| Apolipoprotein A-I amyloidogenic variant L174S, expressed and isolated from stably transfected mammalian cells, is associated with fatty acids. | |
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MedLine Citation:
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PMID: 22295944 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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Sixteen variants of apolipoprotein A-I (ApoA-I) are associated with hereditary systemic amyloidoses, characterized by amyloid deposition in peripheral organs of patients. As these are heterozygous for the amyloidogenic variants, their isolation from plasma is impracticable and recombinant expression systems are needed. Here we report the expression of recombinant ApoA-I amyloidogenic variant Leu174 with Ser (L174S) in stably transfected Chinese hamster ovary-K1 cells. ApoA-I variant L174S was found to be efficiently secreted in the culture medium, from which it was isolated following a one-step purification procedure. Mass spectrometry analyses allowed the qualitative and quantitative definition of the amyloidogenic variant lipid content, which was found to consist of two saturated and two monounsaturated fatty acids. Interestingly, the same lipid species were found to be associated with the wild-type ApoA-I, expressed and isolated using the same cell system, with lower values of the lipid to protein molar ratios with respect to the amyloidogenic variant. A possible role of fatty acids in trafficking and secretion of apolipoproteins may be hypothesized. |
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Authors:
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Daria Maria Monti; Sonia Di Gaetano; Rita Del Giudice; Chiara Giangrande; Angela Amoresano; Maria Monti; Angela Arciello; Renata Piccoli |
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Publication Detail:
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Type: JOURNAL ARTICLE Date: 2012-2-1 |
Journal Detail:
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Title: Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis Volume: - ISSN: 1744-2818 ISO Abbreviation: - Publication Date: 2012 Feb |
Date Detail:
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Created Date: 2012-2-2 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 9433802 Medline TA: Amyloid Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
Affiliation:
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Department of Structural and Functional Biology, University of Naples Federico II, School of Biotechnological Sciences , Naples, Italy. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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