Microsomal fatty acyl-CoA transacylation and hydrolysis: fatty acyl-CoA species dependent modulation by liver fatty acyl-CoA binding proteins. Academic Article

abstract

• arachidonoyl-CoA. In summary, the data established for the first time a role for both L-FABP and ACBP in microsomal phosphatidic acid biosynthesis. By preferentially stimulating microsomal transacylation of unsaturated long chain fatty acyl-CoAs while concomitantly exerting their differential protection from microsomal acyl-CoA hydrolase, L-FABP and ACBP can uniquely function in modulating the pattern of fatty acids esterified to phosphatidic acid, the de novo precursor of phospholipids and triacylglycerols. This may explain in part the simultaneous presence of these proteins in cell types involved in fatty acid absorption and lipoprotein secretion.

authors

• Schroeder, Friedhelm

published proceedings

• Biochim Biophys Acta

author list (cited authors)

• Jolly, C. A., Wilton, D. C., & Schroeder, F.

citation count

• 60

complete list of authors

• Jolly, CA||Wilton, DC||Schroeder, F

publication date

• January 2000

publisher

• Elsevier  Publisher

published in

• Biochimica et Biophysica Acta: international journal of biochemistry and biophysics  Journal

keywords

• Acyl Coenzyme A
• Animals
• Carrier Proteins
• Diazepam Binding Inhibitor
• Enzyme Activation
• Fatty Acid-binding Protein 7
• Fatty Acid-binding Proteins
• Glycerol-3-phosphate O-acyltransferase
• Male
• Microsomes, Liver
• Myelin P2 Protein
• Neoplasm Proteins
• Nerve Tissue Proteins
• Palmitoyl Coenzyme A
• Phosphatidic Acids
• Rats
• Rats, Sprague-Dawley

PubMed Central ID

• 10601707

Digital Object Identifier (DOI)

• 10.1016/s1388-1981(99)00170-5

start page

• 185

end page

• 197

volume

• 1483

issue

• 1

URL

• http://dx.doi.org/10.1016/s1388-1981(99)00170-5