Microvillus inclusion disease
|
1.000 |
GeneticVariation
|
disease |
BEFREE |
Loss-of-function mutations in the nonconventional myosin Vb (Myo5b) result in microvillus inclusion disease (MVID) and massive secretory diarrhea that often begins at birth.
|
31664880 |
2019 |
Microvillus inclusion disease
|
1.000 |
GeneticVariation
|
disease |
BEFREE |
These findings indicate that the effects of the P660L mutation in MYO5B in Navajo MVID patients are not limited to the small intestine, but that certain tissues may be able to compensate functionally for alterations in apical trafficking.
|
29218485 |
2018 |
Microvillus inclusion disease
|
1.000 |
GeneticVariation
|
disease |
BEFREE |
Examination of altered apical trafficking in patients with Microvillus Inclusion disease caused by inactivating mutations in MYO5B has led to insights into the regulation of apical trafficking by elements of the apical recycling system.
|
28264818 |
2018 |
Microvillus inclusion disease
|
1.000 |
GeneticVariation
|
disease |
BEFREE |
Inactivating mutations in MYO5B cause microvillus inclusion disease (MVID), but the physiological cause of the diarrhea associated with this disease is unclear.
|
30144427 |
2018 |
Microvillus inclusion disease
|
1.000 |
Biomarker
|
disease |
GENOMICS_ENGLAND |
Animal models have been generated that formally prove the causality between MYO5B and MVID.
|
29266534 |
2018 |
Microvillus inclusion disease
|
1.000 |
GeneticVariation
|
disease |
BEFREE |
MYO5B mutations cause cholestasis with normal serum gamma-glutamyl transferase activity in children without microvillous inclusion disease.
|
27532546 |
2017 |
Microvillus inclusion disease
|
1.000 |
Biomarker
|
disease |
BEFREE |
The present study used Myo5b loss-of-function human MVID intestine, polarized intestinal cell models of secretory crypt (T84) and villus resembling (CaCo2BBe, C2BBe) enterocytes lacking Myo5b in conjunction with immunofluorescence confocal stimulated emission depletion (gSTED) imaging, immunohistochemical staining, transmission electron microscopy, shRNA silencing, immunoblots, and electrophysiological approaches to examine the distribution, expression, and function of the major BB ion transporters NHE3 (Na(+)), CFTR (Cl(-)), and SLC26A3 (DRA) (Cl(-)/HCO3 (-)) that control intestinal fluid transport.
|
27229121 |
2016 |
Microvillus inclusion disease
|
1.000 |
Biomarker
|
disease |
BEFREE |
Finally, we found that this loss of polarity was specific for MVID: tissue samples of patients with Myo5B-independent absorption disorders showed normal polarity but we identified Cdc42 as a potentially essential biomarker for trichohepatoenteric syndrome.
|
26526116 |
2016 |
Microvillus inclusion disease
|
1.000 |
GeneticVariation
|
disease |
BEFREE |
We propose that the zebrafish gsp/myoVb mutant is a valuable model to study the pathophysiology of MVID.
|
27497746 |
2016 |
Microvillus inclusion disease
|
1.000 |
GeneticVariation
|
disease |
BEFREE |
Mutations in the myosin Vb gene (MYO5B) have been identified in the majority of MVID patients.
|
26392529 |
2015 |
Microvillus inclusion disease
|
1.000 |
Biomarker
|
disease |
MGD |
Myo5b knockout mice closely resemble the phenotype of MVID patients and constitute a useful model to further investigate the underlying molecular mechanism of this disease and to preclinically assess the efficacy of novel therapeutic approaches.
|
26201991 |
2015 |
Microvillus inclusion disease
|
1.000 |
GeneticVariation
|
disease |
BEFREE |
Our aim was to investigate the mechanisms by which MYO5B mutations affect hepatic biliary function and lead to cholestasis in MVID patients.
|
24375397 |
2014 |
Microvillus inclusion disease
|
1.000 |
Biomarker
|
disease |
BEFREE |
Although myosin Vb is implicated in the organization of intracellular transport and cell surface polarity in epithelial cells, its precise role in the pathogenesis of MVID is unknown.
|
24138727 |
2014 |
Microvillus inclusion disease
|
1.000 |
GeneticVariation
|
disease |
BEFREE |
Most patients with MVID have mutations in myosin Vb that cause defects in recycling of apical vesicles.
|
24726755 |
2014 |
Microvillus inclusion disease
|
1.000 |
GeneticVariation
|
disease |
BEFREE |
We observe a similar loss of the subapical enrichment of Rab11a and the kinases and reduced phosphorylation of ezrin in microvillus inclusion disease, which is associated with MYO5B mutations, intestinal microvilli atrophy and malabsorption.
|
24413175 |
2014 |
Microvillus inclusion disease
|
1.000 |
GeneticVariation
|
disease |
UNIPROT |
In patients with MVID, MYO5B-P660L results in global changes in polarity at the villus tips that could account for deficits in apical absorption, loss of microvilli, aberrant junctions, and losses in transcellular ion transport pathways, likely leading to the MVID clinical phenotype of neonatal secretory diarrhea.
|
24892806 |
2014 |
Microvillus inclusion disease
|
1.000 |
GeneticVariation
|
disease |
BEFREE |
In patients with MVID, MYO5B-P660L results in global changes in polarity at the villus tips that could account for deficits in apical absorption, loss of microvilli, aberrant junctions, and losses in transcellular ion transport pathways, likely leading to the MVID clinical phenotype of neonatal secretory diarrhea.
|
24892806 |
2014 |
Microvillus inclusion disease
|
1.000 |
Biomarker
|
disease |
BEFREE |
PDK1 was aberrantly localized in human MVID enterocytes and Myo5b-deficient Caco-2BBe cells.
|
25258405 |
2014 |
Microvillus inclusion disease
|
1.000 |
GeneticVariation
|
disease |
UNIPROT |
We performed correlative immunohistochemistry analyses of sections from duodenal biopsies of a MVID patient, compound heterozygous for two novel MYO5B mutations, predicting loss of function of myosin Vb in duodenal enterocytes together with a stable MYO5B CaCo2 RNAi cell system.
|
24138727 |
2014 |
Microvillus inclusion disease
|
1.000 |
Biomarker
|
disease |
BEFREE |
We also review animal models for MVID and the latest data on functional studies related to the myosin Vb protein.
|
24014347 |
2013 |
Microvillus inclusion disease
|
1.000 |
GeneticVariation
|
disease |
BEFREE |
MYO5B mutations in patients with MVID with renal Fanconi syndrome do not correlate with aberrant apical plasma membrane morphology or altered apical recycling endosome organization in renal tubular epithelial cells.
|
22441677 |
2012 |
Microvillus inclusion disease
|
1.000 |
Biomarker
|
disease |
BEFREE |
Our functional analysis indicates that MYO5B mutations can be correlated with an aberrant subcellular distribution of the myosin Vb protein, and apical recycling endosomes, which, together with the additional compound heterozygous mutations, significantly strengthen the link between MYO5B and MVID.
|
21206382 |
2011 |
Microvillus inclusion disease
|
1.000 |
GeneticVariation
|
disease |
UNIPROT |
Our functional analysis indicates that MYO5B mutations can be correlated with an aberrant subcellular distribution of the myosin Vb protein, and apical recycling endosomes, which, together with the additional compound heterozygous mutations, significantly strengthen the link between MYO5B and MVID.
|
21206382 |
2011 |
Microvillus inclusion disease
|
1.000 |
Biomarker
|
disease |
BEFREE |
Our data indicate that MYO5B mutations are a major cause of microvillus inclusion disease and that MYO5B knock-down recapitulates most of the cellular phenotype in vitro, thus independently showing loss of MYO5B function as the cause of microvillus inclusion disease.
|
20186687 |
2010 |
Microvillus inclusion disease
|
1.000 |
GeneticVariation
|
disease |
BEFREE |
Molecular analysis of the MYO5B gene is helpful in genetic counseling and prenatal diagnosis of recurrent microvillus inclusion disease in subsequent pregnancies.
|
21199752 |
2010 |