Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:4.1.1.6 (CAD)
 4,420 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Apoptosis is a physiological form of cell death that is responsible for the deletion of cells. Epidermal keratinocytes are supposed to be regulated by cell proliferation and cell death leading to structural homeostasis. Psoriatic skin shows marked thickening of the epidermis, suggesting the imbalance of the homeostasis, which might be related to abnormal apoptotic process. We investigated the expression of various apoptosis-related molecules in the psoriatic hyperproliferative epidermis. Real time quantitative RT-PCR analyses revealed that mRNAs of Fas, Bcl-xL, Bax and ICAD (inhibitor of caspase 3-related DNase) of the psoriatic involved epidermis were increased by 4.2-, 2.8-, 2.6- and 5.6-fold, respectively, compared with the uninvolved epidermis. In contrast, Bcl-2 expression in the involved epidermis was one-third suppressed compared with the uninvolved epidermis. No significant difference in the expression of mRNAs of Fas ligand or CAD (caspase 3-related DNase) was detected between the involved and uninvolved epidermis. Western blot analysis and immunohistochemical studies showed compatible results obtained by RT-PCR analyses. Although active caspase 3 was slightly increased in the involved epidermis, apoptotic cells were marginally detected. These results indicate that psoriatic epidermis shows aberrant expression of apoptosis-related molecules representing suppressed apoptotic process, which might be related to characteristic histopathology.
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PMID:Aberrant expression of apoptosis-related molecules in psoriatic epidermis. 1191 6

Apoptotic cell death is characterized by several morphological nuclear changes, such as chromatin condensation and extensive fragmentation of chromosomal DNA. These alterations are primarily triggered through the activation of caspases, which subsequently cleave nuclear substrates. Caspase-3 induces processing of Acinus, which leads to chromatin condensation. DNA fragmentation is dependent on the DNase CAD, which is released from its inhibitor, ICAD, upon cleavage by caspase-3. DNA degradation is also induced by AIF and endonuclease G, which are both released from mitochondria upon death stimuli but do not require prior processing by caspases for their DNase activity. Here we report the identification of a widely expressed helicase designated Helicard, which contains two N-terminal CARD domains and a C-terminal helicase domain. Upon apoptotic stimuli, Helicard is cleaved by caspases, thereby separating the CARD domains from the helicase domain. While Helicard localizes in the cytoplasm, the helicase-containing fragment is found in the nucleus. Helicard accelerates Fas ligand-mediated DNA degradation, whereas a noncleavable or a helicase-dead Helicard mutant does not, implicating Helicard in the nuclear remodeling occurring during apoptosis.
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PMID:Overexpression of Helicard, a CARD-containing helicase cleaved during apoptosis, accelerates DNA degradation. 1201 21

Cisplatin [cis-diamminedichloroplatinum (II)]-treated murine peritoneal macrophages interact with L929 cells in vitro in a sequential manner, resulting in the formation of contact between the two cells. This interaction leads to the death of L929 cells by the process of apoptosis. The detailed investigations have suggested the involvement of two different pathways in macrophage-mediated L929 cell apoptosis. It is observed that the induction of apoptosis in L929 cells by cisplatin-treated macrophages is contact dependent and is mediated through Fas-Fas ligand and tumor necrosis factor-tumor necrosis factor receptor 1 pathways. This conclusion was based on the Western blot and immunoprecipitation analysis of Fas-Fas ligand, tumor necrosis factor-tumor necrosis factor receptor 1, Fas-associated death domain and tumor necrosis factor receptor-associated death domain. The Fas-Fas ligand interaction between macrophages and L929 cells increased the expression of Fas-associated death domain, and tumor necrosis factor-tumor necrosis factor receptor 1 interaction between macrophages and L929 cells increased the expression of tumor necrosis factor receptor-associated death domain in L929 cells. The induction of apoptosis in L929 cells was investigated by DNA fragmentation, Annexin V staining and Western blot analysis of Bax, Bcl-2, Bid, cytochrome c, poly(ADP ribose) polymerase, CAD, caspase-8 and caspase-3.
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PMID:Cisplatin-treated murine peritoneal macrophages induce apoptosis in L929 cells: role of Fas-Fas ligand and tumor necrosis factor-tumor necrosis factor receptor 1. 1715 5