Protein Kinase C-θ Is Required for Murine Neutrophil Recruitment and Adhesion Strengthening under Flow

Bertram, Anna; Zhang, Hong; Vietinghoff, Sibylle von; Pablo, Carmen de; Haller, Hermann; Shushakova, Nelli; Ley, Klaus

doi:10.4049/jimmunol.1101651

Cited by 27 publications

(33 citation statements)

References 51 publications

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“…Phospholipase C signaling downstream of LFA-1 has been reported to be important for firm adhesion of effector T cells (10). PKC/protein kinase D (PKD) signaling are downstream of phospholipase C in cells, and PKC isoforms have recently been implicated in neutrophil adhesion strengthening under conditions of shear flow (17). However, effector T cell adhesion to ICAM-1 under shear flow conditions is independent of PKC (this report), and we have previously reported that it is also independent of PKD (9).…”

Section: Discussionmentioning

confidence: 99%

“…Phospholipase C activity has previously been implicated in LFA-1 regulation in human effector T cells (10), and this enzyme is upstream of protein kinase C (PKC) activation in cells. PKC isoforms have been implicated in LFA-1 adhesion under flow in T cells and neutrophils (16,17). We therefore used the general PKC inhibitor, Ro-318220, to investigate the dependence of effector T cell adhesion under shear flow on PKC activity.…”

Section: Lfa-1-mediated Adhesion Of Effector T Cells Under Flow Condimentioning

confidence: 99%

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The Spontaneously Adhesive Leukocyte Function-associated Antigen-1 (LFA-1) Integrin in Effector T Cells Mediates Rapid Actin- and Calmodulin-dependent Adhesion Strengthening to Ligand under Shear Flow

Lek

Morrison

Conneely³

et al. 2013

Journal of Biological Chemistry

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Background:The effector T cell LFA-1 integrin is important for migration and effector functions. Results: Effector T cell LFA-1 integrin is highly expressed, spontaneously binds ligand, and mediates rapid actin-and calmodulin-dependent adhesion strengthening. Conclusion: LFA-1 in effector T cells binds ligand spontaneously, but firm adhesion requires integrin signaling. Significance: LFA-1 is regulated differently in naïve and effector lymphocytes.

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Section: Discussionmentioning

confidence: 99%

Section: Lfa-1-mediated Adhesion Of Effector T Cells Under Flow Condimentioning

confidence: 99%

The Spontaneously Adhesive Leukocyte Function-associated Antigen-1 (LFA-1) Integrin in Effector T Cells Mediates Rapid Actin- and Calmodulin-dependent Adhesion Strengthening to Ligand under Shear Flow

Lek

Morrison

Conneely³

et al. 2013

Journal of Biological Chemistry

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“…Conversely, the number of adherent neutrophils increases. For stable neutrophil adhesion, additional signaling steps are needed that depend on integrin outside-in signaling (16, 17), provided by both αMβ2 (Mac-1) and αLβ2 (LFA-1).…”

Section: Introductionmentioning

confidence: 99%

Gαi2 and Gαi3 Differentially Regulate Arrest from Flow and Chemotaxis in Mouse Neutrophils

Kuwano

Adler

Zhang

et al. 2016

The Journal of Immunology

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Leukocyte recruitment to inflammation sites progresses in a multistep cascade. Chemokines regulate multiple steps of the cascade including arrest, transmigration and chemotaxis. The most important chemokine receptor in mouse neutrophils is CXCR2, which couples through Gαi2 and Gαi3-containing heterotrimeric G proteins. Neutrophils arrest in response to CXCR2 stimulation. This is defective in Gαi2 deficient neutrophils. Here, we show that Gαi3 deficient neutrophils showed reduced transmigration but normal arrest in mice. We also tested Gαi2 or Gαi3 deficient neutrophils in a CXCL1 gradient generated by a microfluidic device. Gαi3, but not Gαi2, deficient neutrophils showed significantly reduced migration and directionality. This was confirmed in a model of sterile inflammation in vivo. Gαi2, but not Gαi3, deficient neutrophils showed decreased Ca2+ flux in response to CXCR2 stimulation. Conversely, Gαi3, but not Gαi2, deficient neutrophils exhibited reduced AKT phosphorylation upon CXCR2 stimulation. We conclude that Gαi2 controls arrest and Gαi3 controls transmigration and chemotaxis in response to chemokine stimulation of neutrophils.

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“…Since alterations in adhesion forces, cell spreading and membrane tension have been reported as being responsible for defective cell migration [23][24][25][26], we tested the ability of Myo1g-deficient B cells to migrate toward a chemokine gradient. We used CXCL13 to induce migration of resting B lymphocytes over a fibronectincoated surface in a chemotaxis chamber.…”

Section: Slow B-cell Migration In Vitro and Defective Homing In Vivomentioning

confidence: 99%

Myosin 1g regulates cytoskeleton plasticity, cell migration, exocytosis, and endocytosis in B lymphocytes

et al. 2014

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Myosin 1g (Myo1g) is a hematopoietic-specific myosin expressed mainly by lymphocytes. Here, we report the localization of Myo1g in B-cell membrane compartments such as lipid rafts, microvilli, and membrane extensions formed during spreading. By using Myo1g-deficient mouse B cells, we detected abnormalities in the adhesion ability and chemokineinduced directed migration of these lymphocytes. We also assessed a role for Myo1g in phagocytosis and exocytosis processes, as these were also irregular in Myo1g-deficient B cells. Taken together, our results show that Myo1g acts as a main regulator of different membrane/cytoskeleton-dependent processes in B lymphocytes.Keywords: B lymphocyte r Chemotaxis r Cytoskeleton r Exo-endocytosis r Myosin Additional supporting information may be found in the online version of this article at the publisher's web-site IntroductionMyosin I refers to a class of single-headed and actin-dependent molecular motors, which regulates a number of cellular functions, including intracellular transport, formation of cell-surface projections, regulation of the cytoskeleton, and regulation of membranerelated events, which includes exocytosis, endocytosis, and phagocytosis [1][2][3].Members of myosin I family contain a single heavy chain of 110-140 kDa [4,5], are monomeric, and do not form filaments unlike muscular/conventional myosin II. The single heavy chain is divided into the head (or motor), neck, and tail domains. The motor domain contains the ATP-binding (where ATP is adenosine triphosphate) site and the actin-binding site. This domain is Correspondence: Dr. Leopoldo Santos-Argumedo e-mail: lesantos@cinvestav.mx followed by the neck domain, which is involved in the binding of myosin light chains; molecules identified as calmodulin in vertebrate and yeast class I myosins [6]. Following the neck domain is the C-terminal tail region, which is enriched in basic residues and is involved in the binding of membrane phosphoinositides [7,8]. In humans and mice, eight different genes encode the eight heavy chains of class I myosins and are named Myo1a to Myo1h [2].Myosin 1g (Myo1g) is a vertebrate class I myosin, which is highly represented in leukocytes, according to microarray databases [9][10][11]. Immunoblot analyses of different tissues and cell lines recently identified this protein as being an exclusively hematopoietic motor protein [12,13].Mass spectrometric proteomic profiling of lymphocyte proteins indicates that Myo1g is the most abundant class I myosin * These authors contributed equally to this work. 878José L. Maravillas-Montero et al. Eur. J. Immunol. 2014. 44: 877-886 expressed by T lymphocytes [13]. Immunofluorescence assays showed that Myo1g localizes to the plasma membrane linked to phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol 3,4,5-triphosphate [14], is particularly enriched at cell-surface microvilli, and associates in an ATP-releasable manner to the actin cytoskeleton [12,13]. In addition to its localization pattern, it has been proposed that this molecula...

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Protein Kinase C-θ Is Required for Murine Neutrophil Recruitment and Adhesion Strengthening under Flow

Cited by 27 publications

References 51 publications

The Spontaneously Adhesive Leukocyte Function-associated Antigen-1 (LFA-1) Integrin in Effector T Cells Mediates Rapid Actin- and Calmodulin-dependent Adhesion Strengthening to Ligand under Shear Flow

The Spontaneously Adhesive Leukocyte Function-associated Antigen-1 (LFA-1) Integrin in Effector T Cells Mediates Rapid Actin- and Calmodulin-dependent Adhesion Strengthening to Ligand under Shear Flow

Gαi2 and Gαi3 Differentially Regulate Arrest from Flow and Chemotaxis in Mouse Neutrophils

Myosin 1g regulates cytoskeleton plasticity, cell migration, exocytosis, and endocytosis in B lymphocytes

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