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Volumn 9, Issue 5, 1999, Pages 114-118

New aspect of the research on limb-girdle muscular dystrophy 2A: A molecular biologic and biochemical approach to pathology

Author keywords

[No Author keywords available]

Indexed keywords

CALPAIN; CYTOSKELETON PROTEIN; FODRIN; GENE PRODUCT; PROTEINASE;

EID: 0033431885     PISSN: 10501738     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1050-1738(99)00018-3     Document Type: Review
Times cited : (17)

References (36)
  • 1
    • 0031662389 scopus 로고    scopus 로고
    • Characterization of monoclonal antibodies to calpain 3 and protein expression in muscle from patients with limb-girdle muscular dystrophy type 2A
    • Anderson L.V., Davison K., Moss J.A.et al. Characterization of monoclonal antibodies to calpain 3 and protein expression in muscle from patients with limb-girdle muscular dystrophy type 2A. Am J Pathol. 153:1998;1169-1179.
    • (1998) Am J Pathol , vol.153 , pp. 1169-1179
    • Anderson, L.V.1    Davison, K.2    Moss, J.A.3
  • 2
    • 0032941594 scopus 로고    scopus 로고
    • Calpain 3 deficiency is associated with myonuclear apoptosis and profound perturbation of the IkappaB alpha/NF-kappaB pathway in limb-girdle muscular dystrophy type 2A
    • Baghdiguian S., Martin M., Richard I.et al. Calpain 3 deficiency is associated with myonuclear apoptosis and profound perturbation of the IkappaB alpha/NF-kappaB pathway in limb-girdle muscular dystrophy type 2A. Nat Med. 5:1999;503-511.
    • (1999) Nat Med , vol.5 , pp. 503-511
    • Baghdiguian, S.1    Martin, M.2    Richard, I.3
  • 3
    • 0029906609 scopus 로고    scopus 로고
    • Advances in the molecular genetics of the limb-girdle type of autosomal recessive progressive muscular dystrophy
    • Beckmann J.S., Bushby K.M. Advances in the molecular genetics of the limb-girdle type of autosomal recessive progressive muscular dystrophy. Curr Opin Neurol. 9:1996;389-393.
    • (1996) Curr Opin Neurol , vol.9 , pp. 389-393
    • Beckmann, J.S.1    Bushby, K.M.2
  • 4
    • 0026566108 scopus 로고
    • Molecular basis of myotonic dystrophy: Expansion of a trinucleotide (CTG) repeat at the 3′ end of a transcript encoding a protein kinase family member
    • Brook J.D., McCurrach M.E., Harley H.G.et al. Molecular basis of myotonic dystrophy. expansion of a trinucleotide (CTG) repeat at the 3′ end of a transcript encoding a protein kinase family member Cell. 68:1992;799-808.
    • (1992) Cell , vol.68 , pp. 799-808
    • Brook, J.D.1    McCurrach, M.E.2    Harley, H.G.3
  • 5
    • 0032855394 scopus 로고    scopus 로고
    • Making sense of the limb-girdle muscular dystrophies
    • Bushby K.M. Making sense of the limb-girdle muscular dystrophies. Brain. 122:1999;1403-1420.
    • (1999) Brain , vol.122 , pp. 1403-1420
    • Bushby, K.M.1
  • 6
    • 0029334512 scopus 로고
    • The limb-girdle muscular dystrophies - proposal for a new nomenclature
    • Bushby K.M., Beckmann J.S. The limb-girdle muscular dystrophies - proposal for a new nomenclature. Neuromuscul Disord. 5:1995;337-343.
    • (1995) Neuromuscul Disord , vol.5 , pp. 337-343
    • Bushby, K.M.1    Beckmann, J.S.2
  • 7
    • 0028914964 scopus 로고
    • Three muscular dystrophies: Loss of cytoskeleton-extracellular matrix linkage
    • Campbell K.P. Three muscular dystrophies. loss of cytoskeleton-extracellular matrix linkage Cell. 80:1995;675-679.
    • (1995) Cell , vol.80 , pp. 675-679
    • Campbell, K.P.1
  • 8
    • 0031259933 scopus 로고    scopus 로고
    • A new subfamily of vertebrate calpains lacking a calmodulin-like domain: Implications for calpain regulation and evolution
    • Dear N., Matena K., Vingron M.et al. A new subfamily of vertebrate calpains lacking a calmodulin-like domain. implications for calpain regulation and evolution Genomics. 45:1997;175-184.
    • (1997) Genomics , vol.45 , pp. 175-184
    • Dear, N.1    Matena, K.2    Vingron, M.3
  • 9
    • 0029963979 scopus 로고    scopus 로고
    • Juvenile limb-girdle muscular dystrophy: Clinical, histopathological, and genetic data from a small community living in the Reunion Island
    • Fardeau M., Hillaire D., Mignard C.et al. Juvenile limb-girdle muscular dystrophy. clinical, histopathological, and genetic data from a small community living in the Reunion Island Brain. 119:1996;295-308.
    • (1996) Brain , vol.119 , pp. 295-308
    • Fardeau, M.1    Hillaire, D.2    Mignard, C.3
  • 10
    • 0032033322 scopus 로고    scopus 로고
    • Expression of genes (CAPN3, SGCA, SGCB, and TTN) involved in progressive muscular dystrophies during early human development
    • Fougerousse F., Durand M., Suel L.et al. Expression of genes (CAPN3, SGCA, SGCB, and TTN) involved in progressive muscular dystrophies during early human development. Genomics. 48:1998;145-156.
    • (1998) Genomics , vol.48 , pp. 145-156
    • Fougerousse, F.1    Durand, M.2    Suel, L.3
  • 11
    • 0024504659 scopus 로고
    • Two structural states of Z-bands in cardiac muscle
    • Goldstein M.A., Michael L.H., Schroeter J.P.et al. Two structural states of Z-bands in cardiac muscle. Am J Physiol. 256(2 Pt. 2):1989;H552-H559.
    • (1989) Am J Physiol , vol.256 , Issue.2 PT. 2
    • Goldstein, M.A.1    Michael, L.H.2    Schroeter, J.P.3
  • 13
    • 0033050067 scopus 로고    scopus 로고
    • Expression and functional characteristics of calpain 3 isoforms generated through tissue-specific transcriptional and post-transcriptional events
    • Herasse M., Ono Y., Fougerousse F.et al. Expression and functional characteristics of calpain 3 isoforms generated through tissue-specific transcriptional and post-transcriptional events. Mol Cell Biol. 19:1999;4047-4055.
    • (1999) Mol Cell Biol , vol.19 , pp. 4047-4055
    • Herasse, M.1    Ono, Y.2    Fougerousse, F.3
  • 14
    • 0023614188 scopus 로고
    • Dystrophin: The protein product of the Duchenne muscular dystrophy locus
    • Hoffman E.P., Brown R.H. Jr., Kunkel L.M. Dystrophin. the protein product of the Duchenne muscular dystrophy locus Cell. 51:1987;919-928.
    • (1987) Cell , vol.51 , pp. 919-928
    • Hoffman, E.P.1    Brown, R.h.jr.2    Kunkel, L.M.3
  • 15
    • 0031883959 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a novel tissue-specific calpain predominantly expressed in the digestive tract
    • Lee H.J., Sorimachi H., Jeong S.Y.et al. Molecular cloning and characterization of a novel tissue-specific calpain predominantly expressed in the digestive tract. Biol Chem. 379:1998;175-183.
    • (1998) Biol Chem , vol.379 , pp. 175-183
    • Lee, H.J.1    Sorimachi, H.2    Jeong, S.Y.3
  • 16
    • 0031892439 scopus 로고    scopus 로고
    • Molecular cloning and expression of calpain Lp82 from rat lens: A splice variant of muscle p94 mRNA with insert regions deleted
    • Ma H., Fukiage C., Azuma M.et al. Molecular cloning and expression of calpain Lp82 from rat lens. a splice variant of muscle p94 mRNA with insert regions deleted Invest Ophthalmol Vis Sci. 39:1997;454-461.
    • (1997) Invest Ophthalmol Vis Sci , vol.39 , pp. 454-461
    • Ma, H.1    Fukiage, C.2    Azuma, M.3
  • 17
    • 0030982846 scopus 로고    scopus 로고
    • Connectin/titin, giant elastic protein of muscle
    • Maruyama K. Connectin/titin, giant elastic protein of muscle. FASEB J. 11:1997;341-345.
    • (1997) FASEB J , vol.11 , pp. 341-345
    • Maruyama, K.1
  • 18
    • 0031590410 scopus 로고    scopus 로고
    • Identification of a novel, tissue-specific calpain htra-3: A human homologue of the Caenorhabditis elegans sex determination gene
    • Mugita N., Kimura Y., Ogawa M.et al. Identification of a novel, tissue-specific calpain htra-3. a human homologue of the Caenorhabditis elegans sex determination gene Biochem Biophys Res Commun. 239:1997;845-850.
    • (1997) Biochem Biophys Res Commun , vol.239 , pp. 845-850
    • Mugita, N.1    Kimura, Y.2    Ogawa, M.3
  • 19
    • 0032479445 scopus 로고    scopus 로고
    • Functional defects of a muscle-specific calpain, p94, caused by mutations associated with limb-girdle muscular dystrophy type 2A
    • Ono Y., Shimada H., Sorimachi H.et al. Functional defects of a muscle-specific calpain, p94, caused by mutations associated with limb-girdle muscular dystrophy type 2A. J Biol Chem. 273:1998;17,073-17,078.
    • (1998) J Biol Chem , vol.273 , pp. 17
    • Ono, Y.1    Shimada, H.2    Sorimachi, H.3
  • 20
    • 0029985186 scopus 로고    scopus 로고
    • Evidence for implication of muscle-specific calpain (p94) in myofibrillar integrity
    • Poussard S., Duvert M., Balcerzak D.et al. Evidence for implication of muscle-specific calpain (p94) in myofibrillar integrity. Cell Growth Differ. 7:1996;1461-1469.
    • (1996) Cell Growth Differ , vol.7 , pp. 1461-1469
    • Poussard, S.1    Duvert, M.2    Balcerzak, D.3
  • 21
    • 0028905205 scopus 로고
    • Mutations in the proteolytic enzyme calpain 3 cause limb-girdle muscular dystrophy type 2A
    • Richard I., Broux O., Allamand V.et al. Mutations in the proteolytic enzyme calpain 3 cause limb-girdle muscular dystrophy type 2A. Cell. 81:1995;27-40.
    • (1995) Cell , vol.81 , pp. 27-40
    • Richard, I.1    Broux, O.2    Allamand, V.3
  • 22
    • 0033514986 scopus 로고    scopus 로고
    • Familial dilated cardiomyopathy locus maps to chromosome 2q31
    • Siu B.L., Niimura H., Osborne J.A.et al. Familial dilated cardiomyopathy locus maps to chromosome 2q31. Circulation. 99:1999;1022-1026.
    • (1999) Circulation , vol.99 , pp. 1022-1026
    • Siu, B.L.1    Niimura, H.2    Osborne, J.A.3
  • 23
    • 0024369426 scopus 로고
    • Molecular cloning of a novel mammalian calcium-dependent protease distinct form both m- And μ-types
    • Sorimachi H., Imajoh-Ohmi S., Emori Y.et al. Molecular cloning of a novel mammalian calcium-dependent protease distinct form both m- and μ-types. J Biol Chem. 264:1989;20,106-20,111.
    • (1989) J Biol Chem , vol.264 , pp. 20
    • Sorimachi, H.1    Imajoh-Ohmi, S.2    Emori, Y.3
  • 25
    • 0027276561 scopus 로고
    • Muscle-specific calpain, p94, is degraded by autolysis immediately after translation, resulting in disappearance from muscle
    • b
    • Sorimachi H., Toyama-Sorimachi N., Saido T.C.et al. Muscle-specific calpain, p94, is degraded by autolysis immediately after translation, resulting in disappearance from muscle. J Biol Chem. 268:1993;10,593-10,605. b.
    • (1993) J Biol Chem , vol.268 , pp. 10
    • Sorimachi, H.1    Toyama-Sorimachi, N.2    Saido, T.C.3
  • 26
    • 13344285357 scopus 로고
    • Muscle-specific calpain, p94, responsible for limb-girdle muscular dystrophy type 2A, associates with connectin through IS2, a p94-specific sequence
    • Sorimachi H., Kinbara K., Kimura S.et al. Muscle-specific calpain, p94, responsible for limb-girdle muscular dystrophy type 2A, associates with connectin through IS2, a p94-specific sequence. J Biol Chem. 270:1995;31,158-31,162.
    • (1995) J Biol Chem , vol.270 , pp. 31
    • Sorimachi, H.1    Kinbara, K.2    Kimura, S.3
  • 27
    • 10344239870 scopus 로고    scopus 로고
    • Structure and physiological functions of ubiquitous and tissue-specific calpain species
    • Sorimachi H., Kimura S., Kinbara K.et al. Structure and physiological functions of ubiquitous and tissue-specific calpain species. Adv Biophys. 33:1996;101-122.
    • (1996) Adv Biophys , vol.33 , pp. 101-122
    • Sorimachi, H.1    Kimura, S.2    Kinbara, K.3
  • 28
    • 0031213849 scopus 로고    scopus 로고
    • Tissue-specific expression and α-actinin binding properties of the Z-disc titin: Implications for the nature of the vertebrate Z-disc
    • a
    • Sorimachi H., Freiburg A., Kolmerer B.et al. Tissue-specific expression and α-actinin binding properties of the Z-disc titin. implications for the nature of the vertebrate Z-disc J Mol Biol. 270:1997;688-695. a.
    • (1997) J Mol Biol , vol.270 , pp. 688-695
    • Sorimachi, H.1    Freiburg, A.2    Kolmerer, B.3
  • 29
    • 0031452173 scopus 로고    scopus 로고
    • Structure and physiological function of calpains
    • b
    • Sorimachi H., Ishiura S., Suzuki K. Structure and physiological function of calpains. Biochem J. 328:1997;721-732. b.
    • (1997) Biochem J , vol.328 , pp. 721-732
    • Sorimachi, H.1    Ishiura, S.2    Suzuki, K.3
  • 30
    • 0031006931 scopus 로고    scopus 로고
    • Decreased susceptibility to calpains of v-FosFBR but not of v-FosFBJ or v-JunASV17 retroviral proteins compared with their cellular counterparts
    • Steff A.M., Carillo S., Pariat M.et al. Decreased susceptibility to calpains of v-FosFBR but not of v-FosFBJ or v-JunASV17 retroviral proteins compared with their cellular counterparts. Biochem J. 323:1997;685-692.
    • (1997) Biochem J , vol.323 , pp. 685-692
    • Steff, A.M.1    Carillo, S.2    Pariat, M.3
  • 31
    • 0018833064 scopus 로고
    • 2+-activated neutral protease and its inhibitors: In vitro effect on intact myofibrils
    • 2+-activated neutral protease and its inhibitors. in vitro effect on intact myofibrils Muscle Nerve. 3:1980;335-339.
    • (1980) Muscle Nerve , vol.3 , pp. 335-339
    • Sugita, H.1    Ishiura, S.2    Suzuki, K.3
  • 32
    • 0029360698 scopus 로고
    • Calpain: Novel family members, activation, and physiological function
    • Suzuki K., Sorimachi H., Yoshizawa T.et al. Calpain. novel family members, activation, and physiological function Biol Chem Hoppe-Seyler. 376:1995;523-529.
    • (1995) Biol Chem Hoppe-Seyler , vol.376 , pp. 523-529
    • Suzuki, K.1    Sorimachi, H.2    Yoshizawa, T.3
  • 33
    • 0001848892 scopus 로고
    • Calpain substrate specificity
    • In Mellgren RL, Murachi T, eds. Boca Raton, FL, CRC Press
    • Takahashi K: 1990. Calpain substrate specificity. In Mellgren RL, Murachi T, eds. Intracellular Calcium-Dependent Proteolysis. Boca Raton, FL, CRC Press, pp. 55-74.
    • (1990) Intracellular Calcium-Dependent Proteolysis , pp. 55-74
    • Takahashi, K.1
  • 34
    • 13344261948 scopus 로고    scopus 로고
    • Interleukin 6 receptor antibody inhibits muscle atrophy and modulates proteolytic systems in interleukin 6 transgenic mice
    • Tsujinaka T., Fujita J., Ebisui C.et al. Interleukin 6 receptor antibody inhibits muscle atrophy and modulates proteolytic systems in interleukin 6 transgenic mice. J Clin Invest. 97:1996;244-249.
    • (1996) J Clin Invest , vol.97 , pp. 244-249
    • Tsujinaka, T.1    Fujita, J.2    Ebisui, C.3
  • 35
    • 0031925821 scopus 로고    scopus 로고
    • Tibial muscular dystrophy - From clinical description to linkage on chromosome 2q31
    • Udd B., Haravuori H., Kalimo H.et al. Tibial muscular dystrophy - from clinical description to linkage on chromosome 2q31. Neuromuscul Disord. 8:1998;327-332.
    • (1998) Neuromuscul Disord , vol.8 , pp. 327-332
    • Udd, B.1    Haravuori, H.2    Kalimo, H.3
  • 36
    • 0032549173 scopus 로고    scopus 로고
    • Proteolytic regulation of the zinc finger transcription factor YY1, a repressor of muscle-restricted gene expression
    • Walowitz J.L., Bradley M.E., Chen S.et al. Proteolytic regulation of the zinc finger transcription factor YY1, a repressor of muscle-restricted gene expression. J Biol Chem. 273:1998;6656-6661.
    • (1998) J Biol Chem , vol.273 , pp. 6656-6661
    • Walowitz, J.L.1    Bradley, M.E.2    Chen, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.