TY - JOUR
T1 - Human acylation stimulating protein enhances triacylglycerol biosynthesis in plant microsomes
AU - Weselake, Randall J.
AU - Kazala, E. Chris
AU - Cianflone, Katherine
AU - Boehr, David D.
AU - Middleton, Cameron K.
AU - Rennie, Courtney D.
AU - Laroche, André
AU - Recnik, Ingrid
N1 - Funding Information:
This work was supported by a grant to R.J.W. and A.L. from the Alberta Agricultural Research Institute, a Research Grant to R.J.W. from the Natural Sciences and Engineering Research Council of Canada and a grant to K.C. from the Medical Research Council of Canada.
PY - 2000/9/15
Y1 - 2000/9/15
N2 - Diacylglycerol acyltransferase has a universal role in catalyzing the acyl-CoA-dependent formation of triacylglycerol in microorganisms, animals and plants. Acylation stimulating protein, from human blood, is known to enhance diacylglycerol acyltransferase activity and triacylglycerol biosynthesis in human adipocytes. In the current study, acylation stimulating protein was also shown to enhance diacylglycerol acyltransferase activity in microsomes from cell suspension cultures of oilseed rape. Enzyme stimulation occurred over the pH range of 6-9 but the degree of stimulation decreased with increasing ionic strength at pH 7.4. Varying acyl-CoA concentration did not affect the degree of stimulation. Membranes from triacylglycerol producing cells in plants and humans may have similar binding sites for acylation stimulating protein which have been preserved during molecular evolution. The results suggest that human acylation stimulating protein may be useful in modifying lipid biosynthesis in plants. (C) 2000 Federation of European Biochemical Societies.
AB - Diacylglycerol acyltransferase has a universal role in catalyzing the acyl-CoA-dependent formation of triacylglycerol in microorganisms, animals and plants. Acylation stimulating protein, from human blood, is known to enhance diacylglycerol acyltransferase activity and triacylglycerol biosynthesis in human adipocytes. In the current study, acylation stimulating protein was also shown to enhance diacylglycerol acyltransferase activity in microsomes from cell suspension cultures of oilseed rape. Enzyme stimulation occurred over the pH range of 6-9 but the degree of stimulation decreased with increasing ionic strength at pH 7.4. Varying acyl-CoA concentration did not affect the degree of stimulation. Membranes from triacylglycerol producing cells in plants and humans may have similar binding sites for acylation stimulating protein which have been preserved during molecular evolution. The results suggest that human acylation stimulating protein may be useful in modifying lipid biosynthesis in plants. (C) 2000 Federation of European Biochemical Societies.
UR - http://www.scopus.com/inward/record.url?scp=0034666081&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0034666081&partnerID=8YFLogxK
U2 - 10.1016/S0014-5793(00)01996-7
DO - 10.1016/S0014-5793(00)01996-7
M3 - Article
C2 - 10996321
AN - SCOPUS:0034666081
SN - 0014-5793
VL - 481
SP - 189
EP - 192
JO - FEBS Letters
JF - FEBS Letters
IS - 2
ER -