ASGR1

(redirected from ASGPR)

ASGR1

A gene on chromosome 17p13.2 that encodes a subunit of the asialoglycoprotein receptor, which plays a key role in serum glycoprotein homeostasis by mediating the endocytosis and lysosomal degradation of
glycoproteins with exposed terminal galactose or N-acetylgalactosamine residues. Once the ligand binds to the receptor, the ligand-receptor complex is internalised and transported to a sorting organelle, where receptor and ligand part ways. The receptor then returns to the cell membrane to continue the cycle.
References in periodicals archive ?
99m]Tc-GSA) binds to ASGPR expressed on the surfaces of hepatocytes (4).
The activity of ASGPR declines with increasing severity of liver dysfunction because the total volume of ASGPR on the hepatocyte surfaces reflects the total functional volume of the liver.
99m]Tc-GSA--that specifically binds to ASGPR expressed on the membrane surfaces of hepatocytes (4).
Asialoglycoprotein receptor scintigraphy with [sup.99m]Tc-galactosyl human serum albumin ([sup.99m]Tc-GSA) as an early predictor of survival in acute liver failure
SMA smooth musle antibodies, AAA anti-actin antibodies, SLA soluble liver antigen, LP liver-pancreas antigen, LSP liver specific protein, ASGPR asialo-glycoprotein-receptor, LKM liver kidney microsomes, CYP cytochrome P450, AMA anitmitochondrial antibodies, PDH pyruvat dehydrogenase, p-ANCA perinuclear antineutrophile cytoplasmatic antibodies, MRC magnetic resonance cholangiography, HEV hepatitis E virus, HIV human immunodeficiency virus, TTG tissue transglutaminase, TSH thyroid stimulating hormone.
Suspected hepatotoxicity by Cimicifugae racemosae rhizoma (black cohosh, root): critical analysis and structured causality assessment
alternatively, in the same ApoE knockout model, silencing activity was found to be restored by the use of an exogenous GalNAc ligand to engineer iLNPs for targeting to the ASGPR expressed on hepatocytes, with as little as 0.
similarly, in an ASGPR knockout mouse model, in vivo silencing activity of GalNAc-targeted iLNPs was nearly abolished indicating that the GalNAc-ASGPR interaction is responsible for the in vivo activity of the GalNAc-targeted iLNP.
Alnylam Scientists and Collaborators Publish Research on Key Mechanism for Delivery of RNAi Therapeutics with Lipid Nanoparticles (LNPs)
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