Initial kinetics of lysosomal enzyme secretion and superoxide anion generation by human polymorphonuclear leukocytes

Inflammation ◽  
1980 ◽  
Vol 4 (2) ◽  
pp. 145-163 ◽  
Author(s):  
James E. Smolen ◽  
Helen M. Korchak ◽  
Gerald Weissmann
Keyword(s):  
Lysosomal Enzyme ◽  
Superoxide Anion ◽  
Polymorphonuclear Leukocytes ◽  
Enzyme Secretion ◽  
Superoxide Anion Generation ◽  
Human Polymorphonuclear Leukocytes ◽  
Kinetics Of

Inhibitory Effects of N-acetylcysteine on Superoxide Anion Generation in Human Polymorphonuclear Leukocytes

1997 ◽  
Vol 49 (5) ◽  
pp. 525-529 ◽  
Author(s):  
VICTORIA VILLAGRASA ◽  
JULIO CORTIJO ◽  
MIGUEL MARTÍ-CABRERA ◽  
JOSÉ L. ORTIZ ◽  
LUISA BERTO ◽  
...  
Keyword(s):  
Superoxide Anion ◽  
Polymorphonuclear Leukocytes ◽  
Inhibitory Effects ◽  
Superoxide Anion Generation ◽  
Human Polymorphonuclear Leukocytes

scholarly journals Pertussis toxin inhibition of chemotactic factor-induced calcium mobilization and function in human polymorphonuclear leukocytes.

1985 ◽  
Vol 162 (1) ◽  
pp. 145-156 ◽  
Author(s):  
D W Goldman ◽  
F H Chang ◽  
L A Gifford ◽  
E J Goetzl ◽  
H R Bourne
Keyword(s):  
Pertussis Toxin ◽  
Lysosomal Enzyme ◽  
Polymorphonuclear Leukocytes ◽  
Regulatory Protein ◽  
Leukotriene B4 ◽  
Ionophore A23187 ◽  
Enzyme Release ◽  
Adp Ribosylation ◽  
Chemotactic Factors ◽  
Human Polymorphonuclear Leukocytes

Chemotactic factors stimulate a rapid increase in the cytosolic concentration of intracellular calcium ions ([Ca2+]in) in human polymorphonuclear leukocytes (PMNL), which may be an event that is critical to the expression of chemotaxis and other PMNL functions. Treatment of PMNL with pertussis toxin catalyzes ADP-ribosylation of a protein similar or identical to the inhibiting regulatory protein of adenylate cyclase, Gi, and suppresses the increase in [Ca2+]in elicited by leukotriene B4(LTB4) and formyl-methionyl-leucyl-phenylalanine. Chemotactic migration and lysosomal enzyme release elicited by chemotactic factors were inhibited by pertussis toxin with a concentration-dependence similar to that for inhibition of the increase in [Ca2+]in, without an effect on lysosomal enzyme release induced by the ionophore A23187 and phorbol myristate acetate. Activated pertussis toxin catalyzed the [32P]ADP-ribosylation of a 41 kD protein in homogenates of PMNL. The extent of [32P]ADP-ribosylation of this protein was reduced 59% by pretreatment of intact PMNL with pertussis toxin. Pertussis toxin selectively decreased the number of high-affinity receptors for LTB4 on PMNL by 60% without altering the number or binding properties of the low-affinity subset of receptors. Pertussis toxin modification of a membrane protein of PMNL analogous to Gi thus simultaneously alters chemotactic receptors and attenuates the changes in cytosolic calcium concentration and PMNL function caused by chemotactic factors.

Sign in / Sign up

Export Citation Format

Share Document