—New Way To Hit Alzheimer’s Target: Caspase-6 Inhibitor “Drug Discovery: Agent with novel mechanism improves selectivity for caspase-6 enzyme” An agent that inhibits the protease enzyme caspase-6 in a totally new way could help lead to a novel type of medication for Alzheimer’s disease, a condition in which caspase-6 may play a key role. Drug researchers in academia and the pharmaceutical industry have been actively pursuing inhibitors of caspase-6 and other caspases as potential Alzheimer’s medications for several years. But inhibitors against caspases have been found to cause serious side effects, and none has passed clinical trials.
by Stu Borman | June 18, 2012
—New target for anti-inflammatory agents “Study shows that caspases are secondary targets for nonsteroidal anti-inflammatory drugs” Researchers have discovered that caspases, enzymes that promote inflammation and cell death, are secondary targets for some nonsteroidal anti-inflammatory drugs (NSAIDs) (CellChem.
by Stu Borman | March 06, 2017
Many proteins are involved in triggering a cell's demise, but the protein caspase-3 does the dirty work. This executioner protein catalyzes the hydrolysis of more than 100 protein targets. These cleavage events ultimately lead to cell suicide, or apoptosis. Most tumors have disruptions in the protein signal cascades that produce active caspase-3.
by Sarah Everts | September 13, 2006
After injecting the drugs into mice with human versions of the cancers, the researchers found that the deglycosylated bleomycin induced caspase-3-dependent apoptosis, which kills the cancer cells, but it did not activate caspase-1, which seems responsible for bleomycin’s lung toxicity. In addition, bleomycin, but not deglycosylated bleomycin, induced formation of inflammation-related molecules, including cytokines and reactive oxygen species, which are also associated with lung damage. However, the mechanism by which bleomycin damages lung tissue is still not fully understood, although caspase-1 seems to play a major role. More tests are needed to determine whether deglycosylated bleomycin can be substituted for bleomycin in patients. /articles/94/i8/Removing-Sugar-Cancer-Drug-Eliminates.html 20160226 Oncology: Deglycosylated bleomycin kills cancer in mice without causing lung damage Concentrates 94 8 /magazine/94/09408.html Removing Sugar From Cancer Drug Eliminates Side Effect oncology, bleomycin, deglycosylation, cancer drug con scitech Celia Henry Arnaud pharmaceuticals Removing the disaccharide (red) from bleomycin eliminates the compound’s lung toxicity without altering its antitumor activity.
by Celia Henry Arnaud | February 26, 2016
The biotech firm was formed to commercialize caspase activation technology developed in the lab of Jim Wells, chair of the pharmaceutical chemistry department in UCSF’s School of Pharmacy. Wells has found several small molecules that convert caspases from an inactive form into enzymes that destroy cancer cells.
by Lisa M. Jarvis | July 12, 2010
In its active form, caspase-3 is critical for carrying out the final steps of apoptosis. The UCSF team showed that compound 1541 and some of its analogs induce apoptosis in a variety of cell lines, including cancer cell lines, by activating the caspases. The researchers propose that these compounds work by trapping a form of the proenzyme that is more capable of activating itself.
by Carmen Drahl | November 09, 2009
Once released from mitochondria, however, cytochrome c binds to an adaptor molecule called apoptotic protease activating factor-1 and to the inactive form of a caspase known as pro-caspase-9 to form a complex known as an apoptosome. The result is the cleavage and activation of pro-caspase-9, which then activates other pro-caspases that carry out the breakdown steps of apoptosis.
by REBECCA L. RAWLS, C&EN WASHINGTON | October 01, 2001
The ensuing steps that lead to destruction of the cell involve cysteine proteases known as caspases. Blocking the action of caspases stops apoptosis, but in some cases is not enough to prevent the cell's death. Instead, the cell self-destructs through a type of necrosis. Harvard Medical School cell biologists Junying Yuan and Alexei Degterev and their colleagues have discovered that it is possible to block this kind of necrosis, which they call necroptosis.
by SOPHIE ROVNER | July 04, 2005
The ensuing steps that lead to destruction of the cell involve cysteine proteases known as caspases. Blocking the action of caspases stops apoptosis, but in some cases is not enough to prevent the cell's death. Instead, the cell self-destructs through a type of necrosis. Harvard Medical School cell biologists Junying Yuan and Alexei Degterev and their colleagues have discovered that it is possible to block this kind of necrosis, which they call necroptosis.
by Sophie L. Rovner | July 04, 2005
Pressure Systems, http://pressuresystems.com CASPASES Product guide features 16 pages of technical, application, and product information on more than 240 enzymes, antibodies, inhibitors, assay kits, and other products for researchers studying the role of caspases in apoptosis and inflammation. Colorful diagrams illustrate the signaling pathways associated with various caspases.
by Melissa Braddock | June 21, 2004