ラミンA
- 関
- lamin type A
WordNet
- the 1st letter of the Roman alphabet (同)a
- the blood group whose red cells carry the A antigen (同)type_A, group A
PrepTutorEJDIC
- answer / ampere
- …‘を'打つ,たたく,なぐる / 打つ,たたく,なぐる
- すばやくずらかる
- arsenicの化学記号
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2016/02/08 16:11:09」(JST)
[Wiki en表示]
Lamin A/C |
PDB rendering based on 1ifr.
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Available structures |
PDB |
Ortholog search: PDBe, RCSB |
List of PDB id codes |
1IFR, 1IVT, 1X8Y, 2XV5, 2YPT, 3GEF, 3V4Q, 3V4W, 3V5B
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Identifiers |
Symbols |
LMNA ; CDCD1; CDDC; CMD1A; CMT2B1; EMD2; FPL; FPLD; FPLD2; HGPS; IDC; LDP1; LFP; LGMD1B; LMN1; LMNC; LMNL1; PRO1 |
External IDs |
OMIM: 150330 MGI: 96794 HomoloGene: 41321 ChEMBL: 1293235 GeneCards: LMNA Gene |
Gene ontology |
Molecular function |
• structural molecule activity
• protein binding
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Cellular component |
• nucleus
• nuclear envelope
• lamin filament
• nuclear lamina
• nucleoplasm
• cytoplasm
• cytosol
• intermediate filament
• nuclear matrix
• nuclear speck
• nuclear membrane
• perinuclear region of cytoplasm
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Biological process |
• mitotic cell cycle
• apoptotic process
• cellular component disassembly involved in execution phase of apoptosis
• mitotic nuclear envelope disassembly
• mitotic nuclear envelope reassembly
• spermatogenesis
• muscle organ development
• programmed cell death
• regulation of cell migration
• establishment or maintenance of microtubule cytoskeleton polarity
• endoplasmic reticulum unfolded protein response
• protein localization to nucleus
• sterol regulatory element binding protein import into nucleus
• IRE1-mediated unfolded protein response
• cellular protein metabolic process
• ventricular cardiac muscle cell development
• cellular response to hypoxia
• negative regulation of release of cytochrome c from mitochondria
• positive regulation of cell aging
• regulation of protein localization to nucleus
• negative regulation of extrinsic apoptotic signaling pathway
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Sources: Amigo / QuickGO |
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RNA expression pattern |
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More reference expression data |
Orthologs |
Species |
Human |
Mouse |
Entrez |
4000 |
16905 |
Ensembl |
ENSG00000160789 |
ENSMUSG00000028063 |
UniProt |
P02545 |
P48678 |
RefSeq (mRNA) |
NM_001257374 |
NM_001002011 |
RefSeq (protein) |
NP_001244303 |
NP_001002011 |
Location (UCSC) |
Chr 1:
156.08 – 156.14 Mb |
Chr 3:
88.48 – 88.51 Mb |
PubMed search |
[1] |
[2] |
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Lamin A/C also known as LMNA is a protein that in humans is encoded by the LMNA gene.[1][2] Lamin A/C belongs to the lamin family of proteins.
Contents
- 1 Function
- 2 Clinical significance
- 3 Interactions
- 4 References
- 5 Further reading
- 6 External links
Function
Biogenesis of lamin A in normal cells and the failure to generate mature lamin A in Hutchinson-Gilford progeria syndrome.
In the setting of ZMPSTE24 deficiency, the final step of lamin processing does not occur, resulting in an accumulation of farnesyl-prelamin A. In Hutchinson-Gilford progeria syndrome, a 50-amino acid deletion in prelamin A (amino acids 607–656) removes the site for the second endoproteolytic cleavage. Consequently, no mature lamin A is formed, and a farnesylated mutant prelamin A (progerin) accumulates in cells.[3] The nuclear lamina consist of a two-dimensional matrix of proteins located next to the inner nuclear membrane. The lamin family of proteins make up the matrix and are highly conserved in evolution. During mitosis, the lamina matrix is reversibly disassembled as the lamin proteins are phosphorylated. Lamin proteins are thought to be involved in nuclear stability, chromatin structure and gene expression. Vertebrate lamins consist of two types, A and B. Through alternate splicing, this gene encodes three type A lamin isoforms.[4]
Early in mitosis, maturation promoting factor (abbreviated MPF, also called mitosis-promoting factor or M-phase-promoting factor) phosphorylates specific serine residues in all three nuclear lamins, causing depolymerization of the lamin intermediate filaments. The phosphorylated lamin B dimers remain associated with the nuclear membrane via their isoprenyl anchor. Lamin A is targeted to the nuclear membrane by an isoprenyl group but it is cleaved shortly after arriving at the membrane. It stays associated with the membrane through protein-protein interactions of itself and other membrane associated proteins, such as LAP1. Depolymerization of the nuclear lamins leads to disintegration of the nuclear envelope. Transfection experiments demonstrate that phosphorylation of human lamin A is required for lamin depolymerization, and thus for disassembly of the nuclear envelope, which normally occurs early in mitosis.
Clinical significance
Wild type (left) and mutated (right) form of lamin A (LMNA, PDB: 1IFR). Normally, arginine 527 (blue) forms salt bridge with glutamate 537 (magenta), but R527L substitution results in braking this interaction (leucine is too short to reach glutamate). Models are presented in surface (upper) and in cartoon representation (down).
[5]
Mutations in the LMNA gene are associated with several diseases, including Emery-Dreifuss muscular dystrophy, familial partial lipodystrophy, limb girdle muscular dystrophy, dilated cardiomyopathy, Charcot-Marie-Tooth disease, restrictive dermopathy and Hutchinson-Gilford progeria syndrome. A truncated version of lamin A, commonly known as progerin, causes Hutchinson-Gilford progeria syndrome.[6][7] To date over 1,400 SNPs are known [3]. They can manifest in changes on mRNA, splicing or protein (e.g. Arg471Cys,[8] Arg482Gln,[9] Arg527Leu,[10] Arg527Cys,[11] Ala529Val [12] ) level.
Interactions
LMNA has been shown to interact with:
- ALOX12[13]
- EMD[14][15][16][17]
- NARF[18]
- SREBF1[19]
- TMPO[20][21]
- ZNF239[22]
- SIRT1[23]
References
- ^ Kamat AK, Rocchi M, Smith DI, Miller OJ (March 1993). "Lamin A/C gene and a related sequence map to human chromosomes 1q12.1-q23 and 10". Somat. Cell Mol. Genet. 19 (2): 203–8. doi:10.1007/BF01233534. PMID 8511676.
- ^ Wydner KL, McNeil JA, Lin F, Worman HJ, Lawrence JB (March 1996). "Chromosomal assignment of human nuclear envelope protein genes LMNA, LMNB1, and LBR by fluorescence in situ hybridization". Genomics 32 (3): 474–8. doi:10.1006/geno.1996.0146. PMID 8838815.
- ^ Coutinho HD, Falcão-Silva VS, Gonçalves GF, da Nóbrega RB (2009). "Molecular ageing in progeroid syndromes: Hutchinson-Gilford progeria syndrome as a model". Immun Ageing 6: 4. doi:10.1186/1742-4933-6-4. PMC 2674425. PMID 19379495.
- ^ "Entrez Gene: LMNA lamin A/C".
- ^ Al-Haggar M, Madej-Pilarczyk A, Kozlowski L, Bujnicki JM, Yahia S, Abdel-Hadi D, Shams A, Ahmad N, Hamed S, Puzianowska-Kuznicka M (2012). "A novel homozygous p.Arg527Leu LMNA mutation in two unrelated Egyptian families causes overlapping mandibuloacral dysplasia and progeria syndrome". Eur J Hum Genet. 20 (11): 1134–40. doi:10.1038/ejhg.2012.77. PMC 3476705. PMID 22549407.
- ^ Capell BC, Collins FS (December 2006). "Human laminopathies: nuclei gone genetically awry". Nat. Rev. Genet. 7 (12): 940–52. doi:10.1038/nrg1906. PMID 17139325.
- ^ Rankin J, Ellard S (October 2006). "The laminopathies: a clinical review". Clin. Genet. 70 (4): 261–74. doi:10.1111/j.1399-0004.2006.00677.x. PMID 16965317.
- ^ Zirn B, Kress W, Grimm T, Berthold LD, Neubauer B, Kuchelmeister K, Müller U, Hahn A (2008). "Association of homozygous LMNA mutation R471C with new phenotype: mandibuloacral dysplasia, progeria, and rigid spine muscular dystrophy". Am J Med Genet A 146A (8): 1049–1054. doi:10.1002/ajmg.a.32259. PMID 18348272.
- ^ Cao H, Hegele RA (2002). "Nuclear lamin A/C R482Q mutation in Canadian kindreds with Dunnigan-type familial partial lipodystrophy". Hum. Molec. Genet. 9 (1): 109–12. doi:10.1093/hmg/9.1.109. PMID 10587585.
- ^ Al-Haggar M, Madej-Pilarczyk A, Kozlowski L, Bujnicki JM, Yahia S, Abdel-Hadi D, Shams A, Ahmad N, Hamed S, Puzianowska-Kuznicka M (2012). "A novel homozygous p.Arg527Leu LMNA mutation in two unrelated Egyptian families causes overlapping mandibuloacral dysplasia and progeria syndrome". Eur J Hum Genet. 20 (11): 1134–40. doi:10.1038/ejhg.2012.77. PMC 3476705. PMID 22549407.
- ^ Agarwal AK, Kazachkova I, Ten S, Garg A (2008). "Severe mandibuloacral dysplasia-associated lipodystrophy and progeria in a young girl with a novel homozygous Arg527Cys LMNA mutation". J Clin Endocrinol Metab 93 (12): 4617–4623. doi:10.1210/jc.2008-0123. PMC 2626450. PMID 18796515.
- ^ Garg A, Cogulu O, Ozkinay F, Onay H, Agarwal AK (2005). "A novel homozygous Ala529Val LMNA mutation in Turkish patients with mandibuloacral dysplasia". J. Clin. Endocrinol. Metab. 90 (9): 5259–64. doi:10.1210/jc.2004-2560. PMID 15998779.
- ^ Tang K, Finley RL, Nie D, Honn KV (March 2000). "Identification of 12-lipoxygenase interaction with cellular proteins by yeast two-hybrid screening". Biochemistry 39 (12): 3185–91. doi:10.1021/bi992664v. PMID 10727209.
- ^ Wilkinson FL, Holaska JM, Zhang Z, Sharma A, Manilal S, Holt I, Stamm S, Wilson KL, Morris GE (June 2003). "Emerin interacts in vitro with the splicing-associated factor, YT521-B". Eur. J. Biochem. 270 (11): 2459–66. doi:10.1046/j.1432-1033.2003.03617.x. PMID 12755701.
- ^ Lattanzi G, Cenni V, Marmiroli S, Capanni C, Mattioli E, Merlini L, Squarzoni S, Maraldi NM (April 2003). "Association of emerin with nuclear and cytoplasmic actin is regulated in differentiating myoblasts". Biochem. Biophys. Res. Commun. 303 (3): 764–70. doi:10.1016/S0006-291X(03)00415-7. PMID 12670476.
- ^ Sakaki M, Koike H, Takahashi N, Sasagawa N, Tomioka S, Arahata K, Ishiura S (February 2001). "Interaction between emerin and nuclear lamins". J. Biochem. 129 (2): 321–7. doi:10.1093/oxfordjournals.jbchem.a002860. PMID 11173535.
- ^ Clements L, Manilal S, Love DR, Morris GE (January 2000). "Direct interaction between emerin and lamin A". Biochem. Biophys. Res. Commun. 267 (3): 709–14. doi:10.1006/bbrc.1999.2023. PMID 10673356.
- ^ Barton RM, Worman HJ (October 1999). "Prenylated prelamin A interacts with Narf, a novel nuclear protein". J. Biol. Chem. 274 (42): 30008–18. doi:10.1074/jbc.274.42.30008. PMID 10514485.
- ^ Lloyd DJ, Trembath RC, Shackleton S (April 2002). "A novel interaction between lamin A and SREBP1: implications for partial lipodystrophy and other laminopathies". Hum. Mol. Genet. 11 (7): 769–77. doi:10.1093/hmg/11.7.769. PMID 11929849.
- ^ Markiewicz E, Dechat T, Foisner R, Quinlan RA, Hutchison CJ (December 2002). "Lamin A/C binding protein LAP2alpha is required for nuclear anchorage of retinoblastoma protein". Mol. Biol. Cell 13 (12): 4401–13. doi:10.1091/mbc.E02-07-0450. PMC 138642. PMID 12475961.
- ^ Dechat T, Korbei B, Vaughan OA, Vlcek S, Hutchison CJ, Foisner R (October 2000). "Lamina-associated polypeptide 2alpha binds intranuclear A-type lamins". J. Cell. Sci. 113 (19): 3473–84. PMID 10984438.
- ^ Dreuillet C, Tillit J, Kress M, Ernoult-Lange M (November 2002). "In vivo and in vitro interaction between human transcription factor MOK2 and nuclear lamin A/C". Nucleic Acids Res. 30 (21): 4634–42. doi:10.1093/nar/gkf587. PMC 135794. PMID 12409453.
- ^ Liu B, Ghosh S, Yang X, Zheng H, Liu X, Wang Z, Jin G, Zheng B, Kennedy BK, Suh Y, Kaeberlein M, Tryggvason K, Zhou Z (2012). "Resveratrol Rescues SIRT1-Dependent Adult Stem Cell Decline and Alleviates Progeroid Features in Laminopathy-Based Progeria". Cell Metabolism 16 (6): 738–750. doi:10.1016/j.cmet.2012.11.007. PMID 23217256.
Further reading
- Gruenbaum Y, Wilson KL, Harel A, Goldberg M, Cohen M (2000). "Review: nuclear lamins--structural proteins with fundamental functions". J. Struct. Biol. 129 (2–3): 313–23. doi:10.1006/jsbi.2000.4216. PMID 10806082.
- Worman HJ, Courvalin JC (2000). "The inner nuclear membrane". J. Membr. Biol. 177 (1): 1–11. doi:10.1007/s002320001096. PMID 10960149.
- Burke B, Mounkes LC, Stewart CL (2002). "The nuclear envelope in muscular dystrophy and cardiovascular diseases". Traffic 2 (10): 675–83. doi:10.1034/j.1600-0854.2001.21001.x. PMID 11576443.
- Mounkes LC, Burke B, Stewart CL (2001). "The A-type lamins: nuclear structural proteins as a focus for muscular dystrophy and cardiovascular diseases". Trends Cardiovasc. Med. 11 (7): 280–5. doi:10.1016/S1050-1738(01)00126-8. PMID 11709282.
- Vigouroux C, Magré J, Desbois-Mouthon C, Lascols O, Cherqui G, Caron M, Capeau J (2002). "[Major insulin resistance syndromes: clinical and physiopathological aspects]". J. Soc. Biol. 195 (3): 249–57. PMID 11833462.
- Helbling-Leclerc A, Bonne G, Schwartz K (2002). "Emery-Dreifuss muscular dystrophy". Eur. J. Hum. Genet. 10 (3): 157–61. doi:10.1038/sj.ejhg.5200744. PMID 11973618.
- Burke B, Stewart CL (2002). "Life at the edge: the nuclear envelope and human disease". Nat. Rev. Mol. Cell Biol. 3 (8): 575–85. doi:10.1038/nrm879. PMID 12154369.
- Novelli G, D'Apice MR (2004). "The strange case of the "lumper" lamin A/C gene and human premature ageing". Trends in molecular medicine 9 (9): 370–5. doi:10.1016/S1471-4914(03)00162-X. PMID 13129702.
- Pasotti M, Repetto A, Pisani A, Arbustini E (2004). "[Diseases associated with lamin A/C gene defects: what the clinical cardiologist ought to know]". Italian heart journal. Supplement : official journal of the Italian Federation of Cardiology 5 (2): 98–111. PMID 15080529.
- Al-Shali KZ, Hegele RA (2005). "Laminopathies and atherosclerosis". Arterioscler. Thromb. Vasc. Biol. 24 (9): 1591–5. doi:10.1161/01.ATV.0000136392.59656.8b. PMID 15205220.
- Garg A, Cogulu O, Ozkinay F, Onay H, Agarwal AK (2005). "A novel homozygous Ala529Val LMNA mutation in Turkish patients with mandibuloacral dysplasia". J. Clin. Endocrinol. Metab. 90 (9): 5259–64. doi:10.1210/jc.2004-2560. PMID 15998779.
- Lees-Miller SP (2006). "Dysfunction of lamin A triggers a DNA damage response and cellular senescence". DNA Repair (Amst.) 5 (2): 286–9. doi:10.1016/j.dnarep.2005.10.007. PMID 16344005.
- Donadille B, Lascols O, Capeau J, Vigouroux C (2006). "Etiological investigations in apparent type 2 diabetes: when to search for lamin A/C mutations?". Diabetes Metab. 31 (6): 527–32. doi:10.1016/S1262-3636(07)70227-6. PMID 16357800.
- Young SG, Meta M, Yang SH, Fong LG (2007). "Prelamin A farnesylation and progeroid syndromes". J. Biol. Chem. 281 (52): 39741–5. doi:10.1074/jbc.R600033200. PMID 17090536.
- Halaschek-Wiener J, Brooks-Wilson A (2007). "Progeria of stem cells: stem cell exhaustion in Hutchinson-Gilford progeria syndrome". J. Gerontol. A Biol. Sci. Med. Sci. 62 (1): 3–8. doi:10.1093/gerona/62.1.3. PMID 17301031.
- Mazereeuw-Hautier J, Wilson LC, Mohammed S, Smallwood D, Shackleton S, Atherton DJ, Harper JI (2007). "Hutchinson-Gilford progeria syndrome: clinical findings in three patients carrying the G608G mutation in LMNA and review of the literature". Br. J. Dermatol. 156 (6): 1308–14. doi:10.1111/j.1365-2133.2007.07897.x. PMID 17459035.
- Sliwińska MA (2007). "[The role of lamins and mutations of LMNA gene in physiological and premature aging] Polish". Postepy Biochem. 53 (1): 46–52. PMID 17718387.
- Genschel J, Schmidt HH (December 2000). "Mutations in the LMNA gene encoding lamin A/C". Hum. Mutat. 16 (6): 451–9. doi:10.1002/1098-1004(200012)16:6<451::AID-HUMU1>3.0.CO;2-9. PMID 11102973.
- Scaffidi P, Misteli T (April 2005). "Reversal of the cellular phenotype in the premature aging disease Hutchinson-Gilford progeria syndrome". Nat Med. 11 (4): 440–5. doi:10.1038/nm1204. PMC 1351119. PMID 15750600.
- "Charcot-Marie-Tooth Neuropathy Type 2". 1993. PMID 20301462.
- "Congenital Muscular Dystrophy Overview". 1993. PMID 20301468.
- "LMNA-Related Dilated Cardiomyopathy". 1993. PMID 20301717.
- "Limb-Girdle Muscular Dystrophy Overview". 1993. PMID 20301582.
- "Emery-Dreifuss Muscular Dystrophy". 1993. PMID 20301609.
- "Hutchinson-Gilford Progeria Syndrome". 1993. PMID 20301300.
- "Dense Deposit Disease/Membranoproliferative Glomerulonephritis Type II". 1993. PMID 20301598.
External links
- Online 'Mendelian Inheritance in Man' (OMIM) Cardiomyopathy, Dilated, 1A; CMD1A -115200
- Online 'Mendelian Inheritance in Man' (OMIM) LAMIN A/C; LMNA -150330
- LMNA protein, human at the US National Library of Medicine Medical Subject Headings (MeSH)
- LOVD mutation database: LMNA
- GeneCards for LMNA
PDB gallery
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1ifr: Structure of Lamin A/C Globular Domain
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1ivt: NMR structures of the C-terminal globular domain of human lamin A/C
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1ufg: Solution structure of immunoglobulin like domain of mouse nuclear lamin
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1x8y: Human lamin coil 2B
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Proteins of the cytoskeleton
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Human |
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Nonhuman |
- Major sperm proteins
- Prokaryotic cytoskeleton
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See also: cytoskeletal defects
Index of cells
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Description |
- Structure
- Organelles
- peroxisome
- cytoskeleton
- centrosome
- epithelia
- cilia
- mitochondria
- Membranes
- Membrane transport
- ion channels
- vesicular transport
- solute carrier
- ABC transporters
- ATPase
- oxidoreduction-driven
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Disease |
- Structural
- peroxisome
- cytoskeleton
- cilia
- mitochondria
- nucleus
- scleroprotein
- Membrane
- channelopathy
- solute carrier
- ATPase
- ABC transporters
- other
- extracellular ligands
- cell surface receptors
- intracellular signalling
- Vesicular transport
- Pore-forming toxins
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UpToDate Contents
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English Journal
- Bilateral stenosis of carotid siphon in Hutchinson-Gilford progeria syndrome.
- Narazaki R, Makimura M, Sanefuji M, Fukamachi S, Akiyoshi H, So H, Yamamura K, Doisaki S, Kojima S, Ihara K, Hara T, Ohga S.SourceDivision of Pediatrics, Tagawa Municipal Hospital, Fukuoka, Japan; Department of Pediatrics, Graduate School of Medical Sciences, Kyushu University, Fukuoka, Japan.
- Brain & development.Brain Dev.2013 Aug;35(7):690-3. doi: 10.1016/j.braindev.2012.10.008. Epub 2012 Nov 8.
- Hutchinson-Gilford progeria syndrome (HGPS) is a rare premature aging disease, caused by a de novo mutation of lamin-A gene, LMNA G608G. Accumulation of abnormal lamin-A (progerin) compromises nuclear membrane integrity and results in the accelerated senescence. Affected patients show a typical feat
- PMID 23141186
- Human Ng2+ adipose stem cells loaded in vivo on a new crosslinked hyaluronic acid-Lys scaffold fabricate a skeletal muscle tissue.
- Desiderio V, De Francesco F, Schiraldi C, De Rosa A, La Gatta A, Paino F, d'Aquino R, Ferraro GA, Tirino V, Papaccio G.SourceDipartimento di Medicina Sperimentale, Sezione di Istologia ed Embriologia Medica, Tissue Engineering and Regenerative (TERM), Seconda Università degli Studi di Napoli, Napoli, Italy.
- Journal of cellular physiology.J Cell Physiol.2013 Aug;228(8):1762-73. doi: 10.1002/jcp.24336.
- Mesenchymal stem cell (MSC) therapy holds promise for treating diseases and tissue repair. Regeneration of skeletal muscle tissue that is lost during pathological muscle degeneration or after injuries is sustained by the production of new myofibers. Human Adipose stem cells (ASCs) have been reported
- PMID 23359523
Japanese Journal
- A new c.1621 C>G, p.R541G lamin A/C mutation in a family with DCM and regional wall motion abnormalities (akinesis/dyskinesis): genotype-phenotype correlation
- Malek Lukasz A.,Labib Sarah,Mazurkiewicz Lukasz [他]
- Journal of human genetics 56(1), 83-86, 2011-01
- NAID 40017436400
- 2.家族性ペースメーカー植込み症例における遺伝的背景の検討 : ―心臓Na+チャネル病,Lamin A/C遺伝子関連心筋症―
- 牧山 武,静田 聡,赤尾 昌治,木村 剛,堀江 稔
- 心電図 30(3), 200-208, 2010
- … 子解析の結果,33例中17例(51.5%)に心臓Na+チャネル遺伝子(SCN5A),またはLamin A/C遺伝子(LMNA)異常を同定した〔SCN5A異常8/33例(24.2%),LMNA異常9/33例(27.2%)〕.SCN5A異常を検出した8例中5例には,ほかの心臓Na+チャネル病の合併(Brugada症候群4例,QT延長症候群1例)を認めた.一方,LMNAは核膜の裏打ち蛋白であるLamin A,Cをコードし,その遺伝子異常により拡張型心筋症,心臓伝導障害,致死 …
- NAID 130000432005
Related Links
- The nuclear lamina consists of a two-dimensional matrix of proteins located next to the inner nuclear membrane. The lamin family of proteins make up the matrix and are highly conserved in evolution. During mitosis, the lamina matrix is ...
★リンクテーブル★
[★]
- 英
- caspase
- 同
- ICEファミリープロテアーゼ ICE family protease
ヒトICEプロテアーゼスーパーファミリー
Family
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Caspase
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Other Name
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Recognition
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Target (Truncation site)
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caspase-1
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caspase-1
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ICE
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WEHD
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pro IL-1β (FEAD/G, YVHD/A), procaspase-3, procaspase-4
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caspase-4
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ICErel-II, TX, ICH-2
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caspase-5
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ICErel-III, TY
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caspase-2
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caspase-2
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ICH-1
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DEHD
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PARP (DEVD/G)
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caspase-9
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ICE-LAP6, Mch6
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LEHD
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PARP, procaspase-3
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caspase-3
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caspase-3
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CPP32, Yama
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DEVD
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PARP, SREBP (DEPD/S), U1snRNP (DGPD/G), lamin B, D4-GDI (DELD/S), DNA-PK (DEVD/N), DFF (DETD/S, DAVD/T), actin (ELPD/G) ?, PKCδ (DMQD/N) ?]]
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caspase-7
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Mch3, ICE-LAP3, CMH-1
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DEVD
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PARP, procaspase-6
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caspase-6
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Mch2
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VEHD
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lamin A (VEID/N)]]
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caspase-8
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FLICE, MACH, Mch5
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LETD
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procaspase-3, Bid
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caspase-10
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Mch4
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LEXD
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caspase-11
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Ich3
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[★]
- 英
- lamin A、lamin type A
[★]
[★]
- 関
- adenoviral、adenovirus