A5066499086- Calpain Protease Function and Regulation
- Muscle Physiology and Disorders
- RNA regulation and disease
- Hereditary Neurological Disorders
- Connexins and lens biology
- Meat and Animal Product Quality
- Genetic Neurodegenerative Diseases
- Signaling Pathways in Disease
- Cardiomyopathy and Myosin Studies
- Alzheimer's disease research and treatments
- Venomous Animal Envenomation and Studies
- Ubiquitin and proteasome pathways
- RNA and protein synthesis mechanisms
- Endoplasmic Reticulum Stress and Disease
- Toxoplasma gondii Research Studies
- Biochemical Analysis and Sensing Techniques
- Peroxisome Proliferator-Activated Receptors
- Cell death mechanisms and regulation
- Glycosylation and Glycoproteins Research
- interferon and immune responses
- Enzyme Production and Characterization
- Nerve injury and regeneration
- Amyloidosis: Diagnosis, Treatment, Outcomes
- Peptidase Inhibition and Analysis
- Plant biochemistry and biosynthesis
Waseda University
1978-2024
Tokyo Metropolitan Institute of Medical Science
2009-2022
Advanced Research Projects Agency - Energy
2016
The University of Tokyo
2000-2015
Laboratoire des Biomolécules
2014
Japan Science and Technology Agency
2003-2010
Kazusa DNA Research Institute
2008
Kindai University
2003
Harvard University
2002
University of Washington
2002
Calpain, calcium-activated neutral protease, stands as a unique receptor for calcium signals in biological systems; its activation leads to irreversible proteolytic processing of substrate proteins, modifying cellular situations manner distinct from that reversible processes including the phosphorylation-dephosphorylation reactions. Because enzyme participates not only normal intracellular signal transduction cascades but also various pathological states ischemia, calpain research has...
Abstract Two types of calcium-dependent protease with distinct calcium requirements (termed muCANP and mCANP) are known in mammalian tissues. These two isozymes consist different large (80-kDa) subunits (mu- or m-types) identical small (30-kDa) subunits. By screening human rat muscle cDNA libraries a probe for the chicken CANP subunit, which has structure similar to both mu- m-types, clone encoding novel member subunit family was obtained. The encoded protein (designated p94) consists 821...
Calpains (calcium-dependent cytoplasmic cysteine proteinases) are implicated in processes such as cytoskeleton remodeling and signal transduction. The 2.3-A crystal structure of full-length heterodimeric [80-kDa (dI-dIV) + 30-kDa (dV+dVI)] human m-calpain crystallized the absence calcium reveals an oval disc-like shape, with papain-like catalytic domain dII two calmodulin-like domains dIV+dVI occupying opposite poles, tumor necrosis factor alpha-like beta-sandwich dIII N-terminal segments...
p94, a muscle-specific member of calpain family, is unique in that it undergoes rapid and exhaustive autolysis with half-life less than 1 h resulting its disappearance from muscle. Recently, p94 was shown to be responsible for limb girdle muscular dystrophy type 2A. To elucidate the proteolytic system mediated by solve mystery unusually autolysis, we searched p94-binding proteins two-hybrid system. Although small subunit plays crucial role regulation ubiquitous calpains, did not associate...
Titin is a giant elastic protein in vertebrate striated muscles with an unprecedented molecular mass of 3-4 megadaltons. Single molecules titin extend from the Z-line to M-line. Here, we define layout within Z-line; most NH2-terminal 30 kD located at periphery border adjacent sarcomere, whereas subsequent 60 spans entire width Z-line. In vitro binding studies reveal that mammalian titins have least four potential sites for alpha-actinin their spanning region. filaments may specify and...
We describe here a novel sarcomeric 145-kD protein, myopalladin, which tethers together the COOH-terminal Src homology 3 domains of nebulin and nebulette with EF hand motifs α-actinin in vertebrate Z-lines. Myopalladin's nebulin/nebulette α-actinin–binding sites are contained two distinct regions within its 90-kD domain. Both highly homologous those found palladin, protein described recently required for actin cytoskeletal assembly (Parast, M.M., C.A. Otey. 2000. J. Cell Biol. 150:643–656)....
The lymphocyte adhesion molecule CD44 recognizes a non-hyaluronate proteoglycan, gp600, secreted by mouse T cell line CTLL2. We now demonstrate that gp600 is identical to serglycin, member of the small proteoglycan family stored in intracellular secretory granules lymphoid, myeloid, and some tumor cells. Purified has ability bind specifically CD44, binding dependent on activation CD44. CD44-binding elements or serglycin are glycosaminoglycans consisting chondroitin 4-sulfate. Serglycin...
MDC9, also known as meltrin gamma, is a membrane-anchored metalloprotease. MDC9 contains several distinct protein domains: signal sequence followed by prodomain and domain showing similarity to snake venom metalloproteases, disintegrin-like domain, cysteine-rich region, an epidermal-growth-factor-like repeat, transmembrane cytoplasmic domain. Here we demonstrate that expressed in COS cells cleaved between the metalloprotease Further, when was co-expressed with amyloid precursor (APP695)...
The COOH-terminal A168-170 region of the giant sarcomeric protein titin interacts with muscle-specific RING finger-1 (MURF-1). To investigate functional significance this interaction, we expressed green fluorescent fusion constructs encoding defined fragments titin's M-line and MURF-1 in cardiac myocytes. Upon expression or its central (containing titin-binding site), integrity was dramatically disrupted. Disruption also resulted a perturbation thick filament components, but, surprisingly,...
We previously identified a third type of the calpain large subunit named p94 as cDNA whose mRNA is expressed exclusively in skeletal muscle at levels approximately 10-fold more abundant than those conventional subunit. Rat fractions were screened by two anti-peptide antibodies raised against specific sequences p94, but protein could not be found. To examine this apparent discrepancy between amounts and protein, wild-type was COS cells. Although normally cells, only very small its presumed...
A fourth type of rat phosphoinositide-specific phospholipase C (PLC IV) has been cloned for cDNA and sequenced. PLC IV is distinct from the other three types I, II, III) with respect to primary structure tissue distribution its mRNAs. contains two homologous regions included commonly in III most similar II (identity: 50.2%). IV, common a sequence N-terminal regulatory domains nonreceptor tyrosine kinases src-family oncogenes. Using an Escherichia coli expression system, we succeeded...