Raras
Buscar doenças, sintomas, genes...
NÃO RARA NA EUROPA: Trombofilia não rara
ORPHA:64738CID-10 · D68.5DOENÇA RARA

Condição caracterizada por um nível anormalmente elevado de trombos. As causas incluem púrpura trombocitopênica trombótica, coagulação intravascular disseminada, distúrbios da medula óssea e síndrome do anticorpo antifosfolípide.

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Introdução

O que você precisa saber de cara

📋

Condição caracterizada por um nível anormalmente elevado de trombos. As causas incluem púrpura trombocitopênica trombótica, coagulação intravascular disseminada, distúrbios da medula óssea e síndrome do anticorpo antifosfolípide.

🏥
SUS: Sem cobertura SUSScore: 0%
CID-10: D68.5
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Sinais e sintomas

O que aparece no corpo e com que frequência cada sintoma acontece

Partes do corpo afetadas

🩸
Sangue
23 sintomas
🧬
Pele e cabelo
8 sintomas
🧠
Neurológico
8 sintomas
🫃
Digestivo
7 sintomas
🫘
Rins
6 sintomas
❤️
Coração
6 sintomas

+ 57 sintomas em outras categorias

Características mais comuns

Embolia pulmonar
Anormalidade do fator de von Willebrand
Atraso no desenvolvimento da coordenação motora e do desenvolvimento comportamental
Esplenomegalia
Hipertensão portal
Infarto esplênico
127sintomas
Sem dados (127)

Os sintomas variam de pessoa para pessoa. Abaixo estão as 127 características clínicas mais associadas, ordenadas por frequência.

Embolia pulmonarPulmonary embolism
Anormalidade do fator de von WillebrandAbnormality of von Willebrand factor
Atraso no desenvolvimento da coordenação motora e do desenvolvimento comportamentalHP:0040412
EsplenomegaliaSplenomegaly
Hipertensão portalPortal hypertension

Linha do tempo da pesquisa

Publicações por ano — veja quando o interesse científico cresceu
Anos de pesquisa11
Últimos 10 anos19publicações
Pico20165 papers
Linha do tempo
20202015Hoje · 2026📈 2016Ano de pico
Publicações por ano (últimos 10 anos)

Encontrou um erro ou informação desatualizada? Sugira uma correção →

Genética e causas

O que está alterado no DNA e como passa nas famílias

Genes associados

14 genes identificados com associação a esta condição.

THBDThrombomodulinDisease-causing germline mutation(s) inDesconhecido
FUNÇÃO

Endothelial cell receptor that plays a critical role in regulating several physiological processes including hemostasis, coagulation, fibrinolysis, inflammation, and angiogenesis (PubMed:10761923). Acts as a cofactor for thrombin activation of protein C/PROC on the surface of vascular endothelial cells leading to initiation of the activated protein C anticoagulant pathway (PubMed:29323190, PubMed:33836597, PubMed:9395524). Also accelerates the activation of the plasma carboxypeptidase B2/CPB2, w

LOCALIZAÇÃO

Membrane

VIAS BIOLÓGICAS (2)
Common Pathway of Fibrin Clot FormationCell surface interactions at the vascular wall
MECANISMO DE DOENÇA

Thrombophilia due to thrombomodulin defect

A hemostatic disorder characterized by a tendency to thrombosis.

EXPRESSÃO TECIDUAL(Ubíquo)
Skin Sun Exposed Lower leg
112.0 TPM
Pulmão
110.4 TPM
Skin Not Sun Exposed Suprapubic
108.2 TPM
Artéria coronária
91.3 TPM
Aorta
87.3 TPM
OUTRAS DOENÇAS (3)
thrombomodulin-related bleeding disorderatypical hemolytic uremic syndrome with complement gene abnormalityatypical hemolytic-uremic syndrome with thrombomodulin anomaly
HGNC:11784UniProt:P07204
MTHFRMethylenetetrahydrofolate reductase (NADPH)Candidate gene tested inTolerante
FUNÇÃO

Catalyzes the conversion of 5,10-methylenetetrahydrofolate to 5-methyltetrahydrofolate, a cosubstrate for homocysteine remethylation to methionine (PubMed:29891918). Represents a key regulatory connection between the folate and methionine cycles (Probable)

LOCALIZAÇÃO

VIAS BIOLÓGICAS (1)
Metabolism of folate and pterines
MECANISMO DE DOENÇA

Homocystinuria due to deficiency of N(5,10)-methylenetetrahydrofolate reductase activity

An autosomal recessive inborn error of folate metabolism. Clinical severity is variable, ranging from severe neurologic features to absence of symptoms. Clinical features include homocysteinuria, homocysteinemia, developmental delay, severe intellectual disability, perinatal death, psychiatric disturbances, and later-onset neurodegenerative disorders.

EXPRESSÃO TECIDUAL(Ubíquo)
Ovário
25.6 TPM
Nervo tibial
24.0 TPM
Pulmão
21.5 TPM
Baço
21.4 TPM
Tireoide
20.6 TPM
OUTRAS DOENÇAS (6)
homocystinuria due to methylene tetrahydrofolate reductase deficiencyisolated anencephalyisolated exencephalyneural tube defects, folate-sensitive
HGNC:7436UniProt:P42898
F13A1Coagulation factor XIII A chainCandidate gene tested inTolerante
FUNÇÃO

Factor XIII is activated by thrombin and calcium ion to a transglutaminase that catalyzes the formation of gamma-glutamyl-epsilon-lysine cross-links between fibrin chains, thus stabilizing the fibrin clot. Also cross-link alpha-2-plasmin inhibitor, or fibronectin, to the alpha chains of fibrin

LOCALIZAÇÃO

CytoplasmSecreted

VIAS BIOLÓGICAS (1)
Common Pathway of Fibrin Clot Formation
MECANISMO DE DOENÇA

Factor XIII subunit A deficiency

An autosomal recessive hematologic disorder characterized by a life-long bleeding tendency, impaired wound healing and spontaneous abortion in affected women.

EXPRESSÃO TECIDUAL(Ubíquo)
Adipose Visceral Omentum
110.3 TPM
Tecido adiposo
106.0 TPM
Bladder
58.6 TPM
Aorta
55.7 TPM
Artéria coronária
55.2 TPM
OUTRAS DOENÇAS (4)
factor XIII, A subunit, deficiency ofcongenital factor XIII deficiencymyocardial infarction, susceptibility tothrombophilia due to thrombin defect
HGNC:3531UniProt:P00488
HABP2Factor VII-activating proteaseCandidate gene tested inTolerante
FUNÇÃO

Cleaves the alpha-chain at multiple sites and the beta-chain between 'Lys-53' and 'Lys-54' but not the gamma-chain of fibrinogen and therefore does not initiate the formation of the fibrin clot and does not cause the fibrinolysis directly (PubMed:11217080). It does not cleave (activate) prothrombin and plasminogen but converts the inactive single chain urinary plasminogen activator (pro-urokinase) to the active two chain form (PubMed:10754382, PubMed:11217080). Activates coagulation factor VII (

LOCALIZAÇÃO

Secreted

MECANISMO DE DOENÇA

Thyroid cancer, non-medullary, 5

A form of non-medullary thyroid cancer (NMTC), a cancer characterized by tumors originating from the thyroid follicular cells. NMTCs represent approximately 95% of all cases of thyroid cancer and are classified into papillary, follicular, Hurthle cell, and anaplastic neoplasms.

EXPRESSÃO TECIDUAL(Tecido-específico)
Fígado
120.6 TPM
Rim - Córtex
8.6 TPM
Pâncreas
6.3 TPM
Rim - Medula
3.6 TPM
Estômago
2.3 TPM
OUTRAS DOENÇAS (3)
familial papillary or follicular thyroid carcinomathrombophilia due to thrombin defectthyroid cancer, nonmedullary, 5
HGNC:4798UniProt:Q14520
F8Coagulation factor VIIIDisease-causing germline mutation(s) inAltamente restrito
FUNÇÃO

Factor VIII, along with calcium and phospholipid, acts as a cofactor for F9/factor IXa when it converts F10/factor X to the activated form, factor Xa

LOCALIZAÇÃO

Secreted, extracellular space

VIAS BIOLÓGICAS (1)
COPII-mediated vesicle transport
MECANISMO DE DOENÇA

Hemophilia A

A disorder of blood coagulation characterized by a permanent tendency to hemorrhage. About 50% of patients have severe hemophilia resulting in frequent spontaneous bleeding into joints, muscles and internal organs. Less severe forms are characterized by bleeding after trauma or surgery.

EXPRESSÃO TECIDUAL(Ubíquo)
Adipose Visceral Omentum
19.6 TPM
Tecido adiposo
15.7 TPM
Coração - Átrio
13.5 TPM
Mama
12.6 TPM
Ovário
12.6 TPM
OUTRAS DOENÇAS (6)
hemophilia Athrombophilia, X-linked, due to factor 8 defectmoderately severe hemophilia Asevere hemophilia A
HGNC:3546UniProt:P00451
ADAMTS13A disintegrin and metalloproteinase with thrombospondin motifs 13Disease-causing germline mutation(s) inTolerante
FUNÇÃO

Cleaves the vWF multimers in plasma into smaller forms thereby controlling vWF-mediated platelet thrombus formation

LOCALIZAÇÃO

Secreted

VIAS BIOLÓGICAS (1)
O-glycosylation of TSR domain-containing proteins
MECANISMO DE DOENÇA

Thrombotic thrombocytopenic purpura, hereditary

An autosomal recessive hematologic disease characterized by hemolytic anemia with fragmentation of erythrocytes, thrombocytopenia, diffuse and non-focal neurologic findings, decreased renal function and fever.

OUTRAS DOENÇAS (1)
congenital thrombotic thrombocytopenic purpura
HGNC:1366UniProt:Q76LX8
HRGHistidine-rich glycoproteinDisease-causing germline mutation(s) inTolerante
FUNÇÃO

Plasma glycoprotein that binds a number of ligands such as heme, heparin, heparan sulfate, thrombospondin, plasminogen, and divalent metal ions. Binds heparin and heparin/glycosaminoglycans in a zinc-dependent manner. Binds heparan sulfate on the surface of liver, lung, kidney and heart endothelial cells. Binds to N-sulfated polysaccharide chains on the surface of liver endothelial cells. Inhibits rosette formation. Acts as an adapter protein and is implicated in regulating many processes such a

LOCALIZAÇÃO

Secreted

VIAS BIOLÓGICAS (1)
Dissolution of Fibrin Clot
MECANISMO DE DOENÇA

Thrombophilia due to histidine-rich glycoprotein deficiency

A hemostatic disorder characterized by a tendency to thrombosis.

EXPRESSÃO TECIDUAL(Tecido-específico)
Fígado
596.2 TPM
Rim - Medula
10.1 TPM
Rim - Córtex
4.9 TPM
Testículo
0.3 TPM
Skin Sun Exposed Lower leg
0.2 TPM
OUTRAS DOENÇAS (1)
hereditary thrombophilia due to congenital histidine-rich (poly-L) glycoprotein deficiency
HGNC:5181UniProt:P04196
F2ProthrombinDisease-causing germline mutation(s) inRestrito
FUNÇÃO

Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C. Functions in blood homeostasis, inflammation and wound healing. Activates coagulation factor XI (F11); activation is promoted by the contact with negatively charged surfaces (PubMed:2019570, PubMed:21976677). Triggers the production of pro-inflammatory cytokines, such as MCP-1/CCL2 and IL8/CXCL8, in endothelial cells (PubMed:3056

LOCALIZAÇÃO

Secreted, extracellular space

VIAS BIOLÓGICAS (10)
Thrombin signalling through proteinase activated receptors (PARs)Common Pathway of Fibrin Clot FormationIntrinsic Pathway of Fibrin Clot FormationRegulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)Defective F8 cleavage by thrombin
MECANISMO DE DOENÇA

Factor II deficiency

A very rare blood coagulation disorder characterized by mucocutaneous bleeding symptoms. The severity of the bleeding manifestations correlates with blood factor II levels.

EXPRESSÃO TECIDUAL(Tecido-específico)
Fígado
599.6 TPM
Cérebro - Hemisfério cerebelar
1.7 TPM
Cerebelo
1.6 TPM
Testículo
1.4 TPM
Artéria tibial
0.6 TPM
OUTRAS DOENÇAS (5)
congenital prothrombin deficiencythrombophilia due to thrombin defectcerebral sinovenous thrombosisobsolete susceptibility to ischemic stroke
HGNC:3535UniProt:P00734
SERPIND1Heparin cofactor 2Disease-causing germline mutation(s) inTolerante
FUNÇÃO

Thrombin inhibitor activated by the glycosaminoglycans, heparin or dermatan sulfate. In the presence of the latter, HC-II becomes the predominant thrombin inhibitor in place of antithrombin III (AT-III). Also inhibits chymotrypsin, but in a glycosaminoglycan-independent manner Peptides at the N-terminal of HC-II have chemotactic activity for both monocytes and neutrophils Shows negligible inhibition, in vitro, of thrombin and tPA and no inhibition of factor Xa, in vitro

LOCALIZAÇÃO

VIAS BIOLÓGICAS (2)
Post-translational protein phosphorylationRegulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)
MECANISMO DE DOENÇA

Thrombophilia due to heparin cofactor 2 deficiency

A hemostatic disorder characterized by a tendency to recurrent thrombosis.

EXPRESSÃO TECIDUAL(Tecido-específico)
Fígado
195.7 TPM
Útero
2.2 TPM
Ovário
2.0 TPM
Brain Nucleus accumbens basal ganglia
2.0 TPM
Cervix Endocervix
1.3 TPM
OUTRAS DOENÇAS (1)
heparin cofactor 2 deficiency
HGNC:HGNC:4838UniProt:P05546
SERPINC1Antithrombin-IIIDisease-causing germline mutation(s) inAltamente restrito
FUNÇÃO

Most important serine protease inhibitor in plasma that regulates the blood coagulation cascade (PubMed:15140129, PubMed:15853774). AT-III inhibits thrombin, matriptase-3/TMPRSS7, as well as factors IXa, Xa and XIa (PubMed:15140129). Its inhibitory activity is greatly enhanced in the presence of heparin

LOCALIZAÇÃO

Secreted, extracellular space

VIAS BIOLÓGICAS (2)
Post-translational protein phosphorylationRegulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)
MECANISMO DE DOENÇA

Antithrombin III deficiency

An important risk factor for hereditary thrombophilia, a hemostatic disorder characterized by a tendency to recurrent thrombosis. Antithrombin-III deficiency is classified into 4 types. Type I: characterized by a 50% decrease in antigenic and functional levels. Type II: has defects affecting the thrombin-binding domain. Type III: alteration of the heparin-binding domain. Plasma AT-III antigen levels are normal in type II and III. Type IV: consists of miscellaneous group of unclassifiable mutations.

EXPRESSÃO TECIDUAL(Tecido-específico)
Fígado
1054.4 TPM
Testículo
1.0 TPM
Rim - Córtex
0.8 TPM
Sangue
0.5 TPM
Baço
0.5 TPM
OUTRAS DOENÇAS (1)
hereditary antithrombin deficiency
HGNC:775UniProt:P01008
PROS1Vitamin K-dependent protein SDisease-causing germline mutation(s) inRestrito
FUNÇÃO

Anticoagulant plasma protein; it is a cofactor to activated protein C in the degradation of coagulation factors Va and VIIIa. It helps to prevent coagulation and stimulating fibrinolysis

LOCALIZAÇÃO

Secreted

VIAS BIOLÓGICAS (1)
Removal of aminoterminal propeptides from gamma-carboxylated proteins
MECANISMO DE DOENÇA

Thrombophilia due to protein S deficiency, autosomal dominant

A hemostatic disorder characterized by impaired regulation of blood coagulation and a tendency to recurrent venous thrombosis. Based on the plasma levels of total and free PROS1 as well as the serine protease-activated protein C cofactor activity, three types of THPH5 have been described: type I, characterized by reduced total and free PROS1 levels together with reduced anticoagulant activity; type III, in which only free PROS1 antigen and PROS1 activity levels are reduced; and the rare type II which is characterized by normal concentrations of both total and free PROS1 antigen, but low cofactor activity.

EXPRESSÃO TECIDUAL(Ubíquo)
Nervo tibial
167.5 TPM
Aorta
164.2 TPM
Artéria coronária
94.2 TPM
Fígado
83.2 TPM
Fibroblastos
65.1 TPM
OUTRAS DOENÇAS (3)
thrombophilia due to protein S deficiency, autosomal recessivethrombophilia due to protein S deficiency, autosomal dominanthereditary thrombophilia due to congenital protein S deficiency
HGNC:9456UniProt:P07225
F5Coagulation factor VDisease-causing germline mutation(s) inTolerante
FUNÇÃO

Central regulator of hemostasis. It serves as a critical cofactor for the prothrombinase activity of factor Xa that results in the activation of prothrombin to thrombin

LOCALIZAÇÃO

Secreted

VIAS BIOLÓGICAS (1)
Common Pathway of Fibrin Clot Formation
MECANISMO DE DOENÇA

Factor V deficiency

A blood coagulation disorder leading to a hemorrhagic diathesis known as parahemophilia.

EXPRESSÃO TECIDUAL(Tecido-específico)
Fígado
34.2 TPM
Sangue
19.2 TPM
Glândula salivar
8.4 TPM
Pituitária
3.9 TPM
Baço
3.7 TPM
OUTRAS DOENÇAS (9)
congenital factor V deficiencythrombophilia due to activated protein C resistancecerebral sinovenous thrombosisfactor V amsterdam bleeding disorder
HGNC:3542UniProt:P12259
F9Coagulation factor IXDisease-causing germline mutation(s) inAltamente restrito
FUNÇÃO

Factor IX is a vitamin K-dependent plasma protein that participates in the intrinsic pathway of blood coagulation by converting factor X to its active form in the presence of Ca(2+) ions, phospholipids, and factor VIIIa (PubMed:8295821, PubMed:2592373, PubMed:20121197, PubMed:20121198, PubMed:1730085, PubMed:19846852, PubMed:39880037)

LOCALIZAÇÃO

Secreted

VIAS BIOLÓGICAS (2)
Intrinsic Pathway of Fibrin Clot FormationProtein hydroxylation
MECANISMO DE DOENÇA

Hemophilia B

An X-linked blood coagulation disorder characterized by a permanent tendency to hemorrhage, due to factor IX deficiency. It is phenotypically similar to hemophilia A, but patients present with fewer symptoms. Many patients are asymptomatic until the hemostatic system is stressed by surgery or trauma.

EXPRESSÃO TECIDUAL(Tecido-específico)
Fígado
235.3 TPM
Testículo
0.1 TPM
Cervix Ectocervix
0.0 TPM
Baço
0.0 TPM
Cervix Endocervix
0.0 TPM
OUTRAS DOENÇAS (7)
thrombophilia, X-linked, due to factor 9 defecthemophilia Bmild hemophilia Bsymptomatic form of hemophilia B in female carriers
HGNC:3551UniProt:P00740
PROCVitamin K-dependent protein CDisease-causing germline mutation(s) inTolerante
FUNÇÃO

Protein C is a vitamin K-dependent serine protease that regulates blood coagulation by inactivating factors Va and VIIIa in the presence of calcium ions and phospholipids (PubMed:25618265, PubMed:39880037). Exerts a protective effect on the endothelial cell barrier function (PubMed:25651845)

LOCALIZAÇÃO

SecretedGolgi apparatusEndoplasmic reticulum

VIAS BIOLÓGICAS (2)
Post-translational protein phosphorylationRegulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)
MECANISMO DE DOENÇA

Thrombophilia due to protein C deficiency, autosomal dominant

A hemostatic disorder characterized by impaired regulation of blood coagulation and a tendency to recurrent venous thrombosis. Individuals with decreased amounts of protein C are classically referred to as having type I protein C deficiency and those with normal amounts of a functionally defective protein as having type II deficiency.

EXPRESSÃO TECIDUAL(Tecido-específico)
Fígado
241.6 TPM
Rim - Córtex
7.2 TPM
Rim - Medula
6.3 TPM
Estômago
1.9 TPM
Hipotálamo
0.8 TPM
OUTRAS DOENÇAS (3)
thrombophilia due to protein C deficiency, autosomal recessivethrombophilia due to protein C deficiency, autosomal dominanthereditary thrombophilia due to congenital protein C deficiency
HGNC:9451UniProt:P04070

Variantes genéticas (ClinVar)

450 variantes patogênicas registradas no ClinVar.

🧬 THBD: NM_000361.3(THBD):c.563C>T (p.Ala188Val) ()
🧬 THBD: NM_000361.3(THBD):c.1440_1441del (p.Cys480_Asp481delinsTer) ()
🧬 THBD: NM_000361.3(THBD):c.127del (p.Ala43fs) ()
🧬 THBD: NM_000361.3(THBD):c.459G>A (p.Trp153Ter) ()
🧬 THBD: NM_000361.3(THBD):c.920C>A (p.Ser307Ter) ()
Ver todas no ClinVar

Vias biológicas (Reactome)

42 vias biológicas associadas aos genes desta condição.

Common Pathway of Fibrin Clot Formation Cell surface interactions at the vascular wall Metabolism of folate and pterines Platelet degranulation Interleukin-4 and Interleukin-13 signaling Intrinsic Pathway of Fibrin Clot Formation Gamma carboxylation, hypusinylation, hydroxylation, and arylsulfatase activation COPII-mediated vesicle transport Cargo concentration in the ER Defective factor IX causes thrombophilia Defective F8 accelerates dissociation of the A2 domain Defective F8 cleavage by thrombin Defective F8 binding to von Willebrand factor Defective F8 binding to the cell membrane Defective cofactor function of FVIIIa variant Defective F8 secretion Defective F9 variant does not activate FX Defective F8 sulfation at Y1699 Defective B3GALTL causes PpS O-glycosylation of TSR domain-containing proteins Platelet Adhesion to exposed collagen Enhanced cleavage of VWF variant by ADAMTS13 Defective VWF cleavage by ADAMTS13 variant Dissolution of Fibrin Clot Gamma-carboxylation of protein precursors Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus Removal of aminoterminal propeptides from gamma-carboxylated proteins Peptide ligand-binding receptors Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) G alpha (q) signalling events Thrombin signalling through proteinase activated receptors (PARs) Platelet Aggregation (Plug Formation) Defective factor XII causes hereditary angioedema Regulation of Complement cascade Dengue Virus-Host Interactions Post-translational protein phosphorylation Dengue Virus Attachment and Entry Extrinsic Pathway of Fibrin Clot Formation Protein hydroxylation Defective F9 secretion Defective F9 activation Defective gamma-carboxylation of F9

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🇧🇷 Atendimento SUS — NÃO RARA NA EUROPA: Trombofilia não rara

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Publicações mais relevantes

Timeline de publicações
0 papers (10 anos)
#1

Population-Scale Studies of Protein S Abnormalities and Thrombosis.

JAMA2025 Apr 22

Clinical decision-making in thrombotic disorders is impeded by long-standing uncertainty regarding the magnitude of venous and arterial thrombosis risk associated with low protein S. Population-scale multiomic datasets offer an unprecedented opportunity to answer questions regarding the epidemiology and clinical impacts of protein S deficiency. To evaluate the risk associated with protein S deficiency across multiple thrombosis phenotypes. Cross-sectional study using longitudinal population cohorts derived from the UK Biobank (n = 426 436) and the US National Institutes of Health All of Us (n = 204 006) biorepositories. UK Biobank participants were enrolled in 2006-2010 (last follow-up, May 19, 2020) and underwent whole exome sequencing, with a subset (n = 44 431) having protein S levels measured by high-throughput plasma proteomics. Recruitment for All of Us began in 2017 and is ongoing, with participants receiving germline whole genome sequencing. Both cohorts include individual-level data on demographics, laboratory measurements, and clinical outcomes. Presence of rare germline genetic variants in PROS1, segmented by functional impact score (FIS), an in silico prediction of the probability that a genetic variant will disrupt protein activity. Firth logistic regression and linear regression modeling were used to evaluate the thrombosis risk associated with low plasma protein S levels and PROS1 variants across a range of FIS ratings. The UK Biobank cohort was 54.3% female, with a median age of 58.3 (IQR, 50.5-63.7) years at enrollment. Most participants (95.6%) were of European ancestry, and 18 011 had experienced a venous thromboembolism (VTE). In this population cohort, heterozygosity for the highest-risk PROS1 variants with an FIS of 1.0 (nonsense, frameshift, and essential splice site disruptions) was rare (adjusted prevalence, 0.0091% in the UK and 0.0178% in the US) and associated with markedly increased risk of VTE (odds ratio [OR], 14.01; 95% CI, 6.98-27.14; P = 9.09 × 10-11). Plasma proteomics (n = 44 431) demonstrated that carriers of these variants had total protein S levels that were 48.0% of normal (P = .02 compared with noncarriers). In contrast, less damaging missense variants (FIS ≥0.7) occurred more commonly (adjusted prevalence, 0.22% in the UK and 0.20% in the US) and were associated with marginally reduced plasma protein S concentrations and a smaller point estimate for VTE risk (OR, 1.977; 95% CI, 1.552-2.483; P = 1.95 × 10-7). Associations between PROS1 and VTE at both FIS cutoffs were independently validated in the All of Us cohort with similar effect sizes. No association was detected between the presence of coding PROS1 variants and 3 forms of arterial thrombosis: myocardial infarction, peripheral artery disease, and noncardioembolic ischemic stroke. The presence of PROS1 variants correlated poorly with low plasma protein S levels, and protein S deficiency was significantly associated with VTE and peripheral artery disease regardless of PROS1 variant carrier status. The elevated risk of VTE associated with germline loss of function in PROS1 was evident in Kaplan-Meier survival analysis and appeared to persist throughout life (log-rank P = .0005). True inherited loss of function in PROS1 is rare but represents a stronger risk factor for VTE in the general population than previously understood. Acquired, environmental, or trans-acting genetic factors are more likely to cause circulating protein S deficiency than coding variation in PROS1, and low plasma protein S is associated with VTE.

#2

Low-dose direct oral anticoagulants for secondary prevention in patients at high risk for recurrence due to history of recurrent venous thromboembolic events or severe thrombophilia: a retrospective analysis of the Italian Survey on anTicoagulated pAtients RegisTry 2.

Journal of thrombosis and haemostasis : JTH2025 Nov

Long-term anticoagulation is recommended in patients with venous thromboembolism (VTE) deemed at high risk for recurrence (HRR). Limited information is available on patients with recurrent VTE and/or severe thrombophilia. In addition, these patients were not included in studies evaluating long-term treatment with low doses of direct oral anticoagulants (DOACs). The aims of our study were to (1) record the drugs and dosages used in HRR patients, and (2) to record adverse events occurring during follow-up. Among 2520 VTE patients enrolled in the Survey on anTicoagulated pAtients RegisTry 2, we retrospectively analyzed the management of patients with a history of recurrent VTE and/or severe thrombophilia (HRR patients). A total of 487 HRR patients were analyzed. Anticoagulants were stopped in 11 of 487 patients (2.3%), full-dose DOACs were continued in 176 patients (36.1%), and 311 patients (63.9%) were shifted to low-dose DOACs (61.4% with apixaban 2.5 mg twice a day and 38.6% with rivaroxaban 10 mg once a day) after a median time of 1.3 years (range, 0.5-20.2 years). During follow-up, no adverse events were recorded in patients who stopped treatment. Among patients who continued treatment, 10 had recurrent VTE (rate, 0.4 × 100 patient-years) and 19 had bleeding (rate, 0.9 × 100 patient-years). The risk of recurrent VTE was similar between patients on full-dose and low-dose anticoagulation. Patients on full-dose anticoagulation had a trend toward a higher bleeding risk (relative risk, 2.2; 95% CI, 0.7-9.0). HRR patients with a history of unprovoked recurrent VTE and/or patients with severe thrombophilia treated with long-term low-dose DOACs showed a low risk for recurrence and bleeding events.

#3

Increased risk of venous thromboembolism in young and middle-aged individuals with hereditary angioedema: a family study.

Blood2024 Jul 25

Hereditary angioedema (HAE), caused by C1 inhibitor protein deficiency, was recently shown to be associated with an increased risk for venous thromboembolism (VTE). To our knowledge, this is the first national family study of HAE, which aimed to determine the familial risk of VTE. The Swedish Multi-Generation Register was linked to the Swedish National Patient Register for the period of 1964 to 2018. Only patients with HAE with a validated diagnosis were included in the study and were linked to their family members. Hazard ratios (HRs) and 95% confidence intervals (CIs) for VTE were calculated for patients with HAE in comparison with relatives without HAE. Among 2006 individuals (from 276 pedigrees of 365 patients with HAE), 103 individuals were affected by VTE. In total, 35 (9.6%) patients with HAE were affected by VTE, whereas 68 (4.1%) non-HAE relatives were affected (P < .001). The adjusted HR for VTE among patients with HAE was 2.51 (95% CI, 1.67-3.77). Patients with HAE were younger at the first VTE than their non-HAE relatives (mean age, 51 years vs 63 years; P < .001). Before the age of 70 years, the HR for VTE among patients with HAE was 3.62 (95% CI, 2.26-5.80). The HR for VTE for patients with HAE born after 1964 was 8.29 (95% CI, 2.90-23.71). The HR for VTE for patients with HAE who were born in 1964 or earlier was 1.82 (95% CI, 1.14-2.91). HAE is associated with VTE among young and middle-aged individuals in Swedish families with HAE. The effect size of the association is in the order of other thrombophilias. We suggest that HAE may be considered a new rare thrombophilia.

#4

Budd-Chiari Syndrome-A Single Center Experience From the United Kingdom.

Journal of pediatric gastroenterology and nutrition2023 Oct 01

Pediatric Budd-Chiari syndrome (BCS) is a rare cause of portal hypertension and liver disease in Europe and North America. In order to understand the long-term effect of radiological intervention on BCS we performed a single center retrospective review. Fourteen cases were identified; 6 of 14 (43%) had a congenital thrombophilia with many having multiple prothrombotic mutations. Two were managed with medical anticoagulation alone and two required super-urgent transplant for acute liver failure. The remaining 10 of 14 (71%) underwent radiological intervention: 1 of 14 thrombolysis, 5 of 14 angioplasty, and 4 of 14 transjugular intrahepatic portosystemic shunt (TIPS). Six of 14 (43%) patients required repeat radiological intervention (1 angioplasty, 5 TIPS) but none required surgical shunts or liver transplantation for chronic liver disease. The time between diagnosis and treatment did not predict the need for repeat radiological intervention. These data show that radiological intervention can be highly effective, and reduces the need for surgery, though it requires specialist multidisciplinary teams for monitoring.

#5

Multicenter study on recent portal venous system thrombosis associated with cytomegalovirus disease.

Journal of hepatology2022 Jan

Recent non-malignant non-cirrhotic portal venous system thrombosis (PVT) is a rare condition. Among risk factors for PVT, cytomegalovirus (CMV) disease is usually listed based on a small number of reported cases. The aim of this study was to determine the characteristics and outcomes of PVT associated with CMV disease. We conducted a French multicenter retrospective study comparing patients with recent PVT and CMV disease ("CMV positive"; n = 23) to patients with recent PVT for whom CMV testing was negative ("CMV negative"; n = 53) or unavailable ("CMV unknown"; n = 297). Compared to patients from the "CMV negative" and "CMV unknown" groups, patients from the "CMV positive" group were younger, more frequently had fever, and had higher heart rate, lymphocyte count and serum ALT levels (p ≤0.01 for all). The prevalence of immunosuppression did not differ between the 3 groups (4%, 4% and 6%, respectively). Extension of PVT was similar between the 3 groups. Thirteen out of 23 "CMV positive" patients had another risk factor for thrombosis. Besides CMV disease, the number of risk factors for thrombosis was similar between the 3 groups. Heterozygosity for the prothrombin G20210A gene variant was more frequent in "CMV positive" patients (22%) than in the "CMV negative" (4%, p = 0.01) and "CMV unknown" (8%, p = 0.03) groups. Recanalization rate was not influenced by CMV status. In patients with recent PVT, features of mononucleosis syndrome should raise suspicion of CMV disease. CMV disease does not influence thrombosis extension nor recanalization. More than half of "CMV positive" patients have another risk factor for thrombosis, with a particular link to the prothrombin G20210A gene variant. Patients with cytomegalovirus (CMV)-associated portal venous system thrombosis have similar thrombosis extension and evolution as patients without CMV disease. However, patients with CMV-associated portal venous system thrombosis more frequently have the prothrombin G20210A gene variant, suggesting that these entities act synergistically to promote thrombosis.

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📚 EuropePMCmostrando 19

2025

Low-dose direct oral anticoagulants for secondary prevention in patients at high risk for recurrence due to history of recurrent venous thromboembolic events or severe thrombophilia: a retrospective analysis of the Italian Survey on anTicoagulated pAtients RegisTry 2.

Journal of thrombosis and haemostasis : JTH
2025

Population-Scale Studies of Protein S Abnormalities and Thrombosis.

JAMA
2024

Increased risk of venous thromboembolism in young and middle-aged individuals with hereditary angioedema: a family study.

Blood
2023

Budd-Chiari Syndrome-A Single Center Experience From the United Kingdom.

Journal of pediatric gastroenterology and nutrition
2022

Multicenter study on recent portal venous system thrombosis associated with cytomegalovirus disease.

Journal of hepatology
2020

Treatment of acquired thrombotic thrombocytopenic purpura without plasma exchange in selected patients under caplacizumab.

Journal of thrombosis and haemostasis : JTH
2020

[Susceptibility genetics of common conditions in clinical practice].

Medecine sciences : M/S
2019

Incidence of acquired thrombotic thrombocytopenic purpura in Germany: a hospital level study.

Orphanet journal of rare diseases
2019

The International Hereditary Thrombotic Thrombocytopenic Purpura Registry: key findings at enrollment until 2017.

Haematologica
2018

Phase 1, single-dose escalating study of marzeptacog alfa (activated), a recombinant factor VIIa variant, in patients with severe hemophilia.

Journal of thrombosis and haemostasis : JTH
2017

Pulmonary thromboembolism in an emergency hospital: Are our patients different?

Romanian journal of internal medicine = Revue roumaine de medecine interne
2017

Clinical and biochemical characterization of the prothrombin Belgrade mutation in a large Serbian pedigree: new insights into the antithrombin resistance mechanism.

Journal of thrombosis and haemostasis : JTH
2016

Immunochip analysis identifies novel susceptibility loci in the human leukocyte antigen region for acquired thrombotic thrombocytopenic purpura.

Journal of thrombosis and haemostasis : JTH
2016

Child-onset and adolescent-onset acquired thrombotic thrombocytopenic purpura with severe ADAMTS13 deficiency: a cohort study of the French national registry for thrombotic microangiopathy.

The Lancet. Haematology
2016

Hypoglycosylation is a common finding in antithrombin deficiency in the absence of a SERPINC1 gene defect.

Journal of thrombosis and haemostasis : JTH
2016

Founder effect is responsible for the p.Leu131Phe heparin-binding-site antithrombin mutation common in Hungary: phenotype analysis in a large cohort.

Journal of thrombosis and haemostasis : JTH
2015

Cancer-Associated Stroke: The Bergen NORSTROKE Study.

Cerebrovascular diseases extra
2016

High prevalence of hereditary thrombotic thrombocytopenic purpura in central Norway: from clinical observation to evidence.

Journal of thrombosis and haemostasis : JTH
2015

Cumulative Review of Thrombotic Microangiopathy, Thrombotic Thrombocytopenic Purpura, and Hemolytic Uremic Syndrome Reports with Subcutaneous Interferon β-1a.

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Referências e fontes

Bases de dados externas citadas neste artigo

Publicações científicas

Artigos indexados no PubMed ligados a esta doença no grafo RarasNet — título, periódico e PMID direto da fonte, sem intermediação de IA.

  1. Population-Scale Studies of Protein S Abnormalities and Thrombosis.
    JAMA· 2025· PMID 40029645mais citado
  2. Low-dose direct oral anticoagulants for secondary prevention in patients at high risk for recurrence due to history of recurrent venous thromboembolic events or severe thrombophilia: a retrospective analysis of the Italian Survey on anTicoagulated pAtients RegisTry 2.
    Journal of thrombosis and haemostasis : JTH· 2025· PMID 40803569mais citado
  3. Increased risk of venous thromboembolism in young and middle-aged individuals with hereditary angioedema: a family study.
    Blood· 2024· PMID 38767511mais citado
  4. Budd-Chiari Syndrome-A Single Center Experience From the United Kingdom.
    Journal of pediatric gastroenterology and nutrition· 2023· PMID 37314703mais citado
  5. Multicenter study on recent portal venous system thrombosis associated with cytomegalovirus disease.
    Journal of hepatology· 2022· PMID 34563580mais citado
  6. Treatment of acquired thrombotic thrombocytopenic purpura without plasma exchange in selected patients under caplacizumab.
    J Thromb Haemost· 2020· PMID 32757435recente
  7. [Susceptibility genetics of common conditions in clinical practice].
    Med Sci (Paris)· 2020· PMID 32452374recente
  8. Incidence of acquired thrombotic thrombocytopenic purpura in Germany: a hospital level study.
    Orphanet J Rare Dis· 2019· PMID 31730475recente

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