'The number of neutrophils in the blood and tissues is controlled by constitutive apoptotic programmed cell death and clearance by phagocytes such as macrophages. Here, we found that calpains cleave the X-linked inhibitor of apoptosis (XIAP) in vitro, producing fragments that are unable to inhibit caspase-3. These fragments were detected ... More
Suppression of cancer cell migration and invasion by protein phosphatase 2A through dephosphorylation of mu- and m-calpains.
AuthorsXu L, Deng X
JournalJ Biol Chem
PubMed ID16982626
'The mu- and m-calpains are major members of the calpain family that play an essential role in regulating cell motility. We have recently discovered that nicotine-activated protein kinase C iota enhances calpain phosphorylation in association with enhanced calpain activity and accelerated migration and invasion of human lung cancer cells. Here ... More
Protein kinase Ciota promotes nicotine-induced migration and invasion of cancer cells via phosphorylation of micro- and m-calpains.
AuthorsXu L, Deng X
JournalJ Biol Chem
PubMed ID16361262
'Nicotine is a major component in cigarette smoke that activates the growth-promoting pathways to facilitate the development of lung cancer. However, it is not clear whether nicotine affects cell motility to facilitate tumor metastasis. Here we discovered that nicotine potently induces phosphorylation of both mu- and m-calpains via activation of ... More
Tumor necrosis factor-alpha-inducible IkappaBalpha proteolysis mediated by cytosolic m-calpain. A mechanism parallel to the ubiquitin-proteasome pathway for nuclear factor-kappab activation.
AuthorsHan Y, Weinman S, Boldogh I, Walker RK, Brasier AR
JournalJ Biol Chem
PubMed ID9873017
'The cytokine tumor necrosis factor alpha (TNF-alpha) induces expression of inflammatory gene networks by activating cytoplasmic to nuclear translocation of the nuclear factor-kappaB (NF-kappaB) transcription factor. NF-kappaB activation results from sequential phosphorylation and hydrolysis of the cytoplasmic inhibitor, IkappaBalpha, through the 26 S proteasome. Here, we show a parallel proteasome-independent ... More
Calpain is required for normal osteoclast function and is down-regulated by calcitonin.
AuthorsMarzia M, Chiusaroli R, Neff L, Kim NY, Chishti AH, Baron R, Horne WC
JournalJ Biol Chem
PubMed ID16461769
'Osteoclast motility is thought to depend on rapid podosome assembly and disassembly. Both mu-calpain and m-calpain, which promote the formation and disassembly of focal adhesions, were observed in the podosome belt of osteoclasts. Calpain inhibitors disrupted the podosome belt, blocked the constitutive cleavage of the calpain substrates filamin A, talin, ... More
TRPM7 activates m-calpain by stress-dependent stimulation of p38 MAPK and c-Jun N-terminal kinase.
TRPM7 is a Ca(2)(+)-permeant and Mg(2)(+)-permeant ion channel in possession of its own kinase domain. In a previous study, we showed that overexpression of the channel-kinase in HEK-293 cells produced cell rounding and loss of adhesion, which was dependent on the Ca(2+)-dependent protease m-calpain. The TRPM7-elicited change in cell morphology ... More
Calpain activity increases in hepatocytes following addition of ATP. Demonstration by a novel fluorescent approach.
AuthorsRosser BG, Powers SP, Gores GJ
JournalJ Biol Chem
PubMed ID8226886
Our aim was to measure calpain protease activity during increases in cytosolic free calcium (Ca2+i) after addition of extracellular ATP. The calpain protease substrate t-butoxycarbonyl-Leu-Met-7-amino-4-chloromethylcoumarin was synthesized. Nonfluorescent t-butoxycarbonyl-Leu-Met-7-amino-4- chloromethyl-coumarin diffuses into the cell where it is conjugated to glutathione forming t-butoxycarbonyl-Leu-Met-7-amino-4-methylcoumarin glutathione conjugate (Boc-Leu-Met-MAC-SG). The nonfluorescent, membrane impermeant Boc-Leu-Met-MAC-SG ... More
Calcium influx through calcium leak channels is responsible for the elevated levels of calcium-dependent proteolysis in dystrophic myotubes.
AuthorsAlderton JM, Steinhardt RA
JournalJ Biol Chem
PubMed ID10734092
To estimate calpain proteolysis, we measured the hydrolysis rate of a fluorogenic calpain substrate in individual resting normal and dystrophic mdx mouse myotubes in culture. Hydrolysis rates were high during myoblast and myotube alignment and fusion. After alignment and fusion ceased, hydrolysis rates declined. For normal myotubes, hydrolysis remained low ... More
Epidermal growth factor receptor activation of calpain is required for fibroblast motility and occurs via an ERK/MAP kinase signaling pathway.
AuthorsGlading A, Chang P, Lauffenburger DA, Wells A
JournalJ Biol Chem
PubMed ID10644690
To become migratory, cells must reorganize their connections to the substratum, and during locomotion they must break rear attachments. The molecular and biochemical mechanisms underlying these biophysical processes are unknown. Recent studies have implicated both extracellular signal-regulated kinase/mitogen-activated protein (ERK/MAP) kinase and calpain (EC 3.4.22.17) in these processes, but it ... More
Evaluation of glutathione-sensitive fluorescent dyes in cortical culture.
AuthorsTauskela JS, Hewitt K, Kang LP, Comas T, Gendron T, Hakim A, Hogan M, Durkin J, Morley P
JournalGlia
PubMed ID10797613
The sensitivity of six fluorophores to glutathione (GSH) was evaluated in living rat cortical neuronal/glial mixed cultures during the first 23 days in vitro (DIV). Four of the dyes require glutathione-S-transferase (GST) to form a fluorescent conjugate, potentially conferring specificity for GSH: these included t-butoxycarbonyl-Leu-Met-7-amino-4-chloromethylcoumarin (CMAC), 7-amino-4-chloromethylcoumarin (CMAC-blue), monochlorobimane (MCB), ... More
Membrane proximal ERK signaling is required for M-calpain activation downstream of epidermal growth factor receptor signaling.
AuthorsGlading A, Uberall F, Keyse SM, Lauffenburger DA, Wells A
JournalJ Biol Chem
PubMed ID11319218
Localization of signaling is critical in directing cellular outcomes, especially in pleiotropic signaling pathways. The extracellular signal-regulated kinase (ERK)/microtubule-associated protein kinase, which promotes cell migration, proliferation, and differentiation is found in the nucleus and throughout the cytoplasm. Recently, it has been shown that nuclear translocation of ERK is required for ... More
The Abnormal Architecture of Healed Diabetic Ulcers Is the Result of FAK Degradation by Calpain 1.
Authors
JournalJ Invest Dermatol
PubMed ID28082186
Involvement of calpain in the process of Jurkat T cell chemotaxis.
Authors
JournalJ Neurosci Res
PubMed ID18831007
Photoreceptor rescue and toxicity induced by different calpain inhibitors.
Authors
JournalJ Neurochem
PubMed ID20807308
Dominant and recessive mutations in rhodopsin activate different cell death pathways.
Authors
JournalHum Mol Genet
PubMed ID27149983
Chemotactic G protein-coupled receptors control cell migration by repressing autophagosome biogenesis.
Authors
JournalAutophagy
PubMed ID27715446
Calpain-Mediated Proteolysis of Talin and FAK Regulates Adhesion Dynamics Necessary for Axon Guidance.
Authors
JournalJ Neurosci
PubMed ID28069919
Activation of Bax in three models of retinitis pigmentosa.
Authors
JournalInvest Ophthalmol Vis Sci
PubMed ID24825107
A retinal model of cerebral malaria.
Authors
JournalSci Rep
PubMed ID30837488
A key role for cyclic nucleotide gated (CNG) channels in cGMP-related retinitis pigmentosa.