H2 receptor-mediated responses of aortic endothelial cells to histamine

1992 ◽  
Vol 262 (1) ◽  
pp. H220-H224 ◽  
Author(s):  
G. Hekimian ◽  
S. Cote ◽  
J. Van Sande ◽  
J. M. Boeynaems
Keyword(s):  
Endothelial Cells ◽  
Inositol Phosphates ◽  
Umbilical Vein ◽  
Bovine Aortic Endothelial Cell ◽  
Camp Content ◽  
Aortic Endothelial Cells ◽  
Bovine Aortic Endothelial Cells ◽  
H2 Antagonist ◽  
Umbilical Vein Endothelial Cells ◽  
Aortic Endothelial

It is well known that umbilical vein endothelial cells express H1 receptors that mediate the various responses of these cells to histamine, including accumulation of inositol phosphates, rise of cytosolic Ca2+, increased permeability to macromolecules, and release of prostacyclin. In bovine aortic endothelial cells, histamine did not increase the level of inositol phosphates nor the release of prostacyclin. In contrast, it increased the adenosine 3',5'-cyclic monophosphate (cAMP) content of these cells. That response was obtained in the 1 to 100 microM range of concentrations and reached a maximum within 2 min of histamine addition. It was mimicked by the H2-specific agonist dimaprit, inhibited by the H2 antagonist ranitidine, and insensitive to the H1 antagonist mepyramine. Histamine reduced the permeability to albumin of bovine aortic endothelial cell monolayers; this paradoxical effect is likely to be mediated by the rise in cAMP, which is known to enhance the barrier property of the endothelium. In conclusion, bovine aortic endothelial cells are responsive to histamine, and this response is mediated by H2 and not H1 receptors.

scholarly journals Bradykinin and thrombin effects on polyphosphoinositide hydrolysis and prostacyclin production in endothelial cells

1989 ◽  
Vol 263 (1) ◽  
pp. 149-155 ◽  
Author(s):  
K Bartha ◽  
R Müller-Peddinghaus ◽  
L A Van Rooijen
Keyword(s):  
Endothelial Cells ◽  
Inositol Phosphates ◽  
Umbilical Vein ◽  
Fold Increase ◽  
Large Degree ◽  
Inositol Polyphosphates ◽  
Aortic Endothelial Cells ◽  
Bovine Aortic Endothelial Cells ◽  
Umbilical Vein Endothelial Cells ◽  
Prostacyclin Production

Prostacyclin (PGI2) production by thrombin- and bradykinin-stimulated bovine aortic endothelial cells (BAEC) and human umbilical vein endothelial cells (HUVEC) was related to the receptor-linked activation of inositide hydrolysis. Bradykinin caused a rapid and transient 3-fold increase in the formation of inositol polyphosphates in BAEC. The increase in InsP3 reflected changes mainly in the Ins(1,4,5)P3 isomer. Thrombin was less effective than bradykinin in increasing InsP3 levels and appeared to only minimally stimulate the production of PGI2 in BAEC. In HUVEC, thrombin caused a 5-fold elevation of Ins(1,4,5)P3, closely related to a rise in PGI2 production. However, bradykinin did not affect inositol phosphates and PGI2 production in HUVEC. Other inositol phosphates were also assessed to obtain information on putative metabolism of Ins(1,4,5)P3. The present study supports the notion that formation of Ins(1,4,5)P3 is linked to an increase in PGI2 production in endothelial cells and furthermore provides evidence for a large degree of heterogeneity in the responses of BAEC and HUVEC to thrombin and bradykinin.

Tunicamycin increases intracellular calcium levels in bovine aortic endothelial cells

1997 ◽  
Vol 273 (4) ◽  
pp. C1298-C1305 ◽  
Author(s):  
Barbara J. Buckley ◽  
A. R. Whorton
Keyword(s):  
Nitric Oxide ◽  
Endothelial Cells ◽  
Intracellular Calcium ◽  
Inositol Phosphates ◽  
Protein Glycosylation ◽  
Aortic Endothelial Cells ◽  
Bovine Aortic Endothelial Cells ◽  
Intracellular Ca ◽  
Oxide Synthase ◽  
Aortic Endothelial

Tunicamycin is a nucleoside antibiotic that inhibits protein glycosylation and palmitoylation. The therapeutic use of tunicamycin is limited in animals because of its toxic effects, particularly in cerebral vasculature. Tunicamycin decreases palmitoylation of the endothelial isoform of nitric oxide synthase, stimulates nitric oxide synthesis, and increases the concentration of intracellular calcium ([Ca2+]i) in bovine aortic endothelial cells (B. J. Buckley and A. R. Whorton. FASEB J. 11: A110, 1997). In the present study, we investigated the mechanism by which tunicamycin alters [Ca2+]iusing the Ca2+-sensitive dye fura 2. We found that tunicamycin increased [Ca2+]iwithout increasing levels of inositol phosphates. When cells were incubated in the absence of extracellular Ca2+, [Ca2+]irapidly rose in response to tunicamycin, although a full response was not achieved. The pool of intracellular Ca2+ mobilized by tunicamycin overlapped with that mobilized by thapsigargin. Extracellular nickel blocked a full response to tunicamycin when cells were incubated in the presence of extracellular Ca2+. The effects of tunicamycin on [Ca2+]iwere partially reversed by washing out the drug, and the remainder of the response was inhibited by removing extracellular Ca2+. These results indicate that tunicamycin mobilizes Ca2+ from intracellular stores in a manner independent of phospholipase C activation and increases the influx of Ca2+ across the plasma membrane.

scholarly journals Prolyl Carboxypeptidase Mediates the C-Terminal Cleavage of (Pyr)-Apelin-13 in Human Umbilical Vein and Aortic Endothelial Cells

2021 ◽  
Vol 22 (13) ◽  
pp. 6698
Author(s):  
Emilie De Hert ◽  
An Bracke ◽  
Isabel Pintelon ◽  
Eline Janssens ◽  
Anne-Marie Lambeir ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Umbilical Vein ◽  
Subcellular Location ◽  
Aortic Endothelial Cells ◽  
Angiotensin Converting Enzyme 2 ◽  
Human Umbilical Vein ◽  
Carboxypeptidase Inhibitor ◽  
Umbilical Vein Endothelial Cells ◽  
Extracellular Environment ◽  
Aortic Endothelial

The aim of this study was to investigate the C-terminal cleavage of (pyr)-apelin-13 in human endothelial cells with respect to the role and subcellular location of prolyl carboxypeptidase (PRCP). Human umbilical vein and aortic endothelial cells, pre-treated with prolyl carboxypeptidase-inhibitor compound 8o and/or angiotensin converting enzyme 2 (ACE2)-inhibitor DX600, were incubated with (pyr)-apelin-13 for different time periods. Cleavage products of (pyr)-apelin-13 in the supernatant were identified by mass spectrometry. The subcellular location of PRCP was examined via immunocytochemistry. In addition, PRCP activity was measured in supernatants and cell lysates of LPS-, TNFα-, and IL-1β-stimulated cells. PRCP cleaved (pyr)-apelin-13 in human umbilical vein and aortic endothelial cells, while ACE2 only contributed to this cleavage in aortic endothelial cells. PRCP was found in endothelial cell lysosomes. Pro-inflammatory stimulation induced the secretion of PRCP in the extracellular environment of endothelial cells, while its intracellular level remained intact. In conclusion, PRCP, observed in endothelial lysosomes, is responsible for the C-terminal cleavage of (pyr)-apelin-13 in human umbilical vein endothelial cells, while in aortic endothelial cells ACE2 also contributes to this cleavage. These results pave the way to further elucidate the relevance of the C-terminal Phe of (pyr)-apelin-13.

Effects of Dipyrone on Prostaglandin Production by Human Platelets and Cultured Bovine Aortic Endothelial Cells

1983 ◽  
Vol 49 (02) ◽  
pp. 132-137 ◽  
Author(s):  
A Eldor ◽  
G Polliack ◽  
I Vlodavsky ◽  
M Levy
Keyword(s):  
Endothelial Cells ◽  
Arachidonic Acid ◽  
Competitive Inhibition ◽  
Inhibitory Effect ◽  
Human Platelets ◽  
Ionophore A23187 ◽  
Aortic Endothelial Cells ◽  
Bovine Aortic Endothelial Cells ◽  
Aortic Endothelial

SummaryDipyrone and its metabolites 4-methylaminoantipyrine, 4-aminoantipyrine, 4-acetylaminoantipyrine and 4-formylaminoan- tipyrine inhibited the formation of thromboxane A2 (TXA2) during in vitro platelet aggregation induced by ADP, epinephrine, collagen, ionophore A23187 and arachidonic acid. Inhibition occurred after a short incubation (30–40 sec) and depended on the concentration of the drug or its metabolites and the aggregating agents. The minimal inhibitory concentration of dipyrone needed to completely block aggregation varied between individual donors, and related directly to the inherent capacity of their platelets to synthesize TXA2.Incubation of dipyrone with cultured bovine aortic endothelial cells resulted in a time and dose dependent inhibition of the release of prostacyclin (PGI2) into the culture medium. However, inhibition was abolished when the drug was removed from the culture, or when the cells were stimulated to produce PGI2 with either arachidonic acid or ionophore A23187.These results indicate that dipyrone exerts its inhibitory effect on prostaglandins synthesis by platelets or endothelial cells through a competitive inhibition of the cyclooxygenase system.

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