Phagocytosis and development: back to the future

Franc, Nathalie C.; White, Kristin; Ezekowitz, R. A. B.

doi:10.1016/s0952-7915(99)80009-0

Cited by 113 publications

(66 citation statements)

References 47 publications

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“…previously characterized Drosophila hemocyte markers plasmatocyte phagocytosis (Franc et al 1996(Franc et al , 1999; (F and G) Figure S1 at http:/ /www.genetics.org/sup visible crystal cells ( Figure 1B). Crystal cells were deplemental/).…”

Section: Dm-mybmentioning

confidence: 73%

Functional Evolution of the Vertebrate Myb Gene Family

et al. 2005

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The duplication of genes and genomes is believed to be a major force in the evolution of eukaryotic organisms. However, different models have been presented about how duplicated genes are preserved from elimination by purifying selection. Preservation of one of the gene copies due to rare mutational events that result in a new gene function (neofunctionalization) necessitates that the other gene copy retain its ancestral function. Alternatively, preservation of both gene copies due to rapid divergence of coding and noncoding regions such that neither retains the complete function of the ancestral gene (subfunctionalization) may result in a requirement for both gene copies for organismal survival. The duplication and divergence of the tandemly arrayed homeotic clusters have been studied in considerable detail and have provided evidence in support of the subfunctionalization model. However, the vast majority of duplicated genes are not clustered tandemly, but instead are dispersed in syntenic regions on different chromosomes, most likely as a result of genome-wide duplications and rearrangements. The Myb oncogene family provides an interesting opportunity to study a dispersed multigene family because invertebrates possess a single Myb gene, whereas all vertebrate genomes examined thus far contain three different Myb genes (A-Myb, B-Myb, and c-Myb). A-Myb and c-Myb appear to have arisen by a second round of gene duplication, which was preceded by the acquisition of a transcriptional activation domain in the ancestral A-Myb/ c-Myb gene generated from the initial duplication of an ancestral B-Myb-like gene. B-Myb appears to be essential in all dividing cells, whereas A-Myb and c-Myb display tissue-specific requirements during spermatogenesis and hematopoiesis, respectively. We now report that the absence of Drosophila Myb (DmMyb) causes a failure of larval hemocyte proliferation and lymph gland development, while Dm-Myb Ϫ/Ϫ hemocytes from mosaic larvae reveal a phagocytosis defect. In addition, we show that vertebrate B-Myb, but neither vertebrate A-Myb nor c-Myb, can complement these hemocyte proliferation defects in Drosophila. Indeed, vertebrate A-Myb and c-Myb cause lethality in the presence or absence of endogenous Dm-Myb. These results are consistent with a neomorphic origin of an ancestral A-Myb/c-Myb gene from a duplicated B-Myb-like gene. In addition, our results suggest that B-Myb and Dm-Myb share essential conserved functions that are required for cell proliferation. Finally, these experiments demonstrate the utility of genetic complementation in Drosophila to explore the functional evolution of duplicated genes in vertebrates.

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Section: Dm-mybmentioning

confidence: 73%

Functional Evolution of the Vertebrate Myb Gene Family

et al. 2005

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“…(Tepass et al 1994) and display similar features to mammalian macrophages (Abrams et al 1993, White et al 1994, Franc et al 1999a). The receptor Croquemort (Crq) is a CD-36 related molecule (Franc et al 1996) and can be a candidate for PS recognition by Drosophila hemocytes.…”

Section: Apoptotic Cell Recognition In Mammalian Systems: Redundancymentioning

confidence: 96%

Apoptotic cell and phagocyte interplay: recognition and consequences in different cell systems

Moreira

Barcinski

2004

An. Acad. Bras. Ciênc.

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Cell death by apoptosis is characterized by specific biochemical changes, including the exposure of multiple ligands, expected to tag the dying cell for prompt recognition by phagocytes. In non-pathological conditions, an efficient clearance is assured by the redundant interaction between apoptotic cell ligands and multiple receptor molecules present on the engulfing cell surface. This review concentrates on the molecular interactions operating in mammalian and non-mammalian systems for apoptotic cell recognition, as well as on the consequences of their signaling. Furthermore, some cellular models where the exposure of the phosphatidylserine (PS) phospholipid, a classical hallmark of the apoptotic phenotype, is not followed by cell death will be discussed.

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“…In addition, the innate immune system may be responsible for the recognition of necrotic and apoptotic cells and self Ags that are released from such cells (1). One family of proteins that function as innate immune system recognition molecules is the pentraxins (2,3).…”

mentioning

confidence: 99%

Serum Amyloid P Component Binds to Fcγ Receptors and Opsonizes Particles for Phagocytosis

Bharadwaj

Mold

Markham

et al. 2001

The Journal of Immunology

148

150

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Serum amyloid P component (SAP) is a member of the pentraxin family of proteins. These proteins are characterized by cyclic pentameric structure, calcium-dependent ligand binding, and frequent regulation as acute-phase serum proteins. SAP is the serum precursor of the P component of amyloid. It binds to a broad group of molecules, including autoantigens, through a pattern recognition binding site. The related pentraxin, C-reactive protein (CRP), is a strong acute-phase reactant in man and an opsonin. We previously determined that the binding of CRP to leukocytes occurs through Fc receptors for IgG (FcγR). We now report that SAP also binds to FcγR and opsonizes particles for phagocytosis by human polymorphonuclear leukocytes (PMN). Specific, saturable binding of SAP to FcγRI, FcγRIIa, and FcγRIIIb expressed on transfected COS cells was detected using SAP-biotin and PE-streptavidin. Zymosan was used to test the functional consequences of SAP and CRP binding to FcγR. Both SAP and CRP bound to zymosan and enhanced its uptake by PMN. This enhanced phagocytosis was abrogated by treatment of PMN with wortmannin, a phosphatidylinositol-3 kinase inhibitor, or with piceatannol, a Syk inhibitor, consistent with uptake through FcγR. Treatment of PMN with phosphatidylinositol-specific phospholipase C to remove FcγRIIIb also decreased phagocytosis of SAP-opsonized zymosan, but not CRP-opsonized zymosan. These results suggest that SAP may function in host defense. In addition, as SAP binds to chromatin, a major immunogen in systemic lupus erythematosus, it may provide a clearance mechanism for this Ag through FcγR bearing cells.

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Phagocytosis and development: back to the future

Cited by 113 publications

References 47 publications

Functional Evolution of the Vertebrate Myb Gene Family

Functional Evolution of the Vertebrate Myb Gene Family

Apoptotic cell and phagocyte interplay: recognition and consequences in different cell systems

Serum Amyloid P Component Binds to Fcγ Receptors and Opsonizes Particles for Phagocytosis

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