LIVIVO - Search results -

Search results

Result 1 - 10 of total 29

Search options

Article ; Online: Hepatic deletion of Mboat7 (LPIAT1) causes activation of SREBP-1c and fatty liver.

Xia, Mingfeng / Chandrasekaran, Preethi / Rong, Shunxing / Fu, Xiaorong / Mitsche, Matthew A

2021 Volume 62, Page(s) 100031

Abstract: Genetic variants that increase the risk of fatty liver disease and cirrhosis have recently been identified in the proximity of membrane-bound O-acyltransferase domain-containing 7 (MBOAT7). To elucidate the link between these variants and fatty liver ... ...

Abstract	Genetic variants that increase the risk of fatty liver disease and cirrhosis have recently been identified in the proximity of membrane-bound O-acyltransferase domain-containing 7 (MBOAT7). To elucidate the link between these variants and fatty liver disease, we characterized Mboat7 liver-specific KO mice (Mboat7 LSKO). Chow-fed Mboat7 LSKO mice developed fatty livers and associated liver injury. Lipidomic analysis of liver using MS revealed a pronounced reduction in 20-carbon PUFA content in phosphatidylinositols (PIs) but not in other phospholipids. The change in fatty acid composition of PIs in these mice was associated with a marked increase in de novo lipogenesis because of activation of SREBP-1c, a transcription factor that coordinates the activation of genes encoding enzymes in the fatty acid biosynthesis pathway. Hepatic removal of both SREBP cleavage-activating protein (Scap) and Mboat7 normalized hepatic triglycerides relative to Scap-only hepatic KO, showing that increased SREBP-1c processing is required for Mboat7-induced steatosis. This study reveals a clear relationship between PI fatty acid composition and regulation of hepatic fat synthesis and delineates the mechanism by which mutations in MBOAT7 cause hepatic steatosis.
MeSH term(s)	Sterol Regulatory Element Binding Protein 1
Chemical Substances	Sterol Regulatory Element Binding Protein 1
Language	English
Publishing date	2021-02-06
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	10.1194/jlr.RA120000856
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 175: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (1.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Patatin-like phospholipase domain–containing protein 3 promotes transfer of essential fatty acids from triglycerides to phospholipids in hepatic lipid droplets.

Mitsche, Matthew A / Hobbs, Helen H / Cohen, Jonathan C

The Journal of biological chemistry

2018 Volume 293, Issue 18, Page(s) 6958–6968

Abstract: Fatty liver disease (FLD) is a burgeoning health problem. A missense variant (I148M) in patatin-like phospholipase domain-containing protein 3 (PNPLA3) confers susceptibility to FLD, although the mechanism is not known. To glean first insights into the ... ...

Abstract	Fatty liver disease (FLD) is a burgeoning health problem. A missense variant (I148M) in patatin-like phospholipase domain-containing protein 3 (PNPLA3) confers susceptibility to FLD, although the mechanism is not known. To glean first insights into the physiological function of PNPLA3, we performed detailed lipidomic profiling of liver lysates and lipid droplets (LDs) from WT and
MeSH term(s)	Animals ; Catalysis ; Cell Line ; Cholesterol Esters/metabolism ; Dietary Sucrose/administration & dosage ; Fatty Acids, Essential/metabolism ; Fatty Acids, Unsaturated/metabolism ; Genetic Variation ; Humans ; Lipid Droplets/metabolism ; Liver/metabolism ; Male ; Mice ; Mice, Knockout ; Non-alcoholic Fatty Liver Disease/metabolism ; Phospholipases A2, Calcium-Independent/genetics ; Phospholipases A2, Calcium-Independent/physiology ; Phospholipids/metabolism ; Triglycerides/metabolism ; Vitamin A/metabolism
Chemical Substances	Cholesterol Esters ; Dietary Sucrose ; Fatty Acids, Essential ; Fatty Acids, Unsaturated ; Phospholipids ; Triglycerides ; Vitamin A (11103-57-4) ; PNPLA3 protein, mouse (EC 3.1.1.3) ; Phospholipases A2, Calcium-Independent (EC 3.1.1.4)
Language	English
Publishing date	2018-03-19
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.RA118.002333
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Uc I Zs.108: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Surface pressure-dependent conformation change of apolipoprotein-derived amphipathic α-helices.

Mitsche, Matthew A / Small, Donald M

Journal of lipid research

2013 Volume 54, Issue 6, Page(s) 1578–1588

Abstract: Amphipathic α-helices (AαH) are the primary structural motif of exchangeable apolipoproteins. AαHs in exchangeable apolipoproteins adsorb, remodel, and desorb at the surface of plasma lipoproteins in response to changes in their size or composition. A ... ...

Abstract	Amphipathic α-helices (AαH) are the primary structural motif of exchangeable apolipoproteins. AαHs in exchangeable apolipoproteins adsorb, remodel, and desorb at the surface of plasma lipoproteins in response to changes in their size or composition. A triolein/water (TO/W) interface was used as a model surface to study adsorption and desorption of AαHs at a lipoprotein-like interface. We previously reported that AαH peptides spontaneously adsorb to a TO/W interface, but they only partially desorb from the surface when the excess peptide was removed from the system. This finding suggests that "exchangeable" apolipoproteins are in fact partially exchangeable and only desorb from a surface in response to compression or change in composition. Here, we develop a thermodynamic and kinetic model to describe this phenomenon based on the change in the interfacial pressure (Π) of the C-terminal 46 amino acids of apolipoprotein A-I (C46) at a TO/W interface. This model suggests that apolipoproteins have at least two interfacial conformations that are in a surface concentration and Π-dependent equilibrium. This two-state surface equilibrium model, which is based on experimental data and is consistent with dynamic changes in Π(t), provides insights into the selective metabolism and clearance of plasma lipoproteins and the process of lipoprotein remodeling.
MeSH term(s)	Apolipoprotein A-I/chemistry ; Humans ; Models, Molecular ; Pressure ; Protein Structure, Secondary
Chemical Substances	Apolipoprotein A-I
Language	English
Publishing date	2013-03-25
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	10.1194/jlr.M034462
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 175: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (1.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Insights into lipid accumulation in skeletal muscle in dysferlin-deficient mice.

Agarwal, Anil K / Tunison, Katie / Mitsche, Matthew A / McDonald, Jeffrey G / Garg, Abhimanyu

Journal of lipid research

2019 Volume 60, Issue 12, Page(s) 2057–2073

Abstract: Loss of dysferlin (DYSF) protein in humans results in limb-girdle muscular dystrophy 2B, characterized by progressive loss of muscles in the distal limbs with impaired locomotion. The DYSF-null (Bla/J) mouse develops severe steatotic muscles upon aging. ... ...

Abstract	Loss of dysferlin (DYSF) protein in humans results in limb-girdle muscular dystrophy 2B, characterized by progressive loss of muscles in the distal limbs with impaired locomotion. The DYSF-null (Bla/J) mouse develops severe steatotic muscles upon aging. Here, we report a marked increase in adipocytes, especially in the psoas and gluteus muscles but not in the soleus and tibialis anterior muscles in aged Bla/J mice compared with WT mice. There was a robust upregulation in the mRNA expression of enzymes involved in lipogenesis and triacylglycerol (TAG) synthesis pathways in the steatotic skeletal muscles. Lipidomic analysis of the steatotic skeletal muscles revealed an increase in several molecular species of TAG, although it is unclear whether it was at the expense of phosphatidylcholine and phosphatidylserine. The adipocytes in steatotic muscles were extramyocellular, as determined by the increased expression of caveolin 1 (a cellular marker for adipocytes) and lipid-droplet protein, perilipin 1. This increase in adipocytes occured as a consequence of the loss of myocytes.
MeSH term(s)	Animals ; Biomarkers/metabolism ; Dysferlin/deficiency ; Lipid Metabolism ; Lipids/biosynthesis ; Mice ; Muscle, Skeletal/metabolism
Chemical Substances	Biomarkers ; Dysferlin ; Lipids
Language	English
Publishing date	2019-10-25
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.RA119000399
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 175: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (1.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: C-terminus of apolipoprotein A-I removes phospholipids from a triolein/phospholipids/water interface, but the N-terminus does not: a possible mechanism for nascent HDL assembly.

Mitsche, Matthew A / Small, Donald M

Biophysical journal

2011 Volume 101, Issue 2, Page(s) 353–361

Abstract: Apolipoprotein A-I (ApoA-I) is the principle protein component of HDL, also known as "good cholesterol," which is an inverse marker for cardiovascular disease. The N-terminal 44 amino acids of ApoA-I (N44) are predicted to be responsible for ... ...

Abstract	Apolipoprotein A-I (ApoA-I) is the principle protein component of HDL, also known as "good cholesterol," which is an inverse marker for cardiovascular disease. The N-terminal 44 amino acids of ApoA-I (N44) are predicted to be responsible for stabilization of soluble ApoA-I, whereas the C-terminal 46 amino acids (C46) are predicted to initiate lipid binding and oligomerization. In this work, we apply what we believe to be a novel application of drop tensiometry to study the adsorption and desorption of N44 and C46 at a triolein/POPC/water (TO/POPC/W) interface. The amount of peptide that adsorbed to the surface was dependent on the surface concentration of 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC) and pressure (Π) before adsorption. At a TO/POPC/W interface, the exclusion pressure (Π(EX)) of C46 was 25.8 mN/m, and was 19.3 mN/m for N44. Once adsorbed, both peptides formed a homogeneous surface with POPC but were progressively ejected from the surface by compression. During a compression, C46 removed POPC from the surface whereas N44 did not. Repeated compressions caused C46 to deplete entirely the surface of phospholipid. If full-length ApoA-I could also remove phospholipid, this could provide a mechanism for the transfer of surface components of chylomicrons and very low density lipoprotein to high density lipoprotein with the assistance of phospholipid transfer protein.
MeSH term(s)	Adsorption ; Apolipoprotein A-I/chemistry ; Apolipoprotein A-I/metabolism ; High-Density Lipoproteins, Pre-beta/metabolism ; Models, Molecular ; Peptides/metabolism ; Phosphatidylcholines/chemistry ; Phospholipids/isolation & purification ; Structure-Activity Relationship ; Temperature ; Triolein/chemistry ; Water/chemistry
Chemical Substances	Apolipoprotein A-I ; High-Density Lipoproteins, Pre-beta ; Peptides ; Phosphatidylcholines ; Phospholipids ; Water (059QF0KO0R) ; Triolein (122-32-7) ; 1-palmitoyl-2-oleoylphosphatidylcholine (TE895536Y5)
Language	English
Publishing date	2011-06-17
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	218078-9
ISSN	1542-0086 ; 0006-3495
ISSN (online)	1542-0086
ISSN	0006-3495
DOI	10.1016/j.bpj.2011.03.055
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 235: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MO 2: Show issues

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Measurement of lipogenic flux by deuterium resolved mass spectrometry.

Fu, Xiaorong / Deja, Stanisław / Fletcher, Justin A / Anderson, Norma N / Mizerska, Monika / Vale, Gonçalo / Browning, Jeffrey D / Horton, Jay D / McDonald, Jeffrey G / Mitsche, Matthew A / Burgess, Shawn C

Nature communications

2021 Volume 12, Issue 1, Page(s) 3756

Abstract: De novo lipogenesis (DNL) is disrupted in a wide range of human disease. Thus, quantification of DNL may provide insight into mechanisms and guide interventions if it can be performed rapidly and noninvasively. DNL flux is commonly measured ... ...

Abstract	De novo lipogenesis (DNL) is disrupted in a wide range of human disease. Thus, quantification of DNL may provide insight into mechanisms and guide interventions if it can be performed rapidly and noninvasively. DNL flux is commonly measured by
MeSH term(s)	Animals ; Deuterium/chemistry ; Fatty Acids/biosynthesis ; Gas Chromatography-Mass Spectrometry/methods ; Lipogenesis/physiology ; Liver/metabolism ; Male ; Mice ; Mice, Inbred C57BL ; Triglycerides/biosynthesis
Chemical Substances	Fatty Acids ; Triglycerides ; Deuterium (AR09D82C7G)
Language	English
Publishing date	2021-06-18
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-021-23958-4
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Three-phase liquid extraction: a simple and fast method for lipidomic workflows.

Vale, Gonçalo / Martin, Sarah A / Mitsche, Matthew A / Thompson, Bonne M / Eckert, Kaitlyn M / McDonald, Jeffrey G

Journal of lipid research

2019 Volume 60, Issue 3, Page(s) 694–706

Abstract: An unbiased sample preparation free of interferents (i.e., competing analytes, detergents, plastics) is critical to any lipid MS workflow. Here we present a novel three-phase lipid extraction (3PLE) technique using a single-step liquid-liquid extraction ( ...

Abstract	An unbiased sample preparation free of interferents (i.e., competing analytes, detergents, plastics) is critical to any lipid MS workflow. Here we present a novel three-phase lipid extraction (3PLE) technique using a single-step liquid-liquid extraction (LLE) that allows both extraction and fractionation of lipids by polarity. 3PLE is composed of one aqueous and two organic phases. The upper organic phase is enriched in neutral lipids (triacylglycerols and cholesteryl esters), while the middle organic phase contains the major glycerophospholipids. Thin-layer chromatography, radioactive labeling, and MS were used to confirm lipid partitioning. 3PLE efficiency was demonstrated for bovine liver, human pooled plasma, mouse liver, mouse brain, and mouse white adipose tissue. Compared with the gold-standard Bligh/Dyer LLE, 3PLE showed significant advantages. For direct-infusion workflows, there was a decrease in ion suppression with a corresponding increased number of lipid species identified. For LC/MS workflows, increased signal intensities were observed for lower-abundance lipid species such as phosphatidic acid and phosphatidylserine. 3PLE also proved to be a valuable tool for fatty acid profiling by GC/MS, allowing for the separate identification of neutral and polar fatty acids.
MeSH term(s)	Animals ; Cattle ; Humans ; Lipidomics/methods ; Liquid-Liquid Extraction/methods ; Mice ; Time Factors ; Workflow
Language	English
Publishing date	2019-01-04
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	10.1194/jlr.D090795
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 175: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (1.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Vibrio deploys type 2 secreted lipase to esterify cholesterol with host fatty acids and mediate cell egress.

Chimalapati, Suneeta / de Souza Santos, Marcela / Lafrance, Alexander E / Ray, Ann / Lee, Wan-Ru / Rivera-Cancel, Giomar / Vale, Gonçalo / Pawlowski, Krzysztof / Mitsche, Matthew A / McDonald, Jeffrey G / Liou, Jen / Orth, Kim

eLife

2020 Volume 9

Abstract: Pathogens find diverse niches for survival including inside a host cell where replication occurs in a relatively protective environment. ...

Abstract	Pathogens find diverse niches for survival including inside a host cell where replication occurs in a relatively protective environment.
MeSH term(s)	Bacterial Proteins/metabolism ; Cholesterol/metabolism ; Esterification ; Fatty Acids/metabolism ; Genomic Islands ; Lipase/metabolism ; Type III Secretion Systems ; Vibrio parahaemolyticus/enzymology ; Vibrio parahaemolyticus/metabolism
Chemical Substances	Bacterial Proteins ; Fatty Acids ; Type III Secretion Systems ; Cholesterol (97C5T2UQ7J) ; Lipase (EC 3.1.1.3)
Language	English
Publishing date	2020-08-18
Publishing country	England
Document type	Journal Article
ZDB-ID	2687154-3
ISSN	2050-084X ; 2050-084X
ISSN (online)	2050-084X
ISSN	2050-084X
DOI	10.7554/eLife.58057
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: A Medicinal Chemistry-Driven Approach Identified the Sterol Isomerase EBP as the Molecular Target of TASIN Colorectal Cancer Toxins.

Theodoropoulos, Panayotis C / Wang, Wentian / Budhipramono, Albert / Thompson, Bonne M / Madhusudhan, Nikhil / Mitsche, Matthew A / McDonald, Jeffrey G / De Brabander, Jef K / Nijhawan, Deepak

Journal of the American Chemical Society

2020 Volume 142, Issue 13, Page(s) 6128–6138

Abstract: TASIN (Truncated APC-Selective Inhibitors) compounds are selectively toxic to colorectal cancer cells ... ...

Abstract	TASIN (Truncated APC-Selective Inhibitors) compounds are selectively toxic to colorectal cancer cells with
MeSH term(s)	Adenomatous Polyposis Coli Protein/genetics ; Antineoplastic Agents/chemistry ; Antineoplastic Agents/pharmacology ; Biosynthetic Pathways/drug effects ; Cholesterol/metabolism ; Colorectal Neoplasms/drug therapy ; Colorectal Neoplasms/genetics ; Colorectal Neoplasms/metabolism ; Drug Discovery ; Enzyme Inhibitors/chemistry ; Enzyme Inhibitors/pharmacology ; HCT116 Cells ; Humans ; Mutation ; Nerve Tissue Proteins/antagonists & inhibitors ; Nerve Tissue Proteins/metabolism ; Oxidoreductases Acting on CH-CH Group Donors/antagonists & inhibitors ; Oxidoreductases Acting on CH-CH Group Donors/metabolism ; Steroid Isomerases/antagonists & inhibitors ; Steroid Isomerases/metabolism
Chemical Substances	APC protein, human ; Adenomatous Polyposis Coli Protein ; Antineoplastic Agents ; Enzyme Inhibitors ; Nerve Tissue Proteins ; Cholesterol (97C5T2UQ7J) ; Oxidoreductases Acting on CH-CH Group Donors (EC 1.3.-) ; DHCR24 protein, human (EC 1.3.1.-) ; 7-dehydrocholesterol reductase (EC 1.3.1.21) ; Steroid Isomerases (EC 5.3.3.-) ; EBP protein, human (EC 5.3.3.5)
Language	English
Publishing date	2020-03-19
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	3155-0
ISSN	1520-5126 ; 0002-7863
ISSN (online)	1520-5126
ISSN	0002-7863
DOI	10.1021/jacs.9b13407
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Bonn / Germany

Z 4' 55/32: Show issues
Z 7.3: Show issues

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Details ▾
- See ZB MED holdings
- Order with fees

Article: C-Terminus of Apolipoprotein A-I Removes Phospholipids from a Triolein/Phospholipids/Water Interface, but the N-Terminus Does Not: A Possible Mechanism for Nascent HDL Assembly

Mitsche, Matthew A / Small, Donald M

Biophysical journal. 2011 July 20, v. 101, no. 2

2011

Abstract: Apolipoprotein A-I (ApoA-I) is the principle protein component of HDL, also known as “good cholesterol,” which is an inverse marker for cardiovascular disease. The N-terminal 44 amino acids of ApoA-I (N44) are predicted to be responsible for ... ...

Abstract	Apolipoprotein A-I (ApoA-I) is the principle protein component of HDL, also known as “good cholesterol,” which is an inverse marker for cardiovascular disease. The N-terminal 44 amino acids of ApoA-I (N44) are predicted to be responsible for stabilization of soluble ApoA-I, whereas the C-terminal 46 amino acids (C46) are predicted to initiate lipid binding and oligomerization. In this work, we apply what we believe to be a novel application of drop tensiometry to study the adsorption and desorption of N44 and C46 at a triolein/POPC/water (TO/POPC/W) interface. The amount of peptide that adsorbed to the surface was dependent on the surface concentration of 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC) and pressure (Π) before adsorption. At a TO/POPC/W interface, the exclusion pressure (ΠEX) of C46 was 25.8 mN/m, and was 19.3 mN/m for N44. Once adsorbed, both peptides formed a homogeneous surface with POPC but were progressively ejected from the surface by compression. During a compression, C46 removed POPC from the surface whereas N44 did not. Repeated compressions caused C46 to deplete entirely the surface of phospholipid. If full-length ApoA-I could also remove phospholipid, this could provide a mechanism for the transfer of surface components of chylomicrons and very low density lipoprotein to high density lipoprotein with the assistance of phospholipid transfer protein.
Keywords	adsorption ; amino acids ; apolipoprotein A-I ; cardiovascular diseases ; cholesterol ; chylomicrons ; desorption ; high density lipoprotein ; peptides ; phospholipids ; triolein ; very low density lipoprotein
Language	English
Dates of publication	2011-0720
Size	p. 353-361.
Publishing place	Elsevier Inc.
Document type	Article
ZDB-ID	218078-9
ISSN	1542-0086 ; 0006-3495
ISSN (online)	1542-0086
ISSN	0006-3495
DOI	10.1016/j.bpj.2011.03.055
Database	NAL-Catalogue (AGRICOLA)

In stock of ZB MED Bonn / Germany

Z 4' 66/63: Show issues

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Details ▾
- See ZB MED holdings
- Order with fees

To top

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

More links

Kategorien

In stock of ZB MED Bonn / Germany

Order via subito

Inter-library loan at ZB MED

More links

Kategorien

In stock of ZB MED Bonn / Germany

Order via subito

Inter-library loan at ZB MED