Human plasma proapoa-I: Isolation and amino-terminal sequence

Brewer, H. Bryan; Fairwell, T; Kay, Linda L.; Meng, M S; Ronan, R; Law, Simon W.; Light, Jimmy A.

doi:10.1016/0006-291x(83)91772-2

Cited by 54 publications

(23 citation statements)

References 19 publications

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“…Moreover, the sequence of the 6 amino-acid propeptide in Tangier disease is identical to normal. 143 ' 144 An alternative view is that there is a normal rate of apo A-l production and conversion of proapo A-l to apo A-l, and then hypercatabolism of the abnormal apo A-l, resulting in a relative enrichment of the preprotein in plasma. …”

Section: Tangier Diseasementioning

confidence: 99%

Clinical, biochemical, and genetic features in familial disorders of high density lipoprotein deficiency.

Schaefer¹

1984

Arteriosclerosis

161

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P lasma high density lipoproteins (HDL, density = 1.063 -1.21 g/ml) mostly have alpha mobility on lipoprotein electrophoresis, and are composed (weight %) of approximately 50% protein, 25% phospholipid, 20% cholesterol (mainly esterified), and triglyceride. 1 " 1 Fluctuations in HDL levels have been associated largely with alterations in HDL (d = 1.063-1.125 g/ml). 5 Cholesterol is the HDL constituent commonly measured (following precipitation of other lipoproteins), and decreased plasma HDL cholesterol concentrations have been associated with premature coronary artery disease (CAD).*" 11 The normal values for this parameter are given in Table 1.

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Section: Tangier Diseasementioning

confidence: 99%

Clinical, biochemical, and genetic features in familial disorders of high density lipoprotein deficiency.

Schaefer¹

1984

Arteriosclerosis

161

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“…18 amino acids are contained within the prepeptide followed by a six amino acid propeptide. PreproapoA-I undergoes cotranslational proteolytic cleavage to proapoA-I, which is secreted into human plasma or lymph (apoA-I+1,,+2 isoforms) still containing the six amino acid propeptide attached to the aminoterminus of mature apoA-I (5,6). In normal subjects proapoA-I is converted in plasma to mature apoA-I (apoA-Io_1, 2 isoforms) by a specific calcium requiring peptidase (7)(8)(9).…”

Section: Introductionmentioning

confidence: 99%

In vivo metabolism of proapolipoprotein A-I in Tangier disease.

Bojanovski¹,

Gregg²,

Zech³

et al. 1987

J. Clin. Invest.

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Tangier disease is a rare familial disorder characterized by extremely low levels of apolipoprotein A-I (apoA-I) and high density lipoproteins (HDL). In normal subjects, proapoA-I is secreted into plasma and converted to mature apoA-I by the cleavage of the amino-terminal six amino acids with the major isoprotein in plasma being mature apoA-I. In contrast, in Tangier disease there is a marked relative increase of proapoA-I as compared with mature apoA-I. ProapoA-I and mature apoA-I were isolated from normal and Tangier disease subjects, radiolabeled, and autologous apoA-I isoproteins injected into normal and Tangier subjects. The in vivo catabolism and conversion of proapoA-I and mature apoA-I in normal and Tangier disease subjects were quantitated. A comparison of the rate of catabolism of apoA-I isoproteins from plasma revealed a significantly faster rate of catabolism of both isoproteins of apoA-I in Tangier subjects when compared with normal subjects. The fractional conversion rate of proapoAI to mature apoA-I was 3.9 d' in normal subjects and 3.6 d ' in Tangier subjects. The results indicate that (a) apoA-I enters plasma as the pro isoprotein in both normal and Tangier subjects, (b) Tangier disease subjects have a normal fractional rate of conversion of proapoA-I to mature apoA-I, (c) proapoA-I is catabolized at the same rate as mature apoA-I in Tangier subjects, and (d) Tangier subjects catabolize both pro and mature apoA-I at a much greater rate than do normal subjects. Therefore, the relative increase in proapoA-I in Tangier disease is due to a marked decrease in mature apoA-I resulting from rapid catabolism of both pro-and mature apoA-I and not to defective conversion of proapoA-I to mature apoA-I.

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“…Some lectins require metal ions for the saccharide-binding activity (Sumner and Howell, 1936). Extensive studies by NMR have revealed a complicated set of interlocking equilibrium involving the apoprotein and various complexes with metal ions and the saccharides (Brewer et al, 1983).…”

Section: Metal Ion Requirementsmentioning

confidence: 99%

Antimicrobial activity of lectins from Antimicrobial Activity of Lectins from Plants

Karnchanatat¹

2012

Antimicrobial Agents

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Human plasma proapoa-I: Isolation and amino-terminal sequence

Cited by 54 publications

References 19 publications

Clinical, biochemical, and genetic features in familial disorders of high density lipoprotein deficiency.

Clinical, biochemical, and genetic features in familial disorders of high density lipoprotein deficiency.

In vivo metabolism of proapolipoprotein A-I in Tangier disease.

Antimicrobial activity of lectins from Antimicrobial Activity of Lectins from Plants

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