Ligation of selectin L and integrin CD11b/CD18 (Mac-1) induces release of gelatinase B (MMP-9) from human neutrophils

Wize, J; Sopata, I; Smerdel, A; Maśliński, S

doi:10.1007/s000110050336

Cited by 43 publications

(32 citation statements)

References 11 publications

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“…These data suggest that this Thy-1-mediated MMP-9 stimulation is exclusively mediated by the interaction of Thy-1 with the b2-integrins on neutrophils. Our data are in accordance with studies showing that cross-linking of Mac-1 on neutrophils with antibodies induced the release of MMP-9 [29]. Additionally, interaction of another b2-integrin, LFA-1, with ICAM-1 on T-lymphoma cells also has been shown to stimulate MMP-9 secretion [30].…”

Section: Discussionsupporting

confidence: 92%

Human Thy‐1 induces secretion of matrix metalloproteinase‐9 and CXCL8 from human neutrophils

et al. 2008

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Neutrophils are the first cells arriving at sites of acute inflammation. On their way from blood to the site of inflammation, neutrophils have to adhere to endothelial cells (EC), to transverse the basement membrane and subsequently to travel through the interstitial matrix. Recently, we have shown that human Thy-1 is an alternate EC receptor for the leukocyte integrin Mac-1 that contributes to leukocyte recruitment to sites of inflammation, providing a new pathway for adhesion and transmigration of neutrophils. Here, we studied the effect of Thy-1-mediated adhesion on neutrophil functions. Binding of neutrophils to recombinant human Thy-1 stimulated the release of MMP-9 from neutrophils, resulting in their enhanced migration through collagen-IV and matrigel. Further, we showed that neutrophil interaction with Thy-1 stimulated secretion of CXCL8 and thus could support the attraction of additional neutrophils to inflammatory sites. Blocking experiments confirmed the pivotal roles of Thy-1 on activated dermal EC or fibroblasts and its counter receptor CD18 on neutrophils for the regulation of MMP-9 and CXCL8 release from neutrophils. Our results support the general concept that the function of 'adhesion molecules' in particular of human Thy-1, may not only be to provide mechanical support but also regulate neutrophil functions.

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Section: Discussionsupporting

confidence: 92%

Human Thy‐1 induces secretion of matrix metalloproteinase‐9 and CXCL8 from human neutrophils

et al. 2008

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“…However, MMP-1 and MMP-9, two of the IL-1-and tumor necrosis factor ␣-inducible MMPs investigated in this study (31), are also known to be secreted by inflammatory cells like neutrophil granulocytes (MMP-9) and monocyte/macrophages (MMP-1 and MMP-9) (32). Ligation of adhesive receptors (Lselectin and integrin CD11b/CD18 [Mac-1]) has been shown to induce the release of MMP-9 from human neutrophils, where it is stored in specific granules (33). Also, differential production of MMP-9 by the synovial membrane has been recently reported (34).…”

Section: Discussionmentioning

confidence: 99%

Synovial fluid exoglycosidases are predictors of rheumatoid arthritis and are effective in cartilage glycosaminoglycan depletion

Ortutay

Polgar

Gömör³

et al. 2003

Arthritis & Rheumatism

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Objective. To analyze enzymes involved in joint damage by simultaneous investigation of glycosidases and matrix metalloproteinases (MMPs) in patients with various joint diseases. In joint diseases, the major clinical symptoms and disability of patients are caused by an irreversible destruction of hyaline cartilage. Enzymes capable of degrading extracellular matrix components (collagen and aggrecan) and concomitantly exposing chondrocytes to a variety of cytotoxic and/or apoptosis-inducing factors are considered to be the major effector molecules in cartilage degradation. Methods. Activities of glycosidases (␤-DRecently, significant advances have been made in our understanding of joint destruction and the mechanism of proteolytic cleavage of cartilage. Active proteases are currently implicated in the destructive processes and include matrix metalloproteinases (MMPs), the ADAM family (1), the ADAM-TS family (2), and serine proteases (elastase, cathepsins, and granzymes) (3-5). Of the 4 groups of MMPs, collagenase (MMP-1 in particular) appears to be responsible for the degradation of interstitial collagens. The gelatinases (including MMP-2 and MMP-9) degrade the denatured form of collagens, thus acting in synergy with MMP-1. The stromelysins (including MMP-3) have a broader substrate specificity for non-connective tissue components.

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“…It was initially observed that antibodies blocking α 5 β 1 integrin-mediated adhesion induced MMP expression in fibroblasts (Werb et al, 1989). Later studies revealed that integrin-mediated signals are general regulators of MMP expression, as α 2 β 1 integrin regulates MMP-1 expression (Riikonen et al, 1995;Dumin et al, 2001), antibodies to α 3 β 1 integrin-tetraspanin complexes induce MMP-2 expression (Sugiura and Berditchevski, 1999), and α M β 2 and α 3 β 1 integrin ligation stimulates MMP-9 expression (Wize et al, 1998;Larjava et al, 1993). The effects on MMP expression are very specific.…”

Section: Expression and Secretion Of Gelatinases And Other Mmpsmentioning

confidence: 99%

Gelatinase-mediated migration and invasion of cancer cells

Björklund

Koivunen

2005

Biochimica et Biophysica Acta (BBA) - Reviews on Cancer

463

609

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Ligation of selectin L and integrin CD11b/CD18 (Mac-1) induces release of gelatinase B (MMP-9) from human neutrophils

Abstract: Ligation of selectin L and integrin CD11b/ CD18 provides stimulatory signals to neutrophils which induce secretion of gelatinase B that may facilitate their transmigration into sites of inflammation.

Cited by 43 publications

References 11 publications

Human Thy‐1 induces secretion of matrix metalloproteinase‐9 and CXCL8 from human neutrophils

Human Thy‐1 induces secretion of matrix metalloproteinase‐9 and CXCL8 from human neutrophils

Synovial fluid exoglycosidases are predictors of rheumatoid arthritis and are effective in cartilage glycosaminoglycan depletion

Gelatinase-mediated migration and invasion of cancer cells

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