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

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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 is an enzymatic protein belonging to the peptidase (or protease) families. In humans, it is coded by the CTSB gene.^[1]^[2]

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]

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.

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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UpToDate Contents

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Biomaterials.Biomaterials.2015 Aug;59:88-101. doi: 10.1016/j.biomaterials.2015.03.039. Epub 2015 May 15.
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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 Pictures

★リンクテーブル★

「B」

Cathepsin B
	; Rendering of 1CSB
Available structures
PDB	Ortholog search: PDBe, RCSB
List of PDB id codes
	1CSB, 1GMY, 1HUC, 1PBH, 2IPP, 2PBH, 3AI8, 3CBJ, 3CBK, 3K9M, 3PBH
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;
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;
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;
	Sources: Amigo / QuickGO
RNA expression pattern
	More reference expression data
Orthologs
	This box: view; talk; edit;

　　[★]

気管分岐部下緑
補体のalternative pathwayに関わる蛋白質

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

[pmid3463996-1] 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.

[pmid8112600-2] 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.

[entrez-3] "Entrez Gene: CTSB cathepsin B". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1508.

[pmid16982417-4] 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.

[pmid17238044-5] Tandon RK (January 2007). "Tropical pancreatitis". J. Gastroenterol. 42 (Suppl 17): 141–7. doi:10.1007/s00535-006-1930-y. PMID 17238044.

[pmid14503883-6] 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.

[pmid11514663-7] 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.

[pmid10777578-8] 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.

[pmid9585570-9] 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.

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案内

cathepsin B