Calpain activation and apoptosis in motor neurons of cultured adult mouse spinal cord

Research output: Contribution to journalArticle

Standard

Calpain activation and apoptosis in motor neurons of cultured adult mouse spinal cord. / Momeni, Hamid Reza; Azadi, Seifollah; Kanje, Martin.

In: Functional Neurology, Vol. 22, No. 2, 2007, p. 105-110.

Research output: Contribution to journalArticle

Harvard

APA

CBE

MLA

Momeni, Hamid Reza, Seifollah Azadi and Martin Kanje. "Calpain activation and apoptosis in motor neurons of cultured adult mouse spinal cord". Functional Neurology. 2007, 22(2). 105-110.

Vancouver

Author

Momeni, Hamid Reza ; Azadi, Seifollah ; Kanje, Martin. / Calpain activation and apoptosis in motor neurons of cultured adult mouse spinal cord. In: Functional Neurology. 2007 ; Vol. 22, No. 2. pp. 105-110.

RIS

TY - JOUR

T1 - Calpain activation and apoptosis in motor neurons of cultured adult mouse spinal cord

AU - Momeni, Hamid Reza

AU - Azadi, Seifollah

AU - Kanje, Martin

PY - 2007

Y1 - 2007

N2 - Calpain, a Ca2+-dependent cysteine protease, has been implicated in neuronal apoptosis following spinal cord injury. In this study, activation of calpain was investigated in motor neurons of adult spinal cord slices from the mouse, using a cell-permeable fluorogenic calpain substrate and Western blotting. Calpain was rapidly activated in the motor neurons of excised spinal cord slices and calpain activity was observed both in the cytoplasm and the nuclei. In these neurons, nuclear and chromatin condensation were pronounced. Both calpain inhibitor VI and EGTA (ethyleneglycol-bis(beta-aminoethyl ether) N',N',N',N'-tetraacetic acid) inhibited calpain activation and subsequent appearance of apoptotic nuclei. In contrast, the general caspase inhibitor Z-VAD.fmk had no effect. Calpain activation was also observed in the slices by Western blotting using an antibody to 150-kD calpain-cleaved a-fodrin fragment. These results show that calpain is rapidly activated in injured motor neurons and imply that this activation could be responsible for execution of caspase-independent apoptosis in injured adult motor neurons.

AB - Calpain, a Ca2+-dependent cysteine protease, has been implicated in neuronal apoptosis following spinal cord injury. In this study, activation of calpain was investigated in motor neurons of adult spinal cord slices from the mouse, using a cell-permeable fluorogenic calpain substrate and Western blotting. Calpain was rapidly activated in the motor neurons of excised spinal cord slices and calpain activity was observed both in the cytoplasm and the nuclei. In these neurons, nuclear and chromatin condensation were pronounced. Both calpain inhibitor VI and EGTA (ethyleneglycol-bis(beta-aminoethyl ether) N',N',N',N'-tetraacetic acid) inhibited calpain activation and subsequent appearance of apoptotic nuclei. In contrast, the general caspase inhibitor Z-VAD.fmk had no effect. Calpain activation was also observed in the slices by Western blotting using an antibody to 150-kD calpain-cleaved a-fodrin fragment. These results show that calpain is rapidly activated in injured motor neurons and imply that this activation could be responsible for execution of caspase-independent apoptosis in injured adult motor neurons.

KW - organ culture

KW - motor neurons

KW - caspase

KW - apoptosis

KW - calpain

KW - spinal cord

M3 - Article

VL - 22

SP - 105

EP - 110

JO - Functional Neurology

JF - Functional Neurology

SN - 0393-5264

IS - 2

ER -