Fibrinopéptido

Fibrinopéptido B
	Nome IUPAC Ácido (4S)-4-[[(2S)-2-[[(2S)-4-amino-2-[[(2S)-2-[[(2S)-4-amino-2-[[(2S)-3-metil-2-[[2-[[(2S)-5-oxopirrolidina-2-carbonil]amino]acetil]amino]butanoil]amino]-4-oxobutanoil]amino]-3-carboxipropanoil]amino]-4-oxobutanoil]amino]-4-carboxibutanoil]amino]-5-[[2-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(1S)-4-carbamimidamido-1-carboxibutil]amino]-1-oxopropan-2-il]amino]-3-hidroxi-1-oxopropan-2-il]amino]-1-oxo-3-fenilpropan-2-il]amino]-1-oxo-3-fenilpropan-2-il]amino]-2-oxoetil]amino]-5-oxopentanoico
	Outros nomes Fibrinopéptido B; Fibrinopéptido B (humano); FpB; FPB
Identificadores
Número CAS	36204-23-6
PubChem	16132131
ChemSpider	17288791
Imaxes 3D Jmol	Image 1
	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 ;
	InChI 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; Key: MYRIFIVQGRMHRF-OECXYHNASA-N;
Propiedades
Fórmula molecular	C66H93N19O25
Masa molar	1.552,56 g mol−1
	Se non se indica outra cousa, os datos están tomados en condicións estándar de 25 °C e 100 kPa.

Fibrinopéptio A
	Nome IUPAC Ácido (4S)-4-[[2-[[(2S)-2-[[(2S)-2-[[(2S)-2-aminopropanoil]amino]-3-carboxipropanoil]amino]-3-hidroxipropanoil]amino]acetil]amino]-5-[[2-[[(2S)-3-carboxi-1-[[(2S)-1-[[1-[[(2S)-1-[[(2S)-4-carboxi-1-[[2-[[2-[[2-[[(2S)-1-[[(1S)-1-carboxi-4-(diaminometilideneamino)butil]amino]-3-metil-1-oxobutan-2-il]amino]-2-oxoetil]amino]-2-oxoetil]amino]-2-oxoetil]amino]-1-oxobutan-2-il]amino]-1-oxopropan-2-il]amino]-4-metil-1-oxopentan-2-il]amino]-1-oxo-3-fenilpropan-2-il]amino]-1-oxopropan-2-il]amino]-2-oxoetil]amino]-5-oxopentanoico
	Outros nomes Fibrinopéptido A; Fibrinopéptido A (humano); FpA; FPA
Identificadores
Número CAS	25422-31-5
PubChem	25078015
ChemSpider	17286499
Imaxes 3D Jmol	Image 1
	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 ;
	InChI 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; Key: JWICNZAGYSIBAR-LEEGLKINSA-N;
Propiedades
Fórmula molecular	C63H97N19O26
Masa molar	1.536,56 g mol−1
	Se non se indica outra cousa, os datos están tomados en condicións estándar de 25 °C e 100 kPa.

Os fibrinopéptidos, que son o fibrinopéptido A (FpA) e o fibrinopéptido B (FpB), son péptidos que formaban parte da rexión central da glicoproteína fibrosa fibrinóxeno (factor I da coagulación do sangue) e que foron cortados e separados de alí polo encima trombina (factor IIa) para converter o fibrinóxeno en monómeros de fibrina (factor IA) unidos covalentemente.^[1]^[2] O N-terminal do FpA é escindido das cadeas Aα do fibrinóxeno e o FpB das cadeas Bβ do fibrinóxeno, e o FpA libérase antes que o FpB.^[3]^[4] Despois da súa formación, os monómeros de fibrina son convertidos en polímeros de fibrina con enlaces cruzados ou reticulados pola acción da factor XIII activado pola trombina (factor estabilizante da fibrina), e estes polímeros de fibrina forman o núcleo dun trombo (coágulo sanguíneo).^[2] Por tanto, os fibrinopéptidos son marcadores sensibles da fibrinoxénese (xeración de fibrina), da actividade da trombina e da coagulación do sangue.^[5]^[6]^[7]^[8]

O FpA é un péptido de 16 aminoácidos.^[8] A vida media do FpA é moi curta, de aproximadamente de 3 a 5 minutos.^[5]^[8] Por tanto, os niveis de FpA proporcionan unha medida relativamente transitoria a activación da coagulación.^[8]

Os niveis de FpA increméntanse coa idade.^[5] Tamén se incrementan conforme avanza o embarazo.^[9]^[10] Igualmente, os niveis de FpA increméntanse coas terapias con estróxenos, como a pílula anticonceptiva combinada ou a terapia hormonal menopáusica, aínda que as investigacións sobre os niveis de FpA con esas terapias parecen ser relativamente limitadas.^[11]^[12]^[13]^[7]

Notas

↑ Weisel JW (2005). "Fibrinogen and fibrin". Adv Protein Chem. Advances in Protein Chemistry 70: 247–99. ISBN 9780120342709. PMID 15837518. doi:10.1016/S0065-3233(05)70008-5.
↑ ^2,0 ^2,1 Gentry PA (novembro de 2004). "Comparative aspects of blood coagulation". Vet J 168 (3): 238–51. PMID 15501141. doi:10.1016/j.tvjl.2003.09.013.
↑ Wolberg AS (setembro de 2012). "Determinants of fibrin formation, structure, and function". Curr Opin Hematol 19 (5): 349–56. PMID 22759629. doi:10.1097/MOH.0b013e32835673c2.
↑ O'Riordan, Máiread N; Higgins, John R (xuño de 2003). "Haemostasis in normal and abnormal pregnancy". Best Practice & Research Clinical Obstetrics & Gynaecology 17 (3): 385–396. ISSN 1521-6934. PMID 12787533. doi:10.1016/S1521-6934(03)00019-1.
↑ ^5,0 ^5,1 ^5,2 Mannucci PM (outubro de 1994). "Mechanisms, markers and management of coagulation activation". Br Med Bull 50 (4): 851–70. PMID 7804735. doi:10.1093/oxfordjournals.bmb.a072930.
↑ Vincent Marks; Thomas Cantor; Dusan Mesko; Rudolf Pullmann; Gabriela Nosalova (6 de decembro de 2012). Differential Diagnosis by Laboratory Medicine: A Quick Reference for Physicians. Springer Science & Business Media. pp. 443–. ISBN 978-3-642-55600-5. OCLC 1262382180.
↑ ^7,0 ^7,1 Farris M, Bastianelli C, Rosato E, Brosens I, Benagiano G (outubro de 2017). "Pharmacodynamics of combined estrogen-progestin oral contraceptives: 2. effects on hemostasis". Expert Rev Clin Pharmacol 10 (10): 1129–1144. PMID 28712325. doi:10.1080/17512433.2017.1356718.
↑ ^8,0 ^8,1 ^8,2 ^8,3 Merlini PA, Ardissino D (1995). "Laboratory Measurement of Thrombin Activity--What Every Clinician Scientist Needs to Know". J Thromb Thrombolysis 2 (2): 85–92. PMID 10608009. doi:10.1007/BF01064374.
↑ Hellgren M (abril de 2003). "Hemostasis during normal pregnancy and puerperium". Semin Thromb Hemost 29 (2): 125–30. PMID 12709915. doi:10.1055/s-2003-38897.
↑ Koltsova, Ekaterina; Balandina, Anna; Serebriyskiy, Ilya; Vuimo, Tatiana; Panteleev, Mikhail; Ataullakhanov, Fazoil (21 de setembro de 2016). "Classic and Global Hemostasis Testing in Pregnancy and during Pregnancy Complications". Seminars in Thrombosis and Hemostasis 42 (7): 696–716. ISSN 0094-6176. PMID 27652600. doi:10.1055/s-0036-1592303.
↑ Douxfils J, Morimont L, Bouvy C (novembro de 2020). "Oral Contraceptives and Venous Thromboembolism: Focus on Testing that May Enable Prediction and Assessment of the Risk". Semin Thromb Hemost 46 (8): 872–886. PMID 33080636. doi:10.1055/s-0040-1714140.
↑ Canonico M (xullo de 2014). "Hormone therapy and hemostasis among postmenopausal women: a review" (PDF). Menopause 21 (7): 753–62. PMID 24937030. doi:10.1097/GME.0000000000000296.
↑ Baker L, Meldrum KK, Wang M, Sankula R, Vanam R, Raiesdana A, Tsai B, Hile K, Brown JW, Meldrum DR (decembro de 2003). "The role of estrogen in cardiovascular disease". J Surg Res 115 (2): 325–44. PMID 14697301. doi:10.1016/s0022-4804(03)00215-4.

[pmid15837518-1] Weisel JW (2005). "Fibrinogen and fibrin". Adv Protein Chem. Advances in Protein Chemistry 70: 247–99. ISBN 9780120342709. PMID 15837518. doi:10.1016/S0065-3233(05)70008-5.

[pmid15501141-2] 2,0 ^2,1 Gentry PA (novembro de 2004). "Comparative aspects of blood coagulation". Vet J 168 (3): 238–51. PMID 15501141. doi:10.1016/j.tvjl.2003.09.013.

[pmid22759629-3] Wolberg AS (setembro de 2012). "Determinants of fibrin formation, structure, and function". Curr Opin Hematol 19 (5): 349–56. PMID 22759629. doi:10.1097/MOH.0b013e32835673c2.

[O'RiordanHiggins2003-4] O'Riordan, Máiread N; Higgins, John R (xuño de 2003). "Haemostasis in normal and abnormal pregnancy". Best Practice & Research Clinical Obstetrics & Gynaecology 17 (3): 385–396. ISSN 1521-6934. PMID 12787533. doi:10.1016/S1521-6934(03)00019-1.

[pmid7804735-5] 5,0 ^5,1 ^5,2 Mannucci PM (outubro de 1994). "Mechanisms, markers and management of coagulation activation". Br Med Bull 50 (4): 851–70. PMID 7804735. doi:10.1093/oxfordjournals.bmb.a072930.

[MarksCantorMesko2012-6] Vincent Marks; Thomas Cantor; Dusan Mesko; Rudolf Pullmann; Gabriela Nosalova (6 de decembro de 2012). Differential Diagnosis by Laboratory Medicine: A Quick Reference for Physicians. Springer Science & Business Media. pp. 443–. ISBN 978-3-642-55600-5. OCLC 1262382180.

[pmid28712325-7] 7,0 ^7,1 Farris M, Bastianelli C, Rosato E, Brosens I, Benagiano G (outubro de 2017). "Pharmacodynamics of combined estrogen-progestin oral contraceptives: 2. effects on hemostasis". Expert Rev Clin Pharmacol 10 (10): 1129–1144. PMID 28712325. doi:10.1080/17512433.2017.1356718.

[pmid10608009-8] 8,0 ^8,1 ^8,2 ^8,3 Merlini PA, Ardissino D (1995). "Laboratory Measurement of Thrombin Activity--What Every Clinician Scientist Needs to Know". J Thromb Thrombolysis 2 (2): 85–92. PMID 10608009. doi:10.1007/BF01064374.

[pmid12709915-9] Hellgren M (abril de 2003). "Hemostasis during normal pregnancy and puerperium". Semin Thromb Hemost 29 (2): 125–30. PMID 12709915. doi:10.1055/s-2003-38897.

[KoltsovaBalandinaSerebriyskiy2016-10] Koltsova, Ekaterina; Balandina, Anna; Serebriyskiy, Ilya; Vuimo, Tatiana; Panteleev, Mikhail; Ataullakhanov, Fazoil (21 de setembro de 2016). "Classic and Global Hemostasis Testing in Pregnancy and during Pregnancy Complications". Seminars in Thrombosis and Hemostasis 42 (7): 696–716. ISSN 0094-6176. PMID 27652600. doi:10.1055/s-0036-1592303.

[pmid33080636-11] Douxfils J, Morimont L, Bouvy C (novembro de 2020). "Oral Contraceptives and Venous Thromboembolism: Focus on Testing that May Enable Prediction and Assessment of the Risk". Semin Thromb Hemost 46 (8): 872–886. PMID 33080636. doi:10.1055/s-0040-1714140.

[pmid24937030-12] Canonico M (xullo de 2014). "Hormone therapy and hemostasis among postmenopausal women: a review" (PDF). Menopause 21 (7): 753–62. PMID 24937030. doi:10.1097/GME.0000000000000296.

[pmid14697301-13] Baker L, Meldrum KK, Wang M, Sankula R, Vanam R, Raiesdana A, Tsai B, Hile K, Brown JW, Meldrum DR (decembro de 2003). "The role of estrogen in cardiovascular disease". J Surg Res 115 (2): 325–44. PMID 14697301. doi:10.1016/s0022-4804(03)00215-4.

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