| First Author | Glass JD | Year | 1998 |
| Journal | J Neurosci Res | Volume | 52 |
| Issue | 6 | Pages | 653-60 |
| PubMed ID | 9669314 | Mgi Jnum | J:48477 |
| Mgi Id | MGI:1270043 | Doi | 10.1002/(SICI)1097-4547(19980615)52:6<653::AID-JNR4>3.0.CO;2-7 |
| Citation | Glass JD, et al. (1998) Cloning of m-calpain 80 kD subunit from the axonal degeneration-resistant WLD(S) mouse mutant. J Neurosci Res 52(6):653-60 |
| abstractText | Calpains are calcium-activated cysteine proteases that are involved in cellular degradation in models of neurodegeneration, Calpains are the effectors of cytoskeletal disruption during axonal degeneration, a pathological feature of many neurological disorders, The WLDS mouse mutant is resistant to axonal degeneration and demonstrates prolonged survival of the cytoskeleton after nerve injury, To investigate the possibility that a mutation in calpain or abnormalities in calpain protein expression is responsible for the resistance to axonal degeneration seen in the WLDS mouse mutant, we 1) cloned and sequenced the large subunit of the high calcium- requiring form of calpain (m-calpain) from nervous system tissues of WLDS and from wild-type C57BL/6 mice, and 2) generated polyclonal m-calpain antibodies for comparison of relative protein levels by Western blot, We found our sequence for mouse m-calpain to be almost identical to another recently published mouse sequence, and the wild- type and WLDS sequences to be identical, Our fusion protein and peptide polyclonal antibodies were specific for the 80 kD subunit and recognized appropriate protein bands from pure m-calpain, fusion protein, and in tissue, There was no apparent difference in m-calpain expression in nerve or spinal cord in noninjured adult animals. These data suggest that a defect in m-calpain 80 kD subunit does not likely underlie the WLDS phenotype, but raise questions about other subunits of calpain and possibly other proteases, (C) 1998 Wiley-Liss,Inc. |
