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Study demonstrated that GPC3 expression is inversely associated with glucose metabolism, suggesting that GPC3 may play a role in regulating glucose metabolism in hepatocellular carcinoma.
Invasive hepatocellular carcinoma (HCC (zeige FAM126A Proteine)) samples and HCC (zeige FAM126A Proteine) cell lines with high metastatic potential exhibited higher MXR7 expression. Overexpression of MXR7 promoted epithelial-mesenchymal transition (EMT (zeige ITK Proteine)) progress, and MXR7 depletion repressed the EMT (zeige ITK Proteine) phenotype. Human MXR7 protein is a mediator of EMT (zeige ITK Proteine) and metastasis in HCC (zeige FAM126A Proteine).
Overexpression of GPC3 was significantly associated with poor prognosis in patients with hepatocellular carcinoma.
These data show that glycanation and convertase maturation are not required for soluble mutant GPC3 to inhibit hepatocellular carcinoma cell proliferation.
Data indicate that several microRNAs targeting the oncogenic functions of glypican-3 (GPC3).
GPC3 as a potential metastasis suppressor gene and suggest its value as a prognostic marker in gastric cancer.
In this study we systematically evaluated a series of CAR constructs targeting glypican-3 (GPC3), which is selectively expressed on several solid tumors. We compared GPC3-specific CARs that encoded CD3zeta (zeige CD247 Proteine) (Gz) alone or with costimulatory domains derived from CD28 (zeige CD28 Proteine) (G28z), 4-1BB (zeige TNFRSF9 Proteine) (GBBz), or CD28 (zeige CD28 Proteine) and 4-1BB (zeige TNFRSF9 Proteine) (G28BBz).
Data indicate that glypican-3 (GPC3) is an important regulator of epithelial-mesenchymal transition (EMT (zeige ITK Proteine)) in breast cancer, and a potential target for procedures against breast cancer metastasis.
Glypican-3 overexpression in Wilms tumor correlates with poor overall survival.
glypican-3 has a role in HBV-related hepatocellular carcinoma
This study provides new insights into the roles of GPC1 (zeige GPC1 Proteine) and GPC3 in mandibular morphogenesis. GPC3-knockout reduces mandibular growth, but GPC1 (zeige GPC1 Proteine) does not. These findings along with previous studies indicate that glypicans could be potential therapeutic agents to manage craniosynostosis and associated bony dysmorphology.
Data show that notum (zeige NOTUM Proteine) and glypican-1 (zeige GPC1 Proteine) and glypican-3 gene expression during colorectal cancer (CRC) development and present evidence to suggest them as potential new biomarkers of CRC pathogenesis.
Coupling of pGPC3 to liposomes was essential for effective priming of GPC3-specific CTLs.
The expression of GPC-3 was altered by DEN treatment.
Data suggest that GPC3 down-regulates hepatocyte proliferation by binding to hedgehog (zeige SHH Proteine) (HH) and down-regulating the HH signaling pathway and binding with CD81 (zeige CD81 Proteine), thus making it unavailable to bind to Hhex (zeige HHEX Proteine) and causing its nuclear translocation.
Finding represents a rare four layer genomic overlap consisting of growth associated quantitative trait locus (QTL), body mass associated Gpc3 gene, highly conserved miRNA gene and mature miRNA seed SNP identified in the lean mouse.
Hepatocyte overexpression of GPC3 suppresses hepatocyte proliferation and liver regeneration and alters gene expression profiles.
glypican-3 is involved in the recruitment of M2-polarized tumor-associated macrophages in hepatocellular carcinoma
GPC3 inhibits the PI3K/Akt (zeige AKT1 Proteine) anti-apoptotic pathway while it stimulates the p38MAPK (zeige MAPK14 Proteine) stress-activated one in murine mammary adenocarcinoma LM3 cells
Gpc3 function in development of Simpson-Golabi-Behmel syndrome is IGF-independent
Cell surface heparan sulfate proteoglycans are composed of a membrane-associated protein core substituted with a variable number of heparan sulfate chains. Members of the glypican-related integral membrane proteoglycan family (GRIPS) contain a core protein anchored to the cytoplasmic membrane via a glycosyl phosphatidylinositol linkage. These proteins may play a role in the control of cell division and growth regulation. The protein encoded by this gene can bind to and inhibit the dipeptidyl peptidase activity of CD26, and it can induce apoptosis in certain cell types. Deletion mutations in this gene are associated with Simpson-Golabi-Behmel syndrome, also known as Simpson dysmorphia syndrome. Alternative splicing results in multiple transcript variants.
, glypican proteoglycan 3
, heparan sulphate proteoglycan
, intestinal protein OCI-5
, secreted glypican-3
, defective in Simpson-Golabi-Behmel overgrowth syndrome
, proteoglycan GPC3
, Intestinal protein OCI-5