同: adenomatous polyposis coli

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2015/07/28 14:38:14」(JST)

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This article refers to the tumor suppressor APC, in which mutations lead to colon cancer. For the cell-cycle regulatory complex, APC/C, see Anaphase-promoting complex.

Adenomatous polyposis coli (APC) also known as deleted in polyposis 2.5 (DP2.5) is a protein that in humans is encoded by the APC gene.^[1] The APC protein is a negative regulator that controls Beta-catenin concentrations and interacts with E-cadherin, which are involved in cell adhesion. Mutations in the APC gene may result in colorectal cancer.^[2]

APC is classified as a tumor suppressor gene. Tumor suppressor genes prevent the uncontrolled growth of cells that may result in cancerous tumors. The protein made by the APC gene plays a critical role in several cellular processes that determine whether a cell may develop into a tumor. The APC protein helps control how often a cell divides, how it attaches to other cells within a tissue, or whether a cell moves within or away from a tissue. This protein also helps ensure that the chromosome number in cells produced through cell division is correct. The APC protein accomplishes these tasks mainly through association with other proteins, especially those that are involved in cell attachment and signaling. The activity of one protein in particular, beta-catenin, is controlled by the APC protein (see: Wnt signaling pathway). Regulation of beta-catenin prevents genes that stimulate cell division from being turned on too often and prevents cell overgrowth.

The human APC gene is located on the long (q) arm of chromosome 5 in band q22.2 The APC gene has been shown to contain an internal ribosome entry site. APC orthologs^[3] have also been identified in all mammals for which complete genome data are available.

Structure

The full-length human protein comprises 2843 amino acids with a (predicted) molecular mass of 311646 Da. Several N-terminal domains have been structurally elucidated in unique atomistic high-resolution complex structures. Most of the protein is predicted to be intrinsically disordered. It is not known if this large predicted unstructured region from amino acid 800 to 2843 persists in vivo or would form stabilised complexes - possibly with yet unidentified interacting proteins.^[4] Recently, it has been experimentally confirmed that the mutation cluster region around the center of APC is intrinsically disordered in vitro.^[5]

Role in cancer

The most common mutation in colon cancer is inactivation of APC. When APC does not have an inactivating mutation, frequently there are activating mutations in beta catenin. Mutations in APC can be inherited, or arise sporadically in the somatic cells, often as the result of mutations in other genes that result in the inability to repair mutations in the DNA. In order for cancer to develop, both alleles (copies of the APC gene) must be mutated. Mutations in APC or β-catenin must be followed by other mutations to become cancerous; however, in carriers of an APC inactivating mutations, the risk of colorectal cancer by age 40 is almost 100%.^[2]

Familial adenomatous polyposis (FAP) is caused by an inherited, inactivating mutation in the APC gene. More than 800 mutations^{[citation needed]}in the APC gene have been identified in families with classic and attenuated types of familial adenomatous polyposis. Most of these mutations cause the production of an APC protein that is abnormally short and presumably nonfunctional. This short protein cannot suppress the cellular overgrowth that leads to the formation of polyps, which can become cancerous. The most common mutation in familial adenomatous polyposis is a deletion of five bases in the APC gene. This mutation changes the sequence of amino acids in the resulting APC protein beginning at position 1309.

Another mutation is carried by approximately 6 percent of people of Ashkenazi (eastern and central European) Jewish heritage. This mutation results in the substitution of the amino acid lysine for isoleucine at position 1307 in the APC protein (also written as I1307K or Ile1307Lys). This change was initially thought to be harmless, but has recently been shown to be associated with a 10 to 20 percent increased risk of colon cancer.

Regulation of proliferation

The (Adenomatous Polyposis Coli) APC protein normally builds a "destruction complex" with glycogen synthase kinase 3-beta( GSK-3β) and axin via interactions with the 20 AA and SAMP repeats^{[citation needed]}. This complex is then able to bind β- catenins in the cytoplasm, that have dissociated from adherens contacts between cells. With the help of casein kinase 1 (CK1), which carries out an initial phosphorylation of β-catenin, GSK-3β is able to phosphorylate β-catenin a second time. This targets β-catenin for ubiquitination and degradation by cellular proteasomes. This prevents it from translocating into the nucleus, where it acts as a transcription factor for proliferation genes. APC is also thought to be targeted to microtubules via the PDZ binding domain, stabilizing them^{[citation needed]}. The deactivation of the APC protein can take place after certain chain reactions in the cytoplasm are started, e.g. through the Wnt signals that destroy the conformation of the complex^{[citation needed]}. In the nucleus it complexes with legless/BCL9, TCF, and Pygo^{[citation needed]}.

The ability of APC to bind β-catenin has been classically considered to be an integral part of the protein's mechanistic function in the destruction complex, along with binding to Axin through the SAMP repeats.^[6] These models have been substantiated by observations that common APC loss of function mutations in the mutation cluster region often remove several β-catenin binding sites and SAMP repeats. However, recent evidence from Yamulla and colleagues have directly tested those models and imply that APC's core mechanistic functions may not require direct binding to β-catenin, but necessitate interactions with Axin.^[7] The researchers hypothesized that APC's many β-catenin binding site increase the protein's efficiency at destroying β-catenin, yet are not absolutely necessary for the protein's mechanistic function. Further research is clearly necessary to elucidate the precise mechanistic function of APC in the destruction complex.

Mutations

Familial Adenomatous Polyposis of the intestine

Mutations in APC often occur early on in cancers such as colon cancer^{[citation needed]}. Patients with familial adenomatous polyposis (FAP) have germline mutations, with 95% being nonsense/frameshift mutations leading to premature stop codons. 33% of mutations occur between amino acids 1061-1309. In somatic mutations, over 60% occur within a mutation cluster region (1286-1513), causing loss of axin binding sites in all but 1 of the 20AA repeats. Mutations in APC lead to loss of β-catenin regulation, altered cell migration and chromosome instability^{[citation needed]}.

Neurological role

Rosenberg et al. found that APC directs cholinergic synapse assembly between neurons, a finding with implications for autonomic neuropathies, for Alzheimer's disease, for age-related hearing loss, and for some forms of epilepsy and schizophrenia ⁽²⁹⁾.

Interactions

APC (gene) has been shown to interact with:

ARHGEF4,^[8]
AXIN1,^[9]
BUB1,^[10]
CTNNB1,^[11]^[12]^[13]^[14]^[15]^[16]^[17]^[18]
CSNK2B,^[16]
CSNK2A1,^[16]
Catenin (cadherin-associated protein), alpha 1,^[11]^[19]
DLG3,^[20]
KIFAP3,^[21]
MAPRE2,^[22]^[23]
JUP,^[19]^[24]
SIAH1,^[25]
TFAP2A,^[26]
TUBA4A^[27] and
XPO1.^[28]

Overview of signal transduction pathways involved in apoptosis.

References

^ Nishisho I, Nakamura Y, Miyoshi Y, Miki Y, Ando H, Horii A et al. (August 1991). "Mutations of chromosome 5q21 genes in FAP and colorectal cancer patients". Science 253 (5020): 665–9. doi:10.1126/science.1651563. PMID 1651563.
^ ^a ^b Markowitz SD, Bertagnolli MM (December 2009). "Molecular origins of cancer: Molecular basis of colorectal cancer". N. Engl. J. Med. 361 (25): 2449–60. doi:10.1056/NEJMra0804588. PMC 2843693. PMID 20018966.
^ "OrthoMaM phylogenetic marker: APC coding sequence".
^ Minde DP, Anvarian Z, Rüdiger SG, Maurice MM (2011). "Messing up disorder: how do missense mutations in the tumor suppressor protein APC lead to cancer?" (PDF). Mol. Cancer 10: 101. doi:10.1186/1476-4598-10-101. PMC 3170638. PMID 21859464.
^ Minde DP, Radli M, Forneris F, Maurice MM, Rüdiger SG (2013). "Large extent of disorder in Adenomatous Polyposis Coli offers a strategy to guard Wnt signalling against point mutations". PLoS ONE 8 (10): e77257. doi:10.1371/journal.pone.0077257. PMC 3793970. PMID 24130866.
^ http://cshperspectives.cshlp.org/content/5/1/a007898.full
^ http://www.genetics.org/content/early/2014/06/12/genetics.114.166496
^ Kawasaki Y, Senda T, Ishidate T, Koyama R, Morishita T, Iwayama Y et al. (2000). "Asef, a link between the tumor suppressor APC and G-protein signaling". Science 289 (5482): 1194–7. doi:10.1126/science.289.5482.1194. PMID 10947987.
^ Nakamura T, Hamada F, Ishidate T, Anai K, Kawahara K, Toyoshima K et al. (1998). "Axin, an inhibitor of the Wnt signalling pathway, interacts with beta-catenin, GSK-3beta and APC and reduces the beta-catenin level". Genes Cells 3 (6): 395–403. doi:10.1046/j.1365-2443.1998.00198.x. PMID 9734785.
^ Kaplan KB, Burds AA, Swedlow JR, Bekir SS, Sorger PK, Näthke IS (2001). "A role for the Adenomatous Polyposis Coli protein in chromosome segregation". Nat. Cell Biol. 3 (4): 429–32. doi:10.1038/35070123. PMID 11283619.
^ ^a ^b Su LK, Vogelstein B, Kinzler KW (1993). "Association of the APC tumor suppressor protein with catenins". Science 262 (5140): 1734–7. doi:10.1126/science.8259519. PMID 8259519.
^ Kucerová D, Sloncová E, Tuhácková Z, Vojtechová M, Sovová V (2001). "Expression and interaction of different catenins in colorectal carcinoma cells". Int. J. Mol. Med. 8 (6): 695–8. doi:10.3892/ijmm.8.6.695. PMID 11712088.
^ Tickenbrock L, Kössmeier K, Rehmann H, Herrmann C, Müller O (2003). "Differences between the interaction of beta-catenin with non-phosphorylated and single-mimicked phosphorylated 20-amino acid residue repeats of the APC protein". J. Mol. Biol. 327 (2): 359–67. doi:10.1016/S0022-2836(03)00144-X. PMID 12628243.
^ Davies G, Jiang WG, Mason MD (2001). "The interaction between beta-catenin, GSK3beta and APC after motogen induced cell-cell dissociation, and their involvement in signal transduction pathways in prostate cancer". Int. J. Oncol. 18 (4): 843–7. doi:10.3892/ijo.18.4.843. PMID 11251183.
^ Ryo A, Nakamura M, Wulf G, Liou YC, Lu KP (2001). "Pin1 regulates turnover and subcellular localization of beta-catenin by inhibiting its interaction with APC". Nat. Cell Biol. 3 (9): 793–801. doi:10.1038/ncb0901-793. PMID 11533658.
^ ^a ^b ^c Homma MK, Li D, Krebs EG, Yuasa Y, Homma Y (2002). "Association and regulation of casein kinase 2 activity by adenomatous polyposis coli protein". Proc. Natl. Acad. Sci. U.S.A. 99 (9): 5959–64. doi:10.1073/pnas.092143199. PMC 122884. PMID 11972058.
^ Satoh K, Yanai H, Senda T, Kohu K, Nakamura T, Okumura N et al. (1997). "DAP-1, a novel protein that interacts with the guanylate kinase-like domains of hDLG and PSD-95". Genes Cells 2 (6): 415–24. doi:10.1046/j.1365-2443.1997.1310329.x. PMID 9286858.
^ Eklof Spink K, Fridman SG, Weis WI (2001). "Molecular mechanisms of beta-catenin recognition by adenomatous polyposis coli revealed by the structure of an APC-beta-catenin complex". EMBO J. 20 (22): 6203–12. doi:10.1093/emboj/20.22.6203. PMC 125720. PMID 11707392.
^ ^a ^b Daniel JM, Reynolds AB (1995). "The tyrosine kinase substrate p120cas binds directly to E-cadherin but not to the adenomatous polyposis coli protein or alpha-catenin". Mol. Cell. Biol. 15 (9): 4819–24. PMC 230726. PMID 7651399.
^ Makino K, Kuwahara H, Masuko N, Nishiyama Y, Morisaki T, Sasaki J et al. (1997). "Cloning and characterization of NE-dlg: a novel human homolog of the Drosophila discs large (dlg) tumor suppressor protein interacts with the APC protein". Oncogene 14 (20): 2425–33. doi:10.1038/sj.onc.1201087. PMID 9188857.
^ Jimbo T, Kawasaki Y, Koyama R, Sato R, Takada S, Haraguchi K et al. (2002). "Identification of a link between the tumour suppressor APC and the kinesin superfamily". Nat. Cell Biol. 4 (4): 323–7. doi:10.1038/ncb779. PMID 11912492.
^ Su LK, Burrell M, Hill DE, Gyuris J, Brent R, Wiltshire R et al. (1995). "APC binds to the novel protein EB1". Cancer Res. 55 (14): 2972–7. PMID 7606712.
^ Nakamura M, Zhou XZ, Lu KP (2001). "Critical role for the EB1 and APC interaction in the regulation of microtubule polymerization". Curr. Biol. 11 (13): 1062–7. doi:10.1016/S0960-9822(01)00297-4. PMID 11470413.
^ Shibata T, Gotoh M, Ochiai A, Hirohashi S (1994). "Association of plakoglobin with APC, a tumor suppressor gene product, and its regulation by tyrosine phosphorylation". Biochem. Biophys. Res. Commun. 203 (1): 519–22. doi:10.1006/bbrc.1994.2213. PMID 8074697.
^ Liu J, Stevens J, Rote CA, Yost HJ, Hu Y, Neufeld KL et al. (2001). "Siah-1 mediates a novel beta-catenin degradation pathway linking p53 to the adenomatous polyposis coli protein". Mol. Cell 7 (5): 927–36. doi:10.1016/S1097-2765(01)00241-6. PMID 11389840.
^ Li Q, Dashwood RH (2004). "Activator protein 2alpha associates with adenomatous polyposis coli/beta-catenin and Inhibits beta-catenin/T-cell factor transcriptional activity in colorectal cancer cells". J. Biol. Chem. 279 (44): 45669–75. doi:10.1074/jbc.M405025200. PMC 2276578. PMID 15331612.
^ Zumbrunn J, Kinoshita K, Hyman AA, Näthke IS (2001). "Binding of the adenomatous polyposis coli protein to microtubules increases microtubule stability and is regulated by GSK3 beta phosphorylation". Curr. Biol. 11 (1): 44–9. doi:10.1016/S0960-9822(01)00002-1. PMID 11166179.
^ Tickenbrock L, Cramer J, Vetter IR, Muller O (2002). "The coiled coil region (amino acids 129-250) of the tumor suppressor protein adenomatous polyposis coli (APC). Its structure and its interaction with chromosome maintenance region 1 (Crm-1)". J. Biol. Chem. 277 (35): 32332–8. doi:10.1074/jbc.M203990200. PMID 12070164.

29. Rosenberg MM1, Yang F, Mohn JL, Storer EK, Jacob MH.The postsynaptic adenomatous polyposis coli (APC) multiprotein complex is required for localizing neuroligin and neurexin to neuronal nicotinic synapses in vivo.J Neurosci. 2010 Aug 18;30(33):11073-85. doi: 10.1523/JNEUROSCI.0983-10.2010.

External links

GeneReviews/NCBI/NIH/UW entry on APC-Associated Polyposis Conditions
OMIM entries on APC-Associated Polyposis Conditions
Adenomatous Polyposis Coli Protein at the US National Library of Medicine Medical Subject Headings (MeSH)
GeneCard
Database concerning peer-reviewed reports on cancer critical alteration in several genes including (APC (protein)), (TP53), (β-catenin)

UpToDate Contents

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1. 大腸癌の分子遺伝学molecular genetics of colorectal cancer [show details]
…stepwise accumulation of multiple somatic mutations. Mutations in the adenomatous polyposis coli (APC) gene, a feature common to both inherited and sporadic CRCs, occur early in the process, while p53 tumor …
2. 家族性腺腫性ポリポーシスの臨床症状および診断clinical manifestations and diagnosis of familial adenomatous polyposis [show details]
… Such patients do not have a family history of FAP. More than 1000 different mutations of the APC gene associated with FAP have been described, most of which lead to frame shifts and premature stop codons …
3. 家族性腺腫性ポリポーシス：患者および家族のスクリーニングおよびマネージメントfamilial adenomatous polyposis screening and management of patients and families [show details]
…Polyposis (FAP) is an autosomal dominant disease caused by mutations in the Adenomatous Polyposis Coli (APC) gene. Patients with FAP are at high risk for the development of colorectal cancer (CRC) as well as upper…
4. ガードナー症候群gardner syndrome [show details]
…specific location of mutations within the APC gene correlates with the occurrence of desmoid tumors, although desmoids can occur with mutations in any APC gene location . Desmoid tumors occur more frequently …
5. デスモイド腫瘍：疫学、危険因子、分子学的病因、臨床症状、診断、および局所療法desmoid tumors epidemiology risk factors molecular pathogenesis clinical presentation diagnosis and local therapy [show details]
…of the APC gene on chromosome 5q are responsible for FAP. More than 300 mutations have been described, most of which lead to frame shifts or premature stop codons, resulting in a truncated APC gene product …

English Journal

Frequency and phenotypic spectrum of germline mutations in POLE and seven other polymerase genes in 266 patients with colorectal adenomas and carcinomas.

Spier I1, Holzapfel S1, Altmüller J2,3, Zhao B4, Horpaopan S1, Vogt S1,5, Chen S4, Morak M6,7, Raeder S1, Kayser K1, Stienen D1, Adam R1, Nürnberg P2, Plotz G8, Holinski-Feder E6,7, Lifton RP4, Thiele H2, Hoffmann P1,9,10, Steinke V1, Aretz S1.
International journal of cancer. Journal international du cancer.Int J Cancer.2015 Jul 15;137(2):320-31. doi: 10.1002/ijc.29396. Epub 2015 Jan 20.
In a number of families with colorectal adenomatous polyposis or suspected Lynch syndrome/HNPCC, no germline alteration in the APC, MUTYH, or mismatch repair (MMR) genes are found. Missense mutations in the polymerase genes POLE and POLD1 have recently been identified as rare cause of multiple color
PMID 25529843

Retrospective analysis of FFPE based Wilms' Tumor samples through copy number and somatic mutation related Molecular Inversion Probe Based Array.

Singh N1, Sahu DK2, Goel M3, Kant R4, Gupta DK5.
Gene.Gene.2015 Jul 10;565(2):295-308. doi: 10.1016/j.gene.2015.04.051. Epub 2015 Apr 22.
In this report, retrospectively, we analyzed fifteen histo-pathologically characterized FFPE based Wilms' Tumor (WT) samples following an integrative approach of copy number (CN) and loss of heterozygosity (LOH) imbalances. The isolated-DNA was tested on CN and somatic-mutation related Molecular-Inv
PMID 25913740

Influence of molecular weight upon mannosylated bio-synthetic hybrids for targeted antigen presenting cell gene delivery.

Jones CH1, Gollakota A1, Chen M1, Chung TC1, Ravikrishnan A1, Zhang G1, Pfeifer BA2.
Biomaterials.Biomaterials.2015 Jul;58:103-11. doi: 10.1016/j.biomaterials.2015.04.033. Epub 2015 May 11.
Given the rise of antibiotic resistant microbes, genetic vaccination is a promising prophylactic strategy that enables rapid design and manufacture. Facilitating this process is the choice of vector, which is often situationally-specific and limited in engineering capacity. Furthermore, these shortc
PMID 25941787

Japanese Journal

Biosynthesis of a stable allophycocyanin beta subunit in metabolically engineered Escherichia coli(ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)

Chen Huaxin,Lin Hanzhi,Li Fuchao [他],Jiang Peng,Qin Song
Journal of bioscience and bioengineering 115(5), 485-489, 2013-05
… Allophycocyanin (APC) is widely used as a fluorescent tag for fluorescence detection techniques. … In this study, the apcB gene from a therinophihc cyanobacterium strain was cloned and ligated into an expression vector to construct a pathway for the biosynthesis of an allophycocyanin beta subunit (holo-apcBT) in Escherichia coli. … The recombinant holo-apcB showed spectroscopic properties similar to native APC. …
NAID 110009611450

Dof transcription factors control the expression of the anaphase promoting complex/cyclosome activator CCS52A1

Takahashi Naoki,Kong Shanshan,Umeda Masaaki
Plant Biotechnology 30(4), 407-410, 2013
… CCS52A1, a substrate-specific activator of the anaphase promoting complex/cyclosome (APC/C), is essential for the transition from mitosis to endoreduplication. … Here, we show that DNA-binding with one finger (Dof) transcription factors directly regulate the transcription of the CCS52A1 gene. …
NAID 130003362444

Cardamonin Suppresses the Proliferation of Colon Cancer Cells by Promoting β-Catenin Degradation

Park Seoyoung,Gwak Jungsug,Han Seung Jin [他],Oh Sangtaek
Biological and Pharmaceutical Bulletin 36(6), 1040-1044, 2013
… Here we show that cardamonin, a chalcone isolated from Aplinia katsumadai <span style="font-variant: small-caps;">Hayata</span>, inhibited CRT in SW480 colon cancer cells that carry inactivating mutation in the adenomatous polyposis coli (APC) gene. …
NAID 130003361462

「APC遺伝子」

Adenomatous polyposis coli
	PDB rendering based on 1deb.
Available structures
PDB	Ortholog search: PDBe, RCSB
List of PDB id codes
	1DEB, 1EMU, 1JPP, 1M5I, 1T08, 1TH1, 1V18, 2RQU, 3AU3, 3NMW, 3NMX, 3NMZ, 3QHE, 3RL7, 3RL8, 3T7U, 4G69
Identifiers
Symbols	APC ; BTPS2; DP2; DP2.5; DP3; GS; PPP1R46
External IDs	OMIM: 611731 MGI: 88039 HomoloGene: 30950 ChEMBL: 3233 GeneCards: APC Gene
Gene ontology
Molecular function	• protein binding; • beta-catenin binding; • microtubule binding; • protein kinase regulator activity; • protein kinase binding; • gamma-catenin binding; • cadherin binding; • microtubule plus-end binding;
Cellular component	• kinetochore; • nucleus; • nucleoplasm; • cytoplasm; • centrosome; • cytosol; • cytoplasmic microtubule; • plasma membrane; • cell-cell adherens junction; • bicellular tight junction; • lateral plasma membrane; • catenin complex; • lamellipodium; • beta-catenin destruction complex; • ruffle membrane; • microtubule plus-end; • axonal growth cone;
Biological process	• mitotic cytokinesis; • kidney development; • hair follicle development; • protein complex assembly; • apoptotic process; • cellular component disassembly involved in execution phase of apoptosis; • cellular response to DNA damage stimulus; • negative regulation of microtubule depolymerization; • cell cycle arrest; • metaphase/anaphase transition of mitotic cell cycle; • mitotic spindle assembly checkpoint; • cell adhesion; • axonogenesis; • negative regulation of cell proliferation; • axis specification; • anterior/posterior pattern specification; • dorsal/ventral pattern formation; • proximal/distal pattern formation; • programmed cell death; • cell migration; • positive regulation of cell migration; • positive regulation of epithelial cell differentiation; • positive regulation of microtubule polymerization; • cytoplasmic microtubule organization; • positive regulation of pseudopodium assembly; • regulation of microtubule-based process; • T cell differentiation in thymus; • somatic stem cell maintenance; • negative regulation of odontogenesis; • positive regulation of apoptotic process; • negative regulation of MAPK cascade; • canonical Wnt signaling pathway involved in negative regulation of apoptotic process; • canonical Wnt signaling pathway involved in positive regulation of apoptotic process; • regulation of osteoblast differentiation; • regulation of osteoclast differentiation; • positive regulation of protein catabolic process; • negative regulation of cyclin-dependent protein serine/threonine kinase activity; • positive regulation of cell adhesion; • muscle cell cellular homeostasis; • thymus development; • regulation of nitrogen compound metabolic process; • chromosome organization; • positive regulation of cell division; • regulation of attachment of spindle microtubules to kinetochore; • retina development in camera-type eye; • canonical Wnt signaling pathway; • negative regulation of epithelial cell proliferation involved in prostate gland development; • bicellular tight junction assembly; • negative regulation of canonical Wnt signaling pathway; • positive regulation of canonical Wnt signaling pathway;
	Sources: Amigo / QuickGO
RNA expression pattern
	More reference expression data
Orthologs
	v; t; e;

　　[★]

英: APC gene
関: 大腸腺腫症遺伝子

「APC」

　　[★]

活性化タンパク質C activated protein C
抗原提示細胞 antigen presenting cell
心房性期外収縮 atrial premature contraction atrial premature complex
大腸ポリポーシス adenomatous polyposis coli
後期促進複合体 anaphase-promoting complex
アルゴンプラズマ焼灼アルゴンプラズマ凝固 argon plasma coaglation

「AP」

　　[★]

「A」

　　[★]

[pmid1651563-1] Nishisho I, Nakamura Y, Miyoshi Y, Miki Y, Ando H, Horii A et al. (August 1991). "Mutations of chromosome 5q21 genes in FAP and colorectal cancer patients". Science 253 (5020): 665–9. doi:10.1126/science.1651563. PMID 1651563.

[Markowitz_2009-2] Markowitz SD, Bertagnolli MM (December 2009). "Molecular origins of cancer: Molecular basis of colorectal cancer". N. Engl. J. Med. 361 (25): 2449–60. doi:10.1056/NEJMra0804588. PMC 2843693. PMID 20018966.

[OrthoMaM-3] "OrthoMaM phylogenetic marker: APC coding sequence".

[pmid21859464-4] Minde DP, Anvarian Z, Rüdiger SG, Maurice MM (2011). "Messing up disorder: how do missense mutations in the tumor suppressor protein APC lead to cancer?" (PDF). Mol. Cancer 10: 101. doi:10.1186/1476-4598-10-101. PMC 3170638. PMID 21859464.

[APC-MCR-5] Minde DP, Radli M, Forneris F, Maurice MM, Rüdiger SG (2013). "Large extent of disorder in Adenomatous Polyposis Coli offers a strategy to guard Wnt signalling against point mutations". PLoS ONE 8 (10): e77257. doi:10.1371/journal.pone.0077257. PMC 3793970. PMID 24130866.

[6] ttp://cshperspectives.cshlp.org/content/5/1/a007898.full

[7] ttp://www.genetics.org/content/early/2014/06/12/genetics.114.166496

[pmid10947987-8] Kawasaki Y, Senda T, Ishidate T, Koyama R, Morishita T, Iwayama Y et al. (2000). "Asef, a link between the tumor suppressor APC and G-protein signaling". Science 289 (5482): 1194–7. doi:10.1126/science.289.5482.1194. PMID 10947987.

[pmid9734785-9] Nakamura T, Hamada F, Ishidate T, Anai K, Kawahara K, Toyoshima K et al. (1998). "Axin, an inhibitor of the Wnt signalling pathway, interacts with beta-catenin, GSK-3beta and APC and reduces the beta-catenin level". Genes Cells 3 (6): 395–403. doi:10.1046/j.1365-2443.1998.00198.x. PMID 9734785.

[pmid11283619-10] Kaplan KB, Burds AA, Swedlow JR, Bekir SS, Sorger PK, Näthke IS (2001). "A role for the Adenomatous Polyposis Coli protein in chromosome segregation". Nat. Cell Biol. 3 (4): 429–32. doi:10.1038/35070123. PMID 11283619.

[pmid8259519-11] Su LK, Vogelstein B, Kinzler KW (1993). "Association of the APC tumor suppressor protein with catenins". Science 262 (5140): 1734–7. doi:10.1126/science.8259519. PMID 8259519.

[pmid11712088-12] Kucerová D, Sloncová E, Tuhácková Z, Vojtechová M, Sovová V (2001). "Expression and interaction of different catenins in colorectal carcinoma cells". Int. J. Mol. Med. 8 (6): 695–8. doi:10.3892/ijmm.8.6.695. PMID 11712088.

[pmid12628243-13] Tickenbrock L, Kössmeier K, Rehmann H, Herrmann C, Müller O (2003). "Differences between the interaction of beta-catenin with non-phosphorylated and single-mimicked phosphorylated 20-amino acid residue repeats of the APC protein". J. Mol. Biol. 327 (2): 359–67. doi:10.1016/S0022-2836(03)00144-X. PMID 12628243.

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リンク元	「APC遺伝子」
関連記事	「APC」「AP」「A」

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APC gene