Down Modulation of N-myc, Heat-Shock Protein 70, and Nucleolin during the Differentiation of Human Neuroblastoma Cells1

Murakami, Tadamasa; Ohmori, Hisamitsu; Gotoh, Sadao; Tsuda, Tohru; Ohya, Ryoichi; Akiya, Shinobu; Higashi, Ken

doi:10.1093/oxfordjournals.jbchem.a123533

Cited by 22 publications

(12 citation statements)

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“…2A, left panels), expression of nucleolin on THP-1 macrophages was lower than that on THP-1 monocytes. This is consistent with the previous observations that expression of nucleolin is lowered when cells differentiate or cell growth slows (55,56). However, in the present study, the ability of THP-1 monocytes to recognize early apoptotic Jurkat cells was suggested to be much lower than that of THP-1 macrophages.…”

Section: Discussionsupporting

confidence: 93%

A Multifunctional Shuttling Protein Nucleolin Is a Macrophage Receptor for Apoptotic Cells

Hirano

Miki

Hirai

et al. 2005

Journal of Biological Chemistry

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Early apoptotic Jurkat T cells undergo capping of CD43, and its polylactosaminyl saccharide chains serve as ligands for phagocytosis by macrophages. This suggests the presence of a polylactosaminoglycan-binding receptor on macrophages. Here we show that this receptor is nucleolin, a multifunctional shuttling protein present in nucleus, cytoplasm, and on the surface of some types of cells. Nucleolin was detected at the surface of macrophages, and antinucleolin antibody inhibited the binding of the early apoptotic cells to macrophages. Nucleolin-transfected HEK293 cells expressed nucleolin on the cell surface and bound the early apoptotic cells but not phosphatidylserine-exposing late apoptotic cells. This binding was inhibited by anti-nucleolin antibody, by polylactosamine-containing oligosaccharides, and by anti-CD43 antibody. Deletion of the antibody binding region of nucleolin resulted in loss of the apoptotic cell-binding ability. Moreover, truncated recombinant nucleolin in solution containing this region blocked the apoptotic cell binding to macrophages, and the blocking effect was cancelled by the oligosaccharides. These results indicate that nucleolin is a macrophage receptor for apoptotic cells.Macrophages and other phagocytes recognize and ingest apoptotic cells in tissue, preventing their lysis and subsequent release of harmful or immunogenic intracellular components. Therefore, clearance of apoptotic cells by phagocytes is crucial in the maintenance of tissue turnover and homeostasis. Moreover, it has been suggested that the apoptotic cell-ingested phagocytes play a role in suppression or resolution of inflammation (1-5).Cells undergoing apoptosis display a variety of "eat me" signals, namely cell-surface changes to be recognized by phagocytes. These include externalization of phosphatidylserine (PS),3 as yet little identified alterations of carbohydrates, and unidentified alterations of other membrane components such as intercellular adhesion molecule-3 and "thrombospondin binding sites" (1-5). Among these, the most common and the best-characterized change is externalization of PS, although the mechanism of externalization has not been fully understood (6, 7).In contrast to the poor understanding of the nature of eat me signals, various proteins of phagocyte membrane or in extracellular fluid have been reported as receptors or bridging factors for apoptotic cells. For externalized PS on apoptotic cells, CD36 (8), CD68 (9), CLA-1 (10), LOX-1 (11), and PS receptor (12) have been reported as phagocyte receptors; a serum protein ␤ 2 -glycoprotein I (13), complement component C3bi (14), and milk fat globule-epidermal growth factor-factor 8 (15) have been reported to bridge apoptotic cells and phagocytes through exposed PS. For intercellular adhesion molecule-3 on apoptotic cells, CD14 was suggested to be a macrophage receptor (16). Thrombospondin is also known as a bridging protein between unidentified sites on apoptotic cells and CD36 or vitronectin receptor (␣ v ␤ 3 integrin) on phagocytes (17). In addi...

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Section: Discussionsupporting

confidence: 93%

A Multifunctional Shuttling Protein Nucleolin Is a Macrophage Receptor for Apoptotic Cells

Hirano

Miki

Hirai

et al. 2005

Journal of Biological Chemistry

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“…Second, as for telomerase, we show that differentiation of APL cells was accompanied by a downregulation of nucleolin in agreement with recent results obtained in other cell models (Murakami et al, 1991;Otake et al, 2005).…”

Section: Discussionsupporting

confidence: 91%

Immunodetection of human telomerase reverse-transcriptase (hTERT) re-appraised: nucleolin and telomerase cross paths

Dudognon

Nguyen

et al. 2006

Journal of Cell Science

112

111

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The involvement of telomerase in cellular immortalization and senescence has often been assessed by means of telomerase expression at the RNA level and quantification of telomerase activity by the telomeric repeat amplification protocol assay. However, these methods either neglected the existence of various telomerase splice variants, or ignored the nonconventional functions of telomerase independent of its ability to elongate and maintain telomere length. Immunodetection of telomerase is now being recognized as a necessary approach to precisely elucidate its roles in oncogenesis and senescence. A few antibodies directed against the catalytic subunit of the human telomerase (hTERT) are currently used but their specificity is not always demonstrated. A survey of the literature showed inconsistencies and led us to comparatively re-evaluate the most frequently used antibodies. Surprisingly, mass spectrometry, two-dimensional gel analysis and immunofluorescent experiments revealed that the most frequently used hTERT immunoprobe, a mouse monoclonal antibody that was claimed to be directed against an hTERT protein epitope, in fact recognizes nucleolin rather than telomerase. Our findings have interesting implications regarding the biology of nucleolin and telomerase in the context of pathophysiological investigations recently carried out.

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“…First of all, the increase of p27 Kip1 , observed in LAN-5, is probably a general response of neuroblastoma (and other tumor) cells to RA. Furthermore, since IMR-32 cells treated with RA cease to divide but do not dierentiate (Murakami et al, 1991), the accumulation of p27 Kip1 might be required only for the RA-dependent growth arrest, which is necessary (but not sucient) to cellular dierentiation. Thus, the lineage program (when occurring) is dependent upon the regulation of further pathways and is probably related to the cellular type and to the stage of development arrest.…”

Section: Discussionmentioning

confidence: 99%

p27Kip1 accumulation is associated with retinoic-induced neuroblastoma differentiation: evidence of a decreased proteasome-dependent degradation

et al. 2000

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Down Modulation of N-myc, Heat-Shock Protein 70, and Nucleolin during the Differentiation of Human Neuroblastoma Cells1

Cited by 22 publications

References 0 publications

A Multifunctional Shuttling Protein Nucleolin Is a Macrophage Receptor for Apoptotic Cells

A Multifunctional Shuttling Protein Nucleolin Is a Macrophage Receptor for Apoptotic Cells

Immunodetection of human telomerase reverse-transcriptase (hTERT) re-appraised: nucleolin and telomerase cross paths

p27Kip1 accumulation is associated with retinoic-induced neuroblastoma differentiation: evidence of a decreased proteasome-dependent degradation

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