Novel Corticosteroid-Binding Globulin Variant That Lacks Steroid Binding Activity
نویسندگان
چکیده
منابع مشابه
Residues in the human corticosteroid-binding globulin reactive center loop that influence steroid binding before and after elastase cleavage.
Corticosteroid-binding globulin (CBG) is a non-inhibitory serine proteinase inhibitor (serpin) that transports cortisol and progesterone in blood. Crystal structures of rat CBG and a thrombin-cleaved human CBG:anti-trypsin (Pittsburgh) chimera show how structural transitions after proteolytic cleavage of the CBG reactive center loop (RCL) could disrupt steroid binding. This ligand release mecha...
متن کاملGlycosylation of human corticosteroid-binding globulin at aspargine 238 is necessary for steroid binding.
Human corticosteroid binding-globulin (CBG) is a plasma glycoprotein that binds and regulates the biological activity of glucocorticoids and progesterone. Carbohydrates comprise approximately 25% of its molecular mass being represented by bi- and triantennary N-linked oligosaccharides of the N-acetyllactosamine type. To assess the impact of these carbohydrate chains on CBG production and steroi...
متن کاملAn amino acid substitution in biobreeding rat corticosteroid binding globulin results in reduced steroid binding affinity.
BioBreeding (BB) rats are derived from an outbred colony of Wistar rats and are used as a model of autoimmune diabetes mellitus. A corticosteroid binding globulin (CBG) variant with reduced affinity for glucocorticoids has now been found in the blood of these animals. The dissociation rate constants of BB CBG for cortisol (4.42 nM) and corticosterone (1.43 nM) are both about 50% higher than tho...
متن کاملSpecific binding of human corticosteroid-binding globulin to cell membranes.
Specific binding sites for corticosteroid-binding globulin were detected on membranes prepared from human prostates. The binding sites are typical of membrane receptors: they are saturable and specific and have high affinity. There was little specific binding at 4 degrees C and 23 degrees C. Maximal specific binding was obtained at 37 degrees C. Scatchard analysis revealed the presence of a sin...
متن کاملCharacterization of mini-protein S, a recombinant variant of protein S that lacks the sex hormone binding globulin-like domain.
Protein S is a vitamin K-dependent glycoprotein involved in the regulation of the anticoagulant activity of activated protein C (APC). Also, an anticoagulant role for protein S, independent of APC, has been described. Protein S has a unique C-terminal sex hormone binding globulin (SHBG)-like domain that represents about half of the molecule. To define the role of this domain in APC cofactor act...
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ژورنال
عنوان ژورنال: Endocrinology
سال: 2010
ISSN: 0013-7227,1945-7170
DOI: 10.1210/endo.151.8.9995