Release of retinol and denaturation of its plasma carrier, retinol-binding protein

Folding and Design

Volumn 3, Issue 4, 1998, Pages 285-291

  Bychkova, Valentina E ^a   Dujsekina, Alexandra E ^a   Fantuzzi, Andrea ^b   Ptitsyn, Oleg B ^a,c   Rossi, Gian Luigi ^b  

^a INSTITUTE OF PROTEIN RESEARCH   (Russian Federation)

^b UNIVERSITY OF PARMA   (Italy)

^c NATIONAL CANCER INSTITUTE   (United States)

Author keywords

Intermediate states; Molten globule; Protein denaturation; Retinol release; Retinol binding protein

Indexed keywords

RETINOL BINDING PROTEIN;

AQUEOUS SOLUTION; ARTICLE; CONFORMATIONAL TRANSITION; DIELECTRIC CONSTANT; DRUG RECEPTOR BINDING; GENE TARGETING; PH; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DENATURATION; TARGET CELL;

EID: 0031870503     PISSN: 13590278     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1359-0278(98)00039-X     Document Type: Article

References (38)

1. Ottonello, S., Petrucco, S. & Maraini, G. (1987). Vitamin A uptake from retinol-binding protein in a cell-free system from pigment epithelial cells of bovine retina. J. Biol. Chem. 262, 3975-3981.
2. Sivaprasadarao, A. & Findlay, J.B.C. (1988). The interaction of retinol-binding protein with its plasma-membrane receptor. Biochem. J, 255, 561-569.
3. Sivaprasadarao, A. & Findlay, J.B.C. (1988). The mechanism of uptake of retinol by plasma-membrane vesicles. Biochem. J. 255, 571-579.
4. Sivaprasadarao, A., Boudjelal, M. & Findlay, J.B.C. (1994). Solubilization and purification of the retinol-binding protein receptor from human placental membrane. Biochem. J. 302, 245-251.
5. Sundaram, M., Sivaprasadarao, A., DeSousa, M.M. & Findlay, J.B.C. (1998). The transfer of retinol from serum retinol-binding protein to cellular retinol-binding protein is mediated by a membrane receptor. J. Biol. Chem. 273, 3336-3342.
6. Fex, G. & Johannesson, G. (1987). Study of the spontaneous transfer of retinol from the retinol:retinol binding protein complex to unilamellar liposomes. Biochim. Biophys. Acta 901, 255-264.
7. Fex, G. & Johannesson, G. (1990). Transfer of retinol from retinol-binding protein complex to liposomes and across liposomal membranes. Methods Enzymol. 189, 394-402.
8. Noy, N. & Blaner, W.S. (1991). Interactions of retinol with binding proteins: studies with cellular retinol-binding protein and with rat retinol-binding protein. Biochemistry 30, 6380-6386.
9. Goodman, DeW.S. & Raz, A. (1972). Extraction and recombinant studies of the interaction of retinol with human plasma retinol-binding protein. J. Lipid Res. 13, 338-347.
10. Bychkova, V.E., Berni, R., Rossi, G.L, Kutyshenko, V.P. & Ptitsyn, O.B. (1992). Retinol-binding protein is in the molten globule state at low pH. Biochemistry 31, 7566-7571.
11. Goodman, DeW.S. & Leslie, R.B. (1972). Fluorescence study of human plasma retinol-binding protein and of the retinol-binding protein-prealbumin complex. Biochim. Biophys. Acta 260, 670-678.
12. Muccio, D.D., Waterhouse, V., Fish, F. & Broillette, C.G. (1992). Analysis of the two state behaviour of the thermal unfolding of serum retinol-binding protein containing a single retinol ligand. Biochemistry 31, 5560-5567.
13. Cowan, S.W., Newcomer, M.E. & Jones, T.A. (1990). Crystallographic refinement of human serum retinol-binding protein at 2 Å resolution. Proteins 8, 44-61.
14. Cogan, U., Kopelman, M., Mokady, S. & Shinitzky, M. (1976). Binding affinities of retinol and related compounds to retinol binding protein. Eur. J. Biochem. 65, 71-78.
15. Bychkova, V.E. & Ptitsyn, O.B. (1993). The molten globule in vitro and in vivo. Chemtracts: Biochem. Mol. Biol. 4, 133-163.
16. Ptitsyn, O.B. (1995). Molten globule and protein folding. Adv. Protein Chem. 47, 83-229.
17. Eisenberg, M., Gresalfi, T., Riccio, T. & McLaughlin, S. (1979). Absorption of monovalent cations to bilayer membranes containing negative phospholipids. Biochemistry 18, 5213-5223.
18. Endo, T. & Schatz, G. (1988). Latent membrane perturbation activity of a mitochondrial precursor protein is exposed by unfolding. EMBO J. 7, 1153-1156.
19. Van der Goot, F.G., Gonzalez-Manas, J.M., Lakey, J.H. & Pattus, F. (1991 ). A 'molten globule' membrane-insertion intermediate of the pore-forming domain of colicin A. Nature 354, 408-410.
20. Ptitsyn, O.B., Bychkova, V.E. & Uversky, V.N. (1995). Kinetic and equilibrium folding intermediates. Phil. Trans. R. Soc. Lon. B 348, 35-41.
21. Lamm, G. & Pack, G.R. (1997). Calculation of dielectric constant near polyelectrolytes in solution. J. Phys. Chem. B 101, 959-965.
22. Wilkinson, K.D. & Mayer, A.N. (1986). Alcohol-induced conformational changes of ubiquitin. Arch. Biochem. Biophys. 250, 390-399.
23. Dufour, E., Bertrand-Harb, C. & Haertle, T. (1993). Reversible effect of medium dielectric constant on structural transformation of β-lactoglobulin and its retinol binding properties. Biopolymers 33, 589-598.
24. Uversky, V.N., Narizhneva, N.V., Kirschstein, S.O., Winter, S. & Loeber, G. (1997). Conformational transitions provoked by organic solvents in β-lactoglobulin: can a molten globule like intermediate be induced by the decrease in dielectric constant? Fold. Des. 2, 163-172.
25. Bychkova, V.E., et al., & Ptitsyn, O.B. (1996). Molten globule-like state of cytochrome c under conditions simulating those near the membrane surface. Biochemistry 35, 6058-6063.
26. Sears, D.W. & Beychok, S. (1973). In Physical Principles and Techniques of Protein Chemistry. (Leach, S.J., ed.), Part C, pp. 495-593, Academic Press, London.
27. Dolgikh, D.A., et al., & Ptitsyn, O.B. (1985). Compact state of a protein molecule with pronounced small-scale mobility: bovine α-lactalbumin. Eur. Biophys. J. 13, 109-121.
28. Bolotina, I.A. & Lugauskas, V.Yu. (1985). Determination of the protein secondary structure from their CD spectra. IV. Evaluation of the aromatic residues contribution in protein CD spectra in the peptide region. Mol. Biol. (Moscow) 19, 1409-1421.
29. Chaffotte, A.F., Guillon, Y. & Goldberg, M.E. (1992). Kinetic resolution of peptide bond and side chain far-UV circular dichroism during the folding of hen egg white lysozyme. Biochemistry 31, 9694-9702.
30. Akerlof, G. (1932). Dielectric constant of some organic solvents-water mixtures at various temperatures. J. Am. Chem. Soc. 54, 4125-4139.
31. Franks, F. & Ives, D.J.G. (1966). Structural properties of alcohol-water mixtures. Q. Rev. Chem. Soc. 20, 1-44.
32. Gast, K., Zirwer, D., Welfle, H., Bychkova, V.E. & Ptitsyn, O.B. (1986). Quasielastic light scattering from human α-lactalbumin: comparison of molecular dimensions in native and "molten globule" states. Int. J. Biol. Macromol. 8, 231-236.
33. Bychkova, V.E., Bartoshevich, S.F. & Klenin, S.I. (1990). Comparative study on diffusion coefficients of α-lactalbumin and lysozyme by polarisation interferometer. Biofizika (Moscow) 35, 242-248.
34. Ptitsyn, O.B. (1992). The molten globule state. In Protein Folding. (Creighton, T.E., ed.), pp. 243-300, W.H. Freeman and Co., New York.
35. Uversky, V.N. (1993). Use of fast protein size-exclusion liquid chromatography to study the unfolding of proteins which denature through the molten globule. Biochemistry 32, 13288-13298.
36. Pinheiro, T.J.T. (1997). Structural and kinetic description of cytochrome c unfolding induced by the interaction with lipid vesicles. Biochemistry 36, 13122-13132.
37. Berni, R., Ottonello, S. & Monaco, H.L (1985). Purification of human plasma retinol binding protein by hydrophobic interaction chromatography. Anal. Biochem. 150, 273-277.
38. Tsvetkov, V.N. & Klenin, S.I. (1953). Diffusion of polystyrene fractions in dichlorethane. Dokl. Acad. Nauk SSSR (Moscow) 88, 49-52.