Редактирование: ID1

DNA-binding protein inhibitor ID-1 (Class B basic helix-loop-helix protein 24) (bHLHb24) (Inhibitor of DNA binding 1) (Inhibitor of differentiation 1) [BHLHB24] [ID]

==Publications==

{{medline-entry
|title=Commentary on Some Recent Theses Relevant to Combating Aging: April 2019.
|pubmed-url=https://pubmed.ncbi.nlm.nih.gov/30957657
|abstract=Theses reviewed in this issue include "Alpha-Synuclein Oligomers: Cellular Mechanisms and Aspects of Antibody Treatment," "Cx3cr1/cx3cl1 Axis Drives the Migration and Maturation of Oligodendroglia in the Central Nervous System," "Genome-Wide Expression Profiling of Human Circulating Monocytes and Macrophages Identifies Diagnostic and Prognostic Signatures for Cancer Outcomes," "Lysosomal Oxidation of Low Density Lipoproteins," and "The Senescence-Associated Secretory Phenotype Induced by [[ID1]]-p16 Axis Contributes to Sorafenib Resistance in Hepatocellular Carcinoma."

|keywords=* aging
* dissertations
* theses
|full-text-url=https://sci-hub.do/10.1089/rej.2019.2201
}}
{{medline-entry
|title=ER stress and distinct outputs of the IRE1α RNase control proliferation and senescence in response to oncogenic Ras.
|pubmed-url=https://pubmed.ncbi.nlm.nih.gov/28847931
|abstract=Oncogenic Ras causes proliferation followed by premature senescence in primary cells, an initial barrier to tumor development. The role of endoplasmic reticulum (ER) stress and the unfolded protein response (UPR) in regulating these two cellular outcomes is poorly understood. During ER stress, the inositol requiring enzyme 1α (IRE1α) endoribonuclease (RNase), a key mediator of the UPR, cleaves [i]Xbp1[/i] mRNA to generate a potent transcription factor adaptive toward ER stress. However, IRE1α also promotes cleavage and degradation of ER-localized mRNAs essential for cell death. Here, we show that oncogenic HRas induces ER stress and activation of IRE1α. Reduction of ER stress or [i]Xbp1[/i] splicing using pharmacological, genetic, and RNAi approaches demonstrates that this adaptive response is critical for HRas-induced proliferation. Paradoxically, reduced ER stress or [i]Xbp1[/i] splicing promotes growth arrest and premature senescence through hyperactivation of the IRE1α RNase. Microarray analysis of IRE1α- and [[XBP1]]-depleted cells, validation using RNA cleavage assays, and 5' RACE identified the prooncogenic basic helix-loop-helix transcription factor [[ID1]] as an IRE1α RNase target. Further, we demonstrate that [i]Id1[/i] degradation by IRE1α is essential for HRas-induced premature senescence. Together, our studies point to IRE1α as an important node for posttranscriptional regulation of the early Ras phenotype that is dependent on both oncogenic signaling as well as stress signals imparted by the tumor microenvironment and could be an important mechanism driving escape from Ras-induced senescence.
|mesh-terms=* Animals
* Apoptosis
* Cell Proliferation
* Endoplasmic Reticulum
* Endoplasmic Reticulum Stress
* Endoribonucleases
* Inositol
* Keratinocytes
* Mice
* Mice, Inbred C57BL
* Primary Cell Culture
* Protein-Serine-Threonine Kinases
* RNA Splicing
* RNA Stability
* RNA, Messenger
* Ribonucleases
* Signal Transduction
* Transcription Factors
* Unfolded Protein Response
* X-Box Binding Protein 1
* ras Proteins
|keywords=* ER stress
* ID1
* IRE1α
* Ras
* oncogene-induced senescence
|full-text-url=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5603998
}}
{{medline-entry
|title=Expansion of adipose tissue-derived stromal cells at "physiologic" hypoxia attenuates replicative senescence.
|pubmed-url=https://pubmed.ncbi.nlm.nih.gov/28589682
|abstract=Multipotent mesenchymal stromal cells are considered as a perspective tool in cell therapy and regenerative medicine. Unfortunately, autologous cell therapy does not always provide positive outcomes in elder donors, perhaps as a result of the alterations of stem cell compartments. The mechanisms of stem and progenitor cell senescence and the factors engaged are investigated intensively. In present paper, we elucidated the effects of tissue-related O  on morphology, functions, and transcriptomic profile of adipose tissue-derived stromal cells (ASCs) in replicative senescence in vitro model. Replicatively senescent ASCs at ambient (20%) O  (12-21 passages) demonstrated an increased average cell size, granularity, reactive oxygen species level, including anion superoxide, lysosomal compartment activity, and IL-6 production. Decreased ASC viability and proliferation, as well as the change of more than 10 senescence-associated gene expression were detected (IGF1, [[CDKN1C]], [[ID1]], [[CCND1]], etc). Long-term ASC expansion at low O  (5%) revoked in part the replicative senescence-associated alterations.
|mesh-terms=* Adipose Tissue
* Cell Culture Techniques
* Cell Hypoxia
* Cells, Cultured
* Cellular Senescence
* Female
* Gene Expression Regulation
* Humans
* Male
* Mesenchymal Stem Cells
|keywords=* ASCs
* ROS
* functional state of organelles
* hypoxia
* paracrine activity
* senescence
* senescence-associated genes
|full-text-url=https://sci-hub.do/10.1002/cbf.3267
}}
{{medline-entry
|title=Endoglin overexpression mediates gastric cancer peritoneal dissemination by inducing mesothelial cell senescence.
|pubmed-url=https://pubmed.ncbi.nlm.nih.gov/27067789
|abstract=Peritoneal dissemination (PD), which is highly frequent in gastric cancer ([[GC]]) patients, is the main cause of death in advanced [[GC]]. Senescence of human peritoneal mesothelial cells (HPMC) may contribute to [[GC]] peritoneal dissemination ([[GC]]PD). In this study of 126 patients, we investigated the association between Endoglin expression in [[GC]] peritoneum and the clinicopathological features. The prognosis of patients was evaluated according to Endoglin and [[ID1]] expression. In vitro, [[GC]] cell ([[GC]]C)-HPMC coculture was established. Endoglin and [[ID1]] expression was evaluated by Western blot. Cell cycle and HPMC senescence were analyzed after harvesting HPMC from the coculture. [[GC]]C adhesion and invasion to HPMC were also assayed. Our results showed that positive staining of Endoglin (38%) was associated with a higher TNM stage and higher incidence of [[GC]]PD (both P < .05). Kaplan-Meier analysis showed that the patients who were Endoglin positive had a shorter survival time compared with Endoglin-negative patients (P = .02). Using the HPMC and [[GC]]C adherence and invasion assay, we demonstrated that transforming growth factor beta 1 (TGF-β)1-induced HPMC senescence was attenuated by silencing the Endoglin expression, which also prevented [[GC]]C attachment and invasion. Our study indicated a positive correlation between Endoglin overexpression and [[GC]]PD. Up-regulated Endoglin expression induced HPMC senescence via TGF-β1 pathway. The findings suggest that Endoglin-induced HPMC senescence may contribute to peritoneal dissemination of [[GC]]Cs. 
|mesh-terms=* Antigens, CD
* Blotting, Western
* Cell Line, Tumor
* Cells, Cultured
* Cellular Senescence
* Coculture Techniques
* Endoglin
* Epithelium
* Fluorescent Antibody Technique
* Humans
* Immunohistochemistry
* Kaplan-Meier Estimate
* Microscopy, Confocal
* Neoplasm Invasiveness
* Peritoneal Neoplasms
* Prognosis
* RNA, Small Interfering
* Receptors, Cell Surface
* Stomach Neoplasms
* Transfection
|keywords=* Endoglin
* Mesothelial cell
* Peritoneal dissemination
* Senescence
* Stomach cancer
* TGF-β receptor
|full-text-url=https://sci-hub.do/10.1016/j.humpath.2015.12.023
}}