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Properties and Function of Phosphatidylcholine Transfer Proteins

  • Chapter
The Enzymes of Biological Membranes

Abstract

When phospholipids extracted from biological membranes are dispersed in water, bilayer structures are spontaneously formed (Bangham et al., 1965). This process of self-association is thermodynamically driven. It involves the extrusion of the hydrophobic acyl chains from the medium and the orientation of the polar head groups at the bilayer-water interface. In general, natural phospholipids have a very low critical micelle concentration. Consequently, the rate at which a monomer molecule dissociates from the bilayer is low, thus resulting in a slow approach to equilibrium (Reynolds, 1982). In agreement with this notion, spontaneous equilibration of phospholipid molecules between model membrane structures by diffusion of soluble monomers is a matter of days (Duckwitz-Peterlein et al, 1977; McLean and Phillips, 1981). Interestingly, equilibration is greatly accelerated when membranes are prepared with phospholipids containing unnatural fatty acids like fluorescently labeled fatty acids (Roseman and Thompson, 1980; Nichols and Pagano, 1981) or myristic acid (Martin and MacDonald, 1976). This acceleration may be a reflection on the stability of these lipid molecules in the bilayer structure apparently resulting in an enhanced establishment of the bilayer-monomer equilibrium. Despite the great tendency for a phospholipid molecule to stay with the bilayer structure, numerous studies with intact cells have indicated that in situ phospholipid movement between subcellular organelles can be very fast (Stein and Stein, 1969; Wirtz and Zilversmit, 1969; Jungalwala and Dawson, 1970). It is believed now that the phospholipid transfer proteins detected in the cytoplasm of mammalian and plant tissues are involved in this intermembranous transfer of phospholipids.

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Wirtz, K.W.A., Teerlink, T., Akeroyd, R. (1985). Properties and Function of Phosphatidylcholine Transfer Proteins. In: Martonosi, A.N. (eds) The Enzymes of Biological Membranes. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-2355-6_3

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