A Monoclonal Antibody to the Membrane Glycoprotein Complex CDw18 (LFA) Inhibits PMN Accumulation and Plasma Leakage in vivo

Arfors, Karl-E.; Lundberg, Claes; Lindbom, Lennart; Lundberg, Kerstin; Harlan, M.

doi:10.1159/000414458

Cited by 100 publications

(127 citation statements)

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“…In addition, derangement of the endothelial barrier function, leading to plasma leakage and edema formation, is a characteristic feature of the inflammatory reaction. Previous studies clearly indicate that emigration of PMN is accompanied by efflux of plasma from the vasculature and that these cells are in a position to trigger permeability changes themselves [64,65]. Of critical importance in a PMN-evoked permeability increase is the PMN adhesion and activation via ␤ 2 -integrins [66].…”

Section: Azurocidin Activates Ecmentioning

confidence: 99%

Neutrophil-derived azurocidin alarms the immune system

Soehnlein

Lindbom

2008

Journal of Leukocyte Biology

102

100

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Azurocidin (heparin-binding protein/ cationic antimicrobial protein of 37 kD) is a protein that is mobilized rapidly from emigrating polymorphonuclear leukocytes (PMN). Initially, this inactive serine protease was recognized for its antimicrobial effects. However, it soon became apparent that azurocidin may act to alarm the immune system in different ways and thus serve as an important mediator during the initiation of the immune response. Azurocidin, released from PMN secretory vesicles or primary granules, acts as a chemoattractant and activator of monocyte and macrophages. The functional consequence is enhancement of cytokine release and bacterial phagocytosis, allowing for a more efficient bacterial clearance. Leukocyte activation by azurocidin is mediated via ␤ 2 -integrins, and azurocidin-induced chemotaxis is dependent on formyl-peptide receptors. In addition, azurocidin activates endothelial cells leading to vascular leakage and edema formation. For these reasons, targeting azurocidin release and its actions may have therapeutic potential in inflammatory disease conditions. J. Leukoc. Biol. 85: 344 -351; 2009.

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Section: Azurocidin Activates Ecmentioning

confidence: 99%

Neutrophil-derived azurocidin alarms the immune system

Soehnlein

Lindbom

2008

Journal of Leukocyte Biology

102

100

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“…Furthermore, PMNL infiltration induced by Streptococcus pneumoniae, Staphylococcus aureus, or HCl aspiration was shown to be ␤ 2 integrin independent even on initial exposure (10 -12). These findings are in marked contrast to PMNL infiltration in other tissues, which is highly ␤ 2 integrin-dependent (12)(13)(14). Despite the accumulated evidence that PMNL recruitment to lung inflammation involves ␤ 2 integrin-independent mechanisms, the alternate mechanisms remain unidentified.…”

mentioning

confidence: 90%

The α4β1 (Very Late Antigen (VLA)-4, CD49d/CD29) and α5β1 (VLA-5, CD49e/CD29) Integrins Mediate β2 (CD11/CD18) Integrin-Independent Neutrophil Recruitment to Endotoxin-Induced Lung Inflammation

Burns

Issekutz

Yagita

et al. 2001

The Journal of Immunology

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The β2 integrin cell adhesion molecules (CAM) mediate polymorphonuclear leukocyte (PMNL) emigration in most inflamed tissues, but, in the lung, other yet to be identified CAMs appear to be involved. In Lewis rats, the intratracheal injection of Escherichia coli-LPS induced acute (6-h) PMNL accumulation in the lung parenchyma (280 × 106 by myeloperoxidase assay; PBS control = 35 × 106) and bronchoalveolar lavage fluid (BALF = 27 × 106; PBS = 0.1 × 106). Parenchymal accumulation was not inhibited by a blocking Ab to β2 integrins and only minimally inhibited (20.5%; p < 0.05) in BALF. We examined the role of α4β1 and α5β1 integrins and of selectins in this PMNL recruitment. Treatment with mAbs to α4β1 or α5β1, even in combination, had no effect on PMNL accumulation induced by intratracheal LPS. However, anti-α4 combined with anti-β2 mAbs inhibited PMNL recruitment to the parenchyma by 56% (p < 0.001) and to BALF by 58% (p < 0.01). The addition of anti-α5 mAb to β2 plus α4 blockade inhibited PMNL accumulation further (by 79%; p < 0.05). In contrast, blockade of L-, P-, and E-selectins in combination or together with β2, α4, and α5 integrins had no effect. LPS-induced BALF protein accumulation was not inhibited by treatment with anti-β2 plus α4 mAbs, but was prevented when α5β1 was also blocked. Thus, while selectins appear to play no role, α4β1 and α5β1 function as major alternate CAMs to the β2 integrins in mediating PMNL migration to lung and to pulmonary vascular and epithelial permeability.

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“…Studies have shown that antibodies raised against these molecules can be effective blockers of neutrophil adhesion in vitro (Sanchez-Madrid et al, 1983;Rothlein et al, 1986), and of inflammation in vivo (Arfors et al, 1987;Rampart & Williams, 1988;Barton et al, 1989;. Recently it has been shown that the Shwartzman reaction, a phenomenon that models disseminated intravascular coagulation, and non-immune complex mediated vasculitis, is both CD18 and ICAM-1 dependent (Argenbright & Barton, 1991).…”

Section: Introductionmentioning

confidence: 99%

Role of adhesion glycoproteins CD 18 and intercellular adhesion molecule‐1 in complement‐mediated reactions of rabbit skin

Norman

Argenbright

Williams

et al. 1994

British J Pharmacology

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The role of the adhesion glycoproteins CD 18 and intercellular adhesion molecule‐1 (ICAM‐1) in inflammatory responses produced during a reversed passive Arthus (RPA) reaction and induced by zymosan and zymosan‐activated plasma (ZAP) were studied in rabbit skin. Oedema formation and haemorrhage were quantified by measuring accumulation of 125I‐albumin and 111In‐labelled red blood cells (111In‐RBC) respectively. Monoclonal antibody (mAb) R15.7 (anti‐CD18), administered intravenously, abolished accumulation of 125I‐albumin and 111In‐RBC in dermal RPA reactions and in response to locally injected zymosan and ZAP. When administered intravenously, the mAb RR1/1 (anti‐ICAM‐1) suppressed 125I‐albumin and 111In‐RBC accumulation in dermal RPA reactions and at sites treated with zymosan and ZAP. Oedema formation in response to platelet‐activating factor (PAF) and bradykinin (BK) either in the presence or absence of prostaglandin E2 (PGE2) were not affected by mAb R15.7 or by mAb RR1/1.1.1. We conclude that oedema formation and haemorrhage associated with RPA reactions and in responses to zymosan and ZAP are completely CD 18‐dependent, and are mediated, at least in part, via ICAM‐1. Responses to the neutrophil‐independent oedema forming mediators, PAF and BK are not dependent upon CD 18 or ICAM‐1.

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A Monoclonal Antibody to the Membrane Glycoprotein Complex CDw18 (LFA) Inhibits PMN Accumulation and Plasma Leakage in vivo

Cited by 100 publications

References 0 publications

Neutrophil-derived azurocidin alarms the immune system

Neutrophil-derived azurocidin alarms the immune system

The α4β1 (Very Late Antigen (VLA)-4, CD49d/CD29) and α5β1 (VLA-5, CD49e/CD29) Integrins Mediate β2 (CD11/CD18) Integrin-Independent Neutrophil Recruitment to Endotoxin-Induced Lung Inflammation

Role of adhesion glycoproteins CD 18 and intercellular adhesion molecule‐1 in complement‐mediated reactions of rabbit skin

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