関: ribonuclease A、RNase A

WordNet

of or involving the pancreas; "pancreatic cancer"
a transferase that catalyzes the hydrolysis of ribonucleic acid (同)ribonucleinase, RNase

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2016/07/13 21:33:58」(JST)

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Pancreatic ribonucleases (EC 3.1.27.5, RNase, RNase I, RNase A, pancreatic RNase, ribonuclease I, endoribonuclease I, ribonucleic phosphatase, alkaline ribonuclease, ribonuclease, gene S glycoproteins, Ceratitis capitata alkaline ribonuclease, SLSG glycoproteins, gene S locus-specific glycoproteins, S-genotype-assocd. glycoproteins, ribonucleate 3'-pyrimidino-oligonucleotidohydrolase) are pyrimidine-specific endonucleases found in high quantity in the pancreas of certain mammals and of some reptiles.^[1]

Specifically, the enzymes are involved in endonucleolytic cleavage of 3'-phosphomononucleotides and 3'-phosphooligonucleotides ending in C-P or U-P with 2',3'-cyclic phosphate intermediates. Ribonuclease can unwind the RNA helix by complexing with single-stranded RNA; the complex arises by an extended multi-site cation-anion interaction between lysine and arginine residues of the enzyme and phosphate groups of the nucleotides.

Notable family members

Bovine pancreatic ribonuclease is the best-studied member of the family and has served as a model system in work related to protein folding, disulfide bond formation, protein crystallography and spectroscopy, and protein dynamics.^[2]

Other proteins belonging to the pancreatic ribonuclease superfamily include: bovine seminal vesicle and brain ribonucleases; kidney non-secretory ribonucleases;^[3] liver-type ribonucleases;^[4] angiogenin, which induces vascularisation of normal and malignant tissues; eosinophil cationic protein,^[5] a cytotoxin and helminthotoxin with ribonuclease activity; and frog liver ribonuclease and frog sialic acid-binding lectin. The sequence of pancreatic ribonucleases contains four conserved disulfide bonds and three amino acid residues involved in the catalytic activity.^[6]

Human genes

Human genes encoding proteins containing this domain include:

ANG,
RNASE1, RNASE10, RNASE12, RNASE2, RNASE3, RNASE4, RNASE6, RNASE7, and RNASE8.

Cytotoxicity

Some members of the pancreatic ribonuclease family have cytotoxic effects. Mammalian cells are protected from these effects due to their extremely high affinity for ribonuclease inhibitor (RI), which protects cellular RNA from degradation by pancreatic ribonucleases.^[7] Pancreatic ribonucleases that are not inhibited by RI are approximately as toxic as alpha-sarcin, diphtheria toxin, or ricin.^[8]

Two pancreatic ribonucleases isolated from the oocytes of the Northern leopard frog - amphinase and ranpirnase - are not inhibited by RI and show differential cytotoxicity against tumor cells.^[9] Ranpirnase was studied in a Phase III clinical trial as a treatment candidate for mesothelioma, but the trial did not demonstrate statistical significance against primary endpoints.^[10]

References

^ Beintema JJ, van der Laan JM (1986). "Comparison of the structure of turtle pancreatic ribonuclease with those of mammalian ribonucleases". FEBS Lett. 194 (2): 338–343. doi:10.1016/0014-5793(86)80113-2. PMID 3940901.
^ Marshall GR, Feng JA, Kuster DJ (2008). "Back to the future: ribonuclease A". Biopolymers 90 (3): 259–77. doi:10.1002/bip.20845. PMID 17868092.
^ Rosenberg HF, Tenen DG, Ackerman SJ (1989). "Molecular cloning of the human eosinophil-derived neurotoxin: a member of the ribonuclease gene family". Proc. Natl. Acad. Sci. U.S.A. 86 (12): 4460–4464. doi:10.1073/pnas.86.12.4460. PMC 287289. PMID 2734298.
^ Hofsteenge J, Matthies R, Stone SR (1989). "Primary structure of a ribonuclease from porcine liver, a new member of the ribonuclease superfamily". Biochemistry 28 (25): 9806–9813. doi:10.1021/bi00451a040. PMID 2611266.
^ Rosenberg HF, Ackerman SJ, Tenen DG (1989). "Human eosinophil cationic protein. Molecular cloning of a cytotoxin and helminthotoxin with ribonuclease activity". J. Exp. Med. 170 (1): 163–176. doi:10.1084/jem.170.1.163. PMC 2189377. PMID 2473157.
^ Raines RT (1998). "Ribonuclease A". Chem. Rev. 98 (3): 1045–1066. doi:10.1021/cr960427h. PMID 11848924.
^ Gaur, D; Swaminathan, S; Batra, JK (6 July 2001). "Interaction of human pancreatic ribonuclease with human ribonuclease inhibitor. Generation of inhibitor-resistant cytotoxic variants.". The Journal of Biological Chemistry 276 (27): 24978–84. doi:10.1074/jbc.m102440200. PMID 11342552.
^ Saxena, SK; Rybak, SM; Winkler, G; Meade, HM; McGray, P; Youle, RJ; Ackerman, EJ (5 November 1991). "Comparison of RNases and toxins upon injection into Xenopus oocytes.". The Journal of Biological Chemistry 266 (31): 21208–14. PMID 1939163.
^ Lee JE, Raines RT (2008). "Ribonucleases as novel chemotherapeutics : the ranpirnase example". BioDrugs 22 (1): 53–58. doi:10.2165/00063030-200822010-00006. PMC 2802594. PMID 18215091.
^ "Alfacell Annual Report 2009" (PDF). Retrieved 2 February 2015.

This article incorporates text from the public domain Pfam and InterPro IPR001427

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English Journal

The multiple forms of bovine seminal ribonuclease: Structure and stability of a C-terminal swapped dimer.

Sica F, Pica A, Merlino A, Russo Krauss I, Ercole C, Picone D.SourceDepartment of Chemical Sciences, University of Naples 'Federico II', via Cintia, 80126 Naples, Italy; Institute of Biostructures and Bioimaging, CNR, Via Mezzocannone 16, 80134 Naples, Italy; National Institute Biostructures and Biosystems, Inter-University Consortium, Viale Medaglie d'Oro 305, I-00136 Rome, Italy.
FEBS letters.FEBS Lett.2013 Nov 29;587(23):3755-62. doi: 10.1016/j.febslet.2013.10.003. Epub 2013 Oct 15.
Bovine seminal ribonuclease (BS-RNase) acquires an interesting anti-tumor activity associated with the swapping on the N-terminal. The first direct experimental evidence on the formation of a C-terminal swapped dimer (C-dimer) obtained from the monomeric derivative of BS-RNase, although under non-na
PMID 24140346

Interactions of gold-based drugs with proteins: crystal structure of the adduct formed between ribonuclease A and a cytotoxic gold(iii) compound.

Messori L, Scaletti F, Massai L, Cinellu MA, Russo Krauss I, di Martino G, Vergara A, Paduano L, Merlino A.SourceDepartment of Chemistry "Ugo Schiff", Via della Lastruccia 3, 50019 Sesto Fiorentino (FI), Italy.
Metallomics : integrated biometal science.Metallomics.2013 Nov 29. [Epub ahead of print]
The reaction of Auoxo6, a dinuclear gold(iii) complex, with the model protein bovine pancreatic ribonuclease is explored here by X-ray diffraction and ESI mass spectrometry. Data provide clues on the processes of adduct formation and of enzyme inhibition and, inductively, on the likely mode of actio
PMID 24287583

RNF43 mutations are recurrent in Chinese patients with mucinous ovarian carcinoma but absent in other subtypes of ovarian cancer.

Zou Y, Wang F, Liu FY, Huang MZ, Li W, Yuan XQ, Huang OP, He M.SourceKey Laboratory of Women's Reproductive Health of Jiangxi Province/Central Lab, Jiangxi Provincial Maternal and Child Health Hospital, Nanchang, Jiangxi 330006, China.
Gene.Gene.2013 Nov 15;531(1):112-6. doi: 10.1016/j.gene.2013.08.054. Epub 2013 Aug 31.
Ring finger protein 43 (RNF43) is an E3 ubiquitin-protein ligase that accepts ubiquitin from an E2 ubiquitin-conjugating enzyme and directly transfers the ubiquitin to targeted substrate proteins. Recently, large-scale sequencing efforts have identified prevalent RNF43 mutations in pancreatic and ov
PMID 24001777

Japanese Journal

Antibodies against pancreatic ribonuclease A hydrolyze RNA and DNA

KRASNORUTSKII Michael A.,BUNEVA Valentina N.,NEVINSKY Georgy A.
International immunology 20(8), 1031-1040, 2008-08-01
NAID 10021926535

圧力で探究するタンパク質疎水性コア構造 : ウシ膵臓リボヌクレアーゼAを例として

茶谷絵理
日本農芸化学会誌 78(4), 407-409, 2004-04-01
NAID 10013140135

Ribonuclease Inhibitors in Malus x domestica (Common Apple) : Isolation and Partial Characterization(Biochemistry & Molecular Biology)

Kosuge Takao,Isemura Mamoru,Takahashi Yoshiaki [他],ODANI Sumiko,ODANI Shoji
Bioscience, biotechnology, and biochemistry 67(4), 698-703, 2003-04-23
… A ribonuclease inhibitory activity was detected in the fruits of common apple, Malus x domestica, cv. … Fuji, and purified by affinity chromatography on ribonuclease A-Sepharose. … It inhibited hydrolysis of cyclic-2' : 3'-CMP by bovine pancreatic ribonuclease A with an apparent inhibition constant of about 5 × 10^<-8>M. …
NAID 110002694123

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リンク元	「RNase A」「ribonuclease A」「膵臓リボヌクレアーゼ」
関連記事	「pancreatic」「ribonuclease」

「RNase A」

Pancreatic ribonuclease
Identifiers
Symbol	RNaseA
Pfam	PF00074
InterPro	IPR001427
SMART	SM00092
PROSITE	PDOC00118
Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

Search
PMC	articles
PubMed	articles
NCBI	proteins

Pancreatic ribonuclease
	Structure of RNase A
Identifiers
EC number	3.1.27.5
CAS number	9001-99-4
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / EGO
Search
PMC	articles
PubMed	articles
NCBI	proteins