Mechanisms of vasodilation elicited by VIP in sterically stabilized liposomes in vivo
| Autor: | Florence Séjourné, Hayat Alkan-Onyuksel, Hideyuki Suzuki, Israel Rubinstein, Hiroyuki Ikezaki, Xiao Pei Gao |
|---|---|
| Rok vydání: | 1997 |
| Předmět: |
Male
medicine.medical_specialty Time Factors Physiology Vasoactive intestinal peptide Hamster Vasodilation Nitric oxide Microcirculation chemistry.chemical_compound Cheek pouch Arteriole Physiology (medical) Internal medicine medicine.artery Cricetinae medicine Animals Humans Drug Carriers Dose-Response Relationship Drug Mesocricetus Chemistry Phosphatidylglycerols Peptide Fragments Arterioles Endocrinology Cheek Liposomes Phosphatidylcholines hormones hormone substitutes and hormone antagonists Intravital microscopy Vasoactive Intestinal Peptide |
| Zdroj: | The American journal of physiology. 273(1 Pt 2) |
| ISSN: | 0002-9513 |
| Popis: | The purpose of this study was to begin to determine the mechanisms underlying vasodilation elicited by vasoactive intestinal peptide (VIP) in sterically stabilized liposomes (SSL) in the in situ peripheral microcirculation. Using intravital microscopy, we found that suffusion of VIP in SSL (0.42 and 0.85 nmol) onto the hamster cheek pouch for 1 h elicited significant and prolonged concentration-dependent vasodilation (P < 0.05). Suffusion of VIP in SSL (0.1 nmol) for 7 min elicited a qualitatively similar response, although its magnitude was significantly smaller than that elicited by 1 h of suffusion of VIP in SSL (P < 0.05). The VIP-receptor antagonist VIP-(10-28), but not the amino-terminal fragment VIP-(1-12), significantly attenuated and delayed the onset of VIP in SSL-induced vasodilation (P < 0.05). The nitric oxide (NO) synthase inhibitor NG-nitro-L-arginine methyl ester (L-NAME), but not NG-nitro-D-arginine methyl ester (D-NAME), abrogated VIP in SSL-induced responses. We conclude that VIP in SSL elicits significant and prolonged vasodilation in the in situ peripheral microcirculation, which is specific, partly receptor dependent, and partly transduced by the L-arginine/NO biosynthetic pathway. |
| Databáze: | OpenAIRE |
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