The involvement of calpain-dependent proteolysis of the tumor suppressor NF2 (merlin) in schwannomas and meningiomas

Nature Medicine

Volumn 4, Issue 8, 1998, Pages 915-922

  Kimurau, Yoriyoshi ^a,b   Koga, Hisashi ^a   Araki, Norie ^a   Mugita, Norifumi ^a   Fujita, Naoyuki ^a   Takeshima, Hideo ^a   Nishi, Tohru ^a   Yamashima, Tetsumori ^c   Saido, Takaomi C ^d   Yamasaki, Toshiki ^b   Moritake, Kouzo ^b   Saya, Hideyuki ^a   Nakao, Mitsuyoshi ^a  

^a KUMAMOTO UNIVERSITY   (Japan)

^b SHIMANE UNIVERSITY   (Japan)

^c KANAZAWA UNIVERSITY   (Japan)

^d RIKEN BRAIN SCIENCE INSTITUTE   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

CALPAIN; CALPASTATIN; CELL PROTEIN; MERLIN; UNCLASSIFIED DRUG;

ARTICLE; CANCER CELL CULTURE; CARCINOGENESIS; DNA SEQUENCE; GENE MUTATION; MENINGIOMA; NEURILEMOMA; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN EXPRESSION; TUMOR SUPPRESSOR GENE;

BASE SEQUENCE; BRAIN NEOPLASMS; CALPAIN; CELL LINE; DNA PRIMERS; ENZYME ACTIVATION; GENES, NEUROFIBROMATOSIS 2; GLIOMA; GLUTATHIONE TRANSFERASE; HUMANS; MEMBRANE PROTEINS; MENINGIOMA; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; NEURILEMMOMA; NEUROFIBROMIN 2; POLYMERASE CHAIN REACTION; RECOMBINANT FUSION PROTEINS; RNA, MESSENGER; TEMPLATES, GENETIC; TRANSCRIPTION, GENETIC; TRANSFECTION; TUMOR CELLS, CULTURED;

FALCO COLUMBARIUS;

EID: 0031902117     PISSN: 10788956     EISSN: None     Source Type: Journal    
DOI: 10.1038/nm0898-915     Document Type: Article

References (50)

1. Evans, D.G. et al. A genetic study of type 2 neurofibromatosis in the United Kinqdom. J. Med. Genet. 29, 841-846 (1992).
2. Martuza, R.L. & Eldridge, R. Neurofibromatosis 2 (bilateral acoustic neurofibromatosis) N. Ingl. J. Med. 318, 684-688 (1988).
3. Eldridge, R. Central neurofibromatosis with bilateral acoustic neurinoma. Adv. Neurol. 29, 57-65 (1981).
4. Rouleau, G.A. et al. Alteration in a new gene encoding a putative membrane-organizing protein causes neurofibromatosis type 2. Nature 363, 515-521 (1993).
5. Trofatter, J.A. et al. A novel moesin-, ezrin-, radixin-like gene is a candidate for the neurofibromatosis 2 tumor suppressor. Cell 72, 791-800 (1993).
6. Tsukita, S. & Yonemura, S. ERM (ezrin/radixin/moesin) family, from cytoskeleton to signal transduction. Curr. Opin. Cell Biol. 9, 70-75 (1997).
7. Algrain, M., Turunen, O., Vaheri, A., Louvard, D. & Arpin, M. Ezrin contains cytoskeleton and membrane binding domains accounting for its proposed role as a membrane-cytoskeletal linker. J. Cell Biol. 120, 129-139 (1993).
8. Koga, H. et al. Impairment of cell adhesion by expression of the mutant neurofibromatosis type 2(NF2) genes which miss exons in the ERM-homology domain. Oncogene (in the press).
9. Ruttledge, M.H. et al. Evidence for the complete inactivation of the NF2 gene in the majority of sporadic meningiomas. Nature Genet. 6, 180-184 (1994).
10. Merel, P. et al. Screening for germ-line mutations in the NF2 gene. Genes Chromosom. Cancer 12, 117-127 (1995).
11. Lekanne, D.R. et al. Frequent NF2 gene transcript mutations in sporadic meninqiomas and vestibular schwannomas. Am. J. Hum. Genet. 54, 1022-1029 (1994).
12. Harada, T. et al. Molecular genetic investigation of the neurofibromatosis type 2 tumor suppressor gene in sporadic meningioma. J. Neurosurg. 84, 847-851 (1996).
13. Bijlsma, E.K., Brouwer, M.R., Bosch, D.A., Westerveld, A. & Hulsebos, T.J. Molecular characterization of chromosome 22 deletions in schwannomas. Genes Chromosom. Cancer 5, 201-205 (1992).
14. Twist, E.C. et al. The neurofibromatosis type 2 gene is inactivated in schwannomas. Hum. Mol. Genet. 3, 147-151 (1994).
15. Arakawa, H., Hayashi, N., Nagase, H., Ogawa, M. & Nakamura, Y. Alternative splicing of the NF2 gene and its mutation analysis of breast and colorectal cancers. Hum. Mol. Genet. 3, 565-568 (1994).
16. Bianchi, A.B. et al. High frequency of inactivating mutations in the neurofibromatosis type 2 gene (NF2) in primary malignant mesotheliomas. Proc. Natl. Acad. Sci. USA 92, 10854-10858 (1995).
17. Sekido, Y. et al. Neurofibromatosis type 2 (NF2) gene is somatically mutated in mesotheliorna but not in lung cancer. Cancer Res. 55, 1227-1231 (1995).
18. MacCollin, M. et al. Mutational analysis of patients with neurofibromatosis 2. Am. J. Hum. Genet. 55, 314-320 (1994).
19. Welling, D.B. et al. Mutational spectrum in the neurofibromatosis type 2 gene in sporadic and familial schwannomas. Hum. Genet. 98, 189-193 (1996).
20. Stemmer-Rachamimov, O.A. et al. Universal absence of merlin, but not other ERM family members, in schwannomas. Am J. Pathol. 151, 1649-1654 (1997).
21. Gutmann, D.H., Giordano, M.J., Fishback, A.S. & Guha, A. Loss of merlin expression in sporadic meningiomas, ependymomas and schwannomas. Neurology 49, 267-270 (1997).
22. Lee, J.H. et al. Reduced expression of schwannomin/merlin in human sporadic meningiomas. Neurosurgery 40, 578-587 (1997).
23. Takeshima, H. et al. Detection of cellular proteins that interact with the NF2 tumor suppressor gene product. Oncogene 9, 2135-2144 (1994).
24. Saido, T.C., Sorimachi, H. & Suzuki, K. Calpain: new perspectives in molecular diversity and physiological-pathological involvement. FASEB J. 8, 814-822 (1994).
25. Suzuki, K., Sorimachi, H., Yoshizawa, T., Kinbara, K. & Ishiura, S. Calpain: novel family members, activation, and physiologic function. Biol. Chem. Hoppe-Seyler 376, 523-529 (1995).
26. Sorimachi, H., Ishiura, S. & Suzuki, K. Structure and physiological function of calpains. Biochem. J. 328, 721-732 (1997).
27. Tsubuki, S., Saito, Y., Tomioka, M., Ito, H. & Kawashima, S. Differential inhibition of calpain and proteasome activities by peptidyl aldehydes of di-leucine and trileucine. J. Biochem. 119, 572-576 (1996).
28. Coux, O., Tanaka, K. & Goldberg, A.L. Structure and functions of the 20S and 26S proteasomes. Annu. Rev. Biochem. 65, 801-847 (1996).
29. Burkhart, W.A., Moyer, M.B., Bailey, J.M. & Miller, C.G. Electroblotting of proteins to Teflon tape and membranes for N-and C-terminal seguence analysis. Anal. Biochem. 236, 364-367 (1996).
30. Miller, C.G. et. al. Techniques in Protein Chemistry Vol. VI, (ed. Crabb, John W.) 219-227 (Academic, San Diego, California, 1995).
31. Nagao, S. et al. Calpain-calpastatin interactions in epidermoid carcinoma KB cells. J. Biochem. 115, 1178-1184 (1994)
32. Billger, M., Wallin, M. & Karlsson, J.O. Proteolysis of tubulin and microtubule-associated proteins 1 and 2 by calpain I and II. Difference in sensitivity of assembled and disassembled microtubules. Cell Calcium 9, 33-44 (1988).
33. Saido, T.C. et al. Autolytic transition of μ-calpain upon activation as resolved by antibodies distinguishing between the pre-and post-autolysis forms. J. Biochem. 111, 81-86 (1992).
34. Siman, R., Baudry, M. & Lynch, C. Brain fodrin: substrate for calpain I, an endogenous calcium-activated protease. Proc. Natl. Acad. Sci. USA 81, 3572-3576 (1984).
35. Yang, L.S. & Ksiezak, R.H. Calpain-induced proteolysis of normal human tau and tau associated with paired helical filaments. Eur. J. Biochem. 233, 9-17 (1995).
36. Inomata, M. et al. Involvement of calpain in integrin-mediated signal transduction. Arch. Biochem. Biophys. 328, 129-134 (1996).
37. Selliah, N., Brooks, W.H. & Roszman, T.L. Proteolytic cleavage of alpha-actinin by calpain in T cells stimulated with anti-CD3 monoclonal antibody. J. Immunol. 156, 3215-3221 (1996).
38. Jay, D. & Stracher, A. Expression in Escherichia coli, phosphorylation with cAMP-dependent protein kinase and proteolysis by calpain of a 71-kDa domain of human endothelial actin binding protein. Biochem. Biophys. Res. Commun. 232, 555-558 (1997).
39. Huang, C. et al. Proteolysis of platelet cortactin by calpain. J. Biol. Chem. 272, 19248-19252 (1997).
40. Du, X. et al. Calpain cleavage of the cytoplasmic domain of the integrin beta 3 subunit. J. Biol. Chem. 270, 26146-26151 (1995).
41. Elvira, M., Diez, J.A., Wang, K.K. & Villalobo, A. Phosphorylation of connexin-32 by protein kinase C prevents its proteolysis by μ-calpain and m-calpain. J. Biol. Chem. 268, 14294-14300 (1993).
42. Litersky, J.M. & Johnson, G.V. Phosphorylation by cAMP-dependent protein kinase inhibits the degradation of tau by calpain. J. Biol. Chem. 267, 1563-1568 (1992).
43. Greenwood, J.A., Troncoso, J.C., Costello, A.C. & Johnson, C.V. Phosphorylation modulates calpain-mediated proteolysis and calmodulin binding of the 200-kDa and 160-kDa neurofilament proteins. J. Neurochem. 61, 191-199 (1993).
44. Scheffner, M., Huibregtse, J.M., Vierstra, R.D. & Howley, P.M. The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53. Cell 75, 495-505 (1993).
45. Kip1 protein: prognostic implications in primary breast cancer. Nature Med. 3, 227-230 (1997).
46. Loda, M. et al. Increased proteasome-dependent degradation of the cyclin-dependent kinase inhibitor p27 in aggressive colorectal carcinomas. Nature Med. 3, 231-234 (1997).
47. Jensen, R.L., Origitano, T.C., Lee, Y.S., Weber, M. & Wurster, R.D. In vitro growth inhibition of growth factor-stimulated meningioma cells by calcium channel antagonists. Neurosurgery 36, 365-373 (1995).
48. Jensen, R.L. et al. Inhibition of in vitro meningioma proliferation after growth factor stimulation by calcium channel antagonists: Part II-Additional growth factors, growth factor receptor immunohistochemistry, and intracellular calcium measurements. Neurosurgery 37, 937-946 (1995).
49. Feigner, P.L. et al. Lipofection: a highly efficient, lipid-mediated DNA-transfection procedure. Proc. Natl. Acad. Sci. USA 84, 741 3-741 7 (1987).
50. Siebert, P.D. & Chenchik, A. Modified acid guanidinium thiocyanate-phenol-chloroform RNA extraction method which greatly reduces DNA contamination. Nucleic Acids Res. 21, 2019-2020 (1993).