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วิกิพีเดีย

แอลฟาทู-แอนติพลาสมิน

แอลฟาทู-แอนติพลาสมิน (อังกฤษ: Alpha 2-antiplasmin หรือ α2-antiplasmin หรือ plasmin inhibitor; A2AP) เป็นโปรตีนในกลุ่มสารยับยั้งซีรีนโปรตีเอส (เซอร์ปิน) ทำหน้าที่ยับยั้งการทำงานของพลาสมินในกระบวนการการจับลิ่มของเลือด ถูกถอดรหัสได้จากยีน SERPINF2 บนโครโมโซมคู่ที่ 17 อย่างไรก็ตาม มีรายงานความผิดปกติที่เกี่ยวข้องกับภาวะพร่องแอลฟาทู-แอนติพลาสมินน้อยมาก เนื่องจากจะมีการรายงานเฉพาะกรณีที่มีภาวะเลือดออกง่ายอย่างรุนแรงจากการทำงานของพลาสมินที่มากผิดปกติเท่านั้น

SERPINF2
Available structures
PDBHuman UniProt search: PDBe RCSB
Identifiers
AliasesSERPINF2, A2AP, AAP, ALPHA-2-PI, API, PLI, serpin family F member 2, alpha2AP
External IDsOMIM: 613168 HomoloGene: 719 GeneCards: SERPINF2
Gene location (Human)
Chr.Chromosome 17 (human)
Band17p13.3Start1,742,836 bp
End1,755,265 bp
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_000934
NM_001165920
NM_001165921

n/a

RefSeq (protein)

NP_000925
NP_001159392
NP_001159393

n/a

Location (UCSC)Chr 17: 1.74 – 1.76 Mbn/a
PubMed searchn/a
Wikidata
View/Edit Human

ในผู้ป่วยโรคตับแข็ง จะมีการผลิต A2AP น้อยกว่าคนปกติประมาณ 2 เท่า ทำให้ขาดแคลน A2AP ที่ใช้ต้านการทำงานของพลาสมิน จนทำให้เกิดการสลายของลิ่มเลือดลดน้อยลง ความผิดปกติดังกล่าวมีความสัมพันธ์กับการเพิ่มขึ้นของความเสี่ยงต่อการเกิดภาวะเลือดออกง่ายในผู้ป่วยโรคตับ

A2AP สามารถถูกทำให้หมดฤทธิ์ได้ด้วยนิวโทรฟิลอีลาสเตส (Neutrophil elastase) โดยนิวโทรฟิลอีลาสเตสจะตัดย่อย A2AP ออกเป็น 2 ส่วน ซึ่งไม่มีฤทธิ์ทางชีววิทยา

แผนภาพแสดงการสลายลิ่มเลือดอย่างง่าย ลูกศรสีน้ำเงินแสดงถึงการกระตุ้น ส่วนลูกศรสีแดงคือการยับยั้ง

ดูเพิ่ม

อ้างอิง

  1. ENSG00000276838 GRCh38: Ensembl release 89: ENSG00000167711, ENSG00000276838 - Ensembl, May 2017
  2. "Human PubMed Reference:".
  3. Wu, Guojie; Quek, Adam J.; Caradoc-Davies, Tom T.; Ekkel, Sue M.; Mazzitelli, Blake; Whisstock, James C.; Law, Ruby H.P. (2019-03-05). "Structural studies of plasmin inhibition". Biochemical Society Transactions. 47 (2): 541–557. doi:10.1042/bst20180211. ISSN 0300-5127. PMID 30837322.
  4. Shieh BH, Travis J (May 1987). "The reactive site of human alpha 2-antiplasmin". The Journal of Biological Chemistry. 262 (13): 6055–9. PMID 2437112.
  5. Wiman B, Collen D (Sep 1979). "On the mechanism of the reaction between human alpha 2-antiplasmin and plasmin". The Journal of Biological Chemistry. 254 (18): 9291–7. PMID 158022.
  6. "Entrez Gene: SERPINF2 serpin peptidase inhibitor, clade F (alpha-2 antiplasmin, pigment epithelium derived factor), member 2".
  7. Sattar, Husain. Fundamentals of Pathology. Pathoma LLC, 2011, p. 36.
  8. Brower MS, Harpel PC (Aug 1982). "Proteolytic cleavage and inactivation of alpha 2-plasmin inhibitor and C1 inactivator by human polymorphonuclear leukocyte elastase". The Journal of Biological Chemistry. 257 (16): 9849–54. PMID 6980881.

แหล่งข้อมูลอื่น

  • Martí-Fàbregas J, Borrell M, Cocho D, Martínez-Ramírez S, Martínez-Corral M, Fontcuberta J, Martí-Vilalta JL (Jan 2008). "Change in hemostatic markers after recombinant tissue-type plasminogen activator is not associated with the chance of recanalization". Stroke: A Journal of Cerebral Circulation. 39 (1): 234–6. doi:10.1161/STROKEAHA.107.493767. PMID 18048863.
  • Nielsen VG (Oct 2007). "Hydroxyethyl starch enhances fibrinolysis in human plasma by diminishing alpha2-antiplasmin-plasmin interactions". Blood Coagulation & Fibrinolysis. 18 (7): 647–56. doi:10.1097/MBC.0b013e3282a167dc. PMID 17890952. S2CID 45608070.
  • Sazonova IY, Thomas BM, Gladysheva IP, Houng AK, Reed GL (Oct 2007). "Fibrinolysis is amplified by converting alpha-antiplasmin from a plasmin inhibitor to a substrate". Journal of Thrombosis and Haemostasis. 5 (10): 2087–94. doi:10.1111/j.1538-7836.2007.02652.x. PMID 17883703. S2CID 2907615.
  • Mutch NJ, Thomas L, Moore NR, Lisiak KM, Booth NA (Apr 2007). "TAFIa, PAI-1 and alpha-antiplasmin: complementary roles in regulating lysis of thrombi and plasma clots". Journal of Thrombosis and Haemostasis. 5 (4): 812–7. doi:10.1111/j.1538-7836.2007.02430.x. PMID 17388801. S2CID 40278627.
  • Christiansen VJ, Jackson KW, Lee KN, McKee PA (Jun 2007). "The effect of a single nucleotide polymorphism on human alpha 2-antiplasmin activity". Blood. 109 (12): 5286–92. doi:10.1182/blood-2007-01-065185. PMC 1890835. PMID 17317851.
  • Hayashido Y, Hamana T, Ishida Y, Shintani T, Koizumi K, Okamoto T (Feb 2007). "Induction of alpha2-antiplasmin inhibits E-cadherin processing mediated by the plasminogen activator/plasmin system, leading to suppression of progression of oral squamous cell carcinoma via upregulation of cell-cell adhesion". Oncology Reports. 17 (2): 417–23. doi:10.3892/or.17.2.417. PMID 17203182.
  • Shibata N, Kawarai T, Meng Y, Lee JH, Lee HS, Wakutani Y, Shibata E, Pathan N, Bi A, Sato C, Sorbi S, Bruni AC, Duara R, Mayeux R, Farrer LA, George-Hyslop PS, Rogaeva E (Jul 2007). "Association studies between the plasmin genes and late-onset Alzheimer's disease". Neurobiology of Aging. 28 (7): 1041–3. doi:10.1016/j.neurobiolaging.2006.05.028. PMC 2647723. PMID 16828203.
  • Liu T, Qian WJ, Gritsenko MA, Camp DG, Monroe ME, Moore RJ, Smith RD (December 2005). "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry". Journal of Proteome Research. 4 (6): 2070–80. doi:10.1021/pr0502065. PMC 1850943. PMID 16335952.
  • Lee KN, Jackson KW, Christiansen VJ, Chung KH, McKee PA (May 2004). "A novel plasma proteinase potentiates alpha2-antiplasmin inhibition of fibrin digestion". Blood. 103 (10): 3783–8. doi:10.1182/blood-2003-12-4240. PMID 14751930.
  • Anderson NL, Polanski M, Pieper R, Gatlin T, Tirumalai RS, Conrads TP, Veenstra TD, Adkins JN, Pounds JG, Fagan R, Lobley A (Apr 2004). "The human plasma proteome: a nonredundant list developed by combination of four separate sources". Molecular & Cellular Proteomics. 3 (4): 311–26. doi:10.1074/mcp.M300127-MCP200. PMID 14718574.
  • Kapadia C, Yousef GM, Mellati AA, Magklara A, Wasney GA, Diamandis EP (Jan 2004). "Complex formation between human kallikrein 13 and serum protease inhibitors". Clinica Chimica Acta; International Journal of Clinical Chemistry. 339 (1–2): 157–67. doi:10.1016/j.cccn.2003.10.009. PMID 14687906.
  • Matsuno H, Okada K, Ueshima S, Matsuo O, Kozawa O (Aug 2003). "Alpha2-antiplasmin plays a significant role in acute pulmonary embolism". Journal of Thrombosis and Haemostasis. 1 (8): 1734–9. doi:10.1046/j.1538-7836.2003.00252.x. PMID 12911586. S2CID 72056689.
  • Magklara A, Mellati AA, Wasney GA, Little SP, Sotiropoulou G, Becker GW, Diamandis EP (Aug 2003). "Characterization of the enzymatic activity of human kallikrein 6: Autoactivation, substrate specificity, and regulation by inhibitors". Biochemical and Biophysical Research Communications. 307 (4): 948–55. doi:10.1016/S0006-291X(03)01271-3. PMID 12878203.
  • Cardoso C, Leventer RJ, Ward HL, Toyo-Oka K, Chung J, Gross A, Martin CL, Allanson J, Pilz DT, Olney AH, Mutchinick OM, Hirotsune S, Wynshaw-Boris A, Dobyns WB, Ledbetter DH (Apr 2003). "Refinement of a 400-kb critical region allows genotypic differentiation between isolated lissencephaly, Miller-Dieker syndrome, and other phenotypes secondary to deletions of 17p13.3". American Journal of Human Genetics. 72 (4): 918–30. doi:10.1086/374320. PMC 1180354. PMID 12621583.
  • Frank PS, Douglas JT, Locher M, Llinás M, Schaller J (Feb 2003). "Structural/functional characterization of the alpha 2-plasmin inhibitor C-terminal peptide". Biochemistry. 42 (4): 1078–85. doi:10.1021/bi026917n. PMID 12549929.
  • Turner RB, Liu L, Sazonova IY, Reed GL (Sep 2002). "Structural elements that govern the substrate specificity of the clot-dissolving enzyme plasmin". The Journal of Biological Chemistry. 277 (36): 33068–74. doi:10.1074/jbc.M203782200. PMID 12080056.
  • Askew YS, Pak SC, Luke CJ, Askew DJ, Cataltepe S, Mills DR, Kato H, Lehoczky J, Dewar K, Birren B, Silverman GA (Dec 2001). "SERPINB12 is a novel member of the human ov-serpin family that is widely expressed and inhibits trypsin-like serine proteinases". The Journal of Biological Chemistry. 276 (52): 49320–30. doi:10.1074/jbc.M108879200. PMID 11604408.
  • Uszynski M, Klyszejko A, Zekanowska E (Dec 2000). "Plasminogen, alpha(2)-antiplasmin and complexes of plasmin-alpha(2)-antiplasmin (PAP) in amniotic fluid and blood plasma of parturient women". European Journal of Obstetrics, Gynecology, and Reproductive Biology. 93 (2): 167–71. doi:10.1016/S0301-2115(00)00283-9. PMID 11074138.
  • Hevessy Z, Patthy A, Kárpáti L, Muszbek L (Aug 2000). "alpha(2)-plasmin inhibitor is a substrate for tissue transglutaminase: an in vitro study". Thrombosis Research. 99 (4): 399–406. doi:10.1016/S0049-3848(00)00261-9. PMID 10963790.
  • ฐานข้อมูลออนไลน์ MEROPS สำหรับเปปทิเดส และสารยับยั้งเปปทิเดส: I04.023
  • alpha-2 Antiplasmin ในหอสมุดแพทยศาสตร์แห่งชาติอเมริกัน สำหรับหัวข้อเนื้อหาทางการแพทย์ (MeSH)
  • ตำแหน่งจีโนม SERPINF2 ของมนุษย์ และหน้าเพจแสดงข้อมูลเกี่ยวกับยีน SERPINF2 ใน UCSC Genome Browser

แอลฟาท, แอนต, พลาสม, งกฤษ, alpha, antiplasmin, หร, antiplasmin, หร, plasmin, inhibitor, a2ap, เป, นโปรต, นในกล, มสารย, บย, งซ, นโปรต, เอส, เซอร, ทำหน, าท, บย, งการทำงานของพลาสม, นในกระบวนการการจ, บล, มของเล, อด, กถอดรห, สได, จากย, serpinf2, บนโครโมโซมค, อย, าง. aexlfathu aexntiphlasmin xngkvs Alpha 2 antiplasmin hrux a2 antiplasmin hrux plasmin inhibitor A2AP epnoprtininklumsarybyngsirinoprtiexs esxrpin thahnathiybyngkarthangankhxngphlasmininkrabwnkarkarcblimkhxngeluxd 3 4 5 thukthxdrhsidcakyin SERPINF2 bnokhromosmkhuthi 17 6 xyangirktam mirayngankhwamphidpktithiekiywkhxngkbphawaphrxngaexlfathu aexntiphlasminnxymak enuxngcakcamikarraynganechphaakrnithimiphawaeluxdxxkngayxyangrunaerngcakkarthangankhxngphlasminthimakphidpktiethannSERPINF2Available structuresPDBHuman UniProt search PDBe RCSBList of PDB id codes2R9YIdentifiersAliasesSERPINF2 A2AP AAP ALPHA 2 PI API PLI serpin family F member 2 alpha2APExternal IDsOMIM 613168 HomoloGene 719 GeneCards SERPINF2Gene location Human Chr Chromosome 17 human 1 Band17p13 3Start1 742 836 bp 1 End1 755 265 bp 1 RNA expression patternMore reference expression dataGene ontologyMolecular function peptidase inhibitor activity protein homodimerization activity protease binding GO 0001948 karcbkboprtin serine type endopeptidase inhibitor activity endopeptidase inhibitor activityCellular component blood microparticle ifbrionecn extracellular region cell surface exkososmchnidphaynxkesll platelet alpha granule lumen phaynxkesll sarekhluxbesllthimikhxllaecnepnswnprakxbBiological process positive regulation of collagen biosynthetic process negative regulation of peptidase activity negative regulation of fibrinolysis negative regulation of plasminogen activation maintenance of blood vessel diameter homeostasis by renin angiotensin blood vessel morphogenesis fibrinolysis collagen fibril organization platelet degranulation positive regulation of JNK cascade response to organic substance acute phase response positive regulation of cell differentiation positive regulation of ERK1 and ERK2 cascade positive regulation of transforming growth factor beta production positive regulation of stress fiber assembly positive regulation of transcription by RNA polymerase II positive regulation of smooth muscle cell proliferation positive regulation of cell cell adhesion mediated by cadherin negative regulation of endopeptidase activitySources Amigo QuickGOOrthologsSpeciesHumanMouseEntrez5345n aEnsemblENSG00000167711ENSG00000276838n aUniProtP08697n aRefSeq mRNA NM 000934NM 001165920NM 001165921n aRefSeq protein NP 000925NP 001159392NP 001159393n aLocation UCSC Chr 17 1 74 1 76 Mbn aPubMed search 2 n aWikidataView Edit Humaninphupwyorkhtbaekhng camikarphlit A2AP nxykwakhnpktipraman 2 etha thaihkhadaekhln A2AP thiichtankarthangankhxngphlasmin cnthaihekidkarslaykhxnglimeluxdldnxylng khwamphidpktidngklawmikhwamsmphnthkbkarephimkhunkhxngkhwamesiyngtxkarekidphawaeluxdxxkngayinphupwyorkhtb 7 A2AP samarththukthaihhmdvththiiddwyniwothrfilxilasets Neutrophil elastase odyniwothrfilxilasetscatdyxy A2AP xxkepn 2 swn sungimmivththithangchiwwithya 4 8 aephnphaphaesdngkarslaylimeluxdxyangngay luksrsinaenginaesdngthungkarkratun swnluksrsiaedngkhuxkarybyngduephim aekikhesxrpin phlasminxangxing aekikh 1 0 1 1 1 2 ENSG00000276838 GRCh38 Ensembl release 89 ENSG00000167711 ENSG00000276838 Ensembl May 2017 Human PubMed Reference Wu Guojie Quek Adam J Caradoc Davies Tom T Ekkel Sue M Mazzitelli Blake Whisstock James C Law Ruby H P 2019 03 05 Structural studies of plasmin inhibition Biochemical Society Transactions 47 2 541 557 doi 10 1042 bst20180211 ISSN 0300 5127 PMID 30837322 4 0 4 1 Shieh BH Travis J May 1987 The reactive site of human alpha 2 antiplasmin The Journal of Biological Chemistry 262 13 6055 9 PMID 2437112 Wiman B Collen D Sep 1979 On the mechanism of the reaction between human alpha 2 antiplasmin and plasmin The Journal of Biological Chemistry 254 18 9291 7 PMID 158022 Entrez Gene SERPINF2 serpin peptidase inhibitor clade F alpha 2 antiplasmin pigment epithelium derived factor member 2 Sattar Husain Fundamentals of Pathology Pathoma LLC 2011 p 36 Brower MS Harpel PC Aug 1982 Proteolytic cleavage and inactivation of alpha 2 plasmin inhibitor and C1 inactivator by human polymorphonuclear leukocyte elastase The Journal of Biological Chemistry 257 16 9849 54 PMID 6980881 aehlngkhxmulxun aekikhMarti Fabregas J Borrell M Cocho D Martinez Ramirez S Martinez Corral M Fontcuberta J Marti Vilalta JL Jan 2008 Change in hemostatic markers after recombinant tissue type plasminogen activator is not associated with the chance of recanalization Stroke A Journal of Cerebral Circulation 39 1 234 6 doi 10 1161 STROKEAHA 107 493767 PMID 18048863 Nielsen VG Oct 2007 Hydroxyethyl starch enhances fibrinolysis in human plasma by diminishing alpha2 antiplasmin plasmin interactions Blood Coagulation amp Fibrinolysis 18 7 647 56 doi 10 1097 MBC 0b013e3282a167dc PMID 17890952 S2CID 45608070 Sazonova IY Thomas BM Gladysheva IP Houng AK Reed GL Oct 2007 Fibrinolysis is amplified by converting alpha antiplasmin from a plasmin inhibitor to a substrate Journal of Thrombosis and Haemostasis 5 10 2087 94 doi 10 1111 j 1538 7836 2007 02652 x PMID 17883703 S2CID 2907615 Mutch NJ Thomas L Moore NR Lisiak KM Booth NA Apr 2007 TAFIa PAI 1 and alpha antiplasmin complementary roles in regulating lysis of thrombi and plasma clots Journal of Thrombosis and Haemostasis 5 4 812 7 doi 10 1111 j 1538 7836 2007 02430 x PMID 17388801 S2CID 40278627 Christiansen VJ Jackson KW Lee KN McKee PA Jun 2007 The effect of a single nucleotide polymorphism on human alpha 2 antiplasmin activity Blood 109 12 5286 92 doi 10 1182 blood 2007 01 065185 PMC 1890835 PMID 17317851 Hayashido Y Hamana T Ishida Y Shintani T Koizumi K Okamoto T Feb 2007 Induction of alpha2 antiplasmin inhibits E cadherin processing mediated by the plasminogen activator plasmin system leading to suppression of progression of oral squamous cell carcinoma via upregulation of cell cell adhesion Oncology Reports 17 2 417 23 doi 10 3892 or 17 2 417 PMID 17203182 Shibata N Kawarai T Meng Y Lee JH Lee HS Wakutani Y Shibata E Pathan N Bi A Sato C Sorbi S Bruni AC Duara R Mayeux R Farrer LA George Hyslop PS Rogaeva E Jul 2007 Association studies between the plasmin genes and late onset Alzheimer s disease Neurobiology of Aging 28 7 1041 3 doi 10 1016 j neurobiolaging 2006 05 028 PMC 2647723 PMID 16828203 Liu T Qian WJ Gritsenko MA Camp DG Monroe ME Moore RJ Smith RD December 2005 Human plasma N glycoproteome analysis by immunoaffinity subtraction hydrazide chemistry and mass spectrometry Journal of Proteome Research 4 6 2070 80 doi 10 1021 pr0502065 PMC 1850943 PMID 16335952 Lee KN Jackson KW Christiansen VJ Chung KH McKee PA May 2004 A novel plasma proteinase potentiates alpha2 antiplasmin inhibition of fibrin digestion Blood 103 10 3783 8 doi 10 1182 blood 2003 12 4240 PMID 14751930 Anderson NL Polanski M Pieper R Gatlin T Tirumalai RS Conrads TP Veenstra TD Adkins JN Pounds JG Fagan R Lobley A Apr 2004 The human plasma proteome a nonredundant list developed by combination of four separate sources Molecular amp Cellular Proteomics 3 4 311 26 doi 10 1074 mcp M300127 MCP200 PMID 14718574 Kapadia C Yousef GM Mellati AA Magklara A Wasney GA Diamandis EP Jan 2004 Complex formation between human kallikrein 13 and serum protease inhibitors Clinica Chimica Acta International Journal of Clinical Chemistry 339 1 2 157 67 doi 10 1016 j cccn 2003 10 009 PMID 14687906 Matsuno H Okada K Ueshima S Matsuo O Kozawa O Aug 2003 Alpha2 antiplasmin plays a significant role in acute pulmonary embolism Journal of Thrombosis and Haemostasis 1 8 1734 9 doi 10 1046 j 1538 7836 2003 00252 x PMID 12911586 S2CID 72056689 Magklara A Mellati AA Wasney GA Little SP Sotiropoulou G Becker GW Diamandis EP Aug 2003 Characterization of the enzymatic activity of human kallikrein 6 Autoactivation substrate specificity and regulation by inhibitors Biochemical and Biophysical Research Communications 307 4 948 55 doi 10 1016 S0006 291X 03 01271 3 PMID 12878203 Cardoso C Leventer RJ Ward HL Toyo Oka K Chung J Gross A Martin CL Allanson J Pilz DT Olney AH Mutchinick OM Hirotsune S Wynshaw Boris A Dobyns WB Ledbetter DH Apr 2003 Refinement of a 400 kb critical region allows genotypic differentiation between isolated lissencephaly Miller Dieker syndrome and other phenotypes secondary to deletions of 17p13 3 American Journal of Human Genetics 72 4 918 30 doi 10 1086 374320 PMC 1180354 PMID 12621583 Frank PS Douglas JT Locher M Llinas M Schaller J Feb 2003 Structural functional characterization of the alpha 2 plasmin inhibitor C terminal peptide Biochemistry 42 4 1078 85 doi 10 1021 bi026917n PMID 12549929 Turner RB Liu L Sazonova IY Reed GL Sep 2002 Structural elements that govern the substrate specificity of the clot dissolving enzyme plasmin The Journal of Biological Chemistry 277 36 33068 74 doi 10 1074 jbc M203782200 PMID 12080056 Askew YS Pak SC Luke CJ Askew DJ Cataltepe S Mills DR Kato H Lehoczky J Dewar K Birren B Silverman GA Dec 2001 SERPINB12 is a novel member of the human ov serpin family that is widely expressed and inhibits trypsin like serine proteinases The Journal of Biological Chemistry 276 52 49320 30 doi 10 1074 jbc M108879200 PMID 11604408 Uszynski M Klyszejko A Zekanowska E Dec 2000 Plasminogen alpha 2 antiplasmin and complexes of plasmin alpha 2 antiplasmin PAP in amniotic fluid and blood plasma of parturient women European Journal of Obstetrics Gynecology and Reproductive Biology 93 2 167 71 doi 10 1016 S0301 2115 00 00283 9 PMID 11074138 Hevessy Z Patthy A Karpati L Muszbek L Aug 2000 alpha 2 plasmin inhibitor is a substrate for tissue transglutaminase an in vitro study Thrombosis Research 99 4 399 406 doi 10 1016 S0049 3848 00 00261 9 PMID 10963790 thankhxmulxxniln MEROPS sahrbeppthieds aelasarybyngeppthieds I04 023 alpha 2 Antiplasmin inhxsmudaephthysastraehngchatixemrikn sahrbhwkhxenuxhathangkaraephthy MeSH SERPINF2 protein human inhxsmudaephthysastraehngchatixemrikn sahrbhwkhxenuxhathangkaraephthy MeSH taaehnngcionm SERPINF2 khxngmnusy aelahnaephcaesdngkhxmulekiywkbyin SERPINF2 in UCSC Genome Browserekhathungcak https th wikipedia org w index php title aexlfathu aexntiphlasmin amp oldid 9094308, wikipedia, วิกิ หนังสือ, หนังสือ, ห้องสมุด,

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