1. The melanocortin system during fasting
Fabrice Bertile, Thierry Raclot Peptides. 2006 Feb;27(2):291-300. doi: 10.1016/j.peptides.2005.03.063. Epub 2005 Nov 7.
This paper sets out to review the implication of the melanocortin system in regulating feeding behavior and energy balance during short- and long-term food deprivation. It is discussed in relation to: (1) body fat exhaustion and the known enhanced drive for refeeding in late fasting and (2) peripheral hormonal status with emphasis on the effect of leptin administration on melanocortin gene expression according to fat store mobilization.
2. Melanocortinergic control of penile erection
H Wessells, J E Blevins, T W Vanderah Peptides. 2005 Oct;26(10):1972-7. doi: 10.1016/j.peptides.2004.11.035.
Melanocortin receptors in the forebrain and spinal cord can be activated by endogenous or synthetic ligands to induce penile erection in rats and human subjects. To better understand how melanocortin circuits play a role in sex behavior, we review the contribution of melanocortin receptors and/or neurons in the hypothalamus, hindbrain, spinal cord and peripheral nerves to erectile function. New information regarding neuropeptides that mediate penile erection has extended our understanding of the central control of sex behavior, and melanocortin agonists may provide alternatives to existing treatment for highly prevalent problems including erectile dysfunction.
3. Effects of intermedin(1-53) on cardiac function and ischemia/reperfusion injury in isolated rat hearts
Jing-Hui Yang, Yue-Xia Jia, Chun-Shui Pan, Jing Zhao, Ming Ouyang, Jun Yang, Jaw-Kang Chang, Chao-Shu Tang, Yong-Fen Qi Biochem Biophys Res Commun. 2005 Feb 18;327(3):713-9. doi: 10.1016/j.bbrc.2004.12.071.
Intermedin (IMD) is a novel member of the calcitonin/calcitonin gene-related peptide (CT/CGRP) family identified from human and other vertebrate tissues. Preprointermedin (preproIMD) can generate a 47 amino acid mature peptide (IMD(1-47)) and a shorter 40 amino acid one (IMD(8-47)) by proteolytic cleavage. Amino acid sequence analysis showed that cleavage sites are located between two basic amino acids at Arg93-Arg94, resulting in the production of preproIMD(95-147), namely IMD(1-53). The present study was designed to observe the effects of IMD(1-53) on cardiac function in ischemia/reperfusion (I/R) injury in isolated rat hearts. Perfusion with high-dose IMD(1-53) gave higher left ventricular systolic pressure (LVSP) and maximal rate of increase and decrease of left ventricle pressure (+/-LVdP/dt(max)), and coronary perfusion flow (CPF) than those of controls. Cardiac I/R induced a marked inhibition of cardiac function and myocardial injury. Reperfusion with IMD(1-53) significantly ameliorated the inhibited cardiac function and bradycardia induced by I/R. Compared with the I/R-treatment alone, IMD(1-53) reperfusion augmented CPF, LVSP, and maximal rate of increase and decrease of left ventricle pressure (+/-LVdP/dt(max)) and decreased LVDP. In addition, reperfusion with IMD(1-53)markedly attenuated the leakage of lactate dehydrogenase and malondialdehyde content in myocardia compared with I/R alone. Reperfusion with IMD(1-53)increased the content of cyclic adenosine monophosphate in comparison with I/R alone. Interestingly, the above IMD(1-53) effects are similar to those of adrenomedullin. These results suggest that IMD(1-53), like adrenomedullin, has cardioprotective effects against myocardial I/R injury.
