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Only multimers of a synthetic peptide of human apolipoprotein-e are biologically-active

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Overview

authors

  • Dyer, C. A.
  • Smith, R. S.
  • Curtiss, Linda

publication date

  • 1991

journal

  • Journal of Biological Chemistry  Journal

abstract

  • Plasma apolipoprotein E (apoE) is a ligand for the cellular uptake of cholesterol-rich plasma lipoproteins. ApoE also inhibits mitogen-stimulated lymphocyte proliferation and gonadotropin-stimulated ovarian theca/interstitial cell androgen production. To address the mechanism(s) by which apoE is active and to understand its interaction with the target cells, we prepared and examined the inhibitory activity of a series of apoE synthetic peptides. ApoE peptides representing amino acid residues 93-112, 141-155, 161-171, 172-182, and 174-193 were not active in either bioassay. However, specific inhibition of both lymphocyte proliferation and ovarian androgen production was observed with a self-conjugate of peptide-(141-155). Furthermore, a synthesized dimeric peptide representing two repeats of sequence-(141-155) (i.e. (141-155)-(141-155] was active as well. In both bioassays, the inhibition observed was not a result of direct cell killing. Furthermore, these apoE peptides exhibited activities with characteristics that were shared with those of native apoE. The results indicate that amino acid residues 141-155 of apoE are responsible for the biological activity of apoE. Furthermore, the results suggest that dimers or multimers of native apoE may be a biologically important species.

subject areas

  • Amino Acid Sequence
  • Androgen Antagonists
  • Androgens
  • Animals
  • Apolipoproteins E
  • Cells, Cultured
  • Electrophoresis, Polyacrylamide Gel
  • Female
  • Humans
  • Liver Neoplasms, Experimental
  • Lymphocyte Activation
  • Lymphocytes
  • Mitogens
  • Molecular Sequence Data
  • Muscle, Smooth
  • Ovary
  • Peptides
  • Rabbits
  • Rats
  • Tumor Cells, Cultured
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Identity

International Standard Serial Number (ISSN)

  • 0021-9258

PubMed ID

  • 1869538
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Additional Document Info

start page

  • 15009

end page

  • 15015

volume

  • 266

issue

  • 23

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