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  • 1
    Language: English
    In: Nature communications, 2016-03-07, Vol.7 (1), p.10764-10764
    Description: The high-mobility group box 1 (HMGB1) protein has a central role in immunological antitumour defense. Here we show that natural killer cell-derived HMGB1 directly eliminates cancer cells by triggering metabolic cell death. HMGB1 allosterically inhibits the tetrameric pyruvate kinase isoform M2, thus blocking glucose-driven aerobic respiration. This results in a rapid metabolic shift forcing cells to rely solely on glycolysis for the maintenance of energy production. Cancer cells can acquire resistance to HMGB1 by increasing glycolysis using the dimeric form of PKM2, and employing glutaminolysis. Consistently, we observe an increase in the expression of a key enzyme of glutaminolysis, malic enzyme 1, in advanced colon cancer. Moreover, pharmaceutical inhibition of glutaminolysis sensitizes tumour cells to HMGB1 providing a basis for a therapeutic strategy for treating cancer.
    Subject(s): Colonic Neoplasms - genetics ; Membrane Proteins - genetics ; Humans ; Thyroid Hormones - genetics ; Colonic Neoplasms - metabolism ; HMGB1 Protein - genetics ; Colonic Neoplasms - physiopathology ; Carrier Proteins - genetics ; Carrier Proteins - metabolism ; Cell Respiration ; Thyroid Hormones - metabolism ; HMGB1 Protein - metabolism ; Cell Death ; Cell Line, Tumor ; Glucose - metabolism ; Glycolysis ; Colonic Neoplasms - enzymology ; Membrane Proteins - metabolism ; Index Medicus
    ISSN: 2041-1723
    E-ISSN: 2041-1723
    Source: Nature Open Access
    Source: PubMed Central
    Source: Directory of Open Access Journals
    Source: © ProQuest LLC All rights reserved〈img src="https://exlibris-pub.s3.amazonaws.com/PQ_Logo.jpg" style="vertical-align:middle;margin-left:7px"〉
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  • 2
    Language: English
    In: International journal of molecular sciences, 2020-02-07, Vol.21 (3), p.1099
    Description: Autophagy is a catabolic process that enables cells to degrade obsolete content and refuel energy depots. In colorectal cancer (CRC) autophagy has been shown to promote tumorigenesis through energy delivery in the condition of uncontrolled proliferation. With this study, we aimed at evaluating whether autophagy sustains CRC cell viability and if it impacts therapy resistance. Initially, a colorectal cancer tissue micro array, containing mucosa ( = 10), adenoma ( = 18) and adenocarcinoma ( = 49) spots, was stained for expression of essential autophagy proteins LC3b, Atg7, p62 and Beclin-1. Subsequently, central autophagy proteins were downregulated in CRC cells using siRNA technology. Viability assays, flow cytometry and immunoblotting were performed and three-dimensional cell culture was utilized to study autophagy in a tissue mimicking environment. In our study we found an upregulation of Atg7 in CRC. Furthermore, we identified Atg7 as crucial factor within the autophagy network for CRC cell viability. Its disruption induced cell death via triggering apoptosis and in combination with conventional chemotherapy it exerted synergistic effects in inducing CRC cell death. Cell death was strictly dependent on nuclear LC3b, since simultaneous knockdown of Atg7 and LC3b completely restored viability. This study unravels a novel cell death preventing function of Atg7 in interaction with LC3b, thereby unmasking a promising therapeutic target in CRC.
    Subject(s): Index Medicus ; apoptosis ; autophagy ; colorectal cancer ; Atg7 ; LC3 ; lc3 ; atg7
    ISSN: 1422-0067
    E-ISSN: 1422-0067
    Source: Academic Search Ultimate
    Source: PubMed Central
    Source: Directory of Open Access Journals
    Source: © ProQuest LLC All rights reserved〈img src="https://exlibris-pub.s3.amazonaws.com/PQ_Logo.jpg" style="vertical-align:middle;margin-left:7px"〉
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  • 3
    Language: English
    In: Cell death & disease, 2016-08-18, Vol.7 (8), p.e2342-e2342
    Description: Colorectal cancer (CRC) is the second most common malignant neoplasia in women and men worldwide. The B-cell lymphoma 2 (Bcl-2) protein family is mainly known for its pivotal role in the regulation of the mitochondrial death pathway. Anti-apoptotic Bcl-2 proteins may provide survival benefits and induce therapy resistance in cancer cells. Among anti-apoptotic Bcl-2 proteins, we found solely Bcl-xL strongly upregulated in human CRC specimens. In order to study protein function in the context of tumor initiation and progression in vivo, we generated a mouse model lacking Bcl-xL in intestinal epithelial cells (Bcl-xL(IEC-KO)). If challenged in an inflammation-driven tumor model, Bcl-xL(IEC-KO) mice showed a significantly reduced tumor burden with lower tumor numbers per animal and decreased tumor sizes. Analysis of cell death events by immunohistochemistry and immunoblotting revealed a striking increase of apoptosis in Bcl-xL-negative tumors. qRT-PCR and immunohistochemistry excluded changes in proliferative capacity and immune cell infiltration as reasons for the reduced tumor load and thereby identify apoptosis as key mechanism. Human CRC tissue was cultured ex vivo and treated with the small molecule compound ABT-737, which inhibits Bcl-xL and Bcl-2. Under ABT-737 treatment, the amount of apoptotic tumor cells significantly increased compared with controls, whereas proliferation levels remained unaltered. In summary, our findings identify Bcl-xL as a driver in colorectal tumorigenesis and cancer progression, making it a valuable target for clinical application.
    Subject(s): Inflammation - pathology ; Apoptosis - drug effects ; Enterocytes - metabolism ; Colorectal Neoplasms - genetics ; Humans ; bcl-X Protein - genetics ; Apoptosis - genetics ; Gene Knockdown Techniques ; Biphenyl Compounds - pharmacology ; Nitrophenols - pharmacology ; Lymphocytes, Tumor-Infiltrating - metabolism ; Cell Culture Techniques ; Gene Expression Regulation, Neoplastic - drug effects ; Oncogenes ; Disease Models, Animal ; Carcinogenesis - genetics ; Up-Regulation - genetics ; Lymphocytes, Tumor-Infiltrating - drug effects ; Organ Specificity ; Sulfonamides - pharmacology ; Piperazines - pharmacology ; Mice, Knockout ; Carcinogenesis - drug effects ; Carcinogenesis - pathology ; Up-Regulation - drug effects ; Phenotype ; Animals ; Enterocytes - drug effects ; Cell Line, Tumor ; Inflammation - genetics ; Cell Proliferation - drug effects ; Mice ; Colorectal Neoplasms - pathology ; bcl-X Protein - metabolism ; Protein expression ; Tumorigenesis ; Colorectal cancer ; Apoptosis ; Index Medicus ; Original
    ISSN: 2041-4889
    E-ISSN: 2041-4889
    Source: Nature Open Access
    Source: PubMed Central
    Source: © ProQuest LLC All rights reserved〈img src="https://exlibris-pub.s3.amazonaws.com/PQ_Logo.jpg" style="vertical-align:middle;margin-left:7px"〉
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  • 4
    Language: English
    In: Hepatology (Baltimore, Md.), 2010-12, Vol.52 (6), p.2023-2033
    Description: The A kinase anchor protein 12 (AKAP12) is a central mediator of protein kinase A and protein kinase C signaling. Although AKAP12 has been described to act as a tumor suppressor and its expression is frequently down‐regulated in several human malignancies, the underlying molecular mechanisms responsible for the AKAP12 reduction are poorly understood. We therefore analyzed the expression of AKAP12 and its genetic and epigenetic regulatory mechanisms in human hepatocarcinogenesis. Based on tissue microarray analyses (n = 388) and western immunoblotting, we observed a significant reduction of AKAP12 in cirrhotic liver (CL), premalignant lesions (DN), and hepatocellular carcinomas (HCCs) compared to histologically normal liver specimens (NL). Analyses of array comparative genomic hybridization data (aCGH) from human HCCs revealed chromosomal losses of AKAP12 in 36% of cases but suggested additional mechanisms underlying the observed reduction of AKAP12 expression in hepatocarcinogenesis. Quantitative methylation analysis by MassARRAY of NL, CL, DN, and HCC tissues, as well as of various tumorigenic and nontumorigenic liver cell lines revealed specific hypermethylation of the AKAP12α promoter but not of the AKAP12β promoter in HCC specimens and in HCC cell lines. Consequently, restoration experiments performed with 5‐aza‐2′deoxycytidine drastically increased AKAP12α mRNA levels in a HCC cell line (AKN1) paralleled by AKAP12α promoter demethylation. As hypermethylation is not observed in CL and DN, we investigated microRNA‐mediated posttranscriptional regulation as an additional mechanism to explain reduced AKAP12 expression. We found that miR‐183 and miR‐186 are up‐regulated in CL and DN and are able to target AKAP12. Conclusion: In addition to genetic alterations, epigenetic mechanisms are responsible for the reduction of the tumor suppressor gene AKAP12 in human hepatocarcinogenesis. (HEPATOLOGY 2010;.)
    Subject(s): Gastroenterology. Liver. Pancreas. Abdomen ; Biological and medical sciences ; Medical sciences ; Liver. Biliary tract. Portal circulation. Exocrine pancreas ; Tumors ; Liver Neoplasms - genetics ; Down-Regulation ; Epigenesis, Genetic ; Humans ; Azacitidine - analogs & derivatives ; MicroRNAs - metabolism ; A Kinase Anchor Proteins - genetics ; Azacitidine - pharmacology ; Promoter Regions, Genetic - physiology ; Carcinoma, Hepatocellular - genetics ; Liver Neoplasms - metabolism ; Cell Cycle Proteins - genetics ; Cell Line, Tumor ; Protein Array Analysis ; Carcinoma, Hepatocellular - metabolism ; Index Medicus
    ISSN: 0270-9139
    E-ISSN: 1527-3350
    Source: Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals
    Source: © ProQuest LLC All rights reserved〈img src="https://exlibris-pub.s3.amazonaws.com/PQ_Logo.jpg" style="vertical-align:middle;margin-left:7px"〉
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  • 5
    Language: English
    In: American journal of medical genetics. Part A, 2016-06, Vol.170 (6), p.1502-1509
    Description: Intellectual disability (ID) with cerebellar ataxia comprises a genetically heterogeneous group of neurodevelopmental disorders. We identified a homozygous frameshift mutation in CWF19L1 (c.467delC; p.(P156Hfs*33)) by a combination of linkage analysis and Whole Exome Sequencing in a consanguineous Turkish family with a 9‐year‐old boy affected by early onset cerebellar ataxia and mild ID. Serial MRI showed mildly progressive cerebellar atrophy. Absent C19L1 protein expression in lymphoblastoid cell lines strongly suggested that c.467delC is a disease‐causing alteration. One further pregnancy of the mother had been terminated at 22 weeks of gestation because of a small cerebellum and agenesis of corpus callosum. The homozygous CWF19L1 variant was also present in the fetus. Postmortem examination of the fetus in addition showed unilateral hexadactyly and vertebral malformations. These features have not been reported and may represent an expansion of the CWF19L1‐related phenotypic spectrum, but could also be due to another, possibly autosomal recessive disorder. The exact function of the evolutionarily highly conserved C19L1 protein is unknown. So far, homozygous or compound heterozygous mutations in CWF19L1 have been identified in two Turkish siblings and a Dutch girl, respectively, affected by cerebellar ataxia and ID. A zebrafish model showed that CWF19L1 loss‐of‐function mutations result in abnormal cerebellar morphology and movement disorders. Our report corroborates that loss‐of‐function mutations in CWF19Ll lead to early onset cerebellar ataxia and (progressive) cerebellar atrophy. © 2016 Wiley Periodicals, Inc.
    Subject(s): developmental delay ; cerebellar hypoplasia ; ataxia ; cerebellar atrophy ; intellectual disability ; CWF19L1 ; Genetic Association Studies ; Humans ; Male ; Developmental Disabilities - genetics ; Brain - abnormalities ; Cerebellum - abnormalities ; Intellectual Disability - genetics ; Exome ; Radiography ; Magnetic Resonance Imaging ; Phenotype ; Comparative Genomic Hybridization ; Pedigree ; Intellectual Disability - diagnosis ; Nervous System Malformations - diagnosis ; Cell Cycle Proteins - genetics ; Consanguinity ; High-Throughput Nucleotide Sequencing ; Polymorphism, Single Nucleotide ; Mutation ; Nervous System Malformations - genetics ; Child ; Developmental Disabilities - diagnosis ; Genetic Linkage ; Index Medicus
    ISSN: 1552-4825
    E-ISSN: 1552-4833
    Source: Alma/SFX Local Collection
    Source: © ProQuest LLC All rights reserved〈img src="https://exlibris-pub.s3.amazonaws.com/PQ_Logo.jpg" style="vertical-align:middle;margin-left:7px"〉
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  • 6
    Language: English
    In: Molecular cancer research, 2007-12-01, Vol.5 (12), p.1232-1240
    Description: Glioblastomas, the most malignant of all brain tumors, are characterized by cellular resistance to apoptosis and a highly invasive growth pattern. These factors contribute to the poor response of glioblastomas to radiochemotherapy and prevent their complete neurosurgical resection. However, the driving force behind the distinct motility of glioma cells is only partly understood. Here, we report that in the absence of cellular stress and proapoptotic stimuli, human glioblastoma cells exhibit a constitutive activation of caspases in vivo and in vitro . The inhibition of caspases by various peptide inhibitors decreases the migration of cells in scrape motility assays and the invasiveness of cells in spheroid assays. Similarly, specific small interfering RNA– or antisense-mediated down-regulation of caspase-3 and caspase-8 results in an inhibition of the migratory potential of glioma cells. The constitutive caspase-dependent motility of glioblastoma cells is independent of CD95 activation and it is not mediated by mitogen-activated protein/extracellular signal-regulated kinase kinase signaling. The basal caspase activity is accompanied by a constant cleavage of the motility-associated gelsolin protein, which may contribute to the caspase-mediated promotion of migration and invasiveness in glioblastoma cells. Our results suggest that the administration of low doses of caspase inhibitors that block glioma cell motility without affecting the execution of apoptotic cell death may be exploited as a novel strategy for the treatment of glioblastomas. (Mol Cancer Res 2007;5(12):1232–40)
    Subject(s): migration ; apoptosis ; brain tumors ; invasion ; gliomas ; caspases ; Brain Neoplasms - enzymology ; Glioblastoma - enzymology ; MAP Kinase Signaling System - physiology ; Gelsolin - metabolism ; Neoplasm Invasiveness ; Humans ; Brain Neoplasms - pathology ; Caspase 3 - metabolism ; Caspase 8 - metabolism ; Enzyme Inhibitors - pharmacology ; fas Receptor - metabolism ; Caspase Inhibitors ; Cell Movement - physiology ; Caspase 8 - genetics ; Glioblastoma - pathology ; Caspase 3 - genetics ; Cell Line, Tumor ; RNA, Small Interfering ; Index Medicus
    ISSN: 1541-7786
    E-ISSN: 1557-3125
    Source: HighWire Press (Free Journals)
    Source: Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals
    Source: © ProQuest LLC All rights reserved〈img src="https://exlibris-pub.s3.amazonaws.com/PQ_Logo.jpg" style="vertical-align:middle;margin-left:7px"〉
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  • 7
    Language: English
    In: EBioMedicine, 2018-06, Vol.32, p.125-133
    Description: A higher capacity to grow under hypoxic conditions can lead to a more aggressive behavior of tumor cells. Determining tumor activity under hypoxia may identify chronic lymphocytic leukemia (CLL) with aggressive clinical course and predict response to chemo-immunotherapy (CIT). A metabolic score was generated by determining pyruvate kinase and lactate dehydrogenase, key enzymes of glycolysis, ex vivo in primary CLL samples under normoxic and hypoxic conditions. This score was further correlated with clinical endpoints and response to CIT in 96 CLL patients. 45 patients were classified as metabolic high risk (HR), 51 as low risk (LR). Treatment-free survival (TFS) was significantly shorter in HR patients (median 394 vs 723 days, p = .021). 15 HR patients and 14 LR patients received CIT after sample acquisition. HR patients had a significantly shorter progression-free survival after treatment compared to LR patients (median 216 days vs not reached, p = .008). Multivariate analysis evaluating age, IGHV, TP53 deletion or mutation and 11q22–23 deletion besides the capacity of tumor cells to grow under severe hypoxic conditions identified the metabolic profile as the strongest independent risk factor for shorter TFS (hazard ratio 2.37, p = .011). The metabolic risk can provide prognostic and predictive information complementary to genetic biomarkers and identify patients who might benefit from alternative treatment approaches. •The activity of distinct glycolytic enzymes can identify CLL patients with resistance to chemo-immunotherapy•The activity of distinct glycolytic enzymes can identify CLL patients who may benefit from specific pathway inhibitors•We provide a tool for the evaluation of specific glycolytic enzymes in primary CLL cells for clinical diagnostics
    Subject(s): LDH ; CLL ; PK M2 ; Metabolism ; High-risk ; Index Medicus
    ISSN: 2352-3964
    E-ISSN: 2352-3964
    Source: PubMed Central
    Source: Directory of Open Access Journals
    Source: © ProQuest LLC All rights reserved〈img src="https://exlibris-pub.s3.amazonaws.com/PQ_Logo.jpg" style="vertical-align:middle;margin-left:7px"〉
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  • 8
    Language: English
    In: Virchows Archiv : an international journal of pathology, 2011-03, Vol.458 (3), p.371-376
    Description: The main cause of death from novel (swine origin) influenza A/H1N1 infection is acute respiratory distress syndrome. Most fatal cases are immunocompromised patients or patients with a severe underlying disease. Here, we report a fatal case of acute interstitial myocarditis associated with novel influenza A/H1N1 infection in an immunocompetent young woman. A previously healthy 18-year-old woman experienced malaise, diarrhea, and fever for several days prior to a sudden collapse at home. Autopsy revealed a predominantly lymphocytic myocarditis in the absence of a significant respiratory tract infection. Infection with novel (swine origin) influenza A/H1N1 was confirmed by PCR analysis of blood as well as myocardial tissue. Influenza-caused diarrhea with consecutive hypokalemia potentially contributed to the fatal outcome of the myocarditis, characterized by ventricular fibrillation. In conclusion, sudden death by myocarditis may be a rare complication of novel influenza A/H1N1 infection in otherwise healthy individuals, even in the absence of significant respiratory tract infection.
    Subject(s): Myocarditis ; Pathology ; Medicine & Public Health ; Swine flu ; H1N1 ; Novel influenza A ; Viral diseases of the respiratory system and ent viral diseases ; Infectious diseases ; Investigative techniques, diagnostic techniques (general aspects) ; Pathology. Cytology. Biochemistry. Spectrometry. Miscellaneous investigative techniques ; Anesthesia. Intensive care medicine. Transfusions. Cell therapy and gene therapy ; Viral diseases ; Biological and medical sciences ; Intensive care medicine ; Medical sciences ; Human viral diseases ; Emergency and intensive care: neonates and children. Prematurity. Sudden death ; Influenza, Human - pathology ; Humans ; DNA, Viral - analysis ; Death, Sudden, Cardiac - etiology ; Myocarditis - virology ; Influenza A Virus, H1N1 Subtype - isolation & purification ; Adolescent ; Death, Sudden, Cardiac - pathology ; Fatal Outcome ; Polymerase Chain Reaction ; Female ; Influenza, Human - virology ; Immunocompetence ; Myocarditis - pathology ; Influenza A Virus, H1N1 Subtype - genetics ; Acute respiratory distress syndrome ; Swine ; Analysis ; Influenza ; Diarrhea ; Youth ; Teenagers ; Cross infection ; Nosocomial infections ; Index Medicus
    ISSN: 0945-6317
    E-ISSN: 1432-2307
    Source: Alma/SFX Local Collection
    Source: © ProQuest LLC All rights reserved〈img src="https://exlibris-pub.s3.amazonaws.com/PQ_Logo.jpg" style="vertical-align:middle;margin-left:7px"〉
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  • 9
    Language: English
    In: Cancer biology & therapy, 2008-12-01, Vol.7 (12), p.1982-1990
    Description: Resistance to apoptosis is one reason for the poor response of malignant brain tumors to therapy. The PPARγ-modulating drug Troglitazone down-regulates the anti-apoptotic FLIP protein and sensitizes glioblastoma cells to apoptosis induced by the death ligand TRAIL. To investigate the molecular basis of an experimental combination therapy for malignant gliomas with TRAIL and Troglitazone, we investigated the Troglitazone-induced signaling cascades and the expression of TRAIL receptors and FLIP in malignant gliomas. Troglitazone down-regulated the FLIP protein through accelerated ubiquitin/proteasome-dependent degradation, which might be mediated by a Troglitazone-induced increase in reactive oxygen species. Moreover, Troglitazone induced the phosphorylation of the MAP kinase ERK1/2 as well as of the BAD protein. Inhibition of either PPARγ or MEK1/2 blocked the Troglitazone-mediated phosphorylation of BAD and further increased the synergistic induction of glioma cell death by TRAIL and Troglitazone. Immunohistochemical analysis demonstrated that FLIP and TRAIL-R2 were significantly higher expressed in anaplastic (WHO grade III) than in diffuse (WHO grade II) gliomas. High FLIP and low TRAIL-R2 expression levels were associated with a poor prognosis of patients. Our findings warrant a further pre-clinical evaluation of an experimental anti-glioma therapy with TRAIL and Troglitazone, potentially in conjunction with a MAP kinase inhibitor.
    Subject(s): Binding ; Proteins ; Landes ; Calcium ; Bioscience ; Biology ; Cell ; Cycle ; Cancer ; Organogenesis ; Cell Line ; Phosphorylation ; Apoptosis - drug effects ; Humans ; Antineoplastic Agents - therapeutic use ; Mitogen-Activated Protein Kinase 1 - drug effects ; Receptors, TNF-Related Apoptosis-Inducing Ligand - metabolism ; Mitogen-Activated Protein Kinase 3 - drug effects ; Thiazolidinediones - therapeutic use ; Chromans - pharmacology ; Chromans - therapeutic use ; Mitogen-Activated Protein Kinase 3 - metabolism ; Glioma - pathology ; bcl-Associated Death Protein - drug effects ; Cell Line, Tumor ; bcl-Associated Death Protein - metabolism ; Antineoplastic Agents - pharmacology ; Receptors, TNF-Related Apoptosis-Inducing Ligand - genetics ; Proteasome Endopeptidase Complex - metabolism ; Thiazolidinediones - pharmacology ; CASP8 and FADD-Like Apoptosis Regulating Protein - metabolism ; Troglitazone ; Mitogen-Activated Protein Kinase 1 - metabolism ; Index Medicus
    ISSN: 1538-4047
    E-ISSN: 1555-8576
    Source: PubMed Central
    Source: Alma/SFX Local Collection
    Source: © ProQuest LLC All rights reserved〈img src="https://exlibris-pub.s3.amazonaws.com/PQ_Logo.jpg" style="vertical-align:middle;margin-left:7px"〉
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  • 10
    Language: English
    In: Apoptosis (London), 2008-03, Vol.13 (3), p.437-447
    Description: The HIPPI (HIP-1 protein interactor) protein is a multifunctional protein that is involved in the regulation of apoptosis. The interaction partners of HIPPI include HIP-1 (Huntingtin-interacting protein-1), Apoptin, Homer1c, Rybp/DEDAF, and BAR (bifunctional apoptosis regulator). In search for other binding partners of HIPPI, we performed a yeast two hybrid screen and identified BLOC1S2 (Biogenesis of lysosome-related organelles complex-1 subunit 2) as a novel HIPPI-interacting protein. In co-immunoprecipitation assays, BLOC1S2 specifically associates with HIPPI, but not with HIP-1. To study the expression of BLOC1S2 on the protein level, we generated a mouse monoclonal antibody specific for BLOC1S2 and a multiple tissue array comprising 70 normal and cancer tissue samples of diverse origin. BLOC1S2 protein is widely expressed in normal tissue as well as in malignant tumors with a tendency towards lower expression levels in certain subtypes of tumors. On the subcellular level, BLOC1S2 is expressed in an organellar-like pattern and co-localizes with mitochondria. Over-expression of BLOC1S2 in the presence or absence of HIPPI does not induce apoptosis. However, BLOC1S2 and HIPPI sensitize NCH89 glioblastoma cells to the pro-apoptotic actions of staurosporine and the death ligand TRAIL by enhancing caspase activation, cytochrome c release, and disruption of the mitochondrial membrane potential. Given its interaction with HIPPI and its pro-apoptotic activity, BLOC1S2 might play an important functional role in cancer and neurodegenerative diseases.
    Subject(s): Biochemistry, general ; Mitochondria ; Biomedicine ; Lysosomes ; Oncology ; Cancer Research ; Huntington’s disease ; Virology ; Cell Biology ; Apoptosis ; Cancer ; Cilia ; Immunohistochemistry ; Apoptosis - drug effects ; Humans ; Caspase 3 - metabolism ; Caspase 8 - metabolism ; Molecular Sequence Data ; Male ; Membrane Potential, Mitochondrial - drug effects ; Tissue Distribution ; Adult ; Female ; Amino Acid Sequence ; Proteins - physiology ; Cytochromes c - secretion ; Mitochondria - metabolism ; Adaptor Proteins, Signal Transducing - physiology ; Sequence Alignment ; Animals ; TNF-Related Apoptosis-Inducing Ligand - physiology ; Glioblastoma - pathology ; Cell Line, Tumor ; Protein Binding ; HeLa Cells ; Neoplasms - pathology ; Staurosporine - pharmacology ; Glioblastoma multiforme ; Index Medicus
    ISSN: 1360-8185
    E-ISSN: 1573-675X
    Source: Alma/SFX Local Collection
    Source: © ProQuest LLC All rights reserved〈img src="https://exlibris-pub.s3.amazonaws.com/PQ_Logo.jpg" style="vertical-align:middle;margin-left:7px"〉
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