Lipopolysaccharide-Induced Gelatinase Granule Mobilization Primes Neutrophils for Activation by Galectin-3 and Formylmethionyl-Leu-Phe

Almkvist, Jenny; Fäldt, Jenny; Dahlgren, Cláes; Leffler, Hakon; Karlsson, Anna

doi:10.1128/iai.69.2.832-837.2001

Cited by 85 publications

(88 citation statements)

References 46 publications

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“…Others and we have shown the ability of galectin-3 to activate cells such as neutrophils to induce the production of reactive oxygen species, IL-8 and L-selectin shedding (43,44,61,67). According to the group of Raz, galectin-3 also has the ability to induce endothelial cell morphogenesis and angiogenesis (68).…”

Section: Discussionmentioning

confidence: 99%

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Role of Galectin-3 in Leukocyte Recruitment in a Murine Model of Lung Infection by Streptococcus pneumoniae

Nieminen

St-Pierre

Bhaumik

et al. 2008

The Journal of Immunology

103

119

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Pneumonia can be caused by a variety of pathogens, among which Streptococcus pneumoniae causes one of the most common forms of community-acquired pneumonia. Depending on the invading pathogen, the elements of the immune response triggered will vary. For most pathogens, such as Escherichia coli, neutrophil recruitment involves a well-described family of adhesion molecules, β2-integrins. In the case of streptococcal pneumonia, however, neutrophil recruitment occurs mainly through a β2-integrin-independent pathway. Despite decades of research on this issue, the adhesion molecules involved in neutrophil recruitment during lung infection by S. pneumoniae have not been identified. We have previously shown that galectin-3, a soluble mammalian lectin, can be found in lungs infected by S. pneumoniae, but not by E. coli, and can mediate the adhesion of neutrophils on the endothelial cell layer, implying its role in the recruitment of neutrophils to lungs infected with S. pneumoniae. In this study, using galectin-3 null mice, we report further evidence of the involvement of this soluble lectin in the recruitment of neutrophils to S. pneumonia-infected lungs. Indeed, in the absence of galectin-3, lower numbers of leukocytes, mainly neutrophils, were recruited to the infected lungs during infection by S. pneumoniae. In the case of β2-integrin-dependent recruitment induced by lung infection with E. coli, the number of recruited neutrophils was not reduced. Thus, taken together, our data suggest that galectin-3 plays a role as a soluble adhesion molecule in the recruitment of neutrophils to lungs infected by S. pneumoniae, which induces β2-integrin-independent migration.

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Section: Discussionmentioning

confidence: 99%

“…Through this interaction, it has been shown to induce IL-1 production by monocytes (36,42), and L-selectin shedding (43), production of IL-8 (43), and reactive oxygen intermediates by neutrophils (44,45). In addition, others and we have demonstrated that soluble galectin-3 can act as an adhesion molecule for neutrophils through ligand cross-linking (29,46,47).…”

mentioning

confidence: 99%

Role of Galectin-3 in Leukocyte Recruitment in a Murine Model of Lung Infection by Streptococcus pneumoniae

Nieminen

St-Pierre

Bhaumik

et al. 2008

The Journal of Immunology

103

119

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“…Interacting with Neutrophils-Upon binding to neutrophils, galectin-3 induces various activities such as production of interleukin 8 (12), L-selectin shedding (12), reactive oxidative intermediate production (26,27,46), and adhesion to the extracellular matrix and endothelial cells (13,14). These activities are not induced in the presence of galectin-3 antagonists, which block the binding, nor by the truncated form of galectin-3, which lacks the N-terminal domain.…”

Section: Detection Of Fret Signal From Galectin-3-tg1-alexamentioning

confidence: 99%

Visualization of Galectin-3 Oligomerization on the Surface of Neutrophils and Endothelial Cells Using Fluorescence Resonance Energy Transfer

Nieminen

Kuno

Hirabayashi

et al. 2007

Journal of Biological Chemistry

204

186

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Galectin-3, a member of the galectin family of carbohydrate binding proteins, is widely expressed, particularly in cells involved in the immune response. Galectin-3 has also been indicated to play a role in various biological activities ranging from cell repression to cell activation and adhesion and has, thus, been recognized as an immunomodulator. Whereas those activities are likely to be associated with ligand cross-linking by this lectin, galectin-3, unlike other members of the galectin family, exists as a monomer. It has consequently been proposed that oligomerization of the N-terminal domains of galectin-3 molecules, after ligand binding by the C-terminal domain, is responsible for this cross-linking. The oligomerization status of galectin-3 could, thus, control the majority of its extracellular activities. However, little is known about the actual mode of action through which galectin-3 exerts its function. In this report we present data suggesting that oligomerization of galectin-3 molecules occurs on cell surfaces with physiological concentrations of the lectin. Using galectin-3 labeled at the C terminus with Alexa 488 or Alexa 555, the oligomerization between galectin-3 molecules on cell surfaces was detected using fluorescence resonance energy transfer. We observed this fluorescence resonance energy transfer signal in different biological settings representing the different modes of action of galectin-3 that we previously proposed; that is, ligand crosslinking leading to cell activation, cell-cell interaction/adhesion, and lattice formation. Furthermore, our data suggest that galectin-3 lattices are robust and could, thus, be involved, as previously proposed, in the restriction of receptor clustering.Galectin-3 is a member of the family of soluble host carbohydrate-binding proteins called galectins (1-3). Members of this lectin family are characterized by conserved peptide sequences in their carbohydrate recognition domains (CRDs), 2 which have an affinity for ␤-galactoside containing glycoconjugates (1-3). Galectin-3 has been implicated in various biological functions such as cell activation and cell adhesion (for a review, see Refs. 4 -7). It has been reported that galectin-3 can induce mast cell degranulation (8), oxidative burst and interleukin-1 production in monocytes (9, 10), and migration of monocytes/macrophages (11) as well as L-selectin shedding and interleukin-8 production in neutrophils (12). Galectin-3 is also involved in cell adhesion of different cell types, such as neutrophils, to extracellular matrix proteins and to the endothelium (13,14).Most galectins are multivalent, being intrinsically composed of two CRDs or existing in a dimerized form (1-3). This multivalency of galectins enables their involvement in cell-cell and cell-pathogen interactions along with signal transduction events and lattice formation upon ligand cross-linking (for a review, see Refs. 4 -7 and 15-19). Interestingly, galectin-3 does not comprise two CRDs nor does it form dimers in solution (20,21). Rather, galec...

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“…The molecular basis for recognition and signaling in response to chemoattractants such as C5a, platelet-activating factor (PAF), 1 interleukin-8 (IL-8), and formylated peptides is the binding to and activation of specific receptors (2), resulting in directed migration, granule mobilization, and activation of the neutrophil NADPH-oxidase. The chemoattractant receptors can be recruited to the cell surface from intracellular storage organelles (3)(4)(5), but the responses are not only influenced by the degree of receptor exposure on the cell surface but also by the survival time of its activated state and the time required for termination of the signals from the occupied receptor (6).…”

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confidence: 99%

Reactivation of Formyl Peptide Receptors Triggers the Neutrophil NADPH-oxidase but Not a Transient Rise in Intracellular Calcium

Bylund

Björstad

Granfeldt

et al. 2003

Journal of Biological Chemistry

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In neutrophils, coupling of chemoattractants to their cell surface receptor at low temperature (<15°C) leads to receptor deactivation/desensitization without any triggering of the superoxide anion-generating NADPHoxidase. We show that the deactivated formyl peptide receptors (FPRs) can be reactivated/resensitized by the cytoskeleton-disrupting drug cytochalasin B. Such cytoskeleton-dependent receptor reactivation occurs also with the closely related receptors FPR-like-1 and C5aR but not with the receptors for interleukin-8 and plateletactivating factor. The reactivation state was further characterized with FPR as a model. The signals generated by receptor reactivation induced superoxide production that was terminated in 5-8 min, after which the neutrophils entered a new state of homologous deactivation. FPR antagonists were potent inhibitors of the superoxide production induced by the reactivated receptors, suggesting that the occupied receptors turn into an actively signaling state when the cytoskeleton is disrupted. The signals generated by the reactivated receptor were pertussis toxin-sensitive, indicating involvement of a G-protein. However, no transient elevation of intracellular Ca 2؉ accompanies the NADPH-oxidase activation. This was not due to a general down-regulation of phospholipase C/Ca 2؉ signaling, and despite the fact that no intracellular Ca 2؉ transient was generated, protein kinase C still appeared to be involved in the response. Further, phosphatidylinositol 3-kinase, mitogen-activated protein kinase, and MEK all participated in the generation of second messengers from the reactivated receptors.

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Lipopolysaccharide-Induced Gelatinase Granule Mobilization Primes Neutrophils for Activation by Galectin-3 and Formylmethionyl-Leu-Phe

Cited by 85 publications

References 46 publications

Role of Galectin-3 in Leukocyte Recruitment in a Murine Model of Lung Infection by Streptococcus pneumoniae

Role of Galectin-3 in Leukocyte Recruitment in a Murine Model of Lung Infection by Streptococcus pneumoniae

Visualization of Galectin-3 Oligomerization on the Surface of Neutrophils and Endothelial Cells Using Fluorescence Resonance Energy Transfer

Reactivation of Formyl Peptide Receptors Triggers the Neutrophil NADPH-oxidase but Not a Transient Rise in Intracellular Calcium

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