Adhesion of Human Neutrophils to and Activation by Type-I Collagen Involving a β2 Integrin

Monboisse, Jean-Claude; Garnotel, Roselyne; Randoux, A; Dufer, Jean; Borel, J.P.

doi:10.1002/jlb.50.4.373

Cited by 62 publications

(39 citation statements)

References 14 publications

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“…During these processes, cells exchange various messages, principally through cytokine production, some of them being triggered by interactions with ECM proteins, that in turn lead to the maintenance of an inflammatory state or, on the contrary, to the restoration of physiological conditions. Previous works of our laboratory have shown that type I collagen was able to deeply influence the metabolism of cells involved in these processes, in the case of fibroblasts (22,23) as well as PMNs (3)(4)(5)(6). In this work, we present new evidences that type I collagen interactions with monocytes are critical events involved in these processes.…”

Section: Discussionmentioning

confidence: 50%

“…A total of 100 l of the Ab solution at the appropriate titer (6 g IgG/ml) was added to 1.5 ϫ 10 6 monocytes in 900 l Dulbecco's solution containing 1.3 mM CaCl 2 and 1 mM MgCl 2 . Microtubes were shaken horizontally at 150 cycles/min for 90 min at 37°C (5,15). Monocyte adhesion and O 2 Ϫ production on collagen I were then evaluated as described above, in the continuous presence of mAbs in the incubation medium.…”

Section: Effect Of Anti-integrin Mabs On Monocytesmentioning

confidence: 99%

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Human Blood Monocytes Interact with Type I Collagen Through αxβ2 Integrin (CD11c-CD18, gp150-95)

Garnotel

Rittié

Poitevin

et al. 2000

The Journal of Immunology

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Section: Discussionmentioning

confidence: 50%

Section: Effect Of Anti-integrin Mabs On Monocytesmentioning

confidence: 99%

Human Blood Monocytes Interact with Type I Collagen Through αxβ2 Integrin (CD11c-CD18, gp150-95)

Garnotel

Rittié

Poitevin

et al. 2000

The Journal of Immunology

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“…7, the distribution of BAP31 and CD11b/CD18 in resting PMN is quite similar. Both proteins mainly localized to secondary granule-enriched fractions (17)(18)(19)(20) with only a minor fraction of protein colocalizing with plasma membrane-enriched fractions (11)(12)(13)(14)(15). After stimulation with fMLP (10 Ϫ7 M, 30 min), there was significant redistribution of BAP31 from cellular granule-enriched fractions (particularly secondary granules) to plasma membraneenriched fractions similar to that observed for CD11b/CD18.…”

Section: Bap31 Associates With Cd11b/cd18mentioning

confidence: 58%

Association of BAP31 with CD11b/CD18

Zen

Utech

Liu

et al. 2004

Journal of Biological Chemistry

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The ␤ 2 integrin CD11b/CD18 is an integral membrane protein that is present in the plasma membrane and secondary granules of neutrophils and functions as a major adhesion molecule. Upon cellular activation, there is translocation of intracellular pools of CD11b/ CD18 to the plasma membrane in concert with enhanced cellular adhesion. Although much is known about the function of CD11b/CD18, how this protein is transported within the cell is less well defined. Here we report that CD11b/CD18 specifically binds to BAP31, a member of a novel class of sorting proteins regulating cellular anterograde transport. Through experiments aimed at identifying CD11b/CD18-binding proteins, we produced a monoclonal antibody termed E1B2 that recognizes a 28-kDa membrane protein that co-precipitates with CD11b/ CD18. Microsequence analysis of the E1B2 antigen revealed that it is BAP31. Co-association of CD11b/CD18 and BAP31 was confirmed in co-immunoprecipitation and protein binding assays. Additional experiments revealed that the binding of BAP31 to CD11b/CD18 was not dependent on divalent cations nor mediated by the I-domain of CD11b. Using glutathione S-transferase fusion chimeras, we determined that binding of CD11b/CD18 to BAP31 is mediated through interactions with the cytoplasmic tail of BAP31. Immunolocalization studies revealed colocalization of BAP31 and CD11b/CD18 within neutrophil secondary granules. Subcellular fractionation studies in polymorphonuclear leukocytes (PMN) revealed similar patterns of redistribution of BAP31 and CD11b/CD18 from fractions enriched in secondary granules to the plasma membrane following stimulation with formylmethionylleucylphenylalanine (fMLP). Given the known sorting properties of BAP31, these findings suggest that BAP31 may play a role in regulating intracellular trafficking of CD11b/CD18 in neutrophils.

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“…On the other hand, some types of mobile cells also interact with collagens, for instance polymorphonuclear neutrophils (PMN), 1 a variety of leukocytes circulating in blood, capable of crossing the vascular wall in order to invade the inflamed tissues and to participate in defenses against bacteria or foreign molecules through their property of phagocytosis. In several previous papers, we demonstrated that PMN and type I collagen do interact and began to describe their interactions (3)(4)(5).…”

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confidence: 99%

The Binding of Type I Collagen to Lymphocyte Function-associated Antigen (LFA) 1 Integrin Triggers the Respiratory Burst of Human Polymorphonuclear Neutrophils

Garnotel

Monboisse

Randoux

et al. 1995

Journal of Biological Chemistry

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The transduction pathways depending on the ␣ L ␤ 2 integrin do not involve a G protein (ruled out by the use of cholera and pertussis toxins), whereas the cytoskeleton was found to participate in the process, as evidenced by inhibition by cytochalasin B. After collagen stimulation, cytoplasmic inositol trisphosphate and calcium ion increased sharply for less than 2 min. The use of the inhibitors staurosporine and calphostin C demonstrated that protein kinase C was involved. Evaluation of the activity of this enzyme showed that, upon stimulation of PMN with collagen I, it was translocated to plasma membrane.Acrylamide gel electrophoresis of the protein bands corresponding to the integrin ␣ L ␤ 2 , followed by immunoblotting using monoclonal antibodies to phosphotyrosine, permitted us to demonstrate that, prior to stimulation by type I collagen, there was no phosphorylation, whereas after stimulation, both ␣ L and ␤ 2 chains were stained by anti-phosphotyrosine antibodies. The adhesion of PMN to pepsinized type I collagen triggered tyrosine phosphorylation of the ␤ 2 chain of the integrin, without stimulating O 2 . production by these cells, whereas their stimulation by complete type I collagen induced the tyrosine phosphorylation of both ␣ L and ␤ 2 subunits. The tyrosine phosphorylation of both integrin subunits during transduction of stimuli is a heretofore undescribed phenomenon that may correspond to a new system of transmembrane communication.Type I collagen, a major component of the extra cellular matrix, promotes the adhesion of a variety of cells in solid tissues, influencing many processes such as proliferation, differentiation, migration, and cell shape changes (1). Several receptor molecules have been demonstrated as promoting the adhesion to type I collagen. Among these receptors, some belong to the family of integrins, for instance ␣ 1 ␤ 1 , ␣ 2 ␤ 1 , and ␣ 3 ␤ 1 (2). On the other hand, some types of mobile cells also interact with collagens, for instance polymorphonuclear neutrophils (PMN), 1 a variety of leukocytes circulating in blood, capable of crossing the vascular wall in order to invade the inflamed tissues and to participate in defenses against bacteria or foreign molecules through their property of phagocytosis. In several previous papers, we demonstrated that PMN and type I collagen do interact and began to describe their interactions (3-5).Purified type I collagen is able to bind to PMN in vitro. This binding is followed by the stimulation of some main functions of PMN, such as emission of pseudopods, secretion of lytic enzymes, and liberation of superoxide. We demonstrated that the stimulation of PMN by collagen occurs through two sequences of the ␣ 1 (I) chain, both located in the C-terminal region of the molecules, an RGD sequence corresponding to residues 915-917, and a DGGRYY sequence corresponding to residues 1034 -1039, located at the C-terminal extremity of the chain. The type I collagen molecule, either fibrillar or denatured, is active, whereas pepsinized collagen, lacking the C...

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Adhesion of Human Neutrophils to and Activation by Type-I Collagen Involving a β2 Integrin

Cited by 62 publications

References 14 publications

Human Blood Monocytes Interact with Type I Collagen Through αxβ2 Integrin (CD11c-CD18, gp150-95)

Human Blood Monocytes Interact with Type I Collagen Through αxβ2 Integrin (CD11c-CD18, gp150-95)

Association of BAP31 with CD11b/CD18

The Binding of Type I Collagen to Lymphocyte Function-associated Antigen (LFA) 1 Integrin Triggers the Respiratory Burst of Human Polymorphonuclear Neutrophils

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