当前位置： SCI文献检索 > JOURNAL OF LIPID RESEARCH期刊下所有文献 > Plasma lipid transport in the hedgehog: partial characterization of structure and function of apolipoprotein A-I.

Plasma lipid transport in the hedgehog: partial characterization of structure and function of apolipoprotein A-I.

Abstract：

:Apart from exhibiting the presence of lipoprotein [a] in its plasma, another interest of the European hedgehog in lipoprotein research lies in the quantitative prominence of a complex spectrum of high density lipoproteins (HDL) and very high density lipoproteins (VHDL) as cholesterol transporters in plasma (Laplaud, P. M. et al. 1989. Biochim. Biophys. Acta. 1005: 143-156). We, therefore, initiated studies in the field of reverse cholesterol transport in the hedgehog. As a first step, we characterized apolipoprotein A-I (apoA-I), the main protein component of hedgehog HDL and VHDL. Proteolytic cleavage of apoA-I (M(r) approx. 27 kDa) using two different enzymes resulted in two sets of peptides that were subsequently purified by high performance liquid chromatography, and that allowed us determination of the complete protein sequence. Hedgehog apoA-I thus consists of 241 amino acid residues and exhibits an overall 58% homology to its human counterpart, i.e., the lowest value observed to date among mammalian species. However, it retained the general organization common to all known apoA-Is, i.e., a series of amphipathic helical segments punctuated by proline residues. Circular dichroism experiments indicated a helical content of approx. 45%, increasing to approx. 58% in the presence of lecithin unilamellar liposomes. Apart from other differences, amino acid composition analysis shows that hedgehog apoA-I contains four isoleucine residues, while this amino acid is totally absent from the corresponding protein in higher mammals. Polyclonal antibodies raised against hedgehog apoA-I failed to detect any cross-reactivity between the animal and human proteins, although comparative prediction of the respective antigenic structures using the Hopp-Woods algorithm indicated that several potentially antigenic sites may occur in similar regions of the protein. Finally, hedgehog apoA-I was shown to be able to activate lecithin:cholesterol acyl transferase, although it was 4 to 5 times less efficient in this respect than the human protein.

journal_name

J Lipid Res

journal_title

Journal of lipid research

authors

Sparrow DA,Laplaud PM,Saboureau M,Zhou G,Dolphin PJ,Gotto AM Jr,Sparrow JT

subject

Has Abstract

pub_date

1995-03-01 00:00:00

pages

485-95

issue

eissn

0022-2275

issn

1539-7262

journal_volume

pub_type

杂志文章

在线工具

Plasma lipid transport in the hedgehog: partial characterization of structure and function of apolipoprotein A-I.