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Guttiferone K effectively suppresses the motility and metastasis of hepatocellular carcinoma cells mainly by restoration of aberrantly reduced PFN1 protein expression
Results collectively suggest that PFN1 promotes cell migration and adhesion in bladder cancer models.
These results suggest that although mutant PFN1 aggregation may contribute to neurodegeneration, it does not trigger its onset. Importantly, these experiments establish a progressive disease model that can contribute toward identifying the mechanisms of ALS pathogenesis and the development of therapeutic treatments.
One potential mechanism for C71G-PFN1 to initiate Amyotrophic lateral sclerosis might be the abnormal interaction with membranes as recently established for SOD1 (show SOD1 Proteins) mutants.
Expression of PFN1 mutants induces accumulation of TDP-43 (show TARDBP Proteins), and promotes conversion of normal TDP-43 (show TARDBP Proteins) into an abnormal form. These results provide new insight into the mechanisms of TDP-43 (show TARDBP Proteins) proteinopathies and other diseases associated with amyloid-like protein deposition.
We suggest that reduction of PFN-1 expression by elevated levels of PrP(c (show PRNP Proteins)) may contribute to protective effects PrP(c (show PRNP Proteins))-overexpressing SH-SY5Y cells confer against STS (show STS Proteins)-induced apoptosis
this study shows that in pancreatic cancer patients, PFN1 expression is substantially decreased in peripheral CD8 (show CD8A Proteins)(+) T cells
mutant profilin1 in various diseases with an emphasis on its contribution to the pathogenesis of amyotrophic lateral sclerosis (Review)
Data suggest 2 major isoforms of profilin (Pfn1 and Pfn2) are co-regulated by a common mechanism involving the action of MKL1 [megakaryoblastic leukemia (translocation) 1 protein] that is independent of its SRF- (serum-response factor)-related activity; cellular externalization of Pfn1, rather than transcription, is affected by the perturbations of MKL1; MKL1 can influence cell migration by modulating Pfn1 expression.
novel profilin-1 variants associated with amyotrophic lateral sclerosis
Profilin1 is expressed in osteocytes and regulates cell shape, migration and bone mass.
overexpression of profilin is sufficient to induce cardiomyocyte hypertrophy and sarcomeric remodelling, and silencing of profilin attenuates the hypertrophic response
Pfn1 is a novel target of BMP and suppresses BMP-induced differentiation of osteoblasts at least in part via transcriptional event.
knockdown of either profilin 1 or profilin 2a led to a significant decrease in cell spreading of astrocytes. Moreover, both isoforms proved to be crucial for forskolin-induced astrocytic stellation.
Inactivation of profilin 1 impaired the radial migration of cerebellar granule neurons
Megakaryocyte-specific Profilin1-deficiency alters microtubule stability and causes a Wiskott-Aldrich syndrome-like platelet defect.
Depleting FMNL1 (show FMNL1 Proteins), another Formin (show FMN1 Proteins) family member, resulted in reduced mDia1 expression, while RhoA (show RHOA Proteins) inhibition did not alter mDia1 expression, which indicated that there was a FMNL1 (show FMNL1 Proteins)-mDia1-Profilin1 signaling pathway in mouse oocytes.
association of cortactin (show CTTN Proteins) with Pfn-1 is regulated by c-Abl (show ABL1 Proteins)-mediated cortactin (show CTTN Proteins) phosphorylation
In glioblastomas endothelial cell-specific Pfn-1 phosphorylation elevates HIF-1alpha (show HIF1A Proteins) expression leading to vascular abnormalities and tumor progression.
Pfn1 as a key effector of the integrin linked kinase/Rho/ROCK pathway which acts in parallel with integrin beta1/LCK/Rac1 and regulates Schwann cells lamellipodia formation, radial sorting and myelination during peripheral nervous system maturation.
biophysical analysis reveals that the open nucleotide pocket of the profilin/actin x-ray structure is unstable and closes in the absence of profilin
nitric oxide and free radicals produced under different conditions could alter the functions of profilin through nitration, such as its interaction with actin and poly (l-proline).
Profilin regulates actin dynamics both within the cytoplasm and inside the nuclei of developing mammalian embryos.
Phosphorylation studies indicate that profilin dimers are not phosphorylated while teramers are preferentially phosphorylated over monomers.
PRF1 coordinates the stochastic dynamic properties of actin filaments by modulating formin-mediated actin nucleation and assembly during plant cell expansion.
formed a filamentous network likely associated with actin filaments
protein CYK-1 and the profilin PFN-1 mediate the Arp2/3-independent assembly of cortical microfilaments and are required for cytokinesis in the early embryo
Thus the model organism Caenorhabditis elegans expresses three profilin isoforms and is the first invertebrate animal with tissue-specific profilin expression.
profilin promotes actin organisation
This gene encodes a member of the profilin family of small actin-binding proteins. The encoded protein plays an important role in actin dynamics by regulating actin polymerization in response to extracellular signals. Deletion of this gene is associated with Miller-Dieker syndrome, and the encoded protein may also play a role in Huntington disease. Multiple pseudogenes of this gene are located on chromosome 1.
, profilin 1
, epididymis tissue protein Li 184a
, profilin I
, actin binding protein