Effects of platelet release products on neutrophilic Fcγ receptors

Sakamoto, Noriko; Sakamoto, Haruhiko; Tanaka, Sumiko; Oryu, Makoto; Ogawa, Yoshitada

doi:10.1002/jlb.64.5.631

Cited by 5 publications

(3 citation statements)

References 12 publications

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“…Such regulatory mechanisms could involve secretion of stored soluble platelet mediators (e.g. by affecting neutrophil F c -receptors [34]), although the dense granule secretion (measured as ATP-release) was low in the present study and the role of soluble mediators was probably of minor importance. Our observations suggest that platelets and platelet-derived fragments not only act as bystanders during the amplification of the neutrophil respiratory burst, but are a prerequisite for an effective recruitment of neutrophils to IgG-coated surfaces: i) microscopic examination revealed that the major part of adhered neutrophils bound to spread platelets or platelet fragments on the IgG-coated particles ii) a substantial neutrophil ROS-production was obtained when the neutrophils were stimulated with viable or fixed platelets that were pre-exposed to IgG-coated particles iii) the stimulatory effect by pre-stimulated platelets was inhibited by filtration (through 0.22 m or 30 kDa MWCO).…”

Section: Discussioncontrasting

confidence: 60%

Platelets stimulated by IgG-coated surfaces bind and activate neutrophils through a selectin-dependent pathway

2003

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Blood platelets bind rapidly to foreign surfaces and interact with adsorbed proteins and neutrophil granulocytes. We demonstrate by use of luminol-amplified chemiluminescence under stirred and nonstirred conditions that platelets at IgG-coated surfaces amplify the neutrophil extracellular release of reactive oxygen species (ROS). The neutrophil response involved tyrosine phosphorylation, but was only in part induced by neutrophil F c -receptor stimulation. The platelet mediated effects were contact-dependent since the respiratory burst was inhibited when the IgG-stimulated platelets were removed by filtration, but not when they were fixed in paraformaldehyde. Bodipyphallacidin-staining of filamentous actin (F-actin) revealed that an actin-dependent platelet adhesion supported the subsequent adhesion and spreading of neutrophils. The neutrophil ROS-response was lowered when the interaction between platelet P-selectin (CD62P) and neutrophil P-selectin glycoprotein ligand-l (PSGL-1 or CD162) was inhibited. The blocking of L-selectin (CD62L) or blocking of the interaction between platelet glycoprotein (Gp) IIb/IIIa and neutrophil complement receptor 3 (CR3) showed no effect. We conclude that platelet activation on immobilized IgG trigger a contact-dependent "frustrated" phagocytosis by neutrophils, associated with a release of toxic ROS. IgG-stimulated platelets activate neutrophils -Wetterö et al.3

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Section: Discussioncontrasting

confidence: 60%

Platelets stimulated by IgG-coated surfaces bind and activate neutrophils through a selectin-dependent pathway

2003

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“…As shown previously, treatment of neutrophils with MAPP does not result in an increase in the number of Fc receptors on neutrophils [40]. This suggests that the effect of MAPP is to strengthen the affinity of Fc receptors with the Fc portion of IgG and to internalize more foreign materials inside the cell.…”

supporting

confidence: 74%

An Apolipoprotein CIII-Derived Peptide, Hatktak, Activates Macromolecular Activators of Phagocytosis from Platelets (MAPPs)

Sakamoto¹,

Ueno²,

Wu³

et al. 2012

Lipoproteins - Role in Health and Diseases

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“…The two specific TfR have already been described on myeloid cells, and Sakamoto et al (43) have reported the existence of TfR on neutrophils. No TfR was detected on rat eosinophils, whereas human eosinophils were found positive for the TfR1 mRNA expression and mouse eosinophils expressed mRNA for the two isoforms.…”

Section: Discussionmentioning

confidence: 86%

Heterogeneity of Expression of IgA Receptors by Human, Mouse, and Rat Eosinophils

Decot

Woerly

Loyens

et al. 2005

The Journal of Immunology

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IgA is the most abundant class of Abs at mucosal surfaces where eosinophils carry out many of their effector functions. Most of the known IgA-mediated functions require interactions with IgA receptors, six of which have been identified in humans. These include the IgA FcR FcαRI/CD89 and the receptor for the secretory component, already identified on human eosinophils, the polymeric IgR, the Fcα/μR, asialoglycoprotein (ASGP)-R, and transferrin (Tf)R/CD71. In rodents, the existence of IgA receptors on mouse and rat eosinophils remains unclear. We have compared the expression and function of IgA receptors by human, rat, and mouse eosinophils. Our results show that human eosinophils express functional polymeric IgR, ASGP-R, and TfR, in addition to CD89 and the receptor for the secretory component, and that IgA receptors are expressed by rodent eosinophils. Indeed, mouse eosinophils expressed only TfR, whereas rat eosinophils expressed ASGP-R and CD89 mRNA. These results provide a molecular basis for the differences observed between human, rat, and mouse regarding IgA-mediated immunity.

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Effects of platelet release products on neutrophilic Fcγ receptors

Cited by 5 publications

References 12 publications

Platelets stimulated by IgG-coated surfaces bind and activate neutrophils through a selectin-dependent pathway

Platelets stimulated by IgG-coated surfaces bind and activate neutrophils through a selectin-dependent pathway

An Apolipoprotein CIII-Derived Peptide, Hatktak, Activates Macromolecular Activators of Phagocytosis from Platelets (MAPPs)

Heterogeneity of Expression of IgA Receptors by Human, Mouse, and Rat Eosinophils

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