Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.1.8 (cholinesterase)
 12,691 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Hepatic binding protein (HBP) is a hepatic cell surface receptor specific for asialoglycoprotein. In vivo estimates of HBP concentration ([HBP]) were compared to classical indicators for hepatic functional reserve to clarify the validity of [HBP] in estimating the hepatic functional reserve in 30 humans. Estimates of [HBP] were obtained based on kinetic analysis of liver and blood time-activity data resulting from the hepatic clearance of a single injection of technetium-99m galactosyl-neoglycoalbumin, which is a synthetic analog radioligand specific to HBP. Estimates of [HBP] ranged 0.054 to 0.720 microM. Estimates of [HBP] in normal volunteers were 0.668 +/- 0.050 microM, whereas that in liver cirrhosis were 0.188 +/- 0.112 microM. The difference between the mean values of [HBP] estimates was statistically significant (p = 0.0001). Good correlations were observed between [HBP] and prothrombin time (r = 0.625, p = 0.0002), serum albumin level (r = 0.687, p = 0.0001), serum cholinesterase level (r = 0.764, p = 0.0001), indocyanine green plasma disappearance rate (r = 0.602, p = 0.0024), and Child-Turcotte classification score (Pugh's modification) (r = -0.797, p = 0.0001). We concluded that excellent correlations of [HBP] with classical indicators for hepatic functional reserve suggest potential value of [HBP] as a sensitive measure of functioning hepatocyte mass.
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PMID:In vivo estimates of hepatic binding protein concentration: correlation with classical indicators of hepatic functional reserve. 238 27

Recent studies have highlighted novel functions of a group of cell adhesion molecules during nervous system development. Members of this protein family are characterized by an extracellular domain with sequence homology to cholinesterases and include the neuroligins, synaptic cell adhesion molecules recently implicated in autism, and neurotactin, a cell surface receptor involved in axonal pathfinding. Although these proteins have a structural organization similar to the enzyme acetylcholinesterase, the cholinesterase domain lacks enzymatic activity and functions as a protein-protein interaction motif. This protein family provides a striking example of how the function of a catalytically active domain has evolved to mediate receptor-ligand interactions that regulate morphogenetic processes during development of the nervous system.
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PMID:Making connections: cholinesterase-domain proteins in the CNS. 1458 2