Abstract
Many secreted polypeptide regulators of angiogenesis are devoid of signal peptides. These proteins are released through nonclassical pathways independent of endoplasmic reticulum and Golgi. In most cases, the nonclassical protein export is induced by stress. It usually serves to stimulate repair or inflammation in damaged tissues. We review the secreted signal peptide-less regulators of angiogenesis and discuss the mechanisms and biological significance of their unconventional export.
Highlights
Many secreted polypeptide regulators of angiogenesis are devoid of signal peptides
Most secreted proteins have in their primary structure a N-terminally located cleavable hydrophobic signal peptide, which is required for the translocation of newly translated polypeptides into the endoplasmic reticulum (ER) followed by the transport through the ERGolgi compartment and release mediated by the fusion of Golgi-derived exocytotic vesicles with the cells membrane [3]
Many polypeptide regulators of angiogenesis are secreted through ER-Golgi-independent pathways, and secretion of these proteins is often induced by stress conditions
Summary
Many secreted polypeptide regulators of angiogenesis are devoid of signal peptides. These proteins are released through nonclassical pathways independent of endoplasmic reticulum and Golgi. Among these polypeptides are growth factors and cytokines, which signal through specific cell membrane receptors. Most secreted proteins have in their primary structure a N-terminally located cleavable hydrophobic signal peptide, which is required for the translocation of newly translated polypeptides into the endoplasmic reticulum (ER) followed by the transport through the ERGolgi compartment and release mediated by the fusion of Golgi-derived exocytotic vesicles with the cells membrane [3]. Many polypeptide regulators of angiogenesis are secreted through ER-Golgi-independent pathways, and secretion of these proteins is often induced by stress conditions.
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