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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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Published in: | Biochemistry (Easton) 1991-10, Vol.30 (42), p.10065-10074 |
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container_end_page | 10074 |
container_issue | 42 |
container_start_page | 10065 |
container_title | Biochemistry (Easton) |
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creator | Ehlers, Mario R. W Riordan, James F |
description | 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. |
doi_str_mv | 10.1021/bi00106a001 |
format | article |
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Psychology</subject><subject>Hydrolysis</subject><subject>Membrane Proteins - metabolism</subject><subject>Molecular and cellular biology</subject><subject>reviews</subject><subject>Solubility</subject><subject>Stereoisomerism</subject><issn>0006-2960</issn><issn>1520-4995</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1991</creationdate><recordtype>article</recordtype><recordid>eNqFkc1rFTEUxYMo9bW6ci3MQuxCRm-SmaSvO6naChVFn25DkrlDU2cmz9wM2v_ePOdRRQQh5Ov8ODm5l7FHHJ5zEPyFCwAclC3zHbbirYC6Wa_bu2wFAKoWawX32SHRdTk2oJsDdsDXsgy9YuEdji7ZCattihnDRNX3kK8qisPsBqx8nKeMaWtTptMqxXIV-4WNww0FqsJU5SusEg5o6Zeaix-Nf_s-YPd6OxA-3K9H7POb15uzi_ry_fnbs5eXtW14k2tshRCgOik72Tu0Xdl3zvrdD32vwGnZK6lKeHDWOSeV77ToOqlEj-haecSeLr7l4W8zUjZjII_DUMLEmYwWXAst_g9yxblqNS_gswX0KRIl7M02hdGmG8PB7Dpg_uhAoR_vbWc3YvebXUpe9Cd73ZK3Q1-K5APdYi3wE3ECBasXLFDGH7eyTV-N0lK3ZvPhk3mlvnzcqPMLs-OPF956MtdxTlMp8j8D_gRBJasy</recordid><startdate>19911001</startdate><enddate>19911001</enddate><creator>Ehlers, Mario R. 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source | ACS CRKN Legacy Archives |
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 |
title | Membrane proteins with soluble counterparts: role of proteolysis in the release of transmembrane proteins |
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