Cellular Lipid Binding Proteins by Jan F. C. Glatz, Joost J. F. P. Luiken, Marc van Bilsen
By Jan F. C. Glatz, Joost J. F. P. Luiken, Marc van Bilsen (auth.), Jan F. C. Glatz (eds.)
It is easily proven that mobile lipid binding proteins serve critical roles in mobile lipid uptake and metabolism. proof has been offered that quite a few metabolic illnesses, comparable to hyperlipidemia, atherosclerosis, insulin resistance, and diabetes, are characterised by means of malfunctioning or deficiencies in mobile lipid binding proteins. For greater realizing of the motion of lipids as signaling compounds and the position of lipids in middleman metabolism, it's necessary to have certain wisdom of the interactions among lipids and their cognant binding proteins. In view of this becoming curiosity in lipid-protein interplay, the 4th foreign convention on Lipid Binding Proteins was once held in Maastricht, The Netherlands, in June 2001. The complaints of the former 3 conferences were released in Molecular and mobile Biochemistry. the current targeted factor of Molecular and mobile Biochemistry includes chosen papers in keeping with the lectures and posters provided throughout the 4th convention, and offers perception into the importance of those proteins for the functioning of the cell.
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Extra resources for Cellular Lipid Binding Proteins
Baier LJ. Ie. Knowler We. Eads J. Paoli sso G. Tataranni PA, Moch izu ki H. Benn ett PH. Boga rdus C. Prochazka M: An amino acid substitut ion in the human intestinal fatty acid bindin g protein is assoc iated with increased fatty acid bind ing. increa sed fat ox idation. and insulin resistance. I Clin Invest 95 : 1281-1 287. 1995 14. Herr I'M. Matare se V. Bernlohr DA. I: Surfac e lysine residues modul ate the collisional transfer of fatty acid from ad ipocyte tatty ac id bindin g protein to memb ranes.
Thu s, tran sfer of fluo rescent FA fro m hum an LFABP to membranes is entirel y consistent with an aq ueou s di ffusion me ch ani sm , whereas fro m hum an IFABP, AFA BP, and HFA BP to SUV occurs during direct protein-membrane interactions. e. AFABP > HFABP > IFABP > LFABP. Taken toget her, the results provide a stro ng demonstration that the rode nt FA BPs are faithful reporters of th e FA tran sport properties of the human FAB Ps. T he high degree of similarity in lipid tran sfer mechani sm s is no doubt a result of th e large degree of ami no acid sequenc e identity between th ese FABP orth ologues.
Mo st of th e fatty acids di ffused only a short distance into the wat er before they rebound the to donor membrane , and nearly half rebound immediately with no visible diffusional path. The average distance that the fatty acid diffuses into the water before rebinding to the donor membrane is referred to as the mean diffusional excursion, and is shown by the broken vertical line in Fig. 3A. Abbreviated dill' the mean diffu sional excursion is a critical determinant of the rate of transfer ofamphipathic molecules between membranes.