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    Regulation of renin processing and secretion: chemiosmotic control and novel secretory pathway

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    Authors
    King, Jean A.
    Lush, David J.
    Fray, John
    UMass Chan Affiliations
    Department of Physiology
    Department of Psychiatry
    Document Type
    Journal Article
    Publication Date
    1993-08-01
    Keywords
    Animals
    Biological Transport
    *Carbohydrate Epimerases
    Carrier Proteins
    Cytoplasmic Granules
    Enzyme Precursors
    Enzymes
    Humans
    Ion Channels
    Osmosis
    Receptors, Cell Surface
    Renin
    Signal Transduction
    Psychiatry
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    Link to Full Text
    http://ajpcell.physiology.org/cgi/reprint/265/2/C305
    Abstract
    The renin-angiotensin-aldosterone system (RAAS) plays an important role in cardiovascular and electrolyte regulation in health and disease. Juxtaglomerular cells in the kidney regulate endocrine RAAS by physiologically controlling conversion of prorenin and secretion of renin. The classical baroceptor, neurogenic, and macula densa mechanisms regulate renin expression at the cellular level by Ca2+, adenosine 3',5'-cyclic monophosphate (cAMP), and chemiosmotic forces (K+, Cl-, and water flux coupled to H+ movement). The baroceptor mechanism (through Ca2+) activates K+ and Cl- channels in the surface membrane and deactivates a KCl-H+ exchange chemiosmotic transporter in the secretory granular membrane. The neurogenic mechanism (through cAMP) promotes prorenin processing to renin. The macula densa mechanism (through K+ and Cl-) involves the processing of prorenin to renin. Ca2+, by inhibiting the KCl-H+ exchange transporter, prevents secretory granules from engaging in chemiosmotically mediated exocytosis. cAMP, on the other hand, by stimulating H+ influx, provides the acidic granular environment for prorenin processing to renin. It is concluded that, in the presence of a favorable chemiosmotic environment, prorenin is processed to renin, which may then be secreted by regulative degranulation or divergence translocation, a novel secretory pathway used by several secretory proteins, including renin.
    Source
    Am J Physiol. 1993 Aug;265(2 Pt 1):C305-20.
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/45832
    PubMed ID
    7690183
    Related Resources
    Link to Article in PubMed
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    UMass Chan Faculty and Researcher Publications

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