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Article ; Online: Correction to Glutamine-451 Confers Sensitivity to Oxidative Inhibition and Heme-Thiolate Sulfenylation of Cytochrome P450 4B1.

Albertolle, Matthew E / Song, Hyun D / Wilkey, Clayton J / Segrest, Jere P / Guengerich, F Peter

2021 Volume 34, Issue 3, Page(s) 930

Language	English
Publishing date	2021-01-21
Publishing country	United States
Document type	Published Erratum
ZDB-ID	639353-6
ISSN	1520-5010 ; 0893-228X
ISSN (online)	1520-5010
ISSN	0893-228X
DOI	10.1021/acs.chemrestox.0c00538
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Article ; Online: Glutamine-451 Confers Sensitivity to Oxidative Inhibition and Heme-Thiolate Sulfenylation of Cytochrome P450 4B1.

Albertolle, Matthew E / Song, Hyun D / Wilkey, Clayton J / Segrest, Jere P / Guengerich, F Peter

Chemical research in toxicology

2019 Volume 32, Issue 3, Page(s) 484–492

Abstract: Human cytochrome P450 (P450) family 4 enzymes are involved in the metabolism of fatty acids and the bioactivation of carcinogenic arylamines and toxic natural products, e.g., 4-ipomeanol. These and other drug-metabolizing P450s are redox sensitive, ... ...

Abstract	Human cytochrome P450 (P450) family 4 enzymes are involved in the metabolism of fatty acids and the bioactivation of carcinogenic arylamines and toxic natural products, e.g., 4-ipomeanol. These and other drug-metabolizing P450s are redox sensitive, showing a loss of activity resulting from preincubation with H
MeSH term(s)	Animals ; Aryl Hydrocarbon Hydroxylases/chemistry ; Aryl Hydrocarbon Hydroxylases/genetics ; Aryl Hydrocarbon Hydroxylases/metabolism ; Glutamine/pharmacology ; Heme/metabolism ; Molecular Dynamics Simulation ; Mutagenesis, Site-Directed ; Oxidation-Reduction ; Rabbits ; Sulfenic Acids/metabolism ; Sulfhydryl Compounds/metabolism
Chemical Substances	Sulfenic Acids ; Sulfhydryl Compounds ; Glutamine (0RH81L854J) ; Heme (42VZT0U6YR) ; Aryl Hydrocarbon Hydroxylases (EC 1.14.14.1) ; cytochrome P-450 CYP4B1 (EC 1.14.14.1)
Language	English
Publishing date	2019-02-11
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	639353-6
ISSN	1520-5010 ; 0893-228X
ISSN (online)	1520-5010
ISSN	0893-228X
DOI	10.1021/acs.chemrestox.8b00353
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Article: Flipped C-Terminal Ends of APOA1 Promote ABCA1-dependent Cholesterol Efflux by Small HDLs.

He, Yi / Pavanello, Chiara / Hutchins, Patrick M / Tang, Chongren / Pourmousa, Mohsen / Vaisar, Tomas / Song, Hyun D / Pastor, Richard W / Remaley, Alan T / Goldberg, Ira J / Costacou, Tina / Davidson, W Sean / Bornfeldt, Karin E / Calabresi, Laura / Segrest, Jere P / Heinecke, Jay W

medRxiv : the preprint server for health sciences

2023

Abstract: Background: Cholesterol efflux capacity (CEC) predicts cardiovascular disease (CVD) independently of HDL cholesterol (HDL-C) levels. Isolated small HDL particles are potent promoters of macrophage CEC by the ABCA1 pathway, but the underlying mechanisms ... ...

Abstract	Background: Cholesterol efflux capacity (CEC) predicts cardiovascular disease (CVD) independently of HDL cholesterol (HDL-C) levels. Isolated small HDL particles are potent promoters of macrophage CEC by the ABCA1 pathway, but the underlying mechanisms are unclear. Methods: We used model system studies of reconstituted HDL and plasma from control and lecithin-cholesterol acyltransferase (LCAT)-deficient subjects to investigate the relationships among the sizes of HDL particles, the structure of APOA1 in the different particles, and the CECs of plasma and isolated HDLs. Results: We quantified macrophage and ABCA1 CEC of four distinct sizes of reconstituted HDL (r-HDL). CEC increased as particle size decreased. MS/MS analysis of chemically crosslinked peptides and molecular dynamics simulations of APOA1 (HDL's major protein) indicated that the mobility of that protein's C-terminus was markedly higher and flipped off the surface in the smallest particles. To explore the physiological relevance of the model system studies, we isolated HDL from LCAT-deficient subjects, whose small HDLs-like r-HDLs-are discoidal and composed of APOA1, cholesterol, and phospholipid. Despite their very low plasma levels of HDL particles, these subjects had normal CEC. In both the LCAT-deficient subjects and control subjects, the CEC of isolated extra-small HDL (a mixture of extra-small and small HDL by calibrated ion mobility analysis) was 3-5-fold greater than that of the larger sizes of isolated HDL. Incubating LCAT-deficient plasma and control plasma with human LCAT converted extra-small and small HDL particles into larger particles, and it markedly inhibited CEC. Conclusions: We present a mechanism for the enhanced CEC of small HDLs. In smaller particles, the C-termini of the two antiparallel molecules of APOA1 are flipped off the lipid surface of HDL. This extended conformation allows them to engage with ABCA1. In contrast, the C-termini of larger HDLs are unable to interact productively with ABCA1 because they form a helical bundle that strongly adheres to the lipid on the particle. Enhanced CEC, as seen with the smaller particles, predicts decreased CVD risk. Thus, extra-small and small HDLs may be key mediators and indicators of HDL's cardioprotective effects.
Language	English
Publishing date	2023-11-04
Publishing country	United States
Document type	Preprint
DOI	10.1101/2023.11.03.23297986
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Article ; Online: Flipped C-Terminal Ends of APOA1 Promote ABCA1-Dependent Cholesterol Efflux by Small HDLs.

He, Yi / Pavanello, Chiara / Hutchins, Patrick M / Tang, Chongren / Pourmousa, Mohsen / Vaisar, Tomas / Song, Hyun D / Pastor, Richard W / Remaley, Alan T / Goldberg, Ira J / Costacou, Tina / Sean Davidson, W / Bornfeldt, Karin E / Calabresi, Laura / Segrest, Jere P / Heinecke, Jay W

Circulation

2023 Volume 149, Issue 10, Page(s) 774–787

Abstract: Background: Cholesterol efflux capacity (CEC) predicts cardiovascular disease independently of high-density lipoprotein (HDL) cholesterol levels. Isolated small HDL particles are potent promoters of macrophage CEC by the ABCA1 (ATP-binding cassette ... ...

Abstract	Background: Cholesterol efflux capacity (CEC) predicts cardiovascular disease independently of high-density lipoprotein (HDL) cholesterol levels. Isolated small HDL particles are potent promoters of macrophage CEC by the ABCA1 (ATP-binding cassette transporter A1) pathway, but the underlying mechanisms are unclear. Methods: We used model system studies of reconstituted HDL and plasma from control and lecithin-cholesterol acyltransferase (LCAT)-deficient subjects to investigate the relationships among the sizes of HDL particles, the structure of APOA1 (apolipoprotein A1) in the different particles, and the CECs of plasma and isolated HDLs. Results: We quantified macrophage and ABCA1 CEC of 4 distinct sizes of reconstituted HDL. CEC increased as particle size decreased. Tandem mass spectrometric analysis of chemically cross-linked peptides and molecular dynamics simulations of APOA1, the major protein of HDL, indicated that the mobility of C-terminus of that protein was markedly higher and flipped off the surface in the smallest particles. To explore the physiological relevance of the model system studies, we isolated HDL from LCAT-deficient subjects, whose small HDLs (like reconstituted HDLs) are discoidal and composed of APOA1, cholesterol, and phospholipid. Despite their very low plasma levels of HDL particles, these subjects had normal CEC. In both the LCAT-deficient subjects and control subjects, the CEC of isolated extra-small HDL (a mixture of extra-small and small HDL by calibrated ion mobility analysis) was 3- to 5-fold greater than that of the larger sizes of isolated HDL. Incubating LCAT-deficient plasma and control plasma with human LCAT converted extra-small and small HDL particles into larger particles, and it markedly inhibited CEC. Conclusions: We present a mechanism for the enhanced CEC of small HDLs. In smaller particles, the C-termini of the 2 antiparallel molecules of APOA1 are "flipped" off the lipid surface of HDL. This extended conformation allows them to engage with ABCA1. In contrast, the C-termini of larger HDLs are unable to interact productively with ABCA1 because they form a helical bundle that strongly adheres to the lipid on the particle. Enhanced CEC, as seen with the smaller particles, predicts decreased cardiovascular disease risk. Thus, extra-small and small HDLs may be key mediators and indicators of the cardioprotective effects of HDL.
MeSH term(s)	Humans ; Apolipoprotein A-I/metabolism ; Cardiovascular Diseases/metabolism ; Lipoproteins, HDL/metabolism ; Cholesterol ; ATP Binding Cassette Transporter 1/genetics ; ATP Binding Cassette Transporter 1/metabolism ; Macrophages/metabolism ; Cholesterol, HDL
Chemical Substances	Apolipoprotein A-I ; Lipoproteins, HDL ; Cholesterol (97C5T2UQ7J) ; ATP Binding Cassette Transporter 1 ; Cholesterol, HDL ; APOA1 protein, human ; ABCA1 protein, human
Language	English
Publishing date	2023-11-29
Publishing country	United States
Document type	Journal Article
ZDB-ID	80099-5
ISSN	1524-4539 ; 0009-7322 ; 0069-4193 ; 0065-8499
ISSN (online)	1524-4539
ISSN	0009-7322 ; 0069-4193 ; 0065-8499
DOI	10.1161/CIRCULATIONAHA.123.065959
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Article ; Online: Conformational flexibility of apolipoprotein A-I amino- and carboxy-termini is necessary for lipid binding but not cholesterol efflux.

Bedi, Shimpi / Morris, Jamie / Shah, Amy / Hart, Rachel C / Jerome, W Gray / Aller, Stephen G / Tang, Chongren / Vaisar, Tomas / Bornfeldt, Karin E / Segrest, Jere P / Heinecke, Jay W / Davidson, W Sean

Journal of lipid research

2022 Volume 63, Issue 3, Page(s) 100168

Abstract: Because of its critical role in HDL formation, significant efforts have been devoted to studying apolipoprotein A-I (APOA1) structural transitions in response to lipid binding. To assess the requirements for the conformational freedom of its termini ... ...

Abstract	Because of its critical role in HDL formation, significant efforts have been devoted to studying apolipoprotein A-I (APOA1) structural transitions in response to lipid binding. To assess the requirements for the conformational freedom of its termini during HDL particle formation, we generated three dimeric APOA1 molecules with their termini covalently joined in different combinations. The dimeric (d)-APOA1C-N mutant coupled the C-terminus of one APOA1 molecule to the N-terminus of a second with a short alanine linker, whereas the d-APOA1C-C and d-APOA1N-N mutants coupled the C-termini and the N-termini of two APOA1 molecules, respectively, using introduced cysteine residues to form disulfide linkages. We then tested the ability of these constructs to generate reconstituted HDL by detergent-assisted and spontaneous phospholipid microsolubilization methods. Using cholate dialysis, we demonstrate WT and all APOA1 mutants generated reconstituted HDL particles of similar sizes, morphologies, compositions, and abilities to activate lecithin:cholesterol acyltransferase. Unlike WT, however, the mutants were incapable of spontaneously solubilizing short chain phospholipids into discoidal particles. We found lipid-free d-APOA1C-N and d-APOA1N-N retained most of WT APOA1's ability to promote cholesterol efflux via the ATP binding cassette transporter A1, whereas d-APOA1C-C exhibited impaired cholesterol efflux. Our data support the double belt model for a lipid-bound APOA1 structure in nascent HDL particles and refute other postulated arrangements like the "double super helix." Furthermore, we conclude the conformational freedom of both the N- and C-termini of APOA1 is important in spontaneous microsolubilization of bulk phospholipid but is not critical for ABCA1-mediated cholesterol efflux.
MeSH term(s)	ATP Binding Cassette Transporter 1/metabolism ; Apolipoprotein A-I/metabolism ; Biological Transport ; Cholesterol/metabolism ; Phosphatidylcholine-Sterol O-Acyltransferase/metabolism ; Phospholipids/metabolism
Chemical Substances	ATP Binding Cassette Transporter 1 ; Apolipoprotein A-I ; Phospholipids ; Cholesterol (97C5T2UQ7J) ; Phosphatidylcholine-Sterol O-Acyltransferase (EC 2.3.1.43)
Language	English
Publishing date	2022-01-17
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	80154-9
ISSN	1539-7262 ; 0022-2275
ISSN (online)	1539-7262
ISSN	0022-2275
DOI	10.1016/j.jlr.2022.100168
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Article ; Online: Apolipoprotein A-I modulates HDL particle size in the absence of apolipoprotein A-II.

Melchior, John T / Street, Scott E / Vaisar, Tomas / Hart, Rachel / Jerome, Jay / Kuklenyik, Zsuzsanna / Clouet-Foraison, Noemie / Thornock, Carissa / Bedi, Shimpi / Shah, Amy S / Segrest, Jere P / Heinecke, Jay W / Davidson, W Sean

Journal of lipid research

2021 Volume 62, Page(s) 100099

Abstract: Human high-density lipoproteins (HDLs) are a complex mixture of structurally related nanoparticles that perform distinct physiological functions. We previously showed that human HDL containing apolipoprotein A-I (APOA1) but not apolipoprotein A-II (APOA2) ...

Abstract	Human high-density lipoproteins (HDLs) are a complex mixture of structurally related nanoparticles that perform distinct physiological functions. We previously showed that human HDL containing apolipoprotein A-I (APOA1) but not apolipoprotein A-II (APOA2), designated LpA-I, is composed primarily of two discretely sized populations. Here, we isolated these particles directly from human plasma by antibody affinity chromatography, separated them by high-resolution size-exclusion chromatography and performed a deep molecular characterization of each species. The large and small LpA-I populations were spherical with mean diameters of 109 Å and 91 Å, respectively. Unexpectedly, isotope dilution MS/MS with [
MeSH term(s)	Apolipoprotein A-I/chemistry ; Apolipoprotein A-II/chemistry ; Cholesterol, HDL/chemistry ; Particle Size
Chemical Substances	Apolipoprotein A-I ; Apolipoprotein A-II ; Cholesterol, HDL
Language	English
Publishing date	2021-07-27
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	80154-9
ISSN	1539-7262 ; 0022-2275
ISSN (online)	1539-7262
ISSN	0022-2275
DOI	10.1016/j.jlr.2021.100099
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Article: Structural domains in vesicular stomatitis virus membrane as studied by differential scanning calorimetry.

Brouillette, C G / Compans, R W / Segrest, J P / Brandts, J F

Biophysical journal

2009 Volume 37, Issue 1, Page(s) 25–26

Language	English
Publishing date	2009-05-08
Publishing country	United States
Document type	Journal Article
ZDB-ID	218078-9
ISSN	1542-0086 ; 0006-3495
ISSN (online)	1542-0086
ISSN	0006-3495
DOI	10.1016/S0006-3495(82)84581-5
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Article ; Online: A thumbwheel mechanism for APOA1 activation of LCAT activity in HDL.

Cooke, Allison L / Morris, Jamie / Melchior, John T / Street, Scott E / Jerome, W Gray / Huang, Rong / Herr, Andrew B / Smith, Loren E / Segrest, Jere P / Remaley, Alan T / Shah, Amy S / Thompson, Thomas B / Davidson, W Sean

Journal of lipid research

2018 Volume 59, Issue 7, Page(s) 1244–1255

Abstract: APOA1 is the most abundant protein in HDL. It modulates interactions that affect HDL's cardioprotective functions, in part via its activation of the enzyme, LCAT. On nascent discoidal HDL, APOA1 comprises 10 α-helical repeats arranged in an anti-parallel ...

Abstract	APOA1 is the most abundant protein in HDL. It modulates interactions that affect HDL's cardioprotective functions, in part via its activation of the enzyme, LCAT. On nascent discoidal HDL, APOA1 comprises 10 α-helical repeats arranged in an anti-parallel stacked-ring structure that encapsulates a lipid bilayer. Previous chemical cross-linking studies suggested that these APOA1 rings can adopt at least two different orientations, or registries, with respect to each other; however, the functional impact of these structural changes is unknown. Here, we placed cysteine residues at locations predicted to form disulfide bonds in each orientation and then measured APOA1's ability to adopt the two registries during HDL particle formation. We found that most APOA1 oriented with the fifth helix of one molecule across from fifth helix of the other (5/5 helical registry), but a fraction adopted a 5/2 registry. Engineered HDLs that were locked in 5/5 or 5/2 registries by disulfide bonds equally promoted cholesterol efflux from macrophages, indicating functional particles. However, unlike the 5/5 registry or the WT, the 5/2 registry impaired LCAT cholesteryl esterification activity (
MeSH term(s)	Apolipoprotein A-I/genetics ; Apolipoprotein A-I/metabolism ; Cholesterol, HDL/metabolism ; Enzyme Activation ; Humans ; Mutation ; Phosphatidylcholine-Sterol O-Acyltransferase/metabolism
Chemical Substances	APOA1 protein, human ; Apolipoprotein A-I ; Cholesterol, HDL ; LCAT protein, human (EC 2.3.1.43) ; Phosphatidylcholine-Sterol O-Acyltransferase (EC 2.3.1.43)
Language	English
Publishing date	2018-05-17
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	80154-9
ISSN	1539-7262 ; 0022-2275
ISSN (online)	1539-7262
ISSN	0022-2275
DOI	10.1194/jlr.M085332
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Article: Dynamics of apolipoprotein-phospholipid interactions.

Brouillette, C G / Segrest, J P / Ng, T / Chung, B H / Ragland, J B

Biophysical journal

2009 Volume 37, Issue 1, Page(s) 172–173

Language	English
Publishing date	2009-05-08
Publishing country	United States
Document type	Journal Article
ZDB-ID	218078-9
ISSN	1542-0086 ; 0006-3495
ISSN (online)	1542-0086
ISSN	0006-3495
DOI	10.1016/S0006-3495(82)84656-0
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Article: Urinary metabolites of collagen.

Segrest, J P

Methods in enzymology

1982 Volume 82 Pt A, Page(s) 398–410

MeSH term(s)	Adult ; Bone and Bones/metabolism ; Child ; Collagen/metabolism ; Collagen/urine ; Humans ; Hydroxylysine/analogs & derivatives ; Hydroxylysine/urine ; Hydroxyproline/urine
Chemical Substances	hydroxylysine glycoside ; Hydroxylysine (2GQB349IUB) ; glucosylgalactosylhydroxylysine (32448-35-4) ; galactosylhydroxylysine (32448-36-5) ; Collagen (9007-34-5) ; Hydroxyproline (RMB44WO89X)
Language	English
Publishing date	1982
Publishing country	United States
Document type	Journal Article
ISSN	0076-6879
ISSN	0076-6879
DOI	10.1016/0076-6879(82)82075-2
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