Results 21 to 30 of about 26,728 (182)

Calpain 1 gene expression in liver tissue and the association of novel calpain 1 single-nucleotide polymorphisms (SNPs) with meat quality in Bali cattle. [PDF]

open access: yesArch Anim Breed
Abstract. Calpain 1 (CAPN1) is an enzyme that influences meat tenderization, and it is involved in post mortem proteolysis. The bovine CAPN1 gene was chosen as a candidate gene for DNA sequencing to identify novel single-nucleotide polymorphisms (SNPs) in exons 8–10 and assess their associations with meat quality in Bali cattle.
Dairoh, Ulum MF, Jakaria, Sumantri C.
europepmc   +4 more sources

Calpain-3 not only proteolyzes calpain-1 and -2 but also is a substrate for calpain-1 and -2

open access: yesThe Journal of Biochemistry, 2023
Abstract Calpain is an intracellular cysteine protease that cleaves its specific substrates in a limited region to modulate cellular function. Calpain-1 (C1) and calpain-2 (C2) are ubiquitously expressed in mammalian cells, but calpain-3 (C3) is a skeletal muscle-specific type.
Koichi Ojima   +4 more
openaire   +2 more sources

Changes in neurodegeneration-related miRNAs in brains from CAPN1−/− mice

open access: yesBBA Advances, 2021
Calpain-1 knock-out (KO) mice exhibit enhanced susceptibility to neurodegeneration due to the lack of the neuroprotective function of calpain-1. Dicer has been shown to play a fundamental role in the biogenesis of most miRNAs.
Wenyue Su   +3 more
doaj   +1 more source

Distinct regulatory functions of calpain 1 and 2 during neural stem cell self-renewal and differentiation. [PDF]

open access: yesPLoS ONE, 2012
Calpains are calcium regulated cysteine proteases that have been described in a wide range of cellular processes, including apoptosis, migration and cell cycle regulation. In addition, calpains have been implicated in differentiation, but their impact on
Daniela M Santos   +4 more
doaj   +1 more source

Calpain-2 compensation promotes angiotensin II-induced ascending and abdominal aortic aneurysms in calpain-1 deficient mice. [PDF]

open access: yesPLoS ONE, 2013
Recently, we demonstrated that angiotensin II (AngII)-infusion profoundly increased both aortic protein and activity of calpains, calcium-activated cysteine proteases, in mice.
Venkateswaran Subramanian   +5 more
doaj   +1 more source

Increased aortic calpain-1 activity mediates age-associated angiotensin II signaling of vascular smooth muscle cells. [PDF]

open access: yesPLoS ONE, 2008
Angiotensin II (Ang II) signaling, including matrix metalloproteinase type II (MMP2) activation, has been linked to an age-associated increase in migration capacity of vascular smooth muscle cells (VSMC), and to other proinflammatory features of arterial
Liqun Jiang   +7 more
doaj   +1 more source

Calpain-1 Cleaves and Activates Caspase-7 [PDF]

open access: yesJournal of Biological Chemistry, 2009
Caspase-7 is an executioner caspase that plays a key role in apoptosis, cancer, and a number of neurodegenerative diseases. The mechanism of caspase-7 activation by granzyme B and caspase-3 has been well characterized. However, whether other proteases such as calpains activate or inactivate caspase-7 is not known.
Juliette, Gafni   +4 more
openaire   +2 more sources

Interaction between calpain-1 and HSP90: new insights into the regulation of localization and activity of the protease. [PDF]

open access: yesPLoS ONE, 2015
Here we demonstrate that heat shock protein 90 (HSP90) interacts with calpain-1, but not with calpain-2, and forms a discrete complex in which the protease maintains its catalytic activity, although with a lower affinity for Ca2+.
Monica Averna   +7 more
doaj   +1 more source

N Terminus of Calpain 1 Is a Mitochondrial Targeting Sequence [PDF]

open access: yesJournal of Biological Chemistry, 2008
The ubiquitous m- and mu-calpains are thought to be localized in the cytosolic compartment, as is their endogenous inhibitor calpastatin. Previously, mu-calpain was found to be enriched in mitochondrial fractions isolated from rat cerebral cortex and SH-SY5Y neuroblastoma cells, but the submitochondrial localization of mu-calpain was not determined. In
RamaKrishna, Badugu   +4 more
openaire   +2 more sources

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