Fibrinopeptide
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{{Chembox
| ImageFile = Fibrinopeptide A.svg
| ImageSize =
| Name = Fibrinopeptide A
| IUPACName =
| OtherNames = Fibrinopeptide A; Fibrinopeptide A (human); FpA; FPA
| Section1 = {{Chembox Identifiers
| CASNo = 25422-31-5
| ChEBI =
| ChEMBL =
| ChemSpiderID = 17286499
| DrugBank =
| EINECS =
| EC_number =
| InChI = 1S/C63H97N19O26/c1-29(2)19-37(57(102)73-32(6)53(98)76-35(15-17-48(91)92)55(100)70-24-43(85)68-23-42(84)69-25-46(88)82-51(30(3)4)61(106)77-36(62(107)108)13-10-18-67-63(65)66)79-58(103)38(20-33-11-8-7-9-12-33)80-59(104)39(21-49(93)94)75-45(87)27-71-54(99)34(14-16-47(89)90)74-44(86)26-72-56(101)41(28-83)81-60(105)40(22-50(95)96)78-52(97)31(5)64/h7-9,11-12,29-32,34-41,51,83H,10,13-28,64H2,1-6H3,(H,68,85)(H,69,84)(H,70,100)(H,71,99)(H,72,101)(H,73,102)(H,74,86)(H,75,87)(H,76,98)(H,77,106)(H,78,97)(H,79,103)(H,80,104)(H,81,105)(H,82,88)(H,89,90)(H,91,92)(H,93,94)(H,95,96)(H,107,108)(H4,65,66,67)/t31-,32-,34-,35-,36-,37?,38-,39-,40-,41-,51-/m0/s1
| InChIKey = JWICNZAGYSIBAR-LEEGLKINSA-N
| KEGG =
| MeSHName =
| PubChem = 25078015
| SMILES = C[C@@H](C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H](CCC(=O)O)C(=O)NCC(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CC1=CC=CC=C1)C(=O)NC(CC(C)C)C(=O)N[C@@H](C)C(=O)N[C@@H](CCC(=O)O)C(=O)NCC(=O)NCC(=O)NCC(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CCCN=C(N)N)C(=O)O)N
}}
| Section2 = {{Chembox Properties
| C=63 | H=97 | N=19 | O=26
| MolarMass = 1536.57 g/mol
| Appearance =
| Density =
| MeltingPt =
| BoilingPt =
| Solubility =
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| Section3 = {{Chembox Hazards
| MainHazards =
| FlashPt =
| AutoignitionPt =
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}}
{{Chembox
| ImageFile = Fibrinopeptide B.svg
| ImageSize =
| Name = Fibrinopeptide B
| IUPACName =
| OtherNames = Fibrinopeptide B; Fibrinopeptide B (human); FpB; FPB
| Section1 = {{Chembox Identifiers
| CASNo = 36204-23-6
| ChEBI =
| ChEMBL =
| ChemSpiderID = 17288791
| DrugBank =
| EINECS =
| EC_number =
| InChI = 1S/C66H93N19O25/c1-31(2)53(85-49(91)29-73-55(99)35-16-19-47(89)75-35)64(108)83-42(26-46(68)88)61(105)82-43(27-52(96)97)62(106)81-41(25-45(67)87)60(104)78-37(18-21-51(94)95)57(101)77-36(17-20-50(92)93)56(100)72-28-48(90)76-39(23-33-11-6-4-7-12-33)58(102)80-40(24-34-13-8-5-9-14-34)59(103)84-44(30-86)63(107)74-32(3)54(98)79-38(65(109)110)15-10-22-71-66(69)70/h4-9,11-14,31-32,35-44,53,86H,10,15-30H2,1-3H3,(H2,67,87)(H2,68,88)(H,72,100)(H,73,99)(H,74,107)(H,75,89)(H,76,90)(H,77,101)(H,78,104)(H,79,98)(H,80,102)(H,81,106)(H,82,105)(H,83,108)(H,84,103)(H,85,91)(H,92,93)(H,94,95)(H,96,97)(H,109,110)(H4,69,70,71)/t32-,35-,36-,37-,38-,39-,40-,41-,42-,43-,44-,53-/m0/s1
| InChIKey = MYRIFIVQGRMHRF-OECXYHNASA-N
| KEGG =
| MeSHName =
| PubChem = 16132131
| SMILES = C[C@@H](C(=O)N[C@@H](CCCNC(=N)N)C(=O)O)NC(=O)[C@H](CO)NC(=O)[C@H](CC1=CC=CC=C1)NC(=O)[C@H](CC2=CC=CC=C2)NC(=O)CNC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CC(=O)N)NC(=O)[C@H](CC(=O)O)NC(=O)[C@H](CC(=O)N)NC(=O)[C@H](C(C)C)NC(=O)CNC(=O)[C@@H]3CCC(=O)N3
}}
| Section2 = {{Chembox Properties
| C=66 | H=93 | N=19 | O=25
| MolarMass = 1552.569 g/mol
| Appearance =
| Density =
| MeltingPt =
| BoilingPt =
| Solubility =
}}
| Section3 = {{Chembox Hazards
| MainHazards =
| FlashPt =
| AutoignitionPt =
}}
}}
The fibrinopeptides, fibrinopeptide A (FpA) and fibrinopeptide B (FpB), are peptides which are located in the central region of the fibrous glycoprotein fibrinogen (factor I) and are cleaved by the enzyme thrombin (factor IIa) to convert fibrinogen into covalently-linked fibrin (factor IA) monomers.{{cite journal | vauthors = Weisel JW | title = Fibrinogen and fibrin | journal = Adv Protein Chem | series = Advances in Protein Chemistry | volume = 70 | issue = | pages = 247–99 | date = 2005 | pmid = 15837518 | doi = 10.1016/S0065-3233(05)70008-5 | isbn = 9780120342709 | url = }}{{cite journal | vauthors = Gentry PA | title = Comparative aspects of blood coagulation | journal = Vet J | volume = 168 | issue = 3 | pages = 238–51 | date = November 2004 | pmid = 15501141 | doi = 10.1016/j.tvjl.2003.09.013 | url = }} The N-terminal FpA is cleaved from the Aα chains of fibrinogen and FpB from the Bβ chains of fibrinogen, with FpA released before FpB.{{cite journal | vauthors = Wolberg AS | title = Determinants of fibrin formation, structure, and function | journal = Curr Opin Hematol | volume = 19 | issue = 5 | pages = 349–56 | date = September 2012 | pmid = 22759629 | doi = 10.1097/MOH.0b013e32835673c2 | s2cid = 11358104 | url = }}{{cite journal | last1 = O'Riordan | first1 = Máiread N | last2 = Higgins | first2 = John R | title = Haemostasis in normal and abnormal pregnancy | journal = Best Practice & Research Clinical Obstetrics & Gynaecology | date = June 2003 | volume = 17 | issue = 3 | pages = 385–396 | issn = 1521-6934 | doi = 10.1016/S1521-6934(03)00019-1 | pmid = 12787533| url = }} Subsequent to their formation, fibrin monomers are converted to cross-linked fibrin polymers by the action of thrombin-activated factor XIII (fibrin stabilizing factor), and these fibrin polymers form the backbone of a thrombus (blood clot). Hence, the fibrinopeptides are sensitive markers of fibrinogenesis (fibrin generation), thrombin activity, and coagulation.{{cite journal | vauthors = Mannucci PM | title = Mechanisms, markers and management of coagulation activation | journal = Br Med Bull | volume = 50 | issue = 4 | pages = 851–70 | date = October 1994 | pmid = 7804735 | doi = 10.1093/oxfordjournals.bmb.a072930 | url = }}{{cite book | author1 = Vincent Marks | author2 = Thomas Cantor | author3 = Dusan Mesko | author4 = Rudolf Pullmann | author5 = Gabriela Nosalova | date = 6 December 2012 | title = Differential Diagnosis by Laboratory Medicine: A Quick Reference for Physicians | publisher = Springer Science & Business Media | pages = 443– | isbn = 978-3-642-55600-5 | oclc = 1262382180 | url = https://books.google.com/books?id=_VjrCAAAQBAJ&pg=PA443}}{{cite journal | vauthors = Farris M, Bastianelli C, Rosato E, Brosens I, Benagiano G | title = Pharmacodynamics of combined estrogen-progestin oral contraceptives: 2. effects on hemostasis | journal = Expert Rev Clin Pharmacol | volume = 10 | issue = 10 | pages = 1129–1144 | date = October 2017 | pmid = 28712325 | doi = 10.1080/17512433.2017.1356718 | s2cid = 205931204 | url = }}
FpA is a 16-amino acid peptide. The half-life of FpA is very short at approximately 3 to 5 minutes.{{cite journal | vauthors = Merlini PA, Ardissino D | title = Laboratory Measurement of Thrombin Activity--What Every Clinician Scientist Needs to Know | journal = J Thromb Thrombolysis | volume = 2 | issue = 2 | pages = 85–92 | date = 1995 | pmid = 10608009 | doi = 10.1007/BF01064374 | s2cid = 28203940 | url = }} Hence, FpA levels provide a relatively transient measure of coagulation activation.
Levels of FpA increase with age. FpA levels also gradually increase throughout pregnancy.{{cite journal | vauthors = Hellgren M | title = Hemostasis during normal pregnancy and puerperium | journal = Semin Thromb Hemost | volume = 29 | issue = 2 | pages = 125–30 | date = April 2003 | pmid = 12709915 | doi = 10.1055/s-2003-38897 | s2cid = 22082884 | url = }}{{cite journal | last1 = Koltsova | first1 = Ekaterina | last2 = Balandina | first2 = Anna | last3 = Serebriyskiy | first3 = Ilya | last4 = Vuimo | first4 = Tatiana | last5 = Panteleev | first5 = Mikhail | last6 = Ataullakhanov | first6 = Fazoil | title = Classic and Global Hemostasis Testing in Pregnancy and during Pregnancy Complications | journal = Seminars in Thrombosis and Hemostasis | date = 21 September 2016 | volume = 42 | issue = 7 | pages = 696–716 | issn = 0094-6176 | eissn = 1098-9064 | doi = 10.1055/s-0036-1592303 | pmid = 27652600 | s2cid = 19571354 | url = }} Likewise, FpA levels have been reported to increase with estrogen therapy, including with combined birth control pills and menopausal hormone therapy, although research on FpA levels with these therapies appears to be relatively limited.{{cite journal | vauthors = Douxfils J, Morimont L, Bouvy C | title = Oral Contraceptives and Venous Thromboembolism: Focus on Testing that May Enable Prediction and Assessment of the Risk | journal = Semin Thromb Hemost | volume = 46 | issue = 8 | pages = 872–886 | date = November 2020 | pmid = 33080636 | doi = 10.1055/s-0040-1714140 | s2cid = 224821517 | url = }}{{cite journal | vauthors = Canonico M | title = Hormone therapy and hemostasis among postmenopausal women: a review | journal = Menopause | volume = 21 | issue = 7 | pages = 753–62 | date = July 2014 | pmid = 24937030 | doi = 10.1097/GME.0000000000000296 | s2cid = 20851353 | url = https://www.hal.inserm.fr/inserm-01148743/file/Canonico_Menopause_2014_2.pdf}}{{cite journal | vauthors = Baker L, Meldrum KK, Wang M, Sankula R, Vanam R, Raiesdana A, Tsai B, Hile K, Brown JW, Meldrum DR | title = The role of estrogen in cardiovascular disease | journal = J Surg Res | volume = 115 | issue = 2 | pages = 325–44 | date = December 2003 | pmid = 14697301 | doi = 10.1016/s0022-4804(03)00215-4 | url = }}{{cite journal | vauthors = Farris M, Bastianelli C, Rosato E, Brosens I, Benagiano G | title = Pharmacodynamics of combined estrogen-progestin oral contraceptives: 2. effects on hemostasis | journal = Expert Rev Clin Pharmacol | volume = 10 | issue = 10 | pages = 1129–1144 | date = October 2017 | pmid = 28712325 | doi = 10.1080/17512433.2017.1356718 | s2cid = 205931204 | url = }}
References
{{Reflist}}
{{Coagulation cascade}}
{{Myeloid blood tests}}