Lipocortin (Annexin) I Heterotetramer Binds to Purine RNA and Pyrimidine DNA

Hirata, Aiko; Hirata, Fusao

doi:10.1006/bbrc.1999.1660

Cited by 21 publications

(11 citation statements)

References 15 publications

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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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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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“…The amount of primer required for half maximal DNA synthesis in the presence of nuclear annexin A1 and Ca 2+ decreased significantly to 1 pmol from 5 pmol in the absence of annexin A1. These observations suggest that mono-ubiquitinated annexin A1 promoted annealing of primer to template, while this primer was not necessarily the best substrate for nuclear annexin A1 with regards to length and base composition (Hirata & Hirata, 1999). It is noteworthy that even when the primer was annealed to the template prior to the experiments, annexin A1 was able to enhance translesion DNA synthesis by Pol β, suggesting that annexin A1 stabilizes the ssDNA region of the template.…”

Section: Translesion Dna Synthesis By Mono-ubiquitinated Annexin A1mentioning

confidence: 97%

“…Accordingly, it was thought that DNA and RNA bind to acidic phospholipid binding sites via ionic interaction. Our laboratory has investigated details of annexin A1 binding to RNA and DNA (Hirata & Hirata, 1999;. Annexin A1 purified from rat liver nuclei binds to purine clusters in RNA, while it preferentially binds to pyrimidine clusters in DNA.…”

Section: Dna Helicase Activity Of Nuclear Annexin A1mentioning

confidence: 99%

“…These damaged DNAs were designated as P14G, P30G, and P37G. We previously demonstrated that nuclear annexin A1 binds to ssDNA in a Ca 2+ -dependent manner, and binding to dsDNA or aggregated DNA occurs in a Mg 2+ -dependent manner (Hirata & Hirata, 1999;. In the presence of 50 μM Ca 2+ , mono-ubiquitinated annexin A1 purified from rat liver exhibited higher affinity for damaged DNA, while SUMOylated annexin A1 did not show much of difference in preference.…”

Section: Dna Damage and Mono-ubiquitinated Annexin A1mentioning

confidence: 99%

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Mono-Ubiquitination of Nuclear Annexin A1 and Mutagenesis

Hirata¹,

Corcoran²,

Hirata³

2012

Mutagenesis

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“…17,21,22) Similarly, annexins are cytoplasmic protein and some annexin family members localizes to the nucleus and binds to RNA. 17,23) It is known that annexins bind to carbohydrates including glycosaminoglycans. [24][25][26][27][28] Although Sfrs, annexins and galectins are distinct genetically, their activities suggest that carbohydrate-binding capacity overlaps with RNA binding-activity.…”

Section: Identification Of Iprmentioning

confidence: 99%

Carbohydrate Mimetic Peptides as Research Reagent and Therapeutic

Hatakeyama

Sato

2012

Biological & Pharmaceutical Bulletin

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Although numerous carbohydrates play significant roles in mammalian cells, development of carbohydrate-based reagents and therapeutics are hampered by the technical difficulty of chemically synthesizing complex carbohydrate structures. Use of carbohydrate mimetic peptides circumvents this difficulty, as short peptide can be easily synthesized and modified. We as well as others identified carbohydrate mimetic peptides by screening peptide displaying phage library using anti-carbohydrate antibodies and lectins. This review introduces our experiences with I-peptide that was used for identification of new carbohydrate binding receptor expressed in the lung endothelial cells, and those with IF7 peptide that can be used as a therapeutic against malignant tumors.

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Lipocortin (Annexin) I Heterotetramer Binds to Purine RNA and Pyrimidine DNA

Cited by 21 publications

References 15 publications

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

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

Mono-Ubiquitination of Nuclear Annexin A1 and Mutagenesis

Carbohydrate Mimetic Peptides as Research Reagent and Therapeutic

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