Expression of Annexin A1 in Normal and Chronically Inflamed Nasal Mucosa

Rodrigo, Juan P.; García-Pedrero, Juana M.; González, Marı́a Victoria; Fernández, María P.; Suárez, Carlos; Herrero, Agustín

doi:10.1001/archotol.130.2.211

Cited by 14 publications

(19 citation statements)

References 17 publications

(35 reference statements)

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“…Pyruvate kinase type M2 [32, 33] and annexin I [34,35,36,37,38] are related to cellular function and the differentiation of various cells, including mast cells [39]. Pyruvate kinase catalyzes the conversion of phosphoenolpyruvate to pyruvate in the glycolytic pathway.…”

Section: Discussionmentioning

confidence: 99%

Granule Formation in NGF-Cultured Mast Cells Is Associated with Expressions of Pyruvate Kinase Type M2 and Annexin I Proteins

Kim

Ro³

2008

Int Arch Allergy Immunol

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Background: Nerve growth factor (NGF) is a potent mediator, which regulates characteristics of mast cells, but its biological function is not well characterized. This study aimed to screen proteins associated with the maturation of human mast cells-1 (HMC-1) or mouse bone marrow-derived mast cells (BMMCs) cultured with NGF, and to examine the functions of proteins involved. Methods: NGF (10 ng/ml) was added to cell culture medium every other day for 10 days for HMC-1 or twice a week for 5 weeks for BMMCs. Granule formation was determined by electron microscopy or May-Grünwald-Giemsa staining, TNF-α by ELISA, expressions of various proteins by two-dimensional gel electrophoresis (2-DE), siRNA transfection by Lipofectamine 2000, and the expressions of pyruvate kinase and annexin I by immunoblotting. Results: After NGF treatment, granule formation and total amounts of granular mediator, TNF-α increased in both mast cells. This TNF-α was released by calcium ionophore or by antigen/antibody reaction. Expressions of pyruvate kinase and annexin I obtained by 2-DE were confirmed by immunoblotting and siRNA-transfected HMC-1 cells. Expressions of proteins, granule formation and TNF-α content were blocked by both the TrkA inhibitor, K252a, and the ERK inhibitor, PD98059, but not by the PI3 kinase inhibitors, LY294002 and wortmannin. Conclusion: These data suggest that pyruvate kinase and annexin I expressed by NGF contribute to granule formation containing TNF-α as well as other mediators in mast cells, which play a major role in allergic diseases via a TrkA/ERK pathway.

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Section: Discussionmentioning

confidence: 99%

Granule Formation in NGF-Cultured Mast Cells Is Associated with Expressions of Pyruvate Kinase Type M2 and Annexin I Proteins

Kim

Ro³

2008

Int Arch Allergy Immunol

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“…In terms of immune function, annexin I is an anti-inflammatory factor produced by endothelial cells (Rodrigo et al 2004), skin, epithelial cells, tissue macrophages, leukocytes and synovial cells (Dreier et al 1998). Annexin 1 modulates T-cell activation and differentiation (D'Acquisto et al 2007) and in chronic inflammatory states like rheumatoid arthritis are characterized by increased annexin I production following steroid exposure (Morand et al 2006).…”

Section: Annexin-imentioning

confidence: 99%

Proteomic Analysis of Human Cerebral Endothelial Cells Activated by Multiple Sclerosis Serum and IFNβ-1b

et al. 2007

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Several groups have recently described the endothelial cell (EC) as an important target of pathological mediators in multiple sclerosis (MS). Despite the recognition of the EC as a significant target in MS and a possible beneficiary of Beta-interferon therapy, the structural changes which occur in the cerebrovascular endothelium and the effects of interferon-beta 1b on these changes have not been closely evaluated. Disruption or dysregulation of the blood brain barrier (BBB) in MS represents a loss of endothelial integrity, which may facilitate the transendothelial migration of activated leukocytes responsible for the development of demyelinating lesions of MS. We used proteomics (2-dimensional gel electrophoresis and MALDI-MS) to characterize the effects of serum from MS patients with active disease (with and without interferon-beta 1b therapy) on human cerebral endothelial cells. The results of this study revealed the up- and down-regulation of expression of several proteins related to blood vessel development, cell structure, and cell cycle control. Using this approach we have identified protein 14-3-3, metavinculin, myosin-9, plasminogen, reticulocalbin-2 and-3, ribonuclease/angiogenin inhibitor 1, annexin A1, tropomyosin and Ras-related protein Rap-1A as potential new markers of active MS disease. A more complete description of cerebrovascular endothelial biomarkers and mediators in MS pathogenesis and how they are regulated by inflammatory cytokines and beta-interferons may lead to the development of more effective therapies and more accurate diagnostic markers in MS.

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“…On the other hand, increased expression of annexin A1 has also been described to occur in other types of cancer (i.e., gastric, pancreatic, or esophageal carcinomas) (1,46,47). In addition, an increase of annexin A1 expression with differentiation has been reported to occur in normal epithelia (37) and in different cell lines. Macrophage-like differentiation induced in U937 cells with phorbol esters is accompanied by increased annexin A1 expression, as also described to occur in A549 human lung carcinoma cells (19,41).…”

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confidence: 99%

Upregulation of Annexin A1 Expression by Butyrate in Human Colon Adenocarcinoma Cells: Role of p53, NF-Y, and p38 Mitogen-Activated Protein Kinase

Lecona

Barrasa

Olmo

et al. 2008

Molecular and Cellular Biology

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Annexin A1 is a member of a phospholipid and calcium binding family of proteins; it is involved in anti-inflammation and in the regulation of differentiation, proliferation, and apoptosis. Here, we show the existence of a functional binding site for the tumor suppressor p53 near the proximal CCAAT box and the fact that the basal expression of annexin A1 in human colon adenocarcinoma cells is driven by p53 at the transcriptional level. Posttranscriptional mechanisms may also play an important role in maintaining constitutive annexin A1 expression. In addition, a p53/NF-Y complex is detected bound to the p53 binding site on its promoter. Butyrate is a natural product of fiber degradation in the colon and a key regulator of colonic epithelium homeostasis. We show that butyrate, a class I and II histone deacetylase inhibitor, induces transcriptional activation of annexin A1 expression correlated with differentiation. The effect of butyrate is mediated through a release of NF-Y from the proximal CCAAT box and an enhancement of p53 binding. The interaction of p53 with the promoter is dependent on p38 MAPK activity either in the absence or in the presence of butyrate. Further, activation of p38 MAPK by this agent is required to increase annexin A1 promoter activity and to increase protein expression.

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Expression of Annexin A1 in Normal and Chronically Inflamed Nasal Mucosa

Cited by 14 publications

References 17 publications

Granule Formation in NGF-Cultured Mast Cells Is Associated with Expressions of Pyruvate Kinase Type M2 and Annexin I Proteins

Granule Formation in NGF-Cultured Mast Cells Is Associated with Expressions of Pyruvate Kinase Type M2 and Annexin I Proteins

Proteomic Analysis of Human Cerebral Endothelial Cells Activated by Multiple Sclerosis Serum and IFNβ-1b

Upregulation of Annexin A1 Expression by Butyrate in Human Colon Adenocarcinoma Cells: Role of p53, NF-Y, and p38 Mitogen-Activated Protein Kinase

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