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FHL1 encodes a member of the four-and-a-half-LIM-only protein family. Additionally we are shipping Four and A Half LIM Domains 1 Antibodies (118) and Four and A Half LIM Domains 1 Proteins (11) and many more products for this protein.
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Altogether, the specific localization of FHL1B and its modulation in disease-patient's myoblasts confirmed FHL1-related Emery-Dreifuss muscular dystrophy as a nuclear envelope disease.
Low FHL1 expression is associated with head and neck squamous cell carcinoma.
We have uncovered FHL1 as a novel potential regulator of calcium homeostasis in both fish and humans and have implicated it in isolated hypoparathyroidism.
Mutations in FHL1 cause unclassifiable cardiomyopathy with coexisting Emery-Dreifuss muscular dystrophy.
results provide evidence that FHL1A interacts with PLEKHG2 and regulates cell morphological change through the activity of PLEKHG2.
a novel FHL1 splice site variant results in the absence of FHL1A and the abundance of FHL1C, which may contribute to the complex and severe phenotype of Uruguay syndrome.
Knockdown of FHL1 with FHL1 small interfering RNA (siRNA) promoted tumor growth and Cyclin D and cyclin E (show CCNE1 ELISA Kits) were markedly elevated at both the protein and mRNA level.
results indicate that anti-FHL1 autoantibodies in peripheral blood have promising potential as a biomarker to identify a subset of severe IIM.
In healthy individuals, FHL1A is the predominant splice variant and is mainly found in skeletal and cardiac muscle. In two individuals with an Emery-Dreifuss plus phenotype with pulmonary artery hypoplasia and facial dysmorphology, there was demonstrated loss of isoform A and B, and an almost 200-fold overexpression of isoform C.
FRG1 mice overexpressing FHL1 showed an improvement in the dystrophic phenotype
KyoT2 downregulates airway remodeling and resistance in asthmatic mice through a Hes1 (show HES1 ELISA Kits)-dependent mechanism.
Results found that osteogenesis increases with the overexpression of Fhl1 and decreases with reduced Fhl1 expression and suggest that Fhl1 mediates interacting estrogen and Wnt (show WNT2 ELISA Kits) signaling during osteogenesis.
Findings indicate that loss of function is responsible for the myopathy in the Fhl1 W122S knock-in mice.
The CSL-KyoT2 corepressor complex is a negative regulator of Notch (show NOTCH1 ELISA Kits) signaling.
Data show that loss of FHL1 function leads to myopathy in vivo and suggest that loss of function of FHL1 may be one of the mechanisms underlying muscle dystrophy in patients with FHL1 mutations.
Fhl1 transcriptional changes provide salutary effects on stressed myocytes in cardiomyopathy.
Data suggest Fhl1 (four-and-a-half LIM domains protein 1) and FHL2 (four-and-a-half LIM domains protein 2 (show FHL2 ELISA Kits)) bind to and regulate activity of Prkd1 (protein kinase D (show PRKD1 ELISA Kits) 1) in cardiac/ventricular myocytes; knockdown of Fhl1 down-regulates Prkd1 (show PRKD1 ELISA Kits) activation.
A novel mechanism involving four-and-a-half LIM domain protein (show PDLIM7 ELISA Kits)-1 and extracellular signal-regulated kinase-2 (show MAPK1 ELISA Kits) regulates titin (show TTN ELISA Kits) phosphorylation and mechanics.
Wnt (show WNT2 ELISA Kits) signaling induces muscle cell differentiation, at least partly, through Fhl1 activation.
FHL1 is a novel regulator of myosin-binding (show PPP1R12A ELISA Kits) protein C (show PROC ELISA Kits) activity that may have a role in sarcomere assembly
The LIM domain protein (show PDLIM7 ELISA Kits) FHL1C interacts with tight junction protein ZO-1 (show TJP1 ELISA Kits) contributing to the epithelial-mesenchymal transition of a breast adenocarcinoma cell line.
This gene encodes a member of the four-and-a-half-LIM-only protein family. Family members contain two highly conserved, tandemly arranged, zinc finger domains with four highly conserved cysteines binding a zinc atom in each zinc finger. Expression of these family members occurs in a cell- and tissue-specific mode and these proteins are involved in many cellular processes. Mutations in this gene have been found in patients with Emery-Dreifuss muscular dystrophy. Multiple alternately spliced transcript variants which encode different protein isoforms have been described.
four and a half LIM domains 1
, four and a half LIM domains protein 1-like
, four and a half LIM domains a
, four and a half LIM domains protein 1
, Four and a half LIM domains protein 1
, four and a half lim domains protein 1
, LIM protein SLIMMER
, four-and-a-half Lin11, Isl-1 and Mec-3 domains 1
, skeletal muscle LIM-protein 1
, RBP-associated molecule 14-1
, four and a half LIM domains 1 protein