Literature DB >> 7493633

Cell type- and differentiation stage-dependent expression of PML domains in rat, detected by monoclonal antibody HIS55.

Y W Lam1, W Ammerlaan, W S O, F Kroese, D Opstelten.   

Abstract

Using mouse monoclonal antibody (mAb) HIS55, we identified a nuclear antigen (ag) that exhibited a staining pattern of discrete foci. Such foci could be detected in cells of many mammalian species. These nuclear foci were not associated with nuclear membrane, nucleoli, or mitotic chromosomes. In isolated rat liver nuclei, HeLa cells, and normal human and rat lymph nodes, staining of HIS55 colocalized with that of 5E10. 5E10 recognizes PML nuclear domains, multimolecular complexes of unknown function containing the product of PML gene and at least two other components. HIS55 foci were expressed widely in many tissues but the expression level varied in a cell type-specific manner, with the number of HIS55 nuclear foci ranging from 0 (as in neurons) to over 100 (as in megakaryocytes) and the size ranging from fine (as in cortical thymocytes) to very large (as in urethra epithelium). HIS55 ag expression level also varied among cells of the same lineage, as observed in embryonic development of rat and in the hemopoietic system of adult rat. The expression level of HIS55 foci roughly correlated with the overall rate of protein synthesis of cells, supporting a role of PML domains as transcription regulatory units. The expression of HIS55 foci, however, did not correlate with the growth index of cell populations. Our observations on normal tissues agreed with the hypothesis that PML domain expression is regulated by external, possibly site-dependent factors. We further supported this by demonstrating that PML domains in rat ventral prostate epithelia were upregulated upon castration.

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Year:  1995        PMID: 7493633     DOI: 10.1006/excr.1995.1384

Source DB:  PubMed          Journal:  Exp Cell Res        ISSN: 0014-4827            Impact factor:   3.905


  5 in total

1.  Heterogeneous nuclear expression of the promyelocytic leukemia (PML) protein in normal and neoplastic human tissues.

Authors:  M Gambacorta; L Flenghi; M Fagioli; S Pileri; L Leoncini; B Bigerna; R Pacini; L N Tanci; L Pasqualucci; S Ascani; A Mencarelli; A Liso; P G Pelicci; B Falini
Journal:  Am J Pathol       Date:  1996-12       Impact factor: 4.307

2.  Role of promyelocytic leukemia (PML) sumolation in nuclear body formation, 11S proteasome recruitment, and As2O3-induced PML or PML/retinoic acid receptor alpha degradation.

Authors:  V Lallemand-Breitenbach; J Zhu; F Puvion; M Koken; N Honoré; A Doubeikovsky; E Duprez; P P Pandolfi; E Puvion; P Freemont; H de Thé
Journal:  J Exp Med       Date:  2001-06-18       Impact factor: 14.307

3.  PML depletion disrupts normal mammary gland development and skews the composition of the mammary luminal cell progenitor pool.

Authors:  Wenjing Li; Brian J Ferguson; Walid T Khaled; Maxine Tevendale; John Stingl; Valeria Poli; Tina Rich; Paolo Salomoni; Christine J Watson
Journal:  Proc Natl Acad Sci U S A       Date:  2009-03-04       Impact factor: 11.205

Review 4.  PML in the Brain: From Development to Degeneration.

Authors:  Erica Korb; Steven Finkbeiner
Journal:  Front Oncol       Date:  2013-09-17       Impact factor: 6.244

5.  Regulation of Neuronal Protein Trafficking and Translocation by SUMOylation.

Authors:  Anja Berndt; Kevin A Wilkinson; Jeremy M Henley
Journal:  Biomolecules       Date:  2012-05-14
  5 in total

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