دورية أكاديمية
أعرض في EDS

Caspase-3-resistant uncleavable form of acidic leucine-rich nuclear phosphoprotein 32B potentiates leukemic cell apoptosis.

التفاصيل البيبلوغرافية
العنوان: Caspase-3-resistant uncleavable form of acidic leucine-rich nuclear phosphoprotein 32B potentiates leukemic cell apoptosis.
المؤلفون: Li CX; Key Laboratory of Cell Differentiation and Apoptosis of Chinese Ministry of Education, Center of Molecular Medicine, Rui‑Jin Hospital, Shanghai Jiao‑Tong University School of Medicine, Shanghai 200025, P.R. China., Shen SM; Key Laboratory of Cell Differentiation and Apoptosis of Chinese Ministry of Education, Center of Molecular Medicine, Rui‑Jin Hospital, Shanghai Jiao‑Tong University School of Medicine, Shanghai 200025, P.R. China., Wang LS; Key Laboratory of Cell Differentiation and Apoptosis of Chinese Ministry of Education, Center of Molecular Medicine, Rui‑Jin Hospital, Shanghai Jiao‑Tong University School of Medicine, Shanghai 200025, P.R. China., Yu Y; Key Laboratory of Cell Differentiation and Apoptosis of Chinese Ministry of Education, Center of Molecular Medicine, Rui‑Jin Hospital, Shanghai Jiao‑Tong University School of Medicine, Shanghai 200025, P.R. China.
المصدر: Molecular medicine reports [Mol Med Rep] 2015 Apr; Vol. 11 (4), pp. 2813-8. Date of Electronic Publication: 2014 Dec 03.
نوع المنشور: Journal Article; Research Support, Non-U.S. Gov't
اللغة: English
بيانات الدورية: Publisher: D. A. Spandidos Country of Publication: Greece NLM ID: 101475259 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1791-3004 (Electronic) Linking ISSN: 17912997 NLM ISO Abbreviation: Mol Med Rep Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Athens, Greece : D. A. Spandidos
مواضيع طبية MeSH: Apoptosis*/genetics , Protein Interaction Domains and Motifs*/genetics, Caspase 3/*metabolism , Leukemia/*metabolism , Nuclear Proteins/*metabolism, Cell Line, Tumor ; Gene Expression ; Humans ; Leucine ; Leukemia/genetics ; Mutation ; Nuclear Proteins/chemistry ; Nuclear Proteins/genetics ; Protein Kinase C-delta/metabolism ; Proteolysis ; Proto-Oncogene Proteins c-bcl-2/metabolism
مستخلص: One member of the highly conserved acidic leucine‑rich nuclear phosphoprotein 32 kDa (ANP32) family of proteins, ANP32B, is critical for normal development, as demonstrated by a study in ANP32B‑deficient mice. Another study indicated that ANP32B was a direct substrate of caspase‑3, and was primarily cleaved at the sequence Ala‑Glu‑Val‑Asp, following Asp‑163. To investigate the significance of ANP32B cleavage in apoptosis, leukemic U937T cell lines were generated with inducible expression of ANP32B(wild type; WT), the uncleavable mutant ANP32B(D163A) and the N‑terminal fragment ANP32B(1‑163). Notably, overexpression of ANP32B(WT) and ANP32B(D163A) moderately increased and significantly enhanced etoposide‑induced apoptosis and caspase‑3 activation, whereas expression of ANP32B(1‑163) produced no effect. Two hypotheses have been generated, which may explain the distinct roles of the various ANP32B forms: i) ANP32B(WT) and ANP32B(D163A) localize in the nucleus while ANP32B(1‑163) mainly resides in the cytosol; or ii) ANP32B(WT) and ANP32B(D163A), but not ANP32B(1‑163), inhibit the expression of the anti‑apoptotic protein Bcl‑2. Based on these observations, caspase‑3‑resistant uncleavable ANP32B(D163A) is hypothesized to be pro‑apoptotic in leukemic cells.
المشرفين على المادة: 0 (ANP32B protein, human)
0 (Nuclear Proteins)
0 (Proto-Oncogene Proteins c-bcl-2)
EC 2.7.11.13 (Protein Kinase C-delta)
EC 3.4.22.- (Caspase 3)
GMW67QNF9C (Leucine)
تواريخ الأحداث: Date Created: 20141209 Date Completed: 20150928 Latest Revision: 20150121
رمز التحديث: 20240628
DOI: 10.3892/mmr.2014.3035
PMID: 25483709
قاعدة البيانات: MEDLINE
الوصف
تدمد:1791-3004
DOI:10.3892/mmr.2014.3035