Membrane proteins with soluble counterparts: role of proteolysis in the release of transmembrane proteins

Many proteins lead a dual existence as both membrane-bound and soluble isoforms. One that has recently received a great deal of attention is the amyloid precursor protein (APP), a C-terminally anchored transmembrane protein that is released by a specific proteolytic cleavage near the membrane anchor...

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Bibliographic Details
Published in:Biochemistry (Easton) 1991-10, Vol.30 (42), p.10065-10074
Main Authors: Ehlers, Mario R. W, Riordan, James F
Format: Article
Language:English
Subjects:
amyloid protein
Animals
Biological and medical sciences
Cell membranes. Ionic channels. Membrane pores
Cell structures and functions
Endopeptidases
Fundamental and applied biological sciences. Psychology
Hydrolysis
Membrane Proteins - metabolism
Molecular and cellular biology
reviews
Solubility
Stereoisomerism
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Summary:Many proteins lead a dual existence as both membrane-bound and soluble isoforms. One that has recently received a great deal of attention is the amyloid precursor protein (APP), a C-terminally anchored transmembrane protein that is released by a specific proteolytic cleavage near the membrane anchor to generate a soluble form. While the functions of either form remain speculative, it has been postulated that inappropriate or aberrant cleavage of the APP leads to the generation of beta -amyloid deposits that are associated with Alzheimer's disease and Down syndrome. This has prompted considerable interest in the proteases that may be involved in this process since they would be prime targets for the design of therapeutic agents.
ISSN:0006-2960
1520-4995
DOI:10.1021/bi00106a001