TY - JOUR
T1 - A lipid droplet-specific capsule is present in rat adrenal-cells
T2 - Evidence from a monoclonal antibody
AU - Wang, Seu Mei
AU - Fong, Tsorng Harn
PY - 1995
Y1 - 1995
N2 - We have used a monoclonal antibody, A2, to study the structure and function on the lipid droplet capsule in steroidogenic adrenal cells. This antibody reacts with a 160-kD protein found in the rat adrenal cortex. Immunofluorescence microscopy shows a dominant rim pattern, which surrounds individual lipid droplets and is distinct from the filamentous vimentin staining. The boundary of lipid droplets in steroidgenic Leydig cells and 3T3 adipocytes is also immunostained by this antibody. The strong association of the 160-kD protein with the lipid droplet is demonstrated by its resistance to Triton X-100 extraction. Stimulation of steroid secretion by adrenocorticotropin results in the detachment of this protein from the lipid droplet and its movement to the cytosol. These findings suggest that the translocation of this 160-kD protein from lipid droplet surface to cytosol on stimulation might be important in facilitating the binding of cholesterol ester hydrolase to the surface of lipid droplets, as proposed for adipocytes, during lipolytic stimulation.
AB - We have used a monoclonal antibody, A2, to study the structure and function on the lipid droplet capsule in steroidogenic adrenal cells. This antibody reacts with a 160-kD protein found in the rat adrenal cortex. Immunofluorescence microscopy shows a dominant rim pattern, which surrounds individual lipid droplets and is distinct from the filamentous vimentin staining. The boundary of lipid droplets in steroidgenic Leydig cells and 3T3 adipocytes is also immunostained by this antibody. The strong association of the 160-kD protein with the lipid droplet is demonstrated by its resistance to Triton X-100 extraction. Stimulation of steroid secretion by adrenocorticotropin results in the detachment of this protein from the lipid droplet and its movement to the cytosol. These findings suggest that the translocation of this 160-kD protein from lipid droplet surface to cytosol on stimulation might be important in facilitating the binding of cholesterol ester hydrolase to the surface of lipid droplets, as proposed for adipocytes, during lipolytic stimulation.
UR - http://www.scopus.com/inward/record.url?scp=0029557653&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0029557653&partnerID=8YFLogxK
U2 - 10.1006/bbrc.1995.2748
DO - 10.1006/bbrc.1995.2748
M3 - Article
C2 - 8526943
AN - SCOPUS:0029557653
SN - 0006-291X
VL - 217
SP - 81
EP - 88
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 1
ER -