Literature: A-K ; L-Z ; subject area
Compiled by: Julian Thorpe
Stress-Activated protein Kinases (SAPKs)
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Please Note: Due to time constraints, the text part of this page has not been updated for some time. However, references are added reasonably frequently. |
 | Giasson et al. (1997: in transgenic mice) have shown that activation
of stress-activated protein kinases (SAPKs) by an upstream
activator (MEKK-1) caused extensive NF-H phosphorylation. (Aberrant
hyperphosphorylation of perikaryal NF-H [neurofilament
heavy chain] is a common feature of many neurological diseases).
SAPK was localised in the neurites as well as the cell body
and they suggested that it could be involved in the phosphorylation of NF-H
in neurites (neuritic NF-H is highly-phosphorylated despite a demonstrated
absence of cyclin-dependent kinase 5
activity in these neurons). |
| Stress-activated serine/threonine protein kinase, p38 mitogen-activated
protein kinase (p38 MAPK), belongs to the MAP
kinase superfamily. Obata et al. (2000) report that it appears to play
a major role in apoptosis, cytokine production, transcriptional regulation,
and cytoskeletal
reorganization, and has been causally implicated in sepsis, ischemic
heart disease, arthritis, human immunodeficiency virus infection, and AD. |
| Stress activated protein kinase 1b (SAPK1b) is a major SAPK
in neurones. Brownlees et al. (2000) showed that this kinase phosphorylates
(multiple phosphorylation sites on) NF-H. They also showed that glutamate
treatment induced activation of the SAPK1b and increased NF-H phosphorylation
in the (primary cortical neuronal) cell bodies. |
| With regard to kinase inhibitors, Borgne and Meijer (1999) anticipate the discovery of novel selective and powerful (kinase) inhibitors which may be of therapeutic value in AD. |
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