Open AccessCirculating ghrelin exists in both lipoprotein bound and free forms
Author(s) -
Earle W. Holmes,
I.G. Davies,
Gordoǹ Lowe,
L.R. Ranganath
Publication year - 2009
Publication title -
annals of clinical biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.6
H-Index - 80
eISSN - 1758-1001
pISSN - 0004-5632
DOI - 10.1258/acb.2009.008254
Subject(s) - ghrelin , endocrinology , medicine , lipoprotein , chemistry , very low density lipoprotein , peptide , biochemistry , cholesterol , biology , receptor
Ghrelin is a gastric peptide that has been implicated in the development of obesity and cardiovascular disease. It has been reported that ghrelin binds to lipoproteins, although the different binding patterns of acylated ghrelin (AG) and unacylated ghrelin (UAG) are still to be determined.Methods Lipoprotein fractions were generated using a self-generating iodixanol gradient. AG and UAG were measured using specific enzyme immunoassays.Results AG bound to all lipoproteins in approximately equal concentrations (VLDL 26%, LDL 22%, HDL 23%) and was present as a plasma protein (27%). UAG bound more specifically to HDL (49%) and was present as a plasma protein (48%).Conclusions The different binding patterns of AG and UAG may have significant implications for their biological effects, including roles in energy metabolism, the development of obesity and potentially in the modulation of cardiovascular disease.