Adherence of neutrophils to cultured human microvascular endothelial cells. Stimulation by chemotactic peptides and lipid mediators and dependence upon the Mac-1, LFA-1, p150,95 glycoprotein family.

Tonnesen, Marcia G.; Anderson, D. C.; Springer, T.A.; Knedler, Ann; Avdi, Natalie J.; Henson, Peter M.

doi:10.1172/jci113928

Cited by 227 publications

(94 citation statements)

References 62 publications

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“…The ability of TNF-a to stimulate synthesis of prostacyclin (PG12) [51], endothelial-derived relaxing factor [48] and of PAF [47] may also be involved in the early and in the sustained vasodilation, increased leukocyte delivery and increased vascular leak. In addition to directly increasing vascular permeability, PAF may induce an early (30 min) adhesion of PMN to the endothelium [52] and may favor subsequent activation and p2-integrin-dependent transmigration of PMN [53]. Despite the fact that TNF-a does not directly injure endothelium, this cytokine renders endothelial cells more susceptible to leukocyte-mediated injury [54].…”

Section: Biological Activitiesmentioning

confidence: 99%

The molecular action of tumor necrosis factor‐α

Camussi

Albano

Tetta

et al. 1991

European Journal of Biochemistry

249

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Tumor necrosis factor‐α (TNF‐α) is a polypeptide hormone newly synthesized by different cell types upon stimulation with endotoxin, inflammatory mediators (C5a anaphylatoxin), or cytokines such as interleukin‐1 and, in an autocrine manner, TNF itself. The net biological effect of TNF‐α may vary depending on relative concentration, duration of cell exposure and presence of other mediators which may act in synergism with this cytokine. TNF‐α may be relevant either in pathological events occurring in cachexia and endotoxic shock and inflammation or in beneficial processes such as host defense, immunity and tissue homeostasis. The biological effects of TNF‐α are triggered by the binding to specific cell surface receptors. The formation of TNF‐α‐receptor complex activates a variety of biochemical pathways that include the transduction of the signal at least in part controlled by guanine‐nucleotide‐binding regulatory proteins (G proteins), its amplification through activation of adenyl cyclase, phospholipases and protein kinases with the generation of second messenger pathways. The transduction of selected genes in different cell types determines the characteristics of the cell response to TNF‐α. The full understanding of the molecular mechanisms of TNF‐α will provide the basis for a pharmacological approach intended to inhibit or potentiate selected biological actions of this cytokine.

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Section: Biological Activitiesmentioning

confidence: 99%

The molecular action of tumor necrosis factor‐α

Camussi

Albano

Tetta

et al. 1991

European Journal of Biochemistry

249

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“…The first involves activation of the PMNs by chemotactic factors (n-formylmethionyl-leucylphenylalanine [fMLP], leukom'ene 134, C5a) and agents such as PMA, resulting in altered expression of surface adhesive proteins (CD,/CD~s heterodimers) (Anderson et al, 1986) that are members of the integrin superfamily (Kishimoto et al, 1987). At least one of these, CD,b/CD~s, interacts with molecular targets on ECs (Wallis et al, 1986;Zimmerman and Mclntyre, 1988;Tonnesen et al, 1989). Intercellular adhesion molecule 1 (ICAM-1) on ECs appears to be a ligand for CD,/CD~s molecules on stimulated PMNs (Smith et al, 1988).…”

mentioning

confidence: 99%

Endothelial cell-associated platelet-activating factor: a novel mechanism for signaling intercellular adhesion.

Zimmerman

McIntyre

Mehra

et al. 1990

The Journal of Cell Biology

358

153

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Abstract. The binding of neutrophils (polymorphonuclear leukocytes [PMNs]) to endothelial cells (ECs) presents special requirements in the regulation of intercellular adhesion. ECs that are stimulated by certain agonists, including thrombin and cytokines (tumor necrosis factor or, interleukin-1), generate molecular signals that induce the adhesion of PMNs (endothelial cell-dependent neutrophil adhesion). Our experiments demonstrate that the mechanism of binding induced by thrombin is distinct from that induced by the cytokines based on the time courses, the requirement for protein synthesis, and differential binding of HL60 promyelocytic leukemia cells to ECs activated by the two classes of agonists. The rapid EC-dependent PMN adhesion (initiated in minutes) that occurs when the ECs are stimulated by thrombin is temporally coupled with the accumulation of platelet-activating factor, a biologically active phosphoglyceride that remains associated with ECs and that activates PMNs by binding to a cell surface receptor. A portion of the newly synthesized plateletactivating factor (PAF) is on the EC surface, as demonstrated by experiments in which the rate of hydrolysis of PAF synthesized by activated ECs was accelerated by extracellular PAF acetylhydrolase. When ECs were treated with exogenous PAF they became adhesive for PMNs; the PMN binding was prevented by incubating the ECs with PAF acetylhydrolase or by treating the PMNs with competitive PAF receptor antagonists. Thus PAF associated with the EC plasma membrane induces PMN binding, an observation supported by experiments in which PAF in model membranes (liposomes) stimulated rapid PMN adhesion to ECs and to cell-free surfaces. In addition, competitive antagonists of the PAF receptor inhibited the binding of PMNs to ECs activated by thrombin and other rapidly acting agonists, but not to ECs activated by tumor necrosis factor c~, indicating that PAF that is endogenously synthesized by ECs can mediate neutrophil adhesion. These experiments demonstrate a novel mechanism by which a cell-associated phospholipid, PAF, can serve as a signal for an intercellular adhesive event.

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“…Opsonized particles bind to PMN cell surface complement receptors, as shown by Anderson et al (1986), who demonstrated that anti-CR1 and anti-CR3 monoclonal antibodies inhibit phagocytic ingestion and the evolution of CL stimulated by opsonized zymosan. And it has been reported that the activation with chemoattractant such as C5a or formyl-methionyl-leucyl-phenylalanine (FMLP) increases the expressions by translocation of receptors from already synthesized intracellular pool to the cell membrane and facilitate phagocytosis of microbes that are coated with C3b and iC3b after activation of complement system (Miller et al 1987;Tonnesen et al 1989). Moore et al (1986) have described that the expressions of CRl and CR3 increase in the burn patients which leads to the activation of PMN function.…”

Section: Discussionmentioning

confidence: 99%

Perioperative Alterations in Polymorphonuclear Leukocyte Function of Gastrointestinal Surgery.

Yokota

Shineha

Nishihira

et al. 1993

Tohoku J. Exp. Med.

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To characterize the alteration of perioperative polymorphonuclear leukocytes (PMNs) function in surgical stress, we studied twenty six patients undergoing gastrointestinal surgery. Seventeen patients with thoracic esophageal cancer underwent total thoracic esophagectomy through a right thoracotmy (severe surgical stress group). Nine patients underwent cholecystectomy (slight surgical stress group). Phagocytic oxygendependent microbicidal activity in the esophagectomy patients significantly increased postoperatively, by measuring 02 -production (35.3±7.0 nmol/106 cells/ ml/20 min on postoperative day 1 vs. 28.6± 6.2 preoperatively, p <0.01) and luminol-dependent chemiluminescence ( 99.5 ± 29.9 x 105 cpm/ 105 cells on postoperative day 3 vs. 67.5 + 12.8 preoperatively, p <0.01). On the other hand, only a slight change was seen in the cholecystectomy patients. We conclude that the postoperative PMN function in terms of oxygen-dependent microbicidal activity significantly increases when the degree of surgical stress is sufficient. In order to gain insight into the mechanism of PMN activation, we specifically analyzed the expression of complement receptors. Up-regulation of complement receptors were seen in the esophagectomy patients, which parallels the activation of PMN microbicidal activities. It was suggested that phagocytic PMN function in severe surgical stress significantly increases postoperatively, in part, based on the upregulation of cell surface complement receptors.

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Adherence of neutrophils to cultured human microvascular endothelial cells. Stimulation by chemotactic peptides and lipid mediators and dependence upon the Mac-1, LFA-1, p150,95 glycoprotein family.

Abstract: The process of neutrophil adhesion to and migration through the microvascular endothelium, an early event in the induction of the acute inflammatory response, has been attributed to the generation of extravascular chemoattractants.

Cited by 227 publications

References 62 publications

The molecular action of tumor necrosis factor‐α

The molecular action of tumor necrosis factor‐α

Endothelial cell-associated platelet-activating factor: a novel mechanism for signaling intercellular adhesion.

Perioperative Alterations in Polymorphonuclear Leukocyte Function of Gastrointestinal Surgery.

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