Редактирование: CASP7

Caspase-7 precursor (EC 3.4.22.60) (CASP-7) (Apoptotic protease Mch-3) (CMH-1) (ICE-like apoptotic protease 3) (ICE-LAP3) [Contains: Caspase-7 subunit p20; Caspase-7 subunit p11] [MCH3]

==Publications==

{{medline-entry
|title=Global Characteristics of CSIG-Associated Gene Expression Changes in Human HEK293 Cells and the Implications for CSIG Regulating Cell Proliferation and Senescence.
|pubmed-url=https://pubmed.ncbi.nlm.nih.gov/26029164
|abstract=Cellular senescence-inhibited gene (CSIG), also named as ribosomal_L1 domain-containing 1 (RSL1D1), is implicated in various processes including cell cycle regulation, cellular senescence, apoptosis, and tumor metastasis. However, little is known about the regulatory mechanism underlying its functions. To screen important targets and signaling pathways modulated by CSIG, we compared the gene expression profiles in CSIG-silencing and control HEK293 cells using Affymetrix microarray Human Genome U133 Plus 2.0 GeneChips. A total of 590 genes displayed statistically significant expression changes, with 279 genes up-regulated and 311 down-regulated, respectively. These genes are involved in a broad array of biological processes, mainly in transcriptional regulation, cell cycle, signal transduction, oxidation reduction, development, and cell adhesion. The differential expression of genes such as [[ZNF616]], [[KPNA5]], and [[MAP3K3]] was further validated by real-time PCR and western blot analysis. Furthermore, we investigated the correlated expression patterns of Cdc14B, [[ESCO1]], [[KPNA5]], [[MAP3K3]], and CSIG during cell cycle and senescence progression, which imply the important pathways CSIG regulating cell cycle and senescence. The mechanism study showed that CSIG modulated the mRNA half-life of Cdc14B, [[CASP7]], and [[CREBL2]]. This study shows that expression profiling can be used to identify genes that are transcriptionally or post-transcriptionally modified following CSIG knockdown and to reveal the molecular mechanism of cell proliferation and senescence regulated by CSIG. 

|keywords=* CSIG/RSL1D1
* cell cycle
* gene expression
* microarray
* senescence
|full-text-url=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4432801
}}
{{medline-entry
|title=Dual role of the caspase enzymes in satellite cells from aged and young subjects.
|pubmed-url=https://pubmed.ncbi.nlm.nih.gov/24336075
|abstract=Satellite cell (SC) proliferation and differentiation have critical roles in skeletal muscle recovery after injury and adaptation in response to hypertrophic stimuli. Normal ageing hinders SC proliferation and differentiation, and is associated with increased expression of a number of pro-apoptotic factors in skeletal muscle. In light of previous studies that have demonstrated age-related altered expression of genes involved in SC antioxidant and repair activity, this investigation was aimed at evaluating the incidence of apoptotic features in human SCs. Primary cells were obtained from vastus lateralis of nine young (27.3±2.0 years old) and nine old (71.1±1.8 years old) subjects, and cultured in complete medium for analyses at 4, 24, 48, and 72 h. Apoptosis was assessed using AnnexinV/propidium iodide staining, the terminal deoxynucleotidyl transferase dUTP nick-end labelling technique, RT-PCR, DNA microarrays, flow cytometry, and immunofluorescence analysis. There was an increased rate of apoptotic cells in aged subjects at all of the experimental time points, with no direct correlation between AnnexinV-positive cells and caspase-8 activity. On the other hand, [[CASP2]], [[CASP6]], [[CASP7]], and [[CASP9]] and a number of cell death genes were upregulated in the aged SCs. Altogether, our data show age-related enhanced susceptibility of human SCs to apoptosis, which might be responsible for their reduced response to muscle damage. 
|mesh-terms=* Adult
* Aged
* Aging
* Apoptosis
* Caspase 2
* Caspase 8
* Caspase 9
* Caspases
* Cysteine Endopeptidases
* Female
* Flow Cytometry
* Humans
* Male
* Real-Time Polymerase Chain Reaction
* Satellite Cells, Skeletal Muscle

|full-text-url=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3877545
}}