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Fukutin and FKRP have functions that affect ocular development in zebrafish independently of dystroglycan.
Muscle pathology in embryos lacking Fukutin or FKRP is different from loss of dystroglycan; knockdown of Fukutin or FKRP leads to a notochord defect and a perturbation of laminin expression before muscle degeneration.
Zebrafish are a useful animal model to reveal the mechanism of muscular dystrophiescaused by mutations in FKRP gene.
It was found that downregulating FKRP in the zebrafish results in embryos which develop a range of abnormalities reminiscent of the developmental defects observed in human muscular dystrophies associated with mutations in FKRP
The FKRP-related disorders should be included as a differential diagnosis in Mexican patients with neuromuscular disorders and normal results on DMD gene deletion/duplication analysis. This and previous reports, along with data from the main genotype databases, collectively suggest that in Mexico the FKRP-related disorders are due to the p.(Asn463Asp) and the common European p.(Leu276Ile) pathogenic variants.
The results suggest that fukutin and FKRP not only participate in the synthesis of O-mannosyl glycans added to alpha-dystroglycan in the endoplasmic reticulum and Golgi complex, but that they could also play a role, that remains to be established, in the nucleus of retinal neurons.
This literature review revealed that pathogenic mutations in the FKRP gene in Asian LGMD2I patients are compound heterozygous rather than homozygous.
Next generation and Sanger sequencing were performed for I-2. Heterozygous FKRP mutations were identified in exon 4: c.1167_1168delGC, p.Gly391Leufs *72 and c.501_502GT>CC, p.Arg167Ser, p.Cys168Arg
Fukutin, FKRP, and TMEM5 form a complex while maintaining each of their enzyme activities. Data showed that endogenous fukutin and FKRP enzyme activities coexist with TMEM5 enzyme activity, and suggest the possibility that formation of this enzyme complex may contribute to specific and prompt biosynthesis of glycans that are required for dystroglycan function.
This study have demonstrated that the clinical heterogeneity in LGMD2I patients, homozygous for FKRP c.826C>A, cannot be explained by histopathological alterations, levels of alpha-DG hypoglycosylation or laminin alpha2 depletion.
Dystrophic Pathology in Diaphragm and Impairment of Cardiac Function in FKRP P448L Mutant Mice
The 13 novel mutations of FKRP significantly expanded the mutation spectrum of MDC1C and LGMD2I, and the different founder mutations indicate the ethnic difference in FKRP mutations.
Fukutin and fukutin-related protein are sequentially acting Rbo5P transferases that use cytidine diphosphate ribitol.
Muscular dystrophies can present with rhabdomyolysis; FKRP mutations are particularly frequent in causing such complication.
This provide a new mouse model of Limb-Girdle Muscular Dystrophy Type 2I homozygous for the Common L276I Mutation.
This study demonistrated that the higher frequency of LGMD2I with cardiomyopathy in mutation of FKRP in Taiwanese patients.
FKRP co-localises with the middle-to-trans-Golgi marker MG160, between the myofibrils in human rectus femoris muscle fibres.
Mutations in FKRP lead to a glycosylation defect and subsequently downregulation of alpha-dystroglycan which constitutes an essential component of the proteoglycan-dystrophin complex.
Study revealed a large homozygous block at the LGMD2I locus, and direct sequencing of FKRP encoding fukutin-related-protein detected the common homozygous c.826 C>A (p.Leu276Ile) mutation.
Two novel heterozygous mutations (c.208T>A and c.1030G>T) in the FKRP gene were identified in Chinese brothers with progressive shoulder and pelvic muscle weakness
This study identified FKRP mutations on both alleles in 88 patients from 69 families with Limb Girdle Muscular Dystrophy Type 2I.
two siblings carrying a homozygous mutation in the start codon of FKRP that is likely to result in a loss of functional FKRP protein. The clinical phenotype of the patients was consistent with Walker-Warburg syndrome
our study confirms that typical clinical symptoms (calf hypertrophy, cardiac involvement, mild LGMD) of LGMD2I due the homozygous c.826C[A mutation, are rather frequent in Germany
Co-injection of fish or human FKRP mRNA along with the morpholino restored normal development and alpha-dystroglycan glycosylation.
This study demonstrated that the Expression of glycosylated alpha-dystroglycan in newborn skeletal and cardiac muscles with FKRP mutation mice.
Reduced Fkrp levels in skeletal muscle are associated with a progressive muscular dystrophy
FKRP mutations are associated with muscular dystrophy.
a reduction in Fkrp influences the ability of tissue-specific forms of alpha-dystroglycan to direct the deposition of several laminin isoforms
investigation of the functional roles of FKRP in muscular dystrophies; FKRP is essential for the functional glycosylation of alpha-dystroglycan;both the mutation itself and the levels of FKRP expression are equally critical for the survival of the animals
Basement membrane (BM) fragility may underlie abnormal phenotypes in fukutin-null embryos, and maintenance of BM function may require fukutin-mediated glycosylation of alpha-dystroglycan early in embryonic development.
data offer the first evidence of a fukutin-related protein (FKRP) complex in muscle and suggest that FKRP may influence the glycosylation status of dystroglycan from within the sarcolemmal dystrophin-glycoprotein complex
results suggest the generation of a mouse model for FKRP related muscular dystrophy requires a knock-down rather than a knock-in strategy in order to give rise to a disease phenotype.
This gene encodes a protein which is targeted to the medial Golgi apparatus and is necessary for posttranslational modification of dystroglycan. Mutations in this gene have been associated with congenital muscular dystrophy, mental retardation, and cerebellar cysts. Several alternatively spliced transcript variants of this gene have been described, but the full-length nature of some of these variants has not been determined.
fukutin related protein
, fukutin-related protein
, fukutin-related protein-like