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Phospholipid transfer proteins in perspective
Author(s) -
Wirtz Karel W.A.
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.06.065
Subject(s) - phospholipid transfer protein , plant lipid transfer proteins , biochemistry , phospholipid , thiolase , phosphatidylinositol , chemistry , biology , peroxisome , microbiology and biotechnology , receptor , signal transduction , membrane , gene
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 β‐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.