カテプシンB
WordNet
- the 2nd letter of the Roman alphabet (同)b
- the blood group whose red cells carry the B antigen (同)type_B, group B
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2013/03/28 13:54:02」(JST)
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| Cathepsin B |
Rendering of 1CSB |
| Available structures |
| PDB |
Ortholog search: PDBe, RCSB |
| List of PDB id codes |
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1CSB, 1GMY, 1HUC, 1PBH, 2IPP, 2PBH, 3AI8, 3CBJ, 3CBK, 3K9M, 3PBH
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| Identifiers |
| Symbols |
CTSB; APPS; CPSB |
| External IDs |
OMIM: 116810 MGI: 88561 HomoloGene: 37550 ChEMBL: 4072 GeneCards: CTSB Gene |
| EC number |
3.4.22.1 |
| Gene Ontology |
| Molecular function |
• cysteine-type endopeptidase activity
• protein binding
• peptidase activity
• cysteine-type peptidase activity
• kininogen binding
• peptide binding
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| Cellular component |
• extracellular space
• intracellular
• nucleolus
• mitochondrion
• lysosome
• caveola
• external side of plasma membrane
• apical plasma membrane
• endolysosome lumen
• sarcolemma
• melanosome
• intracellular membrane-bounded organelle
• perinuclear region of cytoplasm
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| Biological process |
• proteolysis
• autophagy
• skeletal muscle tissue development
• response to wounding
• response to mechanical stimulus
• response to glucose stimulus
• response to organic cyclic compound
• response to amine stimulus
• regulation of apoptotic process
• response to peptide hormone stimulus
• innate immune response
• response to ethanol
• regulation of catalytic activity
• negative regulation of cell death
• response to interleukin-4
• cellular response to thyroid hormone stimulus
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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 |
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| Entrez |
1508 |
13030 |
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| Ensembl |
ENSG00000164733 |
ENSMUSG00000021939 |
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| UniProt |
P07858 |
P10605 |
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| RefSeq (mRNA) |
NM_001908 |
NM_007798 |
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| RefSeq (protein) |
NP_001899 |
NP_031824 |
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| Location (UCSC) |
Chr 8:
11.7 – 11.73 Mb |
Chr 14:
63.12 – 63.15 Mb |
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| PubMed search |
[1] |
[2] |
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Cathepsin B is an enzymatic protein belonging to the peptidase (or protease) families. In humans, it is coded by the CTSB gene.[1][2]
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Contents
- 1 Function
- 2 Clinical significance
- 3 Interactions
- 4 See also
- 5 References
- 6 Further reading
- 7 External links
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Function
The protein encoded by this gene is a lysosomal cysteine protease composed of a dimer of disulfide-linked heavy and light chains, both produced from a single protein precursor. It is a member of the peptidase C1 family. At least five transcript variants encoding the same protein have been found for this gene.[3]
Clinical significance
Cathepsin B was once suspected as a candidate protease participating in the conversion of β-amyloid precursor protein into the amyloid plaques found in Alzheimer's disease patients. However, this function is now known to be mediated by BACE1 protease. It is now thought that cathepsin B can degrade β-amyloid precursor protein into harmless fragments. Thus, it is conceivable cathepsin B may play a pivotal role in the natural defense against Alzheimer's disease.[4] Overexpression of cathepsin B has been associated with esophageal adenocarcinoma and other tumors.[3]
Mutations in the CTSB gene have been linked to tropical pancreatitis, a form of chronic pancreatitis.[5]
Interactions
Cathepsin B has been shown to interact with cystatin B,[6][7] S100A10[8] and cystatin A.[6][9]
See also
References
- ^ Chan SJ, San Segundo B, McCormick MB, Steiner DF (October 1986). "Nucleotide and predicted amino acid sequences of cloned human and mouse preprocathepsin B cDNAs". Proc. Natl. Acad. Sci. U.S.A. 83 (20): 7721–5. doi:10.1073/pnas.83.20.7721. PMC 386793. PMID 3463996.
- ^ Cao L, Taggart RT, Berquin IM, Moin K, Fong D, Sloane BF (February 1994). "Human gastric adenocarcinoma cathepsin B: isolation and sequencing of full-length cDNAs and polymorphisms of the gene". Gene 139 (2): 163–9. doi:10.1016/0378-1119(94)90750-1. PMID 8112600.
- ^ a b "Entrez Gene: CTSB cathepsin B". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1508.
- ^ Mueller-Steiner S, Zhou Y, Arai H, Roberson ED, Sun B, Chen J, Wang X, Yu G, Esposito L, Mucke L, Gan L (September 2006). "Antiamyloidogenic and neuroprotective functions of cathepsin B: implications for Alzheimer's disease". Neuron 51 (6): 703–14. doi:10.1016/j.neuron.2006.07.027. PMID 16982417. Lay summary – Science Blog.
- ^ Tandon RK (January 2007). "Tropical pancreatitis". J. Gastroenterol. 42 (Suppl 17): 141–7. doi:10.1007/s00535-006-1930-y. PMID 17238044.
- ^ a b Pavlova A, Björk I (September 2003). "Grafting of features of cystatins C or B into the N-terminal region or second binding loop of cystatin A (stefin A) substantially enhances inhibition of cysteine proteinases". Biochemistry 42 (38): 11326–33. doi:10.1021/bi030119v. PMID 14503883.
- ^ Pol E, Björk I (September 2001). "Role of the single cysteine residue, Cys 3, of human and bovine cystatin B (stefin B) in the inhibition of cysteine proteinases". Protein Sci. 10 (9): 1729–38. doi:10.1110/ps.11901. PMC 2253190. PMID 11514663.
- ^ Mai J, Finley RL, Waisman DM, Sloane BF (April 2000). "Human procathepsin B interacts with the annexin II tetramer on the surface of tumor cells". J. Biol. Chem. 275 (17): 12806–12. doi:10.1074/jbc.275.17.12806. PMID 10777578.
- ^ Estrada S, Nycander M, Hill NJ, Craven CJ, Waltho JP, Björk I (May 1998). "The role of Gly-4 of human cystatin A (stefin A) in the binding of target proteinases. Characterization by kinetic and equilibrium methods of the interactions of cystatin A Gly-4 mutants with papain, cathepsin B, and cathepsin L". Biochemistry 37 (20): 7551–60. doi:10.1021/bi980026r. PMID 9585570.
Further reading
- Yan S, Sloane BF (2004). "Molecular regulation of human cathepsin B: implication in pathologies.". Biol. Chem. 384 (6): 845–54. doi:10.1515/BC.2003.095. PMID 12887051.
External links
- The MEROPS online database for peptidases and their inhibitors: C01.060
- Cathepsin B at the US National Library of Medicine Medical Subject Headings (MeSH)
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PDB gallery
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1csb: CRYSTAL STRUCTURE OF CATHEPSIN B INHIBITED WITH CA030 AT 2.1 ANGSTROMS RESOLUTION: A BASIS FOR THE DESIGN OF SPECIFIC EPOXYSUCCINYL INHIBITORS
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1gmy: CATHEPSIN B COMPLEXED WITH DIPEPTIDYL NITRILE INHIBITOR
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1huc: THE REFINED 2.15 ANGSTROMS X-RAY CRYSTAL STRUCTURE OF HUMAN LIVER CATHEPSIN B: THE STRUCTURAL BASIS FOR ITS SPECIFICITY
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1pbh: CRYSTAL STRUCTURE OF HUMAN RECOMBINANT PROCATHEPSIN B AT 3.2 ANGSTROM RESOLUTION
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1sp4: Crystal structure of NS-134 in complex with bovine cathepsin B: a two headed epoxysuccinyl inhibitor extends along the whole active site cleft
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2ipp: Crystal Structure of the tetragonal form of human liver cathepsin B
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2pbh: CRYSTAL STRUCTURE OF HUMAN PROCATHEPSIN B AT 3.3 ANGSTROM RESOLUTION
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3pbh: REFINED CRYSTAL STRUCTURE OF HUMAN PROCATHEPSIN B AT 2.5 ANGSTROM RESOLUTION
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Proteases: cysteine proteases (EC 3.4.22)
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| Caspase |
- Caspase 1
- Caspase 2
- Caspase 3
- Caspase 4
- Caspase 5
- Caspase 6
- Caspase 7
- Caspase 8
- Caspase 9
- Caspase 10
- Caspase 12
- Caspase 13
- Caspase 14
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| Fruit-derived |
- Papain
- Ficain
- Bromelain
- Actinidain
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| Calpain |
- CAPN1
- CAPN2
- CAPN3
- CAPN5
- CAPN6
- CAPN7
- CAPN8
- CAPN9
- CAPN10
- CAPN11
- CAPN12
- CAPN13
- CAPN14
- CAPNS1
- CAPNS2
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| Cathepsin |
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| Other |
- Clostripain
- Cancer procoagulant
- Separase
- Autophagin
- Cruzipain
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- B
- enzm
- 1.1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 10
- 11
- 13
- 14
- 15-18
- 2.1
- 2.7.10
- 2.7.11-12
- 3.1
- 4.1
- 5.1
- 6.1-3
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UpToDate Contents
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English Journal
- Synthesis of a novel, sequentially active-targeted drug delivery nanoplatform for breast cancer therapy.
- Satsangi A1, Roy SS2, Satsangi RK3, Tolcher AW4, Vadlamudi RK2, Goins B5, Ong JL6.
- Biomaterials.Biomaterials.2015 Aug;59:88-101. doi: 10.1016/j.biomaterials.2015.03.039. Epub 2015 May 15.
- Breast cancer is the leading cause of cancer deaths among women. Paclitaxel (PTX), an important breast cancer medicine, exhibits reduced bioavailability and therapeutic index due to high hydrophobicity and indiscriminate cytotoxicity. PTX encapsulation in one-level active targeting overcomes such ba
- PMID 25956854
- Synergistic Costimulatory Effect of Chlamydia pneumoniae with Carbon Nanoparticles on NLRP3 Inflammasome-Mediated Interleukin-1β Secretion in Macrophages.
- Matsuo J1, Nakamura S2, Takeda S3, Ishida K4, Yamazaki T4, Yoshida M5, Chiba H6, Hui SP7, Yamaguchi H8.
- Infection and immunity.Infect Immun.2015 Jul;83(7):2917-25. doi: 10.1128/IAI.02968-14. Epub 2015 May 4.
- The obligate intracellular bacterium Chlamydia pneumoniae is not only a causative agent of community-acquired pneumonia but is also associated with a more serious chronic disease, asthma, which might be exacerbated by air pollution containing carbon nanoparticles. Although a detailed mechanism of ex
- PMID 25939513
- Azadirachtin-induced apoptosis involves lysosomal membrane permeabilization and cathepsin L release in Spodoptera frugiperda Sf9 cells.
- Wang Z1, Cheng X2, Meng Q1, Wang P1, Shu B1, Hu Q1, Hu M3, Zhong G4.
- The international journal of biochemistry & cell biology.Int J Biochem Cell Biol.2015 Jul;64:126-35. doi: 10.1016/j.biocel.2015.03.018. Epub 2015 Apr 4.
- Azadirachtin as a kind of botanical insecticide has been widely used in pest control. We previously reported that azadirachtin could induce apoptosis of Spodoptera litura cultured cell line Sl-1, which involves in the up-regulation of P53 protein. However, the detailed mechanism of azadirachtin-indu
- PMID 25849458
Japanese Journal
- Amyloid β oligomers induce interleukin-1β production in primary microglia in a cathepsin B- and reactive oxygen species-dependent manner.
- Taneo Jun,Adachi Takumi,Yoshida Aiko,Takayasu Kunio,Takahara Kazuhiko,Inaba Kayo
- Biochemical and biophysical research communications 458(3), 561-567, 2015-03-13
- … Moreover, Aβ oligomers induced endo/phagolysosome rupture, which released cathepsin B into the cytoplasm. … Aβ oligomer-induced IL-1β production was inhibited not only by the cathepsin B inhibitor CA-074-Me but also by the reactive oxygen species (ROS) inhibitor N-acetylcysteine. … These results indicate that Aβ oligomers, but not fibrils, induce IL-1β production in primary microglia in a cathepsin B- and ROS-dependent manner. …
- NAID 120005575184
- CTSK inhibitor exert its anti-obesity effects through regulating adipocyte differentiation in high-fat diet induced obese mice
- , , , , , ,
- Endocrine Journal 62(4), 309-317, 2015
- … Cathepsin k (CTSK) is highly expressed in adipose tissues of obese patients and animal models. …
- NAID 130005066938
- Inhibition of cathepsin B activity reduces apoptosis by preventing cytochrome c release from mitochondria in porcine parthenotes
- , , , ,
- Journal of Reproduction and Development advpub(0), 2015
- … Cathepsin B, a lysosomal cysteine protease of the papain family, has recently been implicated in the quality and developmental competence of bovine preimplantation embryos. … In this study, to determine whether inhibition of cathepsin B activity can improve porcine oocyte maturation and early embryo developmental competence, we supplemented in vitro maturation or embryo culture media with E-64, a cathepsin B inhibitor. …
- NAID 130005065842
Related Links
- Cathepsin B が切断することにより検出可能な蛍光を生じる蛍光ペプチド基質を使用して，Cathepsin B の酵素活性を 高感度に約 1 時間で測定できるキットです。 ※ 本製品は研究用です。臨床用途には使用できません。
- ^Chan S, San Segundo B, McCormick M, Steiner D (October 1986). "Nucleotide and predicted amino acid sequences of cloned human and mouse preprocathepsin B cDNAs". Proc. Natl. Acad. Sci. U.S.A. 83 (20): 7721–5. doi:10 ...
★リンクテーブル★
[★]
- Mg2+存在下でC3, B, Dが反応してC3bBbとなり、これがC3転換酵素(C3bBb)あるいはC5転換酵素(C3bBb3b)を形成する。これらはP(properdin)と結合して活性化し、それぞれC3、C5を活性化する