenous injection of apolipoprotein A-V reconstituted high-density lipoprotein decreases hypertriglyceridemia in apoav-/- mice and requires glycosylphosphatidylinositol-anchored high-density lipoprotein-binding protein 1.
    Shu X, Nelbach L, Weinstein MM, Burgess BL, Beckstead JA, Young SG, Ryan RO, Forte TM., Free PMC Article

    01/1/2011
    GPIHBP1 is located at the basolateral surface of capillary endothelial cells and actively transports LPL across endothelial cells.

    GPIHBP1 is responsible for the entry of lipoprotein lipase into capillaries.
    Davies BS, Beigneux AP, Barnes RH 2nd, Tu Y, Gin P, Weinstein MM, Nobumori C, Nyrén R, Goldberg I, Olivecrona G, Bensadoun A, Young SG, Fong LG., Free PMC Article

    10/30/2010
    Like ANGPTL4, ANGPTL3 inhibited nonstabilized LPL but not GPIHBP1-stabilized LPL

    GPIHBP1 stabilizes lipoprotein lipase and prevents its inhibition by angiopoietin-like 3 and angiopoietin-like 4.
    Sonnenburg WK, Yu D, Lee EC, Xiong W, Gololobov G, Key B, Gay J, Wilganowski N, Hu Y, Zhao S, Schneider M, Ding ZM, Zambrowicz BP, Landes G, Powell DR, Desai U., Free PMC Article

    03/29/2010
    GPIHBP1 is required for the lipolytic processing of both apo-B48- and apo-B100-containing lipoproteins

    Chylomicronemia elicits atherosclerosis in mice--brief report.
    Weinstein MM, Yin L, Tu Y, Wang X, Wu X, Castellani LW, Walzem RL, Lusis AJ, Fong LG, Beigneux AP, Young SG., Free PMC Article

    01/21/2010
    a structurally intact Ly6 domain (in addition to the acidic domain) in GPIHBP1 is essential for LPL binding

    Highly conserved cysteines within the Ly6 domain of GPIHBP1 are crucial for the binding of lipoprotein lipase.
    Beigneux AP, Gin P, Davies BS, Weinstein MM, Bensadoun A, Fong LG, Young SG., Free PMC Article

    01/21/2010
    Gpihbp1 transcript levels in brown and white adipose tissue were lower in endothelial cell PPARgamma knockout mice than in littermate control mice, suggesting that PPARgamma regulates Gpihbp1 expression in vivo. (GPIHBP1)

    The expression of GPIHBP1, an endothelial cell binding site for lipoprotein lipase and chylomicrons, is induced by peroxisome proliferator-activated receptor-gamma.
    Davies BS, Waki H, Beigneux AP, Farber E, Weinstein MM, Wilpitz DC, Tai LJ, Evans RM, Fong LG, Tontonoz P, Young SG., Free PMC Article

    01/21/2010
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