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Calpain‐dependent proteolysis of NF2 protein: Involvement in schwannomas and meningiomas
Author(s) -
Kimura Yoriyoshi,
Saya Hideyuki,
Nakao Mitsuyoshi
Publication year - 2000
Publication title -
neuropathology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.701
H-Index - 61
eISSN - 1440-1789
pISSN - 0919-6544
DOI - 10.1046/j.1440-1789.2000.00326.x
Subject(s) - merlin (protein) , calpain , neurofibromatosis type 2 , proteolysis , carcinogenesis , cancer research , cleavage (geology) , biology , neurofibromatosis , microbiology and biotechnology , chemistry , suppressor , gene , genetics , enzyme , biochemistry , paleontology , fracture (geology)
The neurofibromatosis type 2 (NF2) protein, known as merlin or schwannomin, is a tumor suppressor, and the NF2 gene has been found to be mutated in the majority of schwannomas and meningiomas, including both sporadically occurring and familial NF2 cases. Although the development of these tumors depends on the loss of merlin, the presence of tumors lacking detectable NF2 mutations suggests different mechanisms for inactivating merlin. Recent studies have demonstrated cleavage of merlin by calpain, a calcium‐dependent neutral cysteine protease, and marked activation of the calpain system resulting in the degradation of merlin in these tumors. Increased turnover of merlin by calpain in some schwannomas and meningiomas exemplifies tumorigenesis linked to the calpain‐mediated proteolytic pathway.