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Mutation of conserved cysteines in the Ly6 domain of GPIHBP1 in familial chylomicronemia.
Open accessAbstract
We investigated a family from northern Sweden in which three of four siblings have congenital chylomicronemia. LPL activity and mass in pre- and postheparin plasma were low, and LPL release into plasma after heparin injection was delayed. LPL activity and mass in adipose tissue biopsies appeared normal. [(35)S]Methionine incorporation studies on adipose tissue showed that newly synthesized LPL was normal in size and normally glycosylated. Breast milk from the affected female subjects contained normal to elevated LPL mass and activity levels. The milk had a lower than normal milk lipid content, and the fatty acid composition was compatible with the milk lipids being derived from de novo lipogenesis, rather than from the plasma lipoproteins. Given the delayed release of LPL into the plasma after heparin, we suspected that the chylomicronemia might be caused by mutations in GPIHBP1. Indeed, all three affected siblings were compound heterozygotes for missense mutations involving highly conserved cysteines in the Ly6 domain of GPIHBP1 (C65S and C68G). The mutant GPIHBP1 proteins reached the surface of transfected Chinese hamster ovary cells but were defective in their ability to bind LPL (as judged by both cell-based and cell-free LPL binding assays). Thus, the conserved cysteines in the Ly6 domain are crucial for GPIHBP1 function.
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“Defective lipolysis occurs with genetic defects in LpL; defects in apoC-II; defective association of LpL with the vascular wall due to antibodies to heparin or defects in glycosylphosphatidylinositol-anchored high-density lipoprotein-binding protein 1, an LpL-binding protein (75, 76); or defective intracellular LpL processing due to mutated lipase maturation factor 1 (77).”
From Evaluation and Treatment of Hypertriglyceridemia: An Endocrine Society Clinical Practice Guideline (2012) · cites this paper as [76]
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GPIHBP1 Is Responsible for the Entry of Lipoprotein Lipase into Capillaries
Davies, B. S. J., Beigneux, A. P., Barnes, R. H., Tu, Y., Gin, P., Weinstein, M. M., Nobumori, C., Nyrén, R., Goldberg, I., Olivecrona, G., et al. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2010.04.016 · Cited by 342
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Self-citationChylomicronaemia–current diagnosis and future therapies
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BackgroundNevo, Y., Ben‐Zeev, B., Tabib, A., Straussberg, R., Anikster, Y., Shorer, Z., Fattal‐Valevski, A., Ta‐Shma, A., Aharoni, S., Rabie, M., et al. (2012) · Blood · doi:10.1182/blood-2012-07-441857 · Cited by 157
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Beigneux, A. P., Miyashita, K., Ploug, M., Blom, D. J., Ai, M., Linton, M. F., Khovidhunkit, W., Dufour, R., Garg, A., McMahon, M. A., et al. (2017) · New England Journal of Medicine · doi:10.1056/nejmoa1611930 · Cited by 155
Self-citationGPIHBP1 and Lipoprotein Lipase, Partners in Plasma Triglyceride Metabolism
Young, S. G., Fong, L. G., Beigneux, A. P., Allan, C. M., He, C. H., Jiang, H., Nakajima, K., Muthuraman, M., Birrane, G., & Ploug, M. (2019) · Cell Metabolism · doi:10.1016/j.cmet.2019.05.023 · Cited by 148
“Soon after the discovery of chylomicronemia in Gpihbp1–/– mice, GPIHBP1 mutations were identified in patients with familial chylomicronemia syndrome (Ariza et al., 2016; Beigneux et al., 2009a; Charriere et al., 2011; Coca-Prieto et al., 2011; Franssen et al., 2010; GonzagaJauregui et al., 2014; Olivecrona et al., 201…”
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Johansen, C. T., & Hegele, R. A. (2011) · Current Opinion in Lipidology · doi:10.1097/mol.0b013e3283471972 · Cited by 127
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“, 2007) or by loss-of-function missense mutations in humans leads to sustained elevations in plasma triglyceride levels—a condition known as familial chylomicronemia (Ariza et al., 2016; Beigneux et al., 2015, 2009b; Olivecrona et al., 2010; Plengpanich et al., 2014).”
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Self-citationGPIHBP1, an endothelial cell transporter for lipoprotein lipase
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Self-citationChylomicronemia With Low Postheparin Lipoprotein Lipase Levels in the Setting of GPIHBP1 Defects
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“…is tightly linked to human disease as a variety of loss-of-function mutations in GPIHBP1 have been encountered in humans with familial chylomicronemia ( Beigneux et al., 2009 ; Buonuomo et al., 2015 ; Olivecrona et al., 2010 ; Plengpanich et al., 2014 ; Rios et al., 2012 ; Surendran et al., 2012 ).”
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ResultGPIHBP1 and Plasma Triglyceride Metabolism
Fong, L. G., Young, S. G., Beigneux, A. P., Bensadoun, A., Oberer, M., Jiang, H., & Ploug, M. (2016) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2016.04.013 · Cited by 87
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Self-citationChylomicronemia from GPIHBP1 autoantibodies
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“GPIHBP1 Constructs Human GPIHBP1 mammalian expression vectors containing an amino-terminal S-protein tag have been described previously.(5,17) For expression of GPIHBP1 in insect cells, we cloned a cDNA encoding human uPAR domain III (uPAR-DIII) in-frame with human GPIHBP1 amino acids 21 to 136, followed by mouse GPIH…”
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“Earlier studies showed that missense mutations in the GPIHBP1 Ly6 domain interfere with LPL binding and transport and cause severe hypertriglyceridemia (12, 13, 15, 16, 21, 23).”
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“[39] identified point mutations in GPIHBP1 that are associated with defective LPL binding and chylomicronemia while Rios et al.”
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“Both variants of p.A98T and p.C14F had been described in individuals with familial LPL deficiency and HTG.[41, 42] The general therapy for gestational HTP is to alleviate TG levels during the acute episodes with a very low-fat diet ( 10% of total caloric intake), hospitalization for intravenous fluid therapy and paren…”
BackgroundInfluentialNovel mutations in the GPIHBP1 gene identified in 2 patients with recurrent acute pancreatitis
Ariza, M. J., Martínez-Hernández, P. L., Ibarretxe, D., Rabacchi, C., Rioja, J., Grande-Aragón, C., Plana, N., Tarugi, P., Olivecrona, G., Calandra, S., et al. (2015) · Journal of clinical lipidology · doi:10.1016/j.jacl.2015.09.007 · Cited by 30
Self-citationNovel Combined GPIHBP1 Mutations in a Patient with Hypertriglyceridemia Associated with CAD
Yamamoto, H., Onishi, M., Miyamoto, N., Oki, R., Ueda, H., Ishigami, M., Hiraoka, H., Matsuzawa, Y., & Kihara, S. (2013) · Journal of Atherosclerosis and Thrombosis · doi:10.5551/jat.18861 · Cited by 28
A protein of capillary endothelial cells, GPIHBP1, is crucial for plasma triglyceride metabolism
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“Plasma TG levels in heterozygotes appear to be normal (26, 75).”
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“Biallelic loss-of-function variants in GPIHBP1 (32–34)—as well as GPIHBP1 autoantibodies—cause chylomi-cronemia (35, 36).”
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“, lipase maturation factor1 (LMF1) and glycosylphosphatidylinositol-anchored high-density lipoprotein-binding protein 1 (GPIHBP1); thus, they are of importance for studying HTG [4,5], although mutations of LPL gene are responsible for the most common form of primary severe HTG.”
BackgroundRabacchi, C., D’Addato, S., Palmisano, S., Lucchi, T. A., Bertolini, S., Calandra, S., & Tarugi, P. (2016) · Journal of clinical lipidology · doi:10.1016/j.jacl.2016.03.009 · Cited by 24
An enzyme-linked immunosorbent assay for measuring GPIHBP1 levels in human plasma or serum
Miyashita, K., Fukamachi, I., Nagao, M., Ishida, T., Kobayashi, J., Machida, T., Nakajima, K., Murakami, M., Ploug, M., Beigneux, A. P., et al. (2017) · Journal of clinical lipidology · doi:10.1016/j.jacl.2017.10.022 · Cited by 24
Self-citationWang, Y., Tong, J., Li, S., Zhang, R., Chen, L., Wang, Y., Zheng, M., Wang, M., Liu, C., Dai, Y., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0020895 · Cited by 23
“One is that hLPL produced by the transgenic mice competes with endogenous mouse LPL the binding sites at GPIHBP1 which is responsible for the transport of LPL into capillaries [6], leading to a limited capacity to transport LPL to the vascular endothelium where it directs the movement of fatty acid into the mammary ce…”
BackgroundSong, W., Beigneux, A. P., Winther, A.-M. L., Kristensen, K. K., Grønnemose, A. L., Yang, Y., Tu, Y., Munguia, P., Morales, J., Jung, H., et al. (2022) · Journal of Clinical Investigation · doi:10.1172/jci157500 · Cited by 22
“The in vivo relevance of the LU domain was firmly established by finding absent intravascular LPL and severe chylomicronemia in knockin mice harboring a single cysteine substitution in the LU domain (16, 17).”
BackgroundSelf-citationReimund, M., Larsson, M., Kovrov, O., Kasvandik, S., Olivecrona, G., & Lõokene, A. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.634626 · Cited by 22
Self-citationGPIHBP1 autoantibody syndrome during interferon β1a treatment
Eguchi, J., Miyashita, K., Fukamachi, I., Nakajima, K., Murakami, M., Kawahara, Y., Yamashita, T., Ohta, Y., Abe, K., Nakatsuka, A., et al. (2018) · Journal of clinical lipidology · doi:10.1016/j.jacl.2018.10.004 · Cited by 22
Self-citationA novel GPIHBP1 mutation related to familial chylomicronemia syndrome: A series of cases
Lima, J. G., Nóbrega, L. H. C., Bandeira, F. T. M., de Sousa, A. G. P., Macedo, T. B. M. D. A., Nogueira, A. C. C., Filho, A. F. D. O., Alves, R. J., Castelo, M. H. C. G., Coelho, F. M. S., et al. (2021) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2021.02.020 · Cited by 21
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Holmes, R. S., & Cox, L. A. (2011) · 3 Biotech · doi:10.1007/s13205-011-0026-4 · Cited by 20
Zhang, G., Yang, Q., Mao, W., Hu, Y., Pu, N., Deng, H., Yu, X., Zhang, J., Zhou, J., Ye, B., et al. (2022) · Journal of clinical lipidology · doi:10.1016/j.jacl.2022.08.001 · Cited by 19
Nyrén, R., Chang, C. L., Lindström, P., Barmina, A., Vorrsjö, E., Ali, Y., Juntti‐Berggren, L., Bensadoun, A., Young, S. G., Olivecrona, T., et al. (2012) · BMC Physiology · doi:10.1186/1472-6793-12-14 · Cited by 19
“Mutations within one of the motifs have been identified in patients with severe chylomicronemia [5-8].”
BackgroundSelf-citationType 1 hyperlipoproteinemia in a child with large homozygous deletion encompassing GPIHBP1
Patni, N., Brothers, J. A., Xing, C., & Garg, A. (2016) · Journal of clinical lipidology · doi:10.1016/j.jacl.2016.04.001 · Cited by 18
Lipoprotein lipase transporter GPIHBP1 and triglyceride-rich lipoprotein metabolism
Liu, C., Li, L., Guo, D., Lv, Y.-C., Zheng, X., Mo, Z., & Xie, W. (2018) · Clinica Chimica Acta · doi:10.1016/j.cca.2018.09.020 · Cited by 18
Catalina Dussaillant, K., Serrano, V., Alberto Maiz, G., Eyheramendy, S., Cataldo, L. R., Chavez, M., Smalley, S. V., Fuentes, M., Rigotti, A., Rubio, L., et al. (2012) · BMC Medical Genetics · doi:10.1186/1471-2350-13-106 · Cited by 20
“Cefalu AB, Noto D, Arpi ML, Yin F, Spina R, Hilden H, Barbagallo CM, Carroccio A, Tarugi P, Squatrito S, Vigneri R, Taskinen MR, Péterfy M, Averna MR: Novel LMF1 Nonsense mutation in a patient with severe hypertriglyceridemia.”
BackgroundInfluentialWeinstein, M. M., Tu, Y., Beigneux, A. P., Davies, B. S. J., Gin, P., Voss, C. V., Walzem, R. L., Reue, K., Tontonoz, P., Bensadoun, A., et al. (2010) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.110.214403 · Cited by 18
Self-citationGPIHBP1 and the processing of triglyceride-rich lipoproteins
Beigneux, A. P. (2010) · Clinical Lipidology · doi:10.2217/clp.10.43 · Cited by 17
Self-citationAllan, C. M., Jung, C. J., Larsson, M., Heizer, P. J., Tu, Y., Sandoval, N. P., Dang, T. L. P., Jung, R. S., Beigneux, A. P., de Jong, P. J., et al. (2017) · Journal of Lipid Research · doi:10.1194/jlr.m076943 · Cited by 17
“Ly6 domain or an adjacent residue (6, 7, 9, 10).”
BackgroundSelf-citationYang, J., Liu, X. E., Wang, D., Ning, C., Wang, H., Zhang, Q., & Jiang, L. (2017) · Scientific Reports · doi:10.1038/s41598-017-08668-6 · Cited by 17
Type 1 hyperlipoproteinemia due to a novel deletion of exons 3 and 4 in the GPIHBP1 gene
Berge, K. E., Retterstøl, K., Romeo, S., Pirazzi, C., & Leren, T. P. (2014) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2014.02.005 · Cited by 17
Kurooka, N., Eguchi, J., & Wada, J. (2023) · Journal of Diabetes Investigation · doi:10.1111/jdi.14056 · Cited by 17
“In the LU domain, many of the mutations involve a cysteine 27 – 29, 32, 35 , which disrupts”
Shetty, S. K., Walzem, R. L., & Davies, B. S. J. (2020) · Journal of Lipid Research · doi:10.1194/jlr.d119000388 · Cited by 18
Self-citationValdivielso, P., Pintó, X., Mateo‐Gállego, R., Masana, L., Álvarez-Sala, L., Jarauta, E., Suárez, M., García-Arias, C., Plana, N., & Laguna, F. (2011) · Medicina Clínica · doi:10.1016/j.medcli.2010.09.028 · Cited by 15
Marmontel, O., Filippo, M. D., Marçais, C., Nony, S., Dumoux, M., Dancer, M. S., Caussy, C., Charrière, S., & Moulin, P. (2017) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2017.07.030 · Cited by 15
An LPL–specific monoclonal antibody, 88B8, that abolishes the binding of LPL to GPIHBP1
Allan, C. M., Larsson, M., Hu, X., He, C. H., Jung, R. S., Mapar, A., Voss, C. V., Miyashita, K., Machida, T., Murakami, M., et al. (2016) · Journal of Lipid Research · doi:10.1194/jlr.m070813 · Cited by 14
Self-citationAdeyo, O., Oberer, M., Ploug, M., Fong, L. G., Young, S. G., & Beigneux, A. P. (2015) · British Journal of Dermatology · doi:10.1111/bjd.13868 · Cited by 14
Self-citationTurlo, K. A., Leung, C. S., Seo, J. J., Goulbourne, C. N., Adeyo, O., Gin, P., Voss, C. V., Bensadoun, A., Fong, L. G., Young, S. G., et al. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2014.03.011 · Cited by 15
“GPIHBP1 deficiency markedly reduces LPL levels within capillaries [24] and results in high plasma triglyceride levels and low levels of LPL in the pre- and post-heparin plasma [25, 26, 28, 29].”
BackgroundSelf-citationLipoprotein lipase reaches the capillary lumen in chickens despite an apparent absence of GPIHBP1
He, C. H., Hu, X., Jung, R. S., Larsson, M., Tu, Y., Duarte‐Vogel, S., Kim, P., Sandoval, N. P., Price, T. R., Allan, C. M., et al. (2017) · JCI Insight · doi:10.1172/jci.insight.96783 · Cited by 13
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Self-citationSEA 2024 Standards for Global Control of Vascular Risk
Mostaza, J. M., Pintó, X., Armario, P., Masana, L., Real, J. T., Valdivielso, P., Arrobas-Velilla, T., Baeza‐Trinidad, R., Calmarza, P., Cebollada, J., et al. (2024) · Clínica e Investigación en Arteriosclerosis (English Edition) · doi:10.1016/j.artere.2024.06.001 · Cited by 11
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“Human patients with GPIHBP1 loss-of-function mutations manifest chylomicronemia, with plasma triglyceride levels greater than 1,500 mg/dl (7-9).”
BackgroundSelf-citationGPIHBP1: Lipoprotein Lipase's Ticket to Ride
Fisher, E. A. A. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2010.06.005 · Cited by 11
“Notably, this shuttle function depended on the ability of GPIHBP1 to bind LPL, a finding supported by the severe hypertriglyceridemia in humans with mutations in GPIHBP1 that impair LPL binding (Beigneux et al., 2009; Franssen et al., 2010; Olivecrona et al., 2010).”
BackgroundVallerie, S. N., & Bornfeldt, K. (2015) · Circulation Research · doi:10.1161/circresaha.115.305819 · Cited by 9
Therapeutic inhibition of apoC-III for the treatment of hypertriglyceridemia
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Triglycerides and Cardiovascular Disease : A Scientific Statement From the
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Mostaza, J. M., Pintó, X., Armario, P., Masana, L., Real, J. T., Valdivielso, P., Arrobas-Velilla, T., Baeza‐Trinidad, R., Calmarza, P., Cebollada, J., et al. (2024) · Clínica e Investigación en Arteriosclerosis · doi:10.1016/j.arteri.2024.02.001 · Cited by 14
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“Cys89Ter (Olivecrona et al., 2010; Charrière et al., 2011; Iacocca et al., 2019) with severe elevation in TG (1,000–6,480 mg/dl, 11.”
Background
Metadata
- Authors
- Olivecrona, G., Ehrenborg, E., Semb, H., Makoveichuk, E., Lindberg, A., Hayden, M. R., Gin, P., Davies, B. S. J., Weinstein, M. M., Fong, L. G., Beigneux, A. P., Young, S. G., Olivecrona, T., & Hernell, O.
- Affiliations
- Umeå University (SE)
- University of British Columbia (CA)
- University of California, Los Angeles (US)
- Corresponding author
- Olivecrona, Gunilla
- ORCID
- Venue
- Journal of Lipid Research
- Publisher
- Elsevier BV
- Published
- 2010-06
- Volume
- 51
- Issue
- 6
- Pages
- 1535-1545
- ISSN
- 0022-2275 (ISSN-L)
- PMC
- PMC3035517
- OpenAlex
- W2168084616
- Cited by
- 118
- References
- 49
- Citations by year
- 2026: 2 · 2025: 2 · 2024: 4 · 2023: 4 · 2022: 6 · 2021: 2 · 2020: 3 · 2019: 4 · 2018: 9 · 2017: 8 · 2016: 8 · 2015: 9 · 2014: 9 · 2013: 7 · 2012: 9
- FWCI
- 8.66
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Lipid Research (publishedVersion, cc-by)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- American Heart Association
- Heart and Stroke Foundation of Canada
- University of Washington
- Heart and Stroke Foundation of British Columbia and Yukon
- Kempe Foundation
- Hjärt-Lungfonden
- Karolinska Institutet
- Riksbankens Jubileumsfond
- Kempestiftelserna
- National Institutes of Health (HL094732, HL090553)
- Medical Research Council
- National Heart, Lung, and Blood Institute (P01HL090553, R01HL087228, R01HL094732)
- Topics
- Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Lipid metabolism and disorders
- Health Sciences › Medicine › Surgery › Lymphatic Disorders and Treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Lipid metabolism and biosynthesis
- Keywords
- familial chylomicronemia, GPIHBP1, conserved cysteines, compound heterozygosity, heparin, breast milk, de novo lipogenesis, adipose tissue, missense mutations
- MeSH terms
- Adipose Tissue, Adolescent, Adult, Alleles, Animals, Base Sequence, Carrier Proteins, Child, Preschool, Chylomicrons, Cricetulus, Cysteine, Female, Gene Expression Regulation, Cricetinae, Heparin, Heterozygote, Humans, Lipoprotein Lipase, Male, Middle Aged, Milk, Human, Mutation, Transfection, CHO Cells, Conserved Sequence, Protein Structure, Tertiary, Receptors, Lipoprotein, Mutation, Missense, Siblings, Lipid Metabolism Disorders, Apolipoprotein C-II
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