Pharmacological characterization of the postsynaptic alpha-adrenoceptors in isolated canine mesenteric arteries and veins

1987 ◽  
Vol 335 (1) ◽  
pp. 44-49 ◽  
Author(s):  
Haruki Itoh ◽  
Jai D. Kohli ◽  
Sol I. Rajfer
2005 ◽  
Vol 19 (5) ◽  
pp. 495-502 ◽  
Author(s):  
Michel R. Corboz ◽  
Maria A. Rivelli ◽  
Lori Varty ◽  
Jennifer Mutter ◽  
Mark Cartwright ◽  
...  

Background Functional α1- and α2-adrenoreceptor subtype pharmacology was characterized in an in vitro human nasal mucosa contractile bioassay. Methods Nasal mucosa was obtained from 49 donor patients and mucosal strips were placed in chambers filled with Krebs–Ringer solution and attached to isometric force transducers. Results Nonselective α-adrenoreceptor agonists epinephrine, norepinephrine, and oxymetazoline produced concentration-dependent contractions of isolated human nasal mucosa (pD2= 5.2, 4.9, and 6.5, respectively). The α2-adrenoreceptor agonist BHT-920 (10 μM)–induced contractions were blocked by yohimbine (0.01–1 μM) and prazosin (0.01–1 μM) inhibited the contractile response to the α1-adrenoreceptor agonist phenylephrine (10 μM). Histological analysis showed that phenylephrine and BHT-920 differentially contracted the arteries and veins of human nasal mucosa, respectively. Conclusion Our results indicate that functional α1- and α2-adrenoceptors are present and functional in human nasal mucosa. The a 2-adrenoceptors display a predominant role in contracting the veins and the α1-adrenoceptors appear to preferentially constrict the human nasal arteries.


1984 ◽  
Vol 120 (1) ◽  
pp. 109-116 ◽  
Author(s):  
STIG STEEN ◽  
TOR V. C. SKÄRBY ◽  
LARS NORGREN ◽  
KARL-ERIK ANDERSSON

1982 ◽  
Vol 319 (1) ◽  
pp. 1-7 ◽  
Author(s):  
Yoshihiko Sakakibara ◽  
Motohatsu Fujiwara ◽  
Ikunobu Muramatsu

2019 ◽  
Vol 2019 ◽  
pp. 1-13 ◽  
Author(s):  
Giacomo Pepe ◽  
Manuela Giovanna Basilicata ◽  
Albino Carrizzo ◽  
Simona Adesso ◽  
Carmine Ostacolo ◽  
...  

Peptides derived from buffalo dairy products possess multiple healthy properties that cannot be exerted as long as they are encrypted in parent proteins. To evaluate the biological activities of encrypted peptide sequences from buffalo ricotta cheese, we performed a simulated gastrointestinal (GI) digestion. Chemical and pharmacological characterization of the digest led to the identification of a novel peptide endowed with antioxidant and antihypertensive action. The GI digest was fractionated by Semiprep-HPLC, and fractions were tested against reactive oxygen species (ROS) release in an H2O2-treated intestinal epithelial cell line. UHPLC-PDA-MS/MS analysis revealed the presence of an abundant β-lactoglobulin peptide (BRP2) in the most active fraction. Pharmacological characterization of BRP2 highlighted its antioxidant activity, involving ROS reduction, nuclear factor erythroid 2-related factor 2 (Nrf2) activation, and cytoprotective enzyme expression. The bioavailability of BRP2 was evaluated in intestinal transport studies through a Caco-2 cell monolayer. Equal bidirectional transport and linear permeability indicate that BRP2 was absorbed mainly through passive diffusion. In addition to its local effects, the BRP2 administration on mouse mesenteric arteries was able to reduce the angiotensin II-induced vasoconstriction by the Nrf2 nuclear translocation, the reduction of the active form of Ras-related C3 botulinum toxin substrate 1 (Rac1), and the NADPH oxidase activity. These data further highlight the role of buffalo ricotta cheese-derived peptides against oxidative stress-related diseases and suggest their health-promoting potential.


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