Modulation of Normal Human Eosinophil Chemotaxis in vitro by Herbimycin A, Erbstatin and Pervanadate

1998 ◽  
Vol 117 (1) ◽  
pp. 10-13 ◽  
Author(s):  
Amr El-Shazly ◽  
Keisuke Masuyama ◽  
Yasuhiro Samejima ◽  
Masao Eura ◽  
Takeru Ishikawa
Keyword(s):  
Human Eosinophil ◽  
Herbimycin A ◽  
Normal Human ◽  
Eosinophil Chemotaxis

Induction of Normal Human Eosinophil Migration in vitro by Substance P

1993 ◽  
Vol 89 (4) ◽  
pp. 213-215 ◽  
Author(s):  
F.J. Wiedermann ◽  
C.M. Kähler ◽  
N. Reinisch ◽  
C.J. Wiedermann
Keyword(s):  
Substance P ◽  
Human Eosinophil ◽  
Eosinophil Migration ◽  
Normal Human

Modulation of human eosinophil chemotaxis and adhesion by anti-allergic drugs in vitro

2008 ◽  
Vol 4 (S4) ◽  
pp. 13-18 ◽  
Author(s):  
R. Sehmi ◽  
G. M. Walsh ◽  
A. Hartnell ◽  
J. Barkans ◽  
J. North ◽  
...  
Keyword(s):  
Human Eosinophil ◽  
Eosinophil Chemotaxis

Inhibition of Human Eosinophil Chemotaxis in Vitro by the Anti-Allergic Agent Emedastine Difumarate

1996 ◽  
Vol 18 (4) ◽  
pp. 587-595 ◽  
Author(s):  
A. E. El-Shazly ◽  
K. Masuyama ◽  
Y. Samejima ◽  
M. Eura ◽  
T. Ishikawa
Keyword(s):  
Human Eosinophil ◽  
Eosinophil Chemotaxis

scholarly journals Role of cyclic GMP on inhibition by nitric oxide donors of human eosinophil chemotaxis in vitro

2004 ◽  
Vol 141 (4) ◽  
pp. 653-660 ◽  
Author(s):  
Sara M Thomazzi ◽  
Juliana Moreira ◽  
Sisi Marcondes ◽  
Gilberto De Nucci ◽  
Edson Antunes
Keyword(s):  
Nitric Oxide ◽  
Cyclic Gmp ◽  
Nitric Oxide Donors ◽  
Human Eosinophil ◽  
Eosinophil Chemotaxis

scholarly journals Novel Co-Operation Between Eotaxin and Substance-P in Inducing Eosinophil-Derived Neurotoxin Release

1999 ◽  
Vol 8 (3) ◽  
pp. 177-179 ◽  
Author(s):  
Amr El-Shazly ◽  
Takeru Ishikawa
Keyword(s):  
Substance P ◽  
Tyrosine Kinases ◽  
Kinase Inhibitor ◽  
Allergic Diseases ◽  
Present Communication ◽  
Human Eosinophil ◽  
Protein Residues ◽  
Herbimycin A ◽  
Sds Page ◽  
Normal Human

Eosinophils, chemokines, and neuropeptides are thought to play effector roles in the pathogenesis of allergic diseases such as rhinitis. Eotaxin is a novel C-C chemokine with a potent and relatively specific eosinophil chemoattractant activity that binds selectively to CCR3 receptor, however, its activity in inducing eosinophil granules proteins release is poorly characterized. This study was performed to determine whether eotaxin primes eosinophil exocytosis and whether this co-operates with the sensory neuroimmune-axis. In the present communication, we show that 10 ng/ml eotaxin primed normal human eosinophil for exaggerated eosonophil-derived neurotoxin (EDN) release stimulated by 10-8M Substance-P (SP). This novel priming was blocked by; 7B11 and Herbimycin A (HA), the CCR3 antagonist and the tyrosine kinase inhibitor, respectively. SDS-Page studies showed significant tyrosine phosphorylation of several protein residues induced by 10-8M SP only after priming with 10 ng/ml eotaxin. These results demonstrate a novel co-operation between eotaxin and SP in inducing eosinophil cytotoxicity, which at least in part involves tyrosine kinases pathway(s).

Effect of Cetirizine on Human Eosinophil Superoxide Generation, Eosinophil Chemotaxis and Eosinophil Peroxidase in vitro

1994 ◽  
Vol 103 (4) ◽  
pp. 384-390 ◽  
Author(s):  
Chiharu Okada ◽  
Ryosuke Eda ◽  
Hidefumi Miyagawa ◽  
Haruhito Sugiyama ◽  
Russell J. Hopp ◽  
...  
Keyword(s):  
Superoxide Generation ◽  
Human Eosinophil ◽  
Eosinophil Peroxidase ◽  
Eosinophil Chemotaxis

Presence and Possible Origin of ɛ(γ-Glutamyl)Lysine Isodipeptide in Human Plasma

1992 ◽  
Vol 67 (01) ◽  
pp. 060-062 ◽  
Author(s):  
J Harsfalvi ◽  
E Tarcsa ◽  
M Udvardy ◽  
G Zajka ◽  
T Szarvas ◽  
...  
Keyword(s):  
Human Plasma ◽  
Fibrinolytic Therapy ◽  
Normal Human Plasma ◽  
Normal Human ◽  
Hplc Technique ◽  
Significant Change

Summaryɛ(γ-glutamyl)lysine isodipeptide has been detected in normal human plasma by a sensitive HPLC technique in a concentration of 1.9-3.6 μmol/1. Incubation of in vitro clotted plasma at 37° C for 12 h resulted in an increased amount of isodipeptide, and there was no further significant change when streptokinase was also present. Increased in vivo isodipeptide concentrations were also observed in hypercoagulable states and during fibrinolytic therapy.

Inhibition of the Activities of α2-Plasmin inhibitor (PI) and CI inhibitor (CI-Inh) by the Synthetic Fibrinolytic Agent, 3-Hydroxypropyl Flufenamide (Flu-HPA)

1979 ◽  
Author(s):  
L Miles ◽  
J Burnier ◽  
M Verlander ◽  
M Goodman ◽  
A Kleiss ◽  
...  
Keyword(s):  
Plasminogen Activators ◽  
Inhibitory Effect ◽  
Mechanisms Of Action ◽  
Flufenamic Acid ◽  
Clot Lysis ◽  
Factor Xiia ◽  
Dependent Inhibition ◽  
Normal Human ◽  
Plasmin Inhibitor

Flu-HPA is one of a series of flufenamic acid derivations that enhances plasminogen-dependent clot lysis in vitro. Studies of possible mechanisms of action of Flu-HPA were undertaken. The influence of Flu-HPA on the inhibition of purified plasmin by purified PI was studied. PI activity was assessed by its inhibition of the clevage of the tripeptide S-2251 (H-D-Val-Leu-Lys-pNA) by plasmin. Flu-HPA was dissolved in DMF or in methonol and preincubated with PI before addition of plasmin. At Flu-HPA concentrations greater than 1mM and up to 60mM, the inhibitory activity of PI was totally lost. The inhibitory effect of normal human plasma on plasmin was also completely abolished at concentrations of Flu-HPA between 2.5 and 40mM. The effect of Flu-HPA on the inhibition of purified plasma kallikrein by purified CI-Inh was also studied. CI-Inh activity was measured by its inhibition of cleavage of the tripeptide Bz-Pro-Phe-Arg-pNA by kallikrein. When Flu-HPA, dissolved in DMF or in methonol, was preincubated with CI-Inh, a concentration dependent inhibition of CI-Inh activity was observed. CI-Inh activity was abolished by concentrations of Flu-HPA greater than 1mM. Flu-HPA also inhibited the activity of CI-Inh on purified Factor XIIa. These observations suggest that this flufenamic acid derivative may enhance fibrinolysis not only by inhibiting PI activity but also by decreasing the inactivation of plasminogen activators by CI-Inh.

The Effect of Practolol, In Vitro Generated Metabolites of Practolol and Chemical Analogues on the Rate of Growth of Human Skin Fibroblasts

1984 ◽  
Vol 12 (2) ◽  
pp. 89-97
Author(s):  
Graham R. Elliott ◽  
H.E. Amos ◽  
James W. Bridges
Keyword(s):  
Human Skin ◽  
Psoriasis Patient ◽  
Skin Fibroblasts ◽  
Human Skin Fibroblasts ◽  
Cell Type ◽  
Normal Human Skin ◽  
Rate Of Growth ◽  
Structural Analogues ◽  
Normal Human

The rate of growth of normal human skin fibroblasts was inhibited in a dose related, reversible, fashion by practolol (N-4-(2-hydroxy)-3 (1-methyl)-aminopropoxyphenylacetamine) (ID50 1.35 ± 0.14 x 10-3M), propranolol (1-(isopropylamino)-3(1-naphthyl-oxy)-2-propranolol) (ID50 0.145 ± 0.02 x 10-3M) and paracetamol (N-(4-hydroxyphenyl) acetamide) (ID50 0.85 ± 0.2 x 10-3M). Skin fibroblasts isolated from a psoriasis patient were more sensitive towards practolol (ID50 0.48 ± 0.14 x 10-3M) and propranolol (ID50 0.032 ± 0.002 x 10-3M), but less sensitive towards paracetamol (ID50 1.3 ± 0.07 x 10-3M). In vitro generated metabolites of practolol, using normal or Arochlor 1254-pretreated hamster liver preparations, and structural analogues of practolol had no effect upon the growth of either cell type.

Sign in / Sign up

Export Citation Format

Share Document