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The protein encoded by HEPACAM is a single-pass type I membrane protein that localizes to the cytoplasmic side of the cell membrane. Zusätzlich bieten wir Ihnen Hepatic and Glial Cell Adhesion Molecule Antikörper (50) und Hepatic and Glial Cell Adhesion Molecule Kits (4) und viele weitere Produktgruppen zu diesem Protein an.
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Out of 20 patients, macrocephaly, classic MRI (zeige C7ORF49 Proteine) features, motor development delay and cognitive impairment were detected in 20(100%), 20(100%), 17(85%) and 4(20%) patients, respectively. 20(100%) were clinically diagnosed with MLC. 19(95%) were genetically diagnosed with 10 novel mutations in MLC1, MLC1 and GlialCAM mutations were identified in 15 and 4 patients, respectively
HepaCAM depletion was discovered in bladder cancer tissues compared with adjacent normal tissues, and the decreased level was associated with the degradation of FoxO3 (zeige FOXO3 Proteine).
HepaCAM proteins were significantly decreased in bladder carcinoma. Low hepaCAM was not statistically associated with clinicopathological characteristics of the patients. HepaCAM overexpression activated caspase 3 (zeige CASP3 Proteine)/8/9, downregulated poly-ADP ribose polymerase (zeige PARP1 Proteine) and p-SMAD2 (zeige SMAD2 Proteine)/3, and decreased apoptosis.
The suppressive roles of HEPACAM in NSCLC.
Due to the ability to reactivate expression of hepaCAM and inhibit growth of bladder cancer cells, AZAC may represent an effective treatment for bladder cancer.
The extracellular domain of GlialCAM is necessary for cell junction targeting and for mediating interactions with itself or with MLC1 and ClC-2 (zeige CLCN2 Proteine).
HepaCAM may prevent the translocation of PKCepsilon (zeige PRKCE Proteine) from cytosolic to particulate fractions, resulting in the inhibition of 786-0 cell proliferation.
GlialCAM is able to interact with all CLC (zeige CLC Proteine) channels tested in this study, targeting them to cell junctions and activating them by stabilizing the open configuration of the common gate
Results allow classifying the effect of HEPACAM gene mutations in different subtypes and authors indicate different cellular mechanisms that lead to megalencephalic leukoencephalopathy pathogenesis.
we demonstrate an evolutionary conserved role for MLC1 in regulating glial surface levels of GLIALCAM, and this interrelationship explains why patients with mutations in either gene (MLC1 or GLIALCAM) share the same clinical phenotype.
Data indicate that membrane protein MLC1 is crucial for proper localization of adhesion molecule (zeige NCAM1 Proteine) GlialCAM and chloride channel (zeige CLCA1 Proteine) ClC-2 (zeige CLCN2 Proteine), and for changing ClC-2 (zeige CLCN2 Proteine) currents.
GlialCAM, an immunoglobulin-like cell adhesion molecule (zeige MCAM Proteine) is expressed in glial cells of the central nervous system.
The protein encoded by this gene is a single-pass type I membrane protein that localizes to the cytoplasmic side of the cell membrane. The encoded protein acts as a homodimer and is involved in cell motility and cell-matrix interactions. The expression of this gene is downregulated or undetectable in many cancer cell lines, so this may be a tumor suppressor gene.
hepatocyte cell adhesion molecule
, protein hepaCAM