Thrombotic thrombocytopenic purpura pathophysiology: Difference between revisions
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==Overview== | ==Overview== | ||
== Pathophysiology == | == Pathophysiology == | ||
* The exact pathogenesis of TTP is not completely understood. | * The exact pathogenesis of TTP is not completely understood.<ref name="pmid20058209">{{cite journal |vauthors=Tsai HM |title=Pathophysiology of thrombotic thrombocytopenic purpura |journal=Int. J. Hematol. |volume=91 |issue=1 |pages=1–19 |date=January 2010 |pmid=20058209 |pmc=3159000 |doi=10.1007/s12185-009-0476-1 |url=}}</ref> | ||
* It is understood that TTP is caused by either deficiency of a plasma metalloprotease, ADAMTS13. | * It is understood that TTP is caused by either deficiency of a plasma metalloprotease, ADAMTS13( ('''A''' '''D'''isintegrin '''A'''nd '''M'''etalloprotease with a '''T'''hrombo'''S'''pondin type 1 motif, member '''13'''). ADAMTS13 is member of human family the ADAMTS.<ref name="pmid15554875">{{cite journal |vauthors=Porter S, Clark IM, Kevorkian L, Edwards DR |title=The ADAMTS metalloproteinases |journal=Biochem. J. |volume=386 |issue=Pt 1 |pages=15–27 |date=February 2005 |pmid=15554875 |pmc=1134762 |doi=10.1042/BJ20040424 |url=}}</ref> | ||
The von Willebrand factor (VWF) is produced by the endothelial cells as an ultra-high-molecular-weight multimers. Normally, VWF is sliced by a plasma metalloproteinase called ADAMTS13 into smaller multimers. When the activity or the amount of the protease is not enough, the ultra-high-molecular-weight multimers of VWF commence platelet aggregation and thrombosis in small vessels.<ref name="pmid20058209" | * ADAMTS13 is a plasma reprolysin-like metalloprotease divides von Willebrand factor (VWF).<ref name="pmid23809107">{{cite journal |vauthors=Zheng XL |title=Structure-function and regulation of ADAMTS-13 protease |journal=J. Thromb. Haemost. |volume=11 Suppl 1 |issue= |pages=11–23 |date=June 2013 |pmid=23809107 |pmc=3713533 |doi=10.1111/jth.12221 |url=}}</ref> | ||
* The von Willebrand factor (VWF) is produced by the endothelial cells as an ultra-high-molecular-weight multimers. Normally, VWF is sliced by a plasma metalloproteinase called ADAMTS13 into smaller multimers. When the activity or the amount of the protease is not enough, the ultra-high-molecular-weight multimers of VWF commence platelet aggregation and thrombosis in small vessels.<ref name="pmid20058209" /> | |||
== Genetics == | == Genetics == | ||
Genes involved in the pathogenesis of TTP include:<ref name="pmid28678087">{{cite journal |vauthors=Conboy E, Partain PI, Warad D, Kluge ML, Arndt C, Chen D, Rodriguez V |title=A Severe Case of Congenital Thrombotic Thrombocytopenia Purpura Resulting From Compound Heterozygosity Involving a Novel ADAMTS13 Pathogenic Variant |journal=J. Pediatr. Hematol. Oncol. |volume=40 |issue=1 |pages=60–62 |date=January 2018 |pmid=28678087 |doi=10.1097/MPH.0000000000000895 |url=}}</ref> | Genes involved in the pathogenesis of TTP include:<ref name="pmid28678087">{{cite journal |vauthors=Conboy E, Partain PI, Warad D, Kluge ML, Arndt C, Chen D, Rodriguez V |title=A Severe Case of Congenital Thrombotic Thrombocytopenia Purpura Resulting From Compound Heterozygosity Involving a Novel ADAMTS13 Pathogenic Variant |journal=J. Pediatr. Hematol. Oncol. |volume=40 |issue=1 |pages=60–62 |date=January 2018 |pmid=28678087 |doi=10.1097/MPH.0000000000000895 |url=}}</ref> | ||
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Editor-In-Chief: C. Michael Gibson, M.S., M.D. [1] Associate Editor(s)-in-Chief: Saeedeh Kowsarnia M.D.[2]
Overview
Pathophysiology
- The exact pathogenesis of TTP is not completely understood.[1]
- It is understood that TTP is caused by either deficiency of a plasma metalloprotease, ADAMTS13( (A Disintegrin And Metalloprotease with a ThromboSpondin type 1 motif, member 13). ADAMTS13 is member of human family the ADAMTS.[2]
- ADAMTS13 is a plasma reprolysin-like metalloprotease divides von Willebrand factor (VWF).[3]
- The von Willebrand factor (VWF) is produced by the endothelial cells as an ultra-high-molecular-weight multimers. Normally, VWF is sliced by a plasma metalloproteinase called ADAMTS13 into smaller multimers. When the activity or the amount of the protease is not enough, the ultra-high-molecular-weight multimers of VWF commence platelet aggregation and thrombosis in small vessels.[1]
Genetics
Genes involved in the pathogenesis of TTP include:[4]
mutations in the ADAMTS13 gene.
The development of TTP is the result of inherited ADAMTS13 deficiency but mild phenotype with increased von Willebrand factor level. Upshaw–Schulman syndrome is hereditary of TTP.
References
- ↑ 1.0 1.1 Tsai HM (January 2010). "Pathophysiology of thrombotic thrombocytopenic purpura". Int. J. Hematol. 91 (1): 1–19. doi:10.1007/s12185-009-0476-1. PMC 3159000. PMID 20058209.
- ↑ Porter S, Clark IM, Kevorkian L, Edwards DR (February 2005). "The ADAMTS metalloproteinases". Biochem. J. 386 (Pt 1): 15–27. doi:10.1042/BJ20040424. PMC 1134762. PMID 15554875.
- ↑ Zheng XL (June 2013). "Structure-function and regulation of ADAMTS-13 protease". J. Thromb. Haemost. 11 Suppl 1: 11–23. doi:10.1111/jth.12221. PMC 3713533. PMID 23809107.
- ↑ Conboy E, Partain PI, Warad D, Kluge ML, Arndt C, Chen D, Rodriguez V (January 2018). "A Severe Case of Congenital Thrombotic Thrombocytopenia Purpura Resulting From Compound Heterozygosity Involving a Novel ADAMTS13 Pathogenic Variant". J. Pediatr. Hematol. Oncol. 40 (1): 60–62. doi:10.1097/MPH.0000000000000895. PMID 28678087.