The Journal of Neuroscience, December 13, 2006, ():
Cell-Surface Actin Binds Plasminogen and Modulates Neurotransmitter Release from Catecholaminergic Cells
J. Neurosci. Miles et al.
26: 13017
Supplemental Data
Files in this Data Supplement:
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Working model for a local (autocrine/paracrine) catecholaminergic cell plasminogen activation system and its interactions with secreted prohormones. When catecholaminergic cells are stimulated with secretagogues, prohormones, e.g. chromogranin A (CgA), and catecholamines (Cats) are co-released with t-PA (tissue plasminogen activator) from catecholamine storage vesicles by exocytosis. Plasminogen binds to the cell surface and is activated to plasmin by locally released t-PA. Plasminogen activation is enhanced when plasminogen is bound to cell surface receptors, including actin. Secreted prohormones are then processed by plasmin to bioactive peptides. For example, CgA is processed by plasmin to produce bioactive peptides that provide a negative-feedback loop to decrease subsequent catecholamine release. The asterisk indicates the active enzyme (plasmin).
