scholarly journals Cell polarity: an examination of its behavioral expression and its consequences for polymorphonuclear leukocyte chemotaxis.

1981 ◽  
Vol 89 (3) ◽  
pp. 585-592 ◽  
Author(s):  
S H Zigmond ◽  
H I Levitsky ◽  
B J Kreel
Keyword(s):  
Cell Polarity ◽  
Polymorphonuclear Leukocyte ◽  
Polymorphonuclear Leukocytes ◽  
Asymmetric Distribution ◽  
Behavioral Expression ◽  
Morphological Polarity ◽  
Chemotactic Factors ◽  
Leukocyte Chemotaxis ◽  
Chemotactic Ability ◽  
Chemotactic Gradient

Locomoting polymorphonuclear leukocytes (PMNs) exhibit a morphological polarity. We demonstrate that they also exhibit a behavioral polarity in their responsiveness to chemotactic factor stimulation. This is demonstrated by (a) the pattern of their locomotion in a homogeneous concentration of chemotactic factors, (b) their responses to increases in the homogeneous concentration of chemotactic factors, and (c) their responses to changes in the direction of a chemotactic gradient. The behavioral polarity is not a function of the rate of locomotion of the particular stimulant used to orient the cells, but may reflect an asymmetric distribution of chemotactic receptors or the motile machinery. The polar behavior affects the chemotactic ability of PMNs. The data are discussed in relation to possible mechanisms of sensing a chemotactic gradient.

Effect of Some Anti-Inflammatory Drugs on Human Neutrophil Chemotaxis

1994 ◽  
Vol 22 (2) ◽  
pp. 100-106 ◽  
Author(s):  
G Hasçelik ◽  
B ŞLener ◽  
Z Hasçelik
Keyword(s):  
Acetylsalicylic Acid ◽  
Polymorphonuclear Leukocyte ◽  
Polymorphonuclear Leukocytes ◽  
Diclofenac Sodium ◽  
Tiaprofenic Acid ◽  
Boyden Chamber ◽  
Random Migration ◽  
Leukocyte Chemotaxis ◽  
Inflammatory Drugs ◽  
Anti Inflammatory

The effects of piroxicam, tenoxicam, diclofenac sodium, acetylsalicylic acid and tiaprofenic acid on the chemotaxis and random migration of human polymorphonuclear leukocytes were investigated, using zymosan-activated serum as chemo-attractant, with a modified Boyden chamber technique. All five compounds significantly reduced chemotaxis. The random migration of polymorphonuclear leukocytes was inhibited by piroxicam, diclofenac sodium and tiaprofenic acid but not by tenoxicam or acetylsalicylic acid. The inhibitory effect of these non-steroidal anti-inflammatory drugs on polymorphonuclear leukocyte chemotaxis and on random migration was generally dose-dependent. The results suggest that the drugs studied may have a direct effect on polymorphonuclear leukocyte chemotaxis and that this activity may contribute to their anti-inflammatory properties.

Cellular augmentation of polymorphonuclear leukocyte chemotaxis

1979 ◽  
Vol 236 (1) ◽  
pp. C22-C29 ◽  
Author(s):  
A. Takeuchi ◽  
R. H. Persellin
Keyword(s):  
Polymorphonuclear Leukocyte ◽  
Polymorphonuclear Leukocytes ◽  
Cellular Response ◽  
Active Component ◽  
Cell Contact ◽  
Cytoplasmic Fraction ◽  
Activated Neutrophils ◽  
Leukocyte Chemotaxis ◽  
Number Of Cells ◽  
Insufficient Number

The density of neutrophils influences the number of cells that will respond to a chemoattractant, endotoxin-activated serium. When fewer than 3 x 10(5) polymorphonuclear leukocytes (PMN) were placed in the top compartment of a modified Boyden chemotaxis chamber, the cellular response was weak. Complete membrane penetration by activated neutrophils rarely was observed. When this number of PMN was exceeded, however, both the number of cells and the percentage of neutrophils responding to the leukoattractant increased. The density of cells required for effective chemotactic response to occur was such that intimate cell-to-cell contact was suggested. This indicated that PMN exerted a kinetic influence upon one another. Extracts of disrupted PMN induced an otherwise insufficient number of neutrophils to respond to the chemotactic stimulus. The active component was isolated in the cytoplasmic fraction (postcentrifugation, 100,000 x g, 60 min) of PMN, but was not present in other subcellular fractions. This cytoplasmic augmentor of chemotaxis (CACh) increased random mobility of neutrophils, but was not, itself, a chemotactic factor. These findings suggest that PMN cooperate in their response to a leukotactic stimulus.

scholarly journals THE RELATIONSHIP OF THE CHEMOTACTIC BEHAVIOR OF THE COMPLEMENT-DERIVED FACTORS, C3a, C5a, AND C567, AND A BACTERIAL CHEMOTACTIC FACTOR TO THEIR ABILITY TO ACTIVATE THE PROESTERASE 1 OF RABBIT POLYMORPHONUCLEAR LEUKOCYTES

1972 ◽  
Vol 135 (2) ◽  
pp. 376-387 ◽  
Author(s):  
Elmer L. Becker
Keyword(s):  
Polymorphonuclear Leukocyte ◽  
Esterase Activity ◽  
Polymorphonuclear Leukocytes ◽  
Quantitative Difference ◽  
Chemotactic Activity ◽  
General Requirement ◽  
Chemotactic Factors ◽  
Relationship Of ◽  
The Relationship ◽  
Chemotactic Behavior

The inhibition profiles obtained when a series of p-nitrophenyl ethyl alkylphosphonates and of p-nitrophenyl ethyl chloroalkylphosphonates were used to interfere with the chemotactic activity of polymorphonuclear leukocytes stimulated by C3a, C5a, and bacterial factor were the same as found previously when C567 was the chemotactic agent. This indicates that as in the chemotactic activity induced by C567, an obligatory step in the chemotaxis caused by C3a, C5a, and bacterial factor is the activation of proesterase 1 of the rabbit polymorphonuclear leukocyte. C5a and C3a activate proesterase 1 of peripheral blood polymophonuclear leukocytes as measured by the increase of acetyl DL-phenylalanine ß-naphthyl esterase activity. Attempts to detect in a like manner the proesterase 1 of the same leukocytes using bacterial factor under varying circumstances have consistently failed. It is concluded that bacterial factor, for unknown reasons, is unable to activate proesterase 1 to the same extent as the complement-derived chemotactic factors. The hypothesis of there being a quantitative difference in the ability of bacterial factor to activate proesterase 1 compared with the complement-derived factors explains the previous observations that bacterial factor can not deactivate to itself or to the complement-derived factors, although these latter factors can deactivate to themselves, to each other, and to the bacterial factor. The quantitative difference in the ability of bacterial factor to activate proesterase 1 compared to the complement-derived factors is also associated with and explains the finding that the maximal chemotactic activity attainable when bacterial factor is the chemotactic agent is distinctly less than that obtained using either C3a, C5a, or C567. These results indicate that the activation of proesterase 1 is a general requirement for the chemotactic activity of rabbit polymorphonuclear leukocytes with known macromolecular chemotactic agents and suggest that under several different circumstances the level of chemotactic activity attained is related to the degree of such activation.

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.

Effects of Erythromycin, Josamycin and Spiramycin on Rat Polymorphonuclear Leukocyte Chemotaxis

Chemotherapy ◽  
1986 ◽  
Vol 32 (4) ◽  
pp. 379-382 ◽  
Author(s):  
A. Eyraud ◽  
J. Descotes ◽  
J.Y. Lombard ◽  
A. Laschi-Loquerie ◽  
P. Tachon ◽  
...  
Keyword(s):  
Polymorphonuclear Leukocyte ◽  
Leukocyte Chemotaxis

scholarly journals Intracellular localization of Rickettsia tsutsugamushi in polymorphonuclear leukocytes.

1979 ◽  
Vol 150 (3) ◽  
pp. 703-708 ◽  
Author(s):  
Y Rikihisa ◽  
S Ito
Keyword(s):  
Guinea Pig ◽  
Cell Cultures ◽  
Polymorphonuclear Leukocyte ◽  
Polymorphonuclear Leukocytes ◽  
Intracellular Localization ◽  
The Other ◽  
Cytoplasmic Organelles

Rickettsia tsutsugamushi (Gilliam strain) was serially propagated in BHK-21 cell cultures and incubated with guinea pig peritoneal polymorphonuclear leukocytes to study the ultrastructural features of rickettsial uptake and entry into the leukocytes. Significant numbers of rickettsiae were phagocytized selectively by these leukocytes within 30 min. About one-half of these rickettsiae remained sequestered in phagosomes but the other one-half were free from the phagosome and localized directly in the polymorphonuclear leukocyte cytoplasm. Various stages of rickettsial release from the phagosomes were observed. Once free within the polymorphonuclear leukocyte cytoplasm, the rickettsiae were preferentially localized in the glycogen-packed areas which are devoid of lysosomes and other cytoplasmic organelles. This study indicates that rickettsiae phagocytized by polymorphonuclear leukocytes can escape from the phagosome into the cytoplasm.

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