985 resultados para Tartarugalzinho - AP
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In Thai.
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Mode of access: Internet.
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Haṛajabanutʻiwn -- Epiphaniou Peri metrōn kai stathmōn = Epipʻanu Haghags chʻaputsʻ ew kshṛotsʻ -- Anania Shirakunoy hamaroghi Haghags kshṛotsʻn ew chʻapʻutsʻ -- Movsisi Khorenatsʻwoy Haghags asparisakan chʻapʻu -- Haghags ěntʻatsʻitsʻ aregakan ew hamaroy chʻapʻutsʻ ěst krkin ōrinakatsʻ Shirakatsʻwoyn -- Batsʻatrutʻiwn chʻapʻuts ew kshṛotsʻ nakhneatsʻ -- Ard i chʻapʻkʻ ew kshiṛkʻ Gaghghiatsʻwotsʻ -- Aṛandzin dasakargutʻiwn kshṛotsʻ ew chʻapʻutsʻ handerdz tachkakan baṛiwkʻ.
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Appeared in fourteen parts, 1836-1842.
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Bibliography: p. [ix]-xii.
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Italian or Latin.
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[It's Final: "M" First in Nation"]
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Chemical abstracts
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Includes index.
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Trägerband: 'E. lin. 4. N. 5'; Vorbesitzer: Karmeliterkloster Frankfurt am Main
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Vorbesitzer: Dominikanerkloster Frankfurt am Main
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The AP-2 transcription factor family is presumed to play an important role in the regulation of the keratinocyte squamous differentiation program; however, limited functional data are available to support this. In the present study, the activity and regulation of AP-2 were examined in differentiating human epidermal keratinocytes. We report that (1) AP-2 transcriptional activity decreases in differentiated keratinocytes but remains unchanged in differentiation-insensitive squamous cell carcinoma cell lines, (2) diminished AP-2 transcriptional activity is associated with a loss of specific DNA-bound AP-2 complexes, and (3) there is an increase in the ability of cytoplasmic extracts, derived from differentiated keratinocytes, to phosphorylate AP-2alpha and AP-2beta when cells differentiate. In contrast, extracts from differentiation-insensitive squamous cell carcinoma cells are unable to phosphorylate AP-2 proteins. Finally, the phosphorylation of recombinant AP-2alpha by cytosolic extracts from differentiated keratinocytes is associated with decreased AP-2 DNA-binding activity. Combined, these data indicate that AP-2 trans-activation and DNA-binding activity decrease as keratinocytes differentiate, and that this decreased activity is associated with an enhanced ability to phosphorylate AP-2alpha and beta.
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Fetal epithelium retains the ability to re-epithelialize a wound in organotypic culture in a manner not dependent on the presence of underlying dermal substrata. This capacity is lost late in the third trimester of gestation or after embryonic day 17 (E-17) in the rat such that embryonic day 19 (E-19) wounds do not re-epithelialize. Moreover, wounds created in E-17 fetuses in utero heal in a regenerative, scar-free fashion. To investigate the molecular events regulating re-epithelialization in fetal skin, the wound-induced expression profile and tissue localization of activator protein 1 (AP-1) transcription factors c-Fos and c-Jun was characterised in E-17 and E-19 skin using organotypic fetal cultures. The involvement of mitogen-activated protein kinase (MAPK) signaling in mediating wound-induced transcription factor expression and wound re-epithelialization was assessed, with the effect of wounding on the expression of keratinocyte differentiation markers determined. Our results show that expression of AP-1 transcription factors was induced immediately by wounding and localized predominantly to the epidermis in E-17 and E-19 skin. c-fos and c-jun induction was transient in E-17 skin with MAPK-dependent c-fos expression necessary for the re-epithelialization of an excisional wound in organotypic culture. In E-19 skin, AP-11 expression persisted beyond 12 h post-wounding, and marked upregulation of the keratinocyte differentiation markers keratin 10 and loricrin was observed. No such changes in the expression of keratin 10 or loricrin occurred in E-17 skin. These findings indicate that re-epithelialization in fetal skin is regulated by wound-induced AP-1 transcription factor expression via MAPK and the differentiation status of keratinocytes.