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Berlin Brandenburg

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  • 1
    Language: English
    In: Journal of cellular biochemistry, 15 February 2005, Vol.94(3), pp.611-26
    Description: Members of the Bcl-2 family of proteins play important roles in the regulation of cell death by apoptosis. The yeast Two-Hybrid system was utilized to identify a protein that interacts with the anti-apoptotic protein Bcl-2, designated BMRP. This protein corresponds to a previously known mitochondrial ribosomal protein (MRPL41). Binding experiments confirmed the interaction of BMRP to Bcl-2 in mammalian cells. Subcellular fractionation by differential centrifugation studies showed that both Bcl-2 and BMRP are localized to the same fractions (fractions that are rich in mitochondria). Northern blot analysis revealed a major bmrp mRNA band of approximately 0.8 kb in several human tissues. Additionally, a larger 2.2 kb mRNA species was also observed in some tissues. Western blot analysis showed that endogenous BMRP runs as a band of 16-17 kDa in SDS-PAGE. Overexpression of BMRP induced cell death in primary embryonic fibroblasts and NIH/3T3 cells. Transfection of BMRP showed similar effects to those observed by overexpression of the pro-apoptotic proteins Bax or Bad. BMRP-stimulated cell death was counteracted by co-expression of Bcl-2. The baculoviral caspase inhibitor p35 also protected cells from BMRP-induced cell death. These findings suggest that BMRP is a mitochondrial ribosomal protein involved in the regulation of cell death by apoptosis, probably affecting pathways mediated by Bcl-2 and caspases.
    Keywords: Apoptosis -- Physiology ; Carrier Proteins -- Physiology ; Proto-Oncogene Proteins C-Bcl-2 -- Metabolism ; Ribosomal Proteins -- Physiology
    ISSN: 0730-2312
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  • 2
    Language: English
    In: Cancer Research, 07/15/2016, Vol.76(14 Supplement), pp.3259-3259
    Description: Angiopoeitin-2 (Ang2) is released from endothelial cells only in response to stimulus (e.g. wound healing, tumor growth) and facilitates blood vessel sprouting and inhibits pericyte-endothelial cell interaction via Tie2 signaling. Combination of an anti-Ang2 antibody and aflibercept,...
    Keywords: Cell Survival ; Vascular Endothelial Growth Factor ; Ovarian Cancer ; Retina ; Immunotherapy ; Animal Models ; Angiogenesis ; Pericytes ; Wound Healing ; Tumors ; Clinical Trials ; Metastases ; Endothelial Cells ; Antibodies ; Blood Vessels ; Immunoglobulin G ; Cell Interactions ; Xenografts ; Products;
    ISSN: 0008-5472
    E-ISSN: 1538-7445
    Source: CrossRef
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  • 3
    Language: English
    In: Journal of Cellular Biochemistry, 15 February 2005, Vol.94(3), pp.611-626
    Description: Members of the Bcl‐2 family of proteins play important roles in the regulation of cell death by apoptosis. The yeast Two‐Hybrid system was utilized to identify a protein that interacts with the anti‐apoptotic protein Bcl‐2, designated BMRP. This protein corresponds to a previously known mitochondrial ribosomal protein (MRPL41). Binding experiments confirmed the interaction of BMRP to Bcl‐2 in mammalian cells. Subcellular fractionation by differential centrifugation studies showed that both Bcl‐2 and BMRP are localized to the same fractions (fractions that are rich in mitochondria). Northern blot analysis revealed a major mRNA band of approximately 0.8 kb in several human tissues. Additionally, a larger 2.2 kb mRNA species was also observed in some tissues. Western blot analysis showed that endogenous BMRP runs as a band of 16–17 kDa in SDS–PAGE. Overexpression of BMRP induced cell death in primary embryonic fibroblasts and NIH/3T3 cells. Transfection of BMRP showed similar effects to those observed by overexpression of the pro‐apoptotic proteins Bax or Bad. BMRP‐stimulated cell death was counteracted by co‐expression of Bcl‐2. The baculoviral caspase inhibitor p35 also protected cells from BMRP‐induced cell death. These findings suggest that BMRP is a mitochondrial ribosomal protein involved in the regulation of cell death by apoptosis, probably affecting pathways mediated by Bcl‐2 and caspases. © 2004 Wiley‐Liss, Inc.
    Keywords: Bcl‐2 ; Apoptosis ; Bmrp ; Mitochondria ; Ribosome ; Yeast Two‐Hybrid Screen
    ISSN: 0730-2312
    E-ISSN: 1097-4644
    Source: John Wiley & Sons, Inc.
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  • 4
    Language: English
    In: Cancer Research, 07/01/2017, Vol.77(13 Supplement), pp.1823-1823
    ISSN: 0008-5472
    E-ISSN: 1538-7445
    Source: CrossRef
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  • 5
  • 6
    Language: English
    In: Liver international : official journal of the International Association for the Study of the Liver, 22 August 2019
    Description: Hepatocellular carcinoma (HCC) is one of the most common causes of cancer-related deaths globally due, in part, to the majority of patients being diagnosed with intermediate or advanced stage disease. Our increased understanding of the heterogeneous molecular pathogenesis of HCC has led to significant developments in novel targeted therapies. Despite these advances, there remains a high unmet need for new treatment options. HCC is a complex disease with multiple pathogenic mechanisms caused by a variety of risk factors, making it difficult to characterize with a single biomarker. In fact, numerous biomarkers have been studied in HCC, but alpha-fetoprotein (AFP) remains the most widely used and accepted serum marker since its discovery over 60 years ago. This review summarizes the most relevant studies associated with the regulation of AFP at the gene and protein levels; the pathophysiology of AFP as a pro-proliferative protein; and the correlation of AFP with molecular HCC subclasses, the vascular endothelial growth factor pathway, and angiogenesis. Also described are the historical and current uses of AFP for screening and surveillance, diagnosis, its utility as a prognostic and predictive biomarker, and its role as a tumor antigen in HCC. Taken together, these data demonstrate the relevance of AFP for patients with HCC and identify several remaining questions that will benefit from future research. This article is protected by copyright. All rights reserved.
    Keywords: Alpha-Fetoprotein ; Biomarkers ; Hepatocellular Carcinoma
    ISSN: 14783223
    E-ISSN: 1478-3231
    Source: MEDLINE/PubMed (U.S. National Library of Medicine)
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