calpain


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Related to calpain: cathepsin, calpastatin

calpain

[′kal‚pān]
(cell and molecular biology)
A calcium-dependent cysteine protease in the cytoplasm that is central to most processes in cell biology (plasma membrane-associated signaling events; cell proliferation, differentiation, activation, and communication; and programmed cell death). Its overactivation has been observed in muscular dystrophy, Alzheimer's disease, AIDS, cataract formation, multiple sclerosis, and arthritis.
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2005) Distinct mechanistic roles of calpain and caspase activation in neurodegeneration as revealed in mice over-expressing their specific inhibitors.
The frontal cortex and midbrain of blast-exposed mice showed significant increase in the expression of calcium-dependent cysteine proteases and calpain 3 and 9, respectively (Tables 3 and 4).
Garlic compounds induced calpain and intrinsic caspase cascade for apoptosis in human malignant neuroblastoma SH-SY5Y cells.
Vitex negundo attenuates calpain activation and cataractogenesis in selenite models.
Inmunochemical and inmunohistochemical study of calpastatin, an endogenous calpain inhibitor, in the masseter muscle of the rabbit.
En el estudio Relative effects of mannitol and hypertonic saline on calpain activity, apoptosis and polymorphonuclear infiltration in traumatic focal brain injury (2006) se comparan los efectos relativos del manitol y la solucion salina hipertonica en la actividad de la calpaina, apoptosis y la respuesta neuroinflamatoria inducida por la contusion cortical experimental.
elegans requiere proteasas reguladas por calcio, las calpain-proteasas (designadas como Calpain 1-10; CAPN 1-10) y las aspartil proteasas que son una familia mas heterogenea; esto demuestra que en este modelo hay dos clases de proteasas involucradas en la necrosis, que son homologas de las calpainas y catepsinas en humanos, en los que pueden mediar la necrosis.
Repetitive nerve stimulation studies were also employed to study the effect of transgenic expression of calpastatin (CS), the natural inhibitor of calpain, in the decremental response observed in the [epsilon]L269F-transgenic.
The calpain proteolytic enzyme system is responsible for the specific peptide bond cleavage which causes early postmortem tenderization [7].
Dual inhibition of protein phosphatase-1/2A and calpain rescues nerve growth factor-differentiated PC12 cells from oxygen glucose-deprivation-induced cell death.
This change is attributed to the increased expression of calpain, a calcium-activated protease.