Phospholipid transfer proteins in perspective.
Since their discovery and subsequent purification from mammalian tissues more than 30 years ago an impressive number of studies have been carried out to characterize and elucidate the biological functions of phosphatidylcholine transfer protein (PC-TP), phosphatidylinositol transfer protein (PI-TP) and non-specific lipid transfer protein, more commonly known as sterol carrier protein 2 (SCP-2). Here I will present information to show that these soluble, low-molecular weight proteins constitute domain structures in StArR-related lipid transfer (START) proteins (i.e. PC-TP), in retinal degeneration protein, type B (RdgB)-related PI-TPs (e.g. Dm RdgB, Nir2, Nir3) and in peroxisomal beta-oxidation enzyme-related SCP-2 (i.e. 3-oxoacyl-CoA thiolase, also denoted as SCP-X and the 80-kDa D-bifunctional protein). Further I will summarize the most recent studies pertaining to the physiological function of these soluble phospholipid transfer proteins in metazoa.
Wirtz
Karel W A
KW
Bijvoet Center for Biomolecular Research, Section of Lipid Biochemistry, Utrecht University, Padualaan 8, 3584CH Utrecht, The Netherlands. k.w.a.wirtz@chem.uu.nl
D000818:Animals; D002352:Carrier Proteins / Q000378:metabolism; D002462:Cell Membrane / Q000378:metabolism; D005227:Fatty Acids / Q000378:metabolism; D006801:Humans; D010713:Phosphatidylcholines / Q000378:metabolism; D049294:Phospholipid Transfer Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D015398:Signal Transduction
D002352:Carrier Proteins; D005227:Fatty Acids; D010713:Phosphatidylcholines; D049294:Phospholipid Transfer Proteins; C072087:sterol carrier proteins