TY - JOUR
T1 - Role of natriuretic peptides in ion transport mechanisms
AU - Kourie, Joseph I.
AU - Rive, Megan J.
PY - 1999
Y1 - 1999
N2 - Natriuretic peptides (NP) act as ligands on the guanylyl cyclase family of receptors. The NP binding site on these receptors is extracellular and the guanylyl cyclase and protein kinase domains are intracellular. The guanylyl cyclase receptor catalyzes the synthesis of the second messenger molecule, cGMP, which activates protein kinase. This in turn is involved in the phosphorylation of various ion transport proteins. Ion transport proteins, which are modulated by NP and are thought to underlie the natriuretic and diuretic actions of NP, include: (a) calcium-activated K+ channels; (b) ATP- sensitive K+ channels; (c) inwardly-rectifying K+ channels; (d) outwardly- rectifying K+ channels; (e) L-type Ca2+ channels; (f) Cl- channels including cystic fibrosis transmembrane conductance regulator Cl- channels; (g) Na+-K+2Cl- co-transporter; (h) Na+-K+ ATPase; (i) Na+ channels; (j) stretch-activated channels; and (k) water channels. It appears that NP modulate the kinetics, rather than the conductance, of ion channels. Some of these channels, like the Ca2+, ATP-sensitive K+ and stretch-activated channels, are also involved in NP secretion. In addition, the structural properties of the NP, e.g., ovCNP-22 and ovCNP-39, appear to confer on them the ability to form ion channels. These CNP-formed ion channels can modify the trans-membrane signal transduction and second messenger systems underlying NP-induced pathological effects.
AB - Natriuretic peptides (NP) act as ligands on the guanylyl cyclase family of receptors. The NP binding site on these receptors is extracellular and the guanylyl cyclase and protein kinase domains are intracellular. The guanylyl cyclase receptor catalyzes the synthesis of the second messenger molecule, cGMP, which activates protein kinase. This in turn is involved in the phosphorylation of various ion transport proteins. Ion transport proteins, which are modulated by NP and are thought to underlie the natriuretic and diuretic actions of NP, include: (a) calcium-activated K+ channels; (b) ATP- sensitive K+ channels; (c) inwardly-rectifying K+ channels; (d) outwardly- rectifying K+ channels; (e) L-type Ca2+ channels; (f) Cl- channels including cystic fibrosis transmembrane conductance regulator Cl- channels; (g) Na+-K+2Cl- co-transporter; (h) Na+-K+ ATPase; (i) Na+ channels; (j) stretch-activated channels; and (k) water channels. It appears that NP modulate the kinetics, rather than the conductance, of ion channels. Some of these channels, like the Ca2+, ATP-sensitive K+ and stretch-activated channels, are also involved in NP secretion. In addition, the structural properties of the NP, e.g., ovCNP-22 and ovCNP-39, appear to confer on them the ability to form ion channels. These CNP-formed ion channels can modify the trans-membrane signal transduction and second messenger systems underlying NP-induced pathological effects.
KW - Channel-forming peptides
KW - Fluid and electrolyte homeostasis
KW - Hypoxia-reperfusion
KW - Ion transport
KW - Relaxation
KW - Signal transduction
KW - Vasodilation
UR - http://www.scopus.com/inward/record.url?scp=0032904325&partnerID=8YFLogxK
U2 - 10.1002/(SICI)1098-1128(199901)19:1<75::AID-MED4>3.0.CO;2-6
DO - 10.1002/(SICI)1098-1128(199901)19:1<75::AID-MED4>3.0.CO;2-6
M3 - Review article
SN - 0198-6325
VL - 19
SP - 75
EP - 94
JO - Medicinal Research Reviews
JF - Medicinal Research Reviews
IS - 1
ER -