Leukocyte aggregation induced by chemotactic factors

O’Flaherty, Joseph T.; Ward, Peter A.

doi:10.1007/bf00910738

Cited by 37 publications

(14 citation statements)

References 44 publications

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“…Similarly human and rabbit LF, a product of the specific granules, will promote adherence to endothelium and PMN aggregation as well as trigger a transient neutropenia (11,12). Not only will chemotactic factors promote PMN stickiness but direct encounter with opsonized bacteria will occasionally result in increased PMN stickiness (33,34). Under the latter circumstance, LF has been demonstrated to be localized to the surface of the PMN independent of nascent phagosomes.…”

Section: _______________________________mentioning

confidence: 99%

Membrane-bound lactoferrin alters the surface properties of polymorphonuclear leukocytes.

Boxer¹,

Haak²,

Yang³

et al. 1982

J. Clin. Invest.

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A B S T R A C T Polymorphonuclear leukocytes (PMN)aggregate and avidly attach to endothelium in response to chemotactic agents. This response may be related in part to the release of the specific granule constituent lactoferrin (LF). We found by using immunohistology and biochemical and biophysical techniques that LF binds to the membrane and alters the surface properties of the PMN. Upon exposure of PMN treated with 5 gg/ml cytochalasin B to 2 X 10' M formyl-methionine-leucine-phenylalanine for 5 min, the PMN mobilized LF to their surface as observed by immunoperoxidase staining for LF. At added LF levels ranging from 4 to 15 tg/107 PMN there was a dosedependent reduction in PMN surface charge reaching 4 mV, when the partitioning into the membrane of a charged amphipathic nitroxide spin label was measured by electron spin resonance spectroscopy, whereas transferrin was without effect. When '25I-FeLF was added to human PMN in increasing amounts and the results corrected for the residual amount of free LF contaminating the cells, the PMN were saturated with LF at concentrations between 100 and 200 nM in the medium. Human PMN bound 1.35 X 106 molecules per cell and the calculated value for the association constant for these receptors was 5.2 X 106 M-'. Additionally, 6 ,ug/ml LF served as an opsonin for rabbit PMN to promote PMN uptake by rabbit macrophages, when assessed by electron microscopy, but lysozyme did not. These studies indicate that LF can bind to the surface of the PMN and reduce its surface charge.

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Section: _______________________________mentioning

confidence: 99%

Membrane-bound lactoferrin alters the surface properties of polymorphonuclear leukocytes.

Boxer¹,

Haak²,

Yang³

et al. 1982

J. Clin. Invest.

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“…In vitro leukocytes stimulated with chemotaxins become adherent to cul tured endothelium (vide infra). Chemotax ins also induce in vitro aggregation of neu trophils [O'Flaherty, 1977], but, interesting ly, this is partially inhibited by a soluble endothelial cell product [Zimmerman and Klein-Knoeckel, 1986], In vivo, when large quantities of chemotaxins. endotoxin or in terleukin-1 (IL-I) gain access to the blood, they induce leukocyte aggregation and their sequestration, primarily in the lungs [re viewed by Cybulsky and Movat, 1983].…”

Section: Introductionmentioning

confidence: 99%

Neutrophil Emigration and Microvascular Injury

Movat

Cybulsky²

1987

Path Immunopathol Res

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“…Three plasma polypeptides, C5a (5, 7), kallikrein (8-1 1), and Factor XIIa (12), which stimulate neutrophils, have been described. Other neutrophil agonists that can produce these responses include the bacterial chemotactic peptide, N-formyl-Met-LeuPhe (13,14), and the nonphysiological stimulator of protein kinase C, phorbol myristate acetate (15). Plow (16) has shown that human neutrophils release elastase during blood coagulation independently of thrombin.…”

Section: Introductionmentioning

confidence: 99%

Fibronectin degradation products containing the cytoadhesive tetrapeptide stimulate human neutrophil degranulation.

Wachtfogel

Abrams²,

Kucich³

et al. 1988

J. Clin. Invest.

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We investigated whether adhesive glycoproteins, such as fibronectin or fibrinogen, could function to provide a nidus for neutrophil degranulation. Elastase release in recalcified plasma was normal in afibrinogenemic plasma, but 73% less in plasma depleted of fibronectin. Proteolytic digests of fibronectin, but not intact fibronectin (50-1,000 gg/ml), induced a concentration-dependent release of neutrophil elastase and lactoferrin. MAbs N293, which recognized the mid-molecule of fibronectin, N294, which was directed toward the 11-kD cell adhesive fragment, and N295, generated against the amino terminal of the 11-kD fragment, inhibited the release of elastase by 7, 24, and 60%, respectively. The cytoadhesive tetrapeptide portion of fibronectin, Arg-Gly-Asp-Ser (250-1,000 pg/ml), released 1.94±0.10 jig/ml of elastase from 107 neutrophils, in contrast to the lack of release by the control hexapeptide, Arg-GlyTyr-Ser-Leu-Gly. Plasmin appeared to be the enzyme responsible for fibronectin cleavage, since neutrophil elastase release in plasma that had been depleted of plasminogen was decreased and reconstitution of plasminogen-deficient plasma with purified plasminogen corrected the abnormal release. Plasmin cleaved fibronectin to multiple degradation products, each < 200 kD. This fibronectin digest released 1.05 jig/ml of elastase from 107 neutrophils. We suggest that the activation of plasminogen leads to the formation of fibronectin degradation products capable of functioning as agonists for neutrophils.

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Leukocyte aggregation induced by chemotactic factors

Cited by 37 publications

References 44 publications

Membrane-bound lactoferrin alters the surface properties of polymorphonuclear leukocytes.

Membrane-bound lactoferrin alters the surface properties of polymorphonuclear leukocytes.

Neutrophil Emigration and Microvascular Injury

Fibronectin degradation products containing the cytoadhesive tetrapeptide stimulate human neutrophil degranulation.

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