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Titolo:
Alteration of argyrophilic nucleolar organizer region associated (Ag-NOR) proteins in apoptosis-induced human salivary gland cells and human oral squamous carcinoma cells
Autore:
Morimoto, Y; Kito, S; Ohba, T; Morimoto, H; Okamura, H; Haneji, T;
Indirizzi:
Univ Tokushima, Sch Dent, Dept Histol & Oral Histol, Tokushima 7708504, Japan Univ Tokushima Tokushima Japan 7708504 Histol, Tokushima 7708504, Japan Kyushu Dent Coll, Dept Dent Radiol, Kitakyushu, Fukuoka 803, Japan Kyushu Dent Coll Kitakyushu Fukuoka Japan 803 akyushu, Fukuoka 803, Japan Kyushu Dent Coll, Dept Oral Anat 1, Kitakyushu, Fukuoka 803, Japan Kyushu Dent Coll Kitakyushu Fukuoka Japan 803 akyushu, Fukuoka 803, Japan
Titolo Testata:
JOURNAL OF ORAL PATHOLOGY & MEDICINE
fascicolo: 4, volume: 30, anno: 2001,
pagine: 193 - 199
SICI:
0904-2512(200104)30:4<193:AOANOR>2.0.ZU;2-G
Fonte:
ISI
Lingua:
ENG
Soggetto:
PHOSPHATASE INHIBITORS; WESTERN BLOTS; OKADAIC ACID; CALYCULIN-A; GRANZYME-A; SILVER; CLEAVAGE; BINDING; PHOSPHORYLATION; IDENTIFICATION;
Keywords:
Ag-NOR proteins; apoptosis; HSG cells; SCC-25 cells;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
31
Recensione:
Indirizzi per estratti:
Indirizzo: Haneji, T Univ Tokushima, Sch Dent, Dept Histol & Oral Histol, 18-15,3 Kuramoto Cho,Tokushima 7708504, Japan Univ Tokushima 18-15,3 Kuramoto Cho Tokushima Japan 7708504 pan
Citazione:
Y. Morimoto et al., "Alteration of argyrophilic nucleolar organizer region associated (Ag-NOR) proteins in apoptosis-induced human salivary gland cells and human oral squamous carcinoma cells", J ORAL PATH, 30(4), 2001, pp. 193-199

Abstract

The level of argyrophilic nucleolar organizer regions (AgNORs) and AgNOR-associated proteins (Ag-NOR proteins) varies with cell activity, including ribosomal biogenesis occurring in proliferating cells. Proteins associated with some AgNORs are detected by a specific silver staining. To investigate a possible relationship between apoptosis and the AgNORs or Ag-NOR proteins, we examined the changes of AgNORs and Ag-NOR proteins during apoptosis ina human salivary gland cell line, HSG cells, and a human oral squamous carcinoma cell line, SCC-25 cells. Apoptosis was induced by treatment of HSG and SCC-25 cells with okadaic acid. Proteins prepared from HSG and SCC-25 cells treated with varying concentrations of okadaic acid (OA) were subjectedto sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) followed by transferring to transfer membranes and staining for Ag-NOR proteins by modified Western blot analysis. Four major bands (110 kDa, 43 kDa, 39kDa, and 37 hDa) were detected in the proteins obtained from the control cells. The level of the 110-kDa protein decreased in the proteins prepared from OA-induced apoptotic cells; however, the reaction intensity of the otherthree bands was changed in apoptotic cells. An additional band of an 80-kDa Ag-NOR protein appeared and increased in the apoptotic cells. Cellular fractionation of HSG cells and SCC-25 cells was done with or without apoptotic induction. An 80-kDa Ag-NOR protein was detected in the nuclear fraction prepared from the apoptotic cells, while the 110-kDa protein decreased in the nuclear fraction of these cells. The 110-kDa Ag-NOR protein may be nucleolin (C23) as deduced from its AgNOR staining features, including molecularweight. The 80-kDa protein may be the cleavage product of the 110-kDa protein, in the cell-free apoptotic system, in which intact nuclei of HSG cellswere incubated with the cytosol fraction of apoptotic HSG and SCC-25 cells, the 80-kDa Ag-NOR protein was detected in nuclei incubated with the cytosol fraction of apoptotic cells, while the level of the 110-kDa protein decreased. The changes of Ag-NOR proteins in nuclei prepared from SCC-25 cells incubated with cytosol fractions prepared from HSG and SCC-25 cells were identical to those of the HSG cells. The alternation of AgNORs in apoptosis-induced HSG cells was also examined using double staining with Hoechst 33342and silver nitrate. Hoechst staining revealed typical apoptotic nuclei, which exhibited highly fluorescent condensed chromatin in OA-treated HSG cells. Silver grains representing AgNORs were not detected in the cells undergoing apoptosis. The dual-imposition view confirmed that AgNORs, which are visible as dots in nucleoli in the control cells, disappeared from the apoptotic nuclei of HSG cells. Our results indicate that the 110-kDa nucleolar Ag-NOR protein is associated with apoptosis and is cleaved during apoptosis.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/12/20 alle ore 01:15:24