Annexins VII and XI are present in a human macrophage-like cell line. Differential translocation on FcR-mediated phagocytosis

Pittis, María Gabriela; García, Rafael Martínez

doi:10.1002/jlb.66.5.845

Cited by 14 publications

(9 citation statements)

References 20 publications

(22 reference statements)

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“…This dichotomy suggests that CaMKII-independent effects are involved in ionophore-induced reductions in the intracellular survival of M. tuberculosis, particularly at later time points. Another class of potential Ca 2ϩ -regulated modulators of phagosomal maturation are the annexins, a family of Ca 2ϩ -dependent phospholipid-binding proteins that are highly enriched on endosomes and regulate homotypic endosome fusion (46,47). In human neutrophils, phagocytosis of the attenuated H37Ra strain of M. tuberculosis also occurs in the absence of a change in [Ca 2ϩ ] c , and the resultant phagosome exhibits a distinctive profile of annexin isoforms, compared with phagosomes encompassing particles that stimulate an increase in [Ca 2ϩ ] c (48).…”

Section: Discussionmentioning

confidence: 99%

Mycobacterium tuberculosis Phagosomes Exhibit Altered Calmodulin-Dependent Signal Transduction: Contribution to Inhibition of Phagosome-Lysosome Fusion and Intracellular Survival in Human Macrophages

Malik

Kusner

2001

The Journal of Immunology

168

171

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Mycobacterium tuberculosis successfully parasitizes macrophages by disrupting the maturation of its phagosome, creating an intracellular compartment with endosomal rather than lysosomal characteristics. We have recently demonstrated that live M. tuberculosis infect human macrophages in the absence of an increase in cytosolic Ca2+ ([Ca2+]c), which correlates with inhibition of phagosome-lysosome fusion and intracellular viability. In contrast, killed M. tuberculosis induces an elevation in [Ca2+]c that is coupled to phagosome-lysosome fusion. We tested the hypothesis that defective activation of the Ca2+-dependent effector proteins calmodulin (CaM) and CaM-dependent protein kinase II (CaMKII) contributes to the intracellular pathogenesis of tuberculosis. Phagosomes containing live M. tuberculosis exhibited decreased levels of CaM and the activated form of CaMKII compared with phagosomes encompassing killed tubercle bacilli. Furthermore, ionophore-induced elevations in [Ca2+]c resulted in recruitment of CaM and activation of CaMKII on phagosomes containing live M. tuberculosis. Specific inhibitors of CaM or CaMKII blocked Ca2+ ionophore-induced phagosomal maturation and enhanced the bacilli’s intracellular viability. These results demonstrate a novel role for CaM and CaMKII in the regulation of phagosome-lysosome fusion and suggest that defective activation of these Ca2+-activated signaling components contributes to the successful parasitism of human macrophages by M. tuberculosis.

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Section: Discussionmentioning

confidence: 99%

Mycobacterium tuberculosis Phagosomes Exhibit Altered Calmodulin-Dependent Signal Transduction: Contribution to Inhibition of Phagosome-Lysosome Fusion and Intracellular Survival in Human Macrophages

Malik

Kusner

2001

The Journal of Immunology

168

171

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“…Besides its role in exocytosis, reports also show that Axn7 may be involved in endocytosis. Axn7 is found to translocate from cytosolic to membrane regions (phagosomes) upon particle ingestion [Pittis and Garcia, 1999;Herr et al, 2003;Kundranda et al, 2004].…”

Section: Possible Role Of Axn7 In Suppressing Hbv Infectionmentioning

confidence: 98%

Antiviral effect of Phyllanthus nanus ethanolic extract against hepatitis B virus (HBV) by expression microarray analysis

Lam

Leung

Law

et al. 2005

J of Cellular Biochemistry

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Ethanolic extract of Phyllanthus nanus (P. nanus) treatment exhibited potent antiviral activity against Hepatitis B virus (HBV). The effects of these extracts on HBV in the HBV genome integrated cell lines--Alexander cells and HepG2 2.2.15 cells were examined. Experimental results showed that the ethanolic extract of P. nanus produced suppressive effect on HBsAg secretion and HBsAg mRNA expression. The extract also inhibited HBV replication as measured by HBV DNA level in vitro. In addition, using a duck HBV (DHBV) primary culture model, the P. nanus ethanolic extract suppressed viral replication of DHBV in DHBV infected primary duck hepatocytes. The gene expression pattern in Alexander cells that had been treated with the ethanolic extract of P. nanus was also revealed by microarray techniques. The microarray results indicated that there was up-regulation of expression of several genes, including annexin A7 (Axn7). The subcellular localization of Axn7 and anti-HBV effect of Axn7 over-expression in Alexander cells were also investigated. Results showed that expression of Axn7-GFP fusion protein are localized around the secretory vesicles and could cause a decrease in HBsAg secretion in Alexander cells. Axn7 protein might play an important role in the medicinal effect of the active principle(s) of P. nanus.

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“…Annexins have been localized to the plasma membrane (9), early endosomes (10,11), late endosomes, multivesicular bodies (11,12), phagosomes (10,12), and Golgi (11). In addition to the vesicular system, annexins have also been detected in mitochondria and the nucleus (5).…”

mentioning

confidence: 99%

Selective Degradation of Annexins by Chaperone-mediated Autophagy

Cuervo¹,

Gomes²,

Barnes³

et al. 2000

Journal of Biological Chemistry

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Annexins are a family of proteins that bind phospholipids in a calcium-dependent manner. Analysis of the sequences of the different members of the annexin family revealed the presence of a pentapeptide biochemically related to KFERQ in some annexins but not in others. Such sequences have been proposed to be a targeting sequence for chaperone-mediated autophagy, a lysosomal pathway of protein degradation that is activated in confluent cells in response to removal of serum growth factors. We demonstrate that annexins II and VI, which contain KFERQ-like sequences, are degraded more rapidly in response to serum withdrawal, while annexins V and XI, without such sequences, are degraded at the same rate in the presence and absence of serum. Using isolated lysosomes, only the annexins containing KFERQ-like sequences are degraded by chaperone mediated-autophagy. Annexins V and XI could associate with lysosomes but did not enter the lysosomes and were not proteolytic substrates. Furthermore, four annexins containing KFERQ-like sequences, annexins I, II, IV, and VI, are enriched in lysosomes with high chaperone-mediated autophagy activity as expected for substrate proteins. These results provide striking evidence for the importance of KFERQ motifs in substrates of chaperone-mediated autophagy.

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Annexins VII and XI are present in a human macrophage-like cell line. Differential translocation on FcR-mediated phagocytosis

Cited by 14 publications

References 20 publications

Mycobacterium tuberculosis Phagosomes Exhibit Altered Calmodulin-Dependent Signal Transduction: Contribution to Inhibition of Phagosome-Lysosome Fusion and Intracellular Survival in Human Macrophages

Mycobacterium tuberculosis Phagosomes Exhibit Altered Calmodulin-Dependent Signal Transduction: Contribution to Inhibition of Phagosome-Lysosome Fusion and Intracellular Survival in Human Macrophages

Antiviral effect of Phyllanthus nanus ethanolic extract against hepatitis B virus (HBV) by expression microarray analysis

Selective Degradation of Annexins by Chaperone-mediated Autophagy

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