Speciation of HDL

Kane, John P.

doi:10.1007/978-1-4684-1262-8_3

Cited by 3 publications

(2 citation statements)

References 45 publications

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“…ApoM fulfills the criteria of a HDL-associated apolipoprotein because the majority of apoM in plasma is associated with HDL [2]. In situ hybridization experiments demonstrated that apoM is exclusively expressed in hepatocytes in the liver and in tubular cells in the kidney [3].…”

Section: Introductionmentioning

confidence: 98%

Correlation of apolipoprotein M with leptin and cholesterol in normal and obese subjects

Nilsson‐Ehle

Åhrén

2004

The Journal of Nutritional Biochemistry

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Section: Introductionmentioning

confidence: 98%

Correlation of apolipoprotein M with leptin and cholesterol in normal and obese subjects

Nilsson‐Ehle

Åhrén

2004

The Journal of Nutritional Biochemistry

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“…Identification of the mechanisms for atheroprotection by HDL could reveal new drug targets. HDL are spherical, heterogeneous particles comprising nearly equal amounts of lipid and protein with a core of neutral lipids surrounded by a surface monolayer of apolipoproteins (apos), cholesterol, and polar lipids, primarily phosphatidylcholine (6)(7)(8). Apos A-I and A-II are the two major HDL proteins.…”

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confidence: 99%

Plasma Factors Required for Human Apolipoprotein A-II Dimerization

Gillard¹,

Chen

Gaubatz

et al. 2004

Biochemistry

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Although plasma high-density lipoproteins (HDL) have been implicated in several cardioprotective pathways, the physiologic role of apolipoprotein (apo) A-II, the second most abundant of the HDL proteins, remains ambiguous. Human apo A-II is distinguished from most other species by a single cysteine (Cys6), which forms a disulfide bond with other cysteine-containing apos. In human plasma, nearly all apo A-II occurs as disulfide-linked homodimers of 17.4 kDa. Although dimerization is an important determinant of human apo A-II metabolism, its mechanism and the plasma and/or cellular sites of its dimerization are not known. Using SDS-PAGE and densitometry we investigated the kinetics of apo A-II dimerization and observed a slow (t(1/2) = approximately 10 days), second-order process in Tris-buffered saline. In 3 M guanidine hydrochloride, which disrupts apo A-II secondary structure and self-association, the rate was 3-fold slower. In contrast, lipid surfaces that promote apo A-II alpha-helix formation and lipophilic interaction profoundly enhanced the rate. Reassembled HDL increased the second-order rate constant k(2) by 7500-fold, unilamellar 1-palmitoyl-2-oleoylphosphatidylcholine vesicles increased k(2) 850-fold, and physiological concentrations of human serum albumin increased k(2) 220-fold. Thus, while dimerization of apo A-II in aqueous buffer is too slow to account for the high fraction of dimer found in plasma, lipids and proteins "catalyze" dimer formation, a process that could occur either intracellularly prior to secretion or in the plasma compartment following secretion. These data suggest that formation of disulfide links within or between polypeptide chains can be controlled, in part, by coexisting lipids and proteins.

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The Aloha Shirt and Ethnicity in Hawai'i

Arthur

2006

TEXTILE

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Speciation of HDL

Cited by 3 publications

References 45 publications

Correlation of apolipoprotein M with leptin and cholesterol in normal and obese subjects

Correlation of apolipoprotein M with leptin and cholesterol in normal and obese subjects

Plasma Factors Required for Human Apolipoprotein A-II Dimerization

The Aloha Shirt and Ethnicity in Hawai'i

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