FEBS Letters
Volume 580, Issue 23 , Pages 5436-5441, 9 October 2006

Phospholipid transfer proteins in perspective

Edited by B. Helms

Bijvoet Center for Biomolecular Research, Section of Lipid Biochemistry, Utrecht University, Padualaan 8, 3584CH Utrecht, The Netherlands

Received 1 June 2006; received in revised form 19 June 2006; accepted 20 June 2006. published online 30 June 2006.

Abstract 

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.

Keywords: Phospholipid transfer proteins, PC-TP, PI-TP, SCP-2, Cholesterol, Metazoa

Abbreviations: PC, phosphatidylcholine, PI, phosphatidylinositol, SPM, sphingomyelin, PIP2, phosphatidylinositol 4,5-bisphosphate

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PII: S0014-5793(06)00782-4

doi:10.1016/j.febslet.2006.06.065

FEBS Letters
Volume 580, Issue 23 , Pages 5436-5441, 9 October 2006