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Vasoactive intestinal peptide fragment VIP10–28 and active vasodilation in human skin

A recent study reported the vasoactive intestinal peptide (VIP) fragment VIP 10–28 inhibited the rise in skin blood flow during heat stress. Our laboratory has reported that the nitric oxide (NO) pathway and histamine receptor-1 (H1)-receptor activation is common to both exogenous VIP-mediated dilation and active vasodilation (AVD). The present study aimed to further examine the specific role for VIP in AVD by using VIP 10–28 to antagonize VIP-mediated dilation in the presence of NO synthase (NOS) inhibition and an H1 antagonist. Study 1 ( n = 12) examined whether VIP 10–28 antagonizes vasodilation to exogenous VIP via inhibition of NO-dependent mechanisms. Study 2 ( n = 6) investigated AVD in skin sites receiving VIP 10–28 alone and in combination with NOS inhibition. Study 3 ( n = 6) examined AVD in sites receiving VIP 10–28 alone and combined VIP 10–28 and H1 antagonism. Due to differences in our findings and those previously published, study 4 ( n = 6) investigated whether an increase in baseline skin blood flow could result in a diminished rise in AVD. Red blood cell flux was measured using laser Doppler flowmetry, and cutaneous vascular conductance (flux/mean arterial pressure) was normalized to maximal vasodilation (28 mM sodium nitroprusside). VIP 10–28 augmented vasodilation to exogenous VIP ( P < 0.05 vs. control) and hyperthermia ( P < 0.05 vs. control). NOS inhibition had no effect on the augmented dilation during exogenous VIP or hyperthermia ( P > 0.05). Similarly, H1-receptor antagonists had no effect on the augmented dilation during hyperthermia ( P > 0.05 vs. VIP 10–28 ). In study 4 , percentage of maximal cutaneous vascular conductance was attenuated when baseline skin blood flow was elevated before whole body heating. Our results suggest that VIP 10–28 may be an unsuitable antagonist for examining a role for VIP-mediated dilation in human skin. histamine receptor-1; cutaneous vascular conductance Address for reprint requests and other correspondence: C. T. Minson, Dept. of Human Physiology, 1240 Univ. of Oregon, Eugene, OR 97403-1240 (e-mail: minson@uoregon.edu ) http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Journal of Applied Physiology The American Physiological Society

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