scholarly journals Signal pathway regulation of interleukin-8-induced actin polymerization in neutrophils

Blood ◽  
1993 ◽  
Vol 82 (8) ◽  
pp. 2546-2551 ◽  
Author(s):  
RL Sham ◽  
PD Phatak ◽  
TP Ihne ◽  
CN Abboud ◽  
CH Packman
Keyword(s):  
Pertussis Toxin ◽  
Actin Polymerization ◽  
Chelating Agent ◽  
Cytosolic Calcium ◽  
Signal Pathway ◽  
Interleukin 8 ◽  
Maximum Increase ◽  
Signal Pathway Regulation ◽  
Pathway Regulation ◽  
Dose Dependent Increase

Abstract Interleukin-8 (IL-8), a recently described peptide cytokine, is a neutrophil chemoattractant and activator that exerts effects similar to fMLP, yet their receptors and their roles in pathophysiology differ. The effect of IL-8 on the neutrophil cytoskeleton has not been well studied; therefore, we compared and contrasted the effects of IL-8 and fMLP on neutrophil actin conformation and on the signal pathway regulation of actin responses. IL-8 caused a rapid, dose-dependent increase in neutrophil F-actin content within 30 seconds. The maximum increase was twofold. These changes were accompanied by the development of F-actin-rich pseudopods, as noted with fluorescence microscopy and scanning electron microscopy. Selected biochemical inhibitors were used to study the regulation of the IL-8-induced actin changes. Incubation of neutrophils with 2 micrograms/mL pertussis toxin resulted in a 67% inhibition of the IL-8-induced F-actin increase. The protein kinase C (PKC) inhibitors, staurosporine and H7, did not inhibit the increase in F-actin caused by IL-8. IL-8 caused a rapid increase in neutrophil intracellular calcium that could be completely inhibited by the chelating agent 1,2-bis(o-aminophenoxy)ethane-N,N-N′,N′-tetraacetic acid (BAPTA). However, BAPTA-treated neutrophils retained the ability to increase F-actin in response to IL-8. Similar results were seen with fMLP, indicating that, similar to fMLP, the IL-8-induced actin response is mediated through pertussis-toxin-sensitive G-proteins but is neither dependent on PKC nor increases in cytosolic calcium. Thus, although IL- 8 and fMLP exert their effects on neutrophils through different receptors, the signal transduction pathways used and the effects on actin conformation and pseudopod formation are similar.

scholarly journals Signal pathway regulation of interleukin-8-induced actin polymerization in neutrophils

Blood ◽  
1993 ◽  
Vol 82 (8) ◽  
pp. 2546-2551 ◽  
Author(s):  
RL Sham ◽  
PD Phatak ◽  
TP Ihne ◽  
CN Abboud ◽  
CH Packman
Keyword(s):  
Pertussis Toxin ◽  
Actin Polymerization ◽  
Chelating Agent ◽  
Cytosolic Calcium ◽  
Signal Pathway ◽  
Interleukin 8 ◽  
Maximum Increase ◽  
Signal Pathway Regulation ◽  
Pathway Regulation ◽  
Dose Dependent Increase

Interleukin-8 (IL-8), a recently described peptide cytokine, is a neutrophil chemoattractant and activator that exerts effects similar to fMLP, yet their receptors and their roles in pathophysiology differ. The effect of IL-8 on the neutrophil cytoskeleton has not been well studied; therefore, we compared and contrasted the effects of IL-8 and fMLP on neutrophil actin conformation and on the signal pathway regulation of actin responses. IL-8 caused a rapid, dose-dependent increase in neutrophil F-actin content within 30 seconds. The maximum increase was twofold. These changes were accompanied by the development of F-actin-rich pseudopods, as noted with fluorescence microscopy and scanning electron microscopy. Selected biochemical inhibitors were used to study the regulation of the IL-8-induced actin changes. Incubation of neutrophils with 2 micrograms/mL pertussis toxin resulted in a 67% inhibition of the IL-8-induced F-actin increase. The protein kinase C (PKC) inhibitors, staurosporine and H7, did not inhibit the increase in F-actin caused by IL-8. IL-8 caused a rapid increase in neutrophil intracellular calcium that could be completely inhibited by the chelating agent 1,2-bis(o-aminophenoxy)ethane-N,N-N′,N′-tetraacetic acid (BAPTA). However, BAPTA-treated neutrophils retained the ability to increase F-actin in response to IL-8. Similar results were seen with fMLP, indicating that, similar to fMLP, the IL-8-induced actin response is mediated through pertussis-toxin-sensitive G-proteins but is neither dependent on PKC nor increases in cytosolic calcium. Thus, although IL- 8 and fMLP exert their effects on neutrophils through different receptors, the signal transduction pathways used and the effects on actin conformation and pseudopod formation are similar.

Morphological polarization of human polymorphonuclear leucocytes in response to three different chemoattractants: an effector response independent of calcium rise and tyrosine kinases

1995 ◽  
Vol 108 (4) ◽  
pp. 1771-1778 ◽  
Author(s):  
H. Lepidi ◽  
Y. Zaffran ◽  
J.L. Ansaldi ◽  
J.L. Mege ◽  
C. Capo
Keyword(s):  
Tyrosine Kinases ◽  
Actin Polymerization ◽  
Kinase Inhibitor ◽  
Cytosolic Calcium ◽  
Interleukin 8 ◽  
Polymorphonuclear Leucocytes ◽  
Filamentous Actin ◽  
Membrane Ruffling ◽  
Cytoskeleton Organization ◽  
Image Digitization

Chemoattractants such as interleukin-8, C5a and N-formylmethionyl-leucyl-phenylalanine induce a cytosolic calcium rise involved in triggering the secretory functions of human polymorphonuclear leucocytes. We studied the possible role of calcium rise in membrane ruffling, actin polymerization, filamentous actin distribution, and morphological polarization, which are all events contributing to chemotaxis. Membrane ruffling was assessed by right-angle light-scatter changes, the cellular content of polymerized actin by fluorescence of bodipy phallacidin, the intracellular distribution of filamentous actin by fluorescence microscopy and image digitization, and morphological polarization by scanning electron microscopy. Pretreatment of polymorphonuclear leucocytes with 50 microM BAPTA/AM, an intracellular calcium chelator, lowered the basal level in cell calcium and inhibited the transient calcium rise stimulated by 2 nM interleukin-8, 2 nM C5a, and 10 nM N-formylmethionyl-leucyl-phenylalanine. However, BAPTA pretreatment of polymorphonuclear leucocytes did not modify membrane ruffling, actin polymerization, filamentous actin distribution, and morphological polarization stimulated by chemoattractants. Downstream effectors may be protein tyrosine kinases. However, the tyrosine kinase inhibitor tyrphostin did not affect the cytoskeletal characteristics elicited by chemoattractants. Taken together, our results suggest that the transductional pathway leading to cytoskeleton organization and morphological polarization of polymorphonuclear leucocytes is different from that leading to secretion.

Curcumin anti-diabetic effect mainly correlates with its anti-apoptotic actions and PI3K/Akt signal pathway regulation in the liver

2020 ◽  
Vol 146 ◽  
pp. 111803
Author(s):  
Zhen-hong Xia ◽  
Sai-ya Zhang ◽  
Yu-si Chen ◽  
Ke Li ◽  
Wen-bo Chen ◽  
...  
Keyword(s):  
Signal Pathway ◽  
Signal Pathway Regulation ◽  
Pathway Regulation

Vaults and the major vault protein: Novel roles in signal pathway regulation and immunity

2008 ◽  
Vol 66 (1) ◽  
pp. 43-61 ◽  
Author(s):  
W. Berger ◽  
E. Steiner ◽  
M. Grusch ◽  
L. Elbling ◽  
M. Micksche
Keyword(s):  
Signal Pathway ◽  
Major Vault Protein ◽  
Signal Pathway Regulation ◽  
Pathway Regulation

Protein Metabolism and Signal Pathway Regulation in Rumen and Mammary Gland

2017 ◽  
Vol 18 (6) ◽  
pp. 636-651
Author(s):  
Ya Jing Wang ◽  
Jian Xin Xiao ◽  
Shengli Li ◽  
Jian Jing Liu ◽  
Gibson Maswayi Alugongo ◽  
...  
Keyword(s):  
Mammary Gland ◽  
Protein Metabolism ◽  
Signal Pathway ◽  
Signal Pathway Regulation ◽  
Pathway Regulation

Actin Polymerization, Calcium-Transients, and Phospholipid Metabolism in Human Neutrophils After Stimulation with Interleukin-8 and N-formyl Peptide

1994 ◽  
Vol 102 (3) ◽  
pp. 310-314 ◽  
Author(s):  
Johannes Norgauer ◽  
Jean Krutmann ◽  
Gustav J. Dobos ◽  
Alexis E. Traynor-Kaplan ◽  
Zenaida G. Oades ◽  
...  
Keyword(s):  
Actin Polymerization ◽  
Phospholipid Metabolism ◽  
Interleukin 8 ◽  
Calcium Transients ◽  
Human Neutrophils ◽  
Formyl Peptide

scholarly journals Activation of human neutrophils by mastoparan. Reorganization of the cytoskeleton, formation of phosphatidylinositol 3,4,5-trisphosphate, secretion up-regulation of complement receptor type 3 and superoxide anion production are stimulated by mastoparan

1992 ◽  
Vol 282 (2) ◽  
pp. 393-397 ◽  
Author(s):  
J Norgauer ◽  
M Eberle ◽  
H D Lemke ◽  
K Aktories
Keyword(s):  
Pertussis Toxin ◽  
Actin Polymerization ◽  
Cytochalasin B ◽  
Superoxide Radical ◽  
Human Neutrophils ◽  
Superoxide Anion Production ◽  
Radical Production ◽  
Rapid Formation ◽  
Primary Granules ◽  
Type 3

In human neutrophils, mastoparan induced rapid F-actin polymerization which was followed by a slow and sustained depolymerization to below the initial F-actin content. Incubation of neutrophils with pertussis toxin inhibited mastoparan-stimulated actin polymerization; however it did not prevent sustained depolymerization of F-actin. Analyses of phospholipids performed in parallel revealed that mastoparan stimulated rapid formation of phosphatidylinositol 3,4,5-trisphosphate (PIP3) and consumption of phosphatidylinositol 4,5-bisphosphate (PIP2). Pertussis toxin treatment blocked mastoparan-induced formation of PIP3. Furthermore, mastoparan stimulated the release of N-acetylglucosaminidase from primary granules. Cytochalasin B enhanced mastoparan-stimulated secretion. Mastoparan triggered superoxide radical production in a cytochalasin B-sensitive manner and induced complement type 3 receptor (CR3) up-regulation.

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