Intact Alzheimer amyloid precursor protein (APP) is present in platelet membranes and is encoded by platelet mRNA

J. E. Gardella, J. Ghiso, G. A. Gorgone, D. Marratta, A. P. Kaplan, B. Frangione, P. D. Gorevic

Research output: Contribution to journalArticlepeer-review

71 Scopus citations

Abstract

Using antibodies directed against N-terminal and C-terminal epitopes we have immunologically detected APP species in the membrane and saline-soluble fractions of unstimulated platelets, and in the conditioned medium of thrombin-stimulated platelets. These studies demonstrate an intact 140kD membrane-associated form of APP that is released on degranulation. Evidence that platelets synthesize at least one form of APP (APP751) was obtained by enzymatic amplification of specific mRNA using Polymerase Chain Reaction (PCR) and direct sequence analysis of PCR product. Processing of APP for release may occur via successive C-terminal truncations, and/or by the release and proteolysis of an intact membrane associated form. An intact form of APP in platelets provides a circulating substrate upon which proteases from many tissues may act to produce beta protein (AB) during pathologic conditions.

Original languageEnglish
Pages (from-to)1292-1298
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume173
Issue number3
DOIs
StatePublished - 31 Dec 1990
Externally publishedYes

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