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Secretion without Golgi
Author(s) -
Prudovsky Igor,
Tarantini Francesca,
Landriscina Matteo,
Neivandt David,
Soldi Raffaella,
Kirov Aleksandr,
Small Deena,
Kathir Karuppanan Muthusamy,
Rajalingam Dakshinamurthy,
Kumar Thallapuranam Krishnaswamy Suresh
Publication year - 2007
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.21513
Subject(s) - endoplasmic reticulum , golgi apparatus , microbiology and biotechnology , secretion , secretory pathway , transmembrane protein , secretory protein , chemistry , fgf1 , unfolded protein response , membrane protein , signal transduction , biology , biochemistry , membrane , receptor , fibroblast growth factor , fibroblast growth factor receptor
A growing number of proteins devoid of signal peptides have been demonstrated to be released through the non‐classical pathways independent of endoplasmic reticulum and Golgi. Among them are two potent proangiogenic cytokines FGF1 and IL1α. Stress‐induced transmembrane translocation of these proteins requires the assembly of copper‐dependent multiprotein release complexes. It involves the interaction of exported proteins with the acidic phospholipids of the inner leaflet of the cell membrane and membrane destabilization. Not only stress, but also thrombin treatment and inhibition of Notch signaling stimulate the export of FGF1. Non‐classical release of FGF1 and IL1α presents a promising target for treatment of cardiovascular, oncologic, and inflammatory disorders. J. Cell. Biochem. 103: 1327–1343, 2008. © 2007 Wiley‐Liss, Inc.