Vitamin D-binding protein (Gc-globulin) binds actin.
Year: 1980
Type: article
Abstract: Actin, an ubiquitous highly conserved intracellular protein, and the serum vitamin D-binding protein (DBP) form tight 1:1 molar complexes in vitro. This interaction, which is not species-specific, explains the widespread occurrence of the 5-6 S protein responsible for the binding of 25-hydroxycholecalciferol in high speed supernatants of all nucleated tissues. Incubation of F-actin, the filamentous form of this protein, with DBP leads to depolymerization of the former. Actin, complexed with deoxyribonuclease I, retains its ability to bind DBP. Erythrocyte actin, prepared from red cell ghosts, also displays binding properties for DBP. The biological significance of this new interaction of actin is not yet understood.
Source: Journal of Biological Chemistry
Authors: H. Van Baelen, R. Bouillon, P. De Moor
Language: English
Topic: Vitamin D Research Studies
Subfield: Endocrinology, Diabetes and Metabolism
Field: Medicine
Domain: Health Sciences
Open Access status: hybrid
Estimated APC paid: $3,430
OpenAlex ID: W2166659336