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Multiple coagulation factor deficiency 2

MCFD2, multiple coagulation factor deficiency 2
This gene encodes a soluble luminal protein with two calmodulin-like EF-hand motifs at its C-terminus. This protein forms a complex with LAMN1 (lectin mannose binding protein 1; also known as ERGIC-53) that facilitates the transport of coagulation factors V (FV) and VIII (FVIII) from the endoplasmic reticulum to the Golgi apparatus via an endoplasmic reticulum Golgi intermediate compartment (ERGIC). Mutations in this gene cause combined deficiency of FV and FVIII (F5F8D); a rare autosomal recessive bleeding disorder characterized by mild to moderate bleeding and coordinate reduction in plasma FV and FVIII levels. This protein has also been shown to maintain stem cell potential in adult central nervous system and is a marker for testicular germ cell tumors. The 3' UTR of this gene contains a transposon-like human repeat element named 'THE 1'. A processed RNA pseudogene of this gene is on chromosome 6p22.1. Alternative splicing results in multiple transcript variants encoding distinct isoforms. [provided by RefSeq, Jun 2010] (from NCBI)
Top mentioned proteins: ERGIC-53, FVIII, CAN, HAD, CD45
Papers on MCFD2
Global analyses of Chromosome 17 and 18 genes of lung telocytes compared with mesenchymal stem cells, fibroblasts, alveolar type II cells, airway epithelial cells, and lymphocytes.
Wang et al., Shanghai, China. In Biol Direct, 2014
Of them, Mapk14 and Trem2 were up-regulated to indicate the biological function of TCs in immune regulation, and up-regulated MCFD2 and down-regulated E4F1 and PDCD2 had an association with tissue homeostasis for TCs.
Genotype and phenotype report on patients with combined deficiency of factor V and factor VIII in Iran.
Menegatti et al., Shīrāz, Iran. In Blood Coagul Fibrinolysis, 2014
All exons and intron-exon junctions of lectin mannose binding protein 1 (LMAN1) gene and multiple coagulation factor deficiency 2 genes were amplified by PCR, and subsequently sequenced by the Sanger method.
Structural basis for disparate sugar-binding specificities in the homologous cargo receptors ERGIC-53 and VIP36.
Kato et al., Nagoya, Japan. In Plos One, 2013
In this study, we determined the crystal structure of ERGIC-53-CRD in complex with their binding partner, MCFD2 and the α1,2 mannotriose which corresponds to the trisaccharide of the D1 arm of high-mannose-type glycans.
Combined deficiency of coagulation factors V and VIII: an update.
Zhang et al., Cleveland, United States. In Semin Thromb Hemost, 2013
Disrupting the LMAN1-MCFD2 receptor, complex formation is the primary molecular defect of missense mutations leading to F5F8D.
Multiple coagulation factor deficiency protein 2 contains the ability to support stem cell self-renewal.
Lai et al., Kunming, China. In Faseb J, 2013
Defects in multiple coagulation factor deficiency protein 2 (MCFD2) are a cause of factor V and factor VIII combined deficiency type 2 (F5F8D).
Structural characterization of carbohydrate binding by LMAN1 protein provides new insight into the endoplasmic reticulum export of factors V (FV) and VIII (FVIII).
Zhang et al., Cleveland, United States. In J Biol Chem, 2013
Mutations in LMAN1 or MCFD2 cause the genetic bleeding disorder combined deficiency of FV and FVIII (F5F8D).
Successful percutaneous coronary intervention in a patient with combined deficiency of FV and FVIII due to novel compound heterozygous mutations in LMAN1.
Zhang et al., Gainesville, United States. In Haemophilia, 2013
We used PCI to treat the coronary artery disease in a patient with the combined deficiency of factor V and factor VIII (F5F8D) and analysed the molecular basis of the disorder for this patient.
Regulation of Mac-2BP secretion is mediated by its N-glycan binding to ERGIC-53.
Yamamoto et al., Kashiwa, Japan. In Glycobiology, 2013
Furthermore, we also provide evidence that MCFD2 is involved in the secretion of Mac-2BP.
The COPII pathway and hematologic disease.
Ginsburg et al., Ann Arbor, United States. In Blood, 2012
F5F8D results from mutations in either LMAN1 (lectin mannose-binding protein 1) or MCFD2 (multiple coagulation factor deficiency protein 2), which encode the ER cargo receptor complex LMAN1-MCFD2.
Identification of a novel mutation in the MCFD2 gene in a Tunisian family with combined factor V and VIII deficiency.
Gouider et al., In Tunis Med, 2012
We present the identification of a novel MCFD2 gene missense mutation by direct sequencing.
Unveiling the unfolding pathway of F5F8D disorder-associated D81H/V100D mutant of MCFD2 via multiple molecular dynamics simulations.
Zhan et al., Lexington, United States. In J Biomol Struct Dyn, 2011
Combined factor deficiency (F5F8D) is a rare autosomal recessive disorder caused by mutations in the LMAN1 or MCFD2 genes.
Mice deficient in LMAN1 exhibit FV and FVIII deficiencies and liver accumulation of α1-antitrypsin.
Ginsburg et al., Cleveland, United States. In Blood, 2011
Mutations in either LMAN1 or MCFD2 cause the combined deficiency of factor V (FV) and factor VIII (FVIII; F5F8D), suggesting an ER-to-Golgi cargo receptor function for the LMAN1-MCFD2 complex.
Inherited and acquired factor V deficiency.
Franchini et al., Parma, Italy. In Blood Coagul Fibrinolysis, 2011
The combined deficiency of factor V and FVIII, commonly known as F5F8D, is a recessive disorder not attributable to the association of isolated factor V and FVIII deficiencies, but rather to defective intracellular processing of both proteins due to mutations involving the LMAN1 and MCFD2 genes, which encode two proteins forming an essential cargo receptor complex.
Crystal structure of the LMAN1-CRD/MCFD2 transport receptor complex provides insight into combined deficiency of factor V and factor VIII.
Lindqvist et al., Stockholm, Sweden. In Febs Lett, 2010
Data present the crystal structure of the LMAN1/MCFD2 complex and relate it to patient mutations. Circular dichroism data show that the majority of the substitution mutations give rise to a disordered or severely destabilized MCFD2 protein.
Structural analysis of two novel mutations in MCFD2 gene causing combined coagulation factors V and VIII deficiency.
Elgaaied et al., In Blood Cells Mol Dis, 2010
The study reports for the first time a case of Combined factor V and factor VIII deficiency disorder in a Tunisian family, resulting from two novel mutations in exon 3 of the MCFD2 gene.
EF-hand domains of MCFD2 mediate interactions with both LMAN1 and coagulation factor V or VIII.
Zhang et al., Cleveland, United States. In Blood, 2010
Data show that mutations in MCFD2 that disrupt the tertiary structure and abolish LMAN1 binding still retain the FV/FVIII binding activities, suggesting that this interaction is independent of Ca(2+)-induced folding of the protein.
Combined Factor V and Factor VIII Deficiency.
Peyvandi et al., Milano, Italy. In Semin Thromb Hemost, 2009
Combined deficiency of factor V (FV) and factor VIII (FVIII) (F5F8D, or FV+FVIII) is a autosomal recessive bleeding disorder caused by mutations in genes encoding two components of the endoplasmic reticulum (ER)-Golgi intermediate compartment (ERGIC-53), that is, lectin mannose binding protein ( LMAN1) and multiple coagulation factor deficiency 2 ( MCFD2), involved in the FV and FVIII intracellular transport rather than by DNA defects in the genes that encode the corresponding coagulation factors.
Recent developments in the understanding of the combined deficiency of FV and FVIII.
Zhang, Cleveland, United States. In Br J Haematol, 2009
Recent studies identified mutations in two genes (LMAN1 and MCFD2) as the cause of F5F8D.
The first case of combined coagulation factor V and coagulation factor VIII deficiency in Poland due to a novel p.Tyr135Asn missense mutation in the MCFD2 gene.
Oldenburg et al., Bonn, Germany. In Blood Coagul Fibrinolysis, 2008
2 related patients were homozygous for a new missense mutation in the 2d elongation factor hand domain. Tyr135Asn is the 3d missense mutation found in the MCFD2 gene. It may disrupt the MCFD2-LMAN1 interaction.
Bleeding due to disruption of a cargo-specific ER-to-Golgi transport complex.
Ginsburg et al., Ann Arbor, United States. In Nat Genet, 2003
inactivating mutations in MCFD2 cause combined deficiency of factor V and factor VIII with a phenotype indistinguishable from that caused by mutations in LMAN1
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