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Genetic Disorders of the Autonomic Nervous System
Published in David Robertson, Italo Biaggioni, Disorders of the Autonomic Nervous System, 2019
DBH occurs in both a soluble and a membrane-bound form (Sokoloff, Frigon and O’Connor, 1985). These are present in approximately equal amounts in the vesicle. The soluble enzyme is released into the synaptic cleft at the time of vesicular exocytosis and is presumably the source of the enzyme present in blood. Much recent study has gone into the identification of the differences between these two forms (O’Connor, Frigon and Stone, 1979). Current evidence suggests that both forms of DBH originate from a single gene and that the soluble form is derived from the membrane bound form (Dhawan et al., 1987). There is evidence that neither glypiation (Stewart and Klinman, 1988) nor retained signal peptide (Taylor, Kent and Fleming, 1989) can account fully for the membrane-binding characteristic of the enzyme.
Overview
Published in Stephen W. Carmichael, Susan L. Stoddard, The Adrenal Medulla 1986 - 1988, 2017
Stephen W. Carmichael, Susan L. Stoddard
Dopamine β-hydroxylase continues to be extensively studied. Dhawan, Duong, Ornberg et al. (1987) characterized this soluble enzyme at the molecular level. Work from the laboratory of Villafranca (e.g., Fitzpatrick and Villafranca, 1987) has expanded the understanding of the mechanisms by which dopamine β-hydroxylase converts dopamine to norepinephrine. Kruse, Kaiser, DeWolf et al. (1986a, b) developed more specific inhibitors of dopamine β-hydroxylase. An alternate strategy for the inhibition of dopamine β-hydroxylase was presented by May, Wimalasena, Herman et al. (1988). The primary structure of human dopamine β-hydroxylase was determined by Lamouroux, Vigny, Faucon Biguet et al. (1987). They also presented data which indicated the soluble and membrane-bound forms of the enzyme is from the same molecule. It appears that post-translational glypiation is responsible for modifying the membranous enzyme.
Clinical development of an anti-GPC-1 antibody for the treatment of cancer
Published in Expert Opinion on Biological Therapy, 2022
Saikat Ghosh, Pie Huda, Nicholas Fletcher, Douglas Campbell, Kristofer J. Thurecht, Bradley Walsh
Proteoglycans are composed of glycosylated proteins with covalently attached glycosaminoglycan (GAG) chains [1]. In 1990, David et al. reported their seminal investigation of a novel membrane-associated proteoglycan present in human lung fibroblasts [2]. The cDNA of the proteoglycan was cloned and sequenced by the research group and the core protein was found to contain short hydrophobic amino acid sequences at its C-terminus without a proper cytoplasmic domain. Both these features were reminiscent of membrane-bound phosphatidylinositol-anchored proteins. At the time, the process of phospholipid anchoring through an enzyme-catalyzed transamidation reaction was known as glypiation. This led to proposal of the name ‘Glypican’ by David et al. for the newly discovered ‘glypiated proteoglycan.’