Annexin A2 Is a Novel RNA-binding Protein

Filipenko, Nolan R.; MacLeod, Travis J.; Yoon, Chanho; Waisman, David M.

doi:10.1074/jbc.m311951200

Cited by 124 publications

(118 citation statements)

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“…In addition, antisense oligonucleotides to annexin A2 retard proliferation of Hela cells [24], and the expression of annexin A2 is regulated during the mammalian cell cycle [25]. Recent study has demonstrated ANXA2 is a RNA-binding protein that interacts with the mRNA of the nuclear oncogene, c-myc, and results in an increase in c-Myc protein [26]. Therefore, the up-regulation of ANXA2 may contribute to tumorigenesis of ccRCC through increasing the c-Myc protein level.…”

Section: Discussionmentioning

confidence: 99%

Identification of differentially expressed genes in clear cell renal cell carcinoma by analysis of full-length enriched cDNA library

et al. 2006

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SummaryRenal cell carcinoma (RCC) is the most common malignancy in adult kidney, and accounts for 3% of malignancies worldwide with increasing incidence. Clear cell RCC (ccRCC) is the major type in RCC. Resection by surgery is the main treatment because the response of ccRCC to traditional therapies is very poor. To identify the tumor-associated genes for better understanding the molecular mechanism of ccRCC, the full-length enriched cDNA libraries of ccRCC and normal kidney tissues were constructed by the oligo-capping method. Nucleotide sequences of the cDNA libraries of ccRCC and normal kidney tissues were sequenced. From the sequence analysis of 19,425 and 12,400 clones of ccRCC and normal kidney tissues, 4356 and 3055 genes were identified, respectively. By comparing the gene-expression patterns of ccRCC and normal tissues, the up-or down-regulated genes were identified. Among these identified genes, the differential expression of annexin A2 and argininosuccinate synthetase genes were further confirmed by quantitative real-time PCR and Western blot analysis.

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Section: Discussionmentioning

confidence: 99%

Identification of differentially expressed genes in clear cell renal cell carcinoma by analysis of full-length enriched cDNA library

et al. 2006

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“…Changes in cellular ion composition may regulate some of the ion channels such as Atp1a1 and Atp2a1. (d) Annexin A2 has been shown to bind with RNAs (29). Under certain conditions, nuclear annexin A2 was detected (30).…”

Section: Discussionmentioning

confidence: 99%

Annexin A2 Interactions with Rab14 in Alveolar Type II Cells

Gou

Mishra

Weng

et al. 2008

Journal of Biological Chemistry

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Annexin A2, a calcium-dependent phospholipid-binding protein, is abundantly expressed in alveolar type II cells where it plays a role in lung surfactant secretion. Nevertheless, little is known about the details of its cellular pathways. To identify annexin A2-regulated or associated proteins, we silenced endogenous annexin A2 expression in rat alveolar type II cells by RNA interference and assessed the change of the cellular transcriptome by DNA microarray analysis. The loss of annexin A2 resulted in the change of 61 genes. Thirteen of the selected genes (11 down-regulated and 2 up-regulated genes) were validated by real time quantitative PCR. When the loss of rat annexin A2 was rescued by overexpressing EGFP-tagged human annexin A2, six of seven selected targets returned to their normal expression level, indicating that these genes are indeed annexin A2-associated targets. One of the targets, Rab14, co-immunoprecipitated with annexin A2. Rab14 also co-localized in part with annexin A2 and lamellar bodies in alveolar type II cells. The silencing of Rab14 resulted in a decrease in surfactant secretion, suggesting that Rab14 may play a role in surfactant secretion.The alveolar epithelium is composed of morphologically and functionally distinct type I and II cells. Type I cells provide the bulk of the surface area for gas exchange, whereas type II cells secrete lung surfactant to maintain mechanical stability of the alveoli (1-3). Lung surfactant is stored and secreted by exocytosis of lamellar bodies, which are specialized organelles found in type II cells. Exocytosis of the lamellar bodies is triggered by several intracellular signaling pathways. A key component of signaling involves the elevation of cytosolic Ca 2ϩ concentration in type II cells (4, 5). Because lung surfactant secretion is regulated by Ca 2ϩ signals, it is important to identify Ca 2ϩ -regulated proteins for exocytosis.Annexins are a family of Ca 2ϩ -dependent phospholipidbinding proteins. More than 50 different annexin isoforms have been identified (6, 7). Each annexin consists of a short variable N-terminal segment and a conserved C-terminal core domain. They have unique Ca 2ϩ -binding sites, which enable them to bind with negatively charged lipids. Annexins participate in many membrane-related events, such as the organization of membrane domains, the linkages of membrane-cytoskeleton, exocytosis and endocytosis, and the regulation of ion fluxes (7). Annexin A2 is abundant in alveolar type II cells. Several studies have indicated that annexin A2 is involved in Ca 2ϩ -regulated exocytosis (8 -10). In permeabilized chromaffin cells, the timedependent loss of secretory capacity can be blocked by the addition of annexin A2 to the culture medium (9). Knockdown of annexin A2 reduces the Ca 2ϩ -evoked exocytosis of WeibelPalade bodies in endothelial cells (10). In alveolar type II cells, accumulating evidence supports a role for annexin A2 in controlling the fusion of lamellar bodies with the plasma membrane and promoting surfactant secretion (11-14)...

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“…Galectins are well-established carbohydrate-binding proteins (22), but several galectin proteins also localize to the nucleus and exhibit pre-mRNA splicing activity (23)(24)(25). The annexins also form a large protein family, and some members localize to the nucleus and bind RNA (25)(26)(27). Annexin 4 binds to N-glycan (28), and Annexins 4, 5, and 6 bind sulfated glycosaminoglycans (28,29).…”

Section: Discussionmentioning

confidence: 99%

Identification of mRNA splicing factors as the endothelial receptor for carbohydrate-dependent lung colonization of cancer cells

Hatakeyama

Sato

Nakayama

et al. 2009

Proc. Natl. Acad. Sci. U.S.A.

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Cell surfaces of epithelial cancer are covered by complex carbohydrates, whose structures function in malignancy and metastasis. However, the mechanism underlying carbohydrate-dependent cancer metastasis has not been defined. Previously, we identified a carbohydrate-mimicry peptide designated I-peptide, which inhibits carbohydrate-dependent lung colonization of sialyl Lewis X-expressing B16-FTIII-M cells in E/P-selectin doubly-deficient mice. We hypothesized that lung endothelial cells express an unknown carbohydrate receptor, designated as I-peptide receptor (IPR), responsible for lung colonization of B16-FTIII-M cells. Here, we visualized IPR by in vivo biotinylation, which revealed that the major IPR is a group of 35-kDa proteins. IPR proteins isolated by I-peptide affinity chromatography were identified by proteomics as Ser/Arg-rich alternative pre-mRNA splicing factors or Sfrs1, Sfrs2, Sfrs5, and Sfrs7 gene products. annexin ͉ galectin ͉ metastasis ͉ selectin ͉ vasculature T he apical cell surface of epithelia is covered by numerous carbohydrates attached to membrane proteins and lipids. When epithelial cells are transformed, the structure of these carbohydrates changes (1). Many investigators have suggested a correlation between cancer-associated carbohydrate antigens and poor patient prognosis, including metastasis (2-8). Despite extensive structural analysis and clinical observations using monoclonal antibodies against cancer-associated carbohydrate antigens, mechanisms underlying carbohydrate-dependent cancer metastasis through the circulation remain elusive. Because E-selectin is expressed on the inflammatory endothelial cell surface and binds to cancer-associated carbohydrate antigens such as sialyl Lewis A (sLeA) and sialyl Lewis X (sLeX), E-selectin provides a mechanism for sLeA and/or sLeX antigenexpressing cancer cells to be metastasized through the hematogenous route (4-6). Involvement of P-selectin and L-selectin in cancer metastasis has been also described (7,8). However, substantial clinical data indicate the existence of selectin-independent but carbohydrate-dependent cancer metastasis (6, 10, 11).In our previous studies, we screened a peptide-displaying phage library using a monoclonal anti-Lewis A antibody (clone 7LE) and identified a short peptide IELLQAR, designated I-peptide (12-14). When I-peptide was injected intravenously into a mouse, it bound to a specific subset of lung capillary endothelial cells but not to blood vessels of other organs including the liver (12). I-peptide administration inhibited carbohydrate-dependent lung colonization of fucosyltransferase-3-transfected sialyl Lewis X antigenpositive B16 (B16-FTIII-M) cells (15) in wild-type mice (12) and in E-and P-selectin doubly-deficient mutant mice (13), suggesting that the lung endothelial surface expresses unknown carbohydratebinding receptor(s) enabling colonization of B16-FTIII-M cells. We designated this presumptive receptor I-peptide receptor (IPR) (13).In this study, we isolated IPR candidate proteins by I-peptideaff...

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Annexin A2 Is a Novel RNA-binding Protein

Abstract: The annexins are a family of more than 160 unique annexin proteins that are present in more than 65 different species ranging from fungi and protists to plants and higher vertebrates (1). ANXA2

Cited by 124 publications

References 56 publications

Identification of differentially expressed genes in clear cell renal cell carcinoma by analysis of full-length enriched cDNA library

Identification of differentially expressed genes in clear cell renal cell carcinoma by analysis of full-length enriched cDNA library

Annexin A2 Interactions with Rab14 in Alveolar Type II Cells

Identification of mRNA splicing factors as the endothelial receptor for carbohydrate-dependent lung colonization of cancer cells

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