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Digitale Medien

Requirement for ceramide-initiated SAPK/JNK signalling in stress-induced apoptosis (1996)

Verheij, Marcel ; Bose, Ron ; Hua Lin, Xin ; [weitere]

[s.l.] : Nature Publishing Group

Nature 380 (1996), S. 75-79

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ISSN: 1476-4687

Quelle: Nature Archives 1869 - 2009

Thema: Biologie , Chemie und Pharmazie , Medizin , Allgemeine Naturwissenschaft , Physik

Notizen: [Auszug] We studied stress effects in two cell types, U937 human mono-blastic leukaemia and bovine aortic endothelial (BAE) cells. Ceramide-initiated apoptosis has been investigated in these systems5'13. Exposure of U937 cells to ionizing radiation (10 Gy), hydrogen peroxide (ImM), ultraviolet-C radiation ...

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1038/380075a0

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Digitale Medien

Protein Kinase C Targeting in Antineoplastic Treatment Strategies (1999)

Jarvis, W. David ; Grant, Steven

Springer

Investigational new drugs 17 (1999), S. 227-240

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ISSN: 1573-0646

Schlagwort(e): apoptosis ; protein kinase C ; sphingoid bases ; safingol ; diglyceride ; bryostatin 1 ; staurosporine ; 7-hydroxy staurosporine (UCN-01) ; 4′-N-benzoyl staurosporine (CGP-41251) ; calphostin C (UCN-1028c)

Quelle: Springer Online Journal Archives 1860-2000

Thema: Chemie und Pharmazie , Medizin

Notizen: Abstract Neoplastic cell survival is governed by a balance between pro-apoptotic and anti-apoptotic signals. Noteworthy among several anti-apoptotic signaling elements is the protein kinase C (PKC) isoenzyme family, which mediates a central cytoprotective effect in the regulation of cell survival. Activation of PKC, and subsequent recruitment of numerous downstream elements such as the mitogen-activated protein kinase (MAPK) cascade, opposes initiation of the apoptotic cell death program by diverse cytotoxic stimuli. The understanding that the lethal actions of numerous antineoplastic agents are, in many instances, antagonized by cytoprotective signaling systems has been an important stimulus for the development of novel antineoplastic strategies. In this regard, inhibition of PKC, which has been shown to initiate apoptosis in a variety of malignant cell types, has recently been the focus of intense interest. Furthermore, there is accumulating evidence that selective targeting of PKC may prove useful in improving the therapeutic efficacy of established antineoplastic agents. Such chemosensitizing strategies can involve either (a) direct inhibition of PKC (e.g., following acute treatment with relatively specific inhibitors such as the synthetic sphingoid base analog safingol, or the novel staurosporine derivatives UCN-01 and CGP-41251) or (b) down-regulation (e.g., following chronic treatment with the non-tumor-promoting PKC activator bryostatin 1). In preclinical model systems, suppression of the cytoprotective function(s) of PKC potentiates the activity of cytotoxic agents (e.g., cytarabine) as well as ionizing radiation, and efforts to translate these findings into the clinical arena in humans are currently underway. Although the PKC-driven cytoprotective signaling systems affected by these treatments have not been definitively characterized, interference with PKC activity has been associated with loss of the mitogen-activated protein kinase (MAPK) response. Accordingly, recent pre-clinical studies have demonstrated that pharmacological disruption of the primary MEK-ERK module can mimic the chemopotentiating and radiopotentiating actions of PKC inhibition and/or down-regulation.