| 1.C.46 The C-type Natriuretic Peptide (CNP) Family
C-type natriuretic peptides (CNPs) are widely distributed in the mammalian central nervous system, the brain, endothelial cells, kidney, and the GI tract. They are also synthesized by many other animals such as fish, frogs, snakes and the platypus. These secreted peptides may play a role in cytokine-associated disorders, septic shock and renal failure in mammals. The CNP from platypus (Ornithorhynchus anatinus) venom yields sustained tonic relaxation of rat uterus. Both human CNP-22 (HsCNP-22) and the highly similar platypus venom CNP-39 (OaCNP-39) form weakly cation-selective, voltage gated, large conductance channels in artificial bilayers. The HsCNP and OaCNP-39 channels exhibit inward rectification, with permeabilities to K+> Na+> Cs>> choline.
The CNP precursor proteins are large, i.e. >100 residue proteins which can be degraded to small peptides, the active channel-forming constituents being derived from the C-termini. For example, the human CNP (126aas) degrades to three peptides CNP-22, CNP-29 and CNP-53, all derived from the C-terminus of the precursor protein.
The transport reaction catalyzed by the oligomeric channels derived from CNP peptides is:
cations (in)  cations (out)
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| References: |
Kourie, J.I. (1999). A component of platypus (Ornithorhynchus anatinus) venom forms slow-kinetic cation channels. J. Mem. Biol. 172: 37-45.
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Kourie, J.I. (1999). Calcium dependence of C-type natriuretic peptide-formed fast K+ channel. Am. J. Physiol. 277: C43-C50.
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Kourie, J.I. (1999). Characterization of a C-type natriuretic peptide (CNP-39)-formed cation-selective channel from platypus (Ornithorhynchus anatinus) venom. J. Physiol. 518: 359-369.
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Kourie, J.I. (1999). Synthetic mammalian C-type natriuretic peptide forms large cation channels. FEBS Lett. 445: 57-62.
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Rubattu, S., S. Marchitti, F. Bianchi, S. Di Castro, R. Stanzione, M. Cotugno, C. Bozzao, S. Sciarretta, and M. Volpe. (2014). The C2238/αANP variant is a negative modulator of both viability and function of coronary artery smooth muscle cells. PLoS One 9: e113108.
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Sothern, R.B., D.L. Vesely, E.L. Kanabrocki, R.C. Hermida, F.W. Bremner, J.L. Third, M.A. Boles, B.M. Nemchausky, J.H. Olwin, and L.E. Scheving. (1995). Temporal (circadian) and functional relationship between atrial natriuretic peptides and blood pressure. Chronobiol Int 12: 106-120.
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| Examples: |
| TC# | Name | Organismal Type | Example |
| 1.C.46.1.1 | CNP precursor protein (CNP-22 and CNP-29) | Animals | CNP precursor protein of Homo sapiens |
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| 1.C.46.1.2 | Full snake Bradykinin-potentiating and C-type natriuretic peptides (265aas)
| Animals | Bradykinin-potentiating peptide of Bothrops jararaca (Q9PW56) |
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| Examples: |
| TC# | Name | Organismal Type | Example |
| 1.C.46.2.1 | Cardiac Peptide (145aas)
| Animals | Cardiac peptide of Salmo salar (Q78AW6) |
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| 1.C.46.2.2 | Full ventricular natriuretic peptide precursor
| Animals | Full ventricular natriuretic peptide of Acipenser transmontanus (P83962) |
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| 1.C.46.2.3 | Sothern et al. 1995
Natriuretic peptide A of 151 aas, NPPA. The atrial NPPA is a hormone
that plays a key role in mediating cardio-renal homeostasis, and is
involved in vascular remodeling and regulating energy metabolism (Sothern et al. 1995). It acts
by specifically binding and stimulating NPR1 to produce cGMP, which in
turn activates effector proteins, such as PRKG1, that drive various
biological responses (Rubattu et al. 2014).It regulates
vasodilation, natriuresis, diuresis and aldosterone synthesis and is
therefore essential for regulating blood pressure, controlling the
extracellular fluid volume and maintaining the fluid-electrolyte balance
(Sothern et al. 1995). | | NPPA of Homo sapiens |
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