Hydrodynamic properties of porcine bestrophin-1 in Triton X-100

Biochimica et Biophysica Acta - Biomembranes

Volumn 1758, Issue 2, 2006, Pages 241-247

  Stanton, J Brett ^a   Goldberg, Andrew F X ^c   Hoppe, George ^d   Marmorstein, Lihua Y ^a,b   Marmorstein, Alan D ^a,b  

^a UNIVERSITY OF ARIZONA COLLEGE OF MEDICINE   (United States)

^b UNIVERSITY OF ARIZONA   (United States)

^c OAKLAND UNIVERSITY   (United States)

^d LERNER RESEARCH INSTITUTE   (United States)

Author keywords

Calcium; Centrifugation; Chloride; Gel exclusion chromatography; Ion channel; Oligomer

Indexed keywords

HOMODIMER; TETRAMER; TRITON X 100;

ANIMAL CELL; ANIMAL TISSUE; ARTICLE; CALCULATION; COMPLEX FORMATION; ELUTION; GEL CHROMATOGRAPHY; HYDRODYNAMICS; MOLECULAR WEIGHT; NONHUMAN; PRIORITY JOURNAL; PROTEIN STRUCTURE; SEDIMENTATION; SPECIES; STOICHIOMETRY; SWINE;

ANIMALS; CELL LINE; CHEMISTRY, PHYSICAL; CHLORIDE CHANNELS; CORNEAL DYSTROPHIES, HEREDITARY; DETERGENTS; EYE PROTEINS; HUMANS; MALE; MOLECULAR WEIGHT; OCTOXYNOL; PIGMENT EPITHELIUM OF EYE; PROTEIN STRUCTURE, QUATERNARY; RECOMBINANT PROTEINS; SUS SCROFA; TISSUE DISTRIBUTION; TRANSFECTION;

ANIMALIA; SUIDAE; SUS SCROFA;

EID: 33646267187     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2006.01.024     Document Type: Article

References (43)

1. Stohr H., Marquardt A., Nanda I., Schmid M., and Weber B.H. Three novel human VMD2-like genes are members of the evolutionary highly conserved RFP-TM family. Eur. J. Hum. Genet. 10 (2002) 281-284
2. Marmorstein A.D., Marmorstein L.Y., Rayborn M., Wang X., Hollyfield J.G., and Petrukhin K. Bestrophin, the product of the Best vitelliform macular dystrophy gene (VMD2), localizes to the basolateral plasma membrane of the retinal pigment epithelium. Proc. Natl. Acad. Sci. U. S. A. 97 (2000) 12758-12763
3. Petrukhin K., Koisti M.J., Bakall B., Li W., Xie G., Marknell T., Sandgren O., Forsman K., Holmgren G., Andreasson S., Vujic M., Bergen A.A., McGarty-Dugan V., Figueroa D., Austin C.P., Metzker M.L., Caskey C.T., and Wadelius C. Identification of the gene responsible for Best macular dystrophy. Nat. Genet. 19 (1998) 241-247
4. Marquardt A., Stohr H., Passmore L.A., Kramer F., Rivera A., and Weber B.H. Mutations in a novel gene, VMD2, encoding a protein of unknown properties cause juvenile-onset vitelliform macular dystrophy (Best's disease). Hum. Mol. Genet. 7 (1998) 1517-1525
5. Yardley J., Leroy B.P., Hart-Holden N., Lafaut B.A., Loeys B., Messiaen L.M., Perveen R., Reddy M.A., Bhattacharya S.S., Traboulsi E., Baralle D., De Laey J.J., Puech B., Kestelyn P., Moore A.T., Manson F.D., and Black G.C. Mutations of VMD2 splicing regulators cause nanophthalmos and autosomal dominant vitreoretinochoroidopathy (ADVIRC). Invest. Ophthalmol. Vis. Sci. 45 (2004) 3683-3689
6. Allikmets R., Seddon J.M., Bernstein P.S., Hutchinson A., Atkinson A., Sharma S., Gerrard B., Li W., Metzker M.L., Wadelius C., Caskey C.T., Dean M., and Petrukhin K. Evaluation of the Best disease gene in patients with age-related macular degeneration and other maculopathies. Hum. Genet. 104 (1999) 449-453
7. Bakall B., Marknell T., Ingvast S., Koisti M.J., Sandgren O., Li W., Bergen A.A., Andreasson S., Rosenberg T., Petrukhin K., and Wadelius C. The mutation spectrum of the bestrophin protein-functional implications. Hum. Genet. 104 (1999) 383-389
8. Kramer F., Mohr N., Kellner U., Rudolph G., and Weber B.H. Ten novel mutations in VMD2 associated with Best macular dystrophy (BMD). Hum. Mutat. 22 (2003) 418
9. Seddon J.M., Afshari M.A., Sharma S., Bernstein P.S., Chong S., Hutchinson A., Petrukhin K., and Allikmets R. Assessment of mutations in the Best macular dystrophy (VMD2) gene in patients with adult-onset foveomacular vitelliform dystrophy, age-related maculopathy, and bull's-eye maculopathy. Ophthalmology 108 (2001) 2060-2067
10. White K., Marquardt A., and Weber B.H. VMD2 mutations in vitelliform macular dystrophy (Best disease) and other maculopathies. Hum. Mutat. 15 (2000) 301-308
11. Godel V., Chaine G., Regenbogen L., and Coscas G. Best's vitelliform macular dystrophy. Acta Ophthalmol., Suppl. 175 (1986) 1-31
12. Marmor M.F., and Small K. In: Marmor M.F., and Wolfensberger T. (Eds). The Retinal Pigment Epithelium (1998), Oxford Press, New York 330-333
13. Gass D.J.M. In: Gass D.J.M. (Ed). Stereoscopic Atlas of Macular Diseases, Diagnosis and Treatment (1997), Mosby, St. Louis 303-313
14. Cross H.E., and Bard L. Electro-oculography in Best's muscular dystrophy. Am. J. Ophthalmol. 77 (1974) 46-50
15. Kramer F., White K., Pauleikhoff D., Gehrig A., Passmore L., Rivera A., Rudolph G., Kellner U., Andrassi M., Lorenz B., Rohrschneider K., Blankenagel A., Jurklies B., Schilling H., Schutt F., Holz F.G., and Weber B.H. Mutations in the VMD2 gene are associated with juvenile-onset vitelliform macular dystrophy (Best disease) and adult vitelliform macular dystrophy but not age-related macular degeneration. Eur. J. Hum. Genet. 8 (2000) 286-292
16. Han D.P., and Lewandowski M.F. Electro-oculography in autosomal dominant vitreoretinochoroidopathy. Arch. Ophthalmol. 110 (1992) 1563-1567
17. Steinberg R.H., Linsenmeier R.A., and Griff E.R. In: Osborne N.N., and Chader G.J. (Eds). Progress in Retinal Research (1985), Pergamon Press, Oxford 33-66
18. Gallemore R.P., and Steinberg R.H. Effects of DIDS on the chick retinal pigment epithelium: II. Mechanism of the light peak and other responses originating at the basal membrane. J. Neurosci. 9 (1989) 1977-1984
19. Gallemore R.P., and Steinberg R.H. Light-evoked modulation of basolateral membrane Cl-conductance in chick retinal pigment epithelium: the light peak and fast oscillation. J. Neurophysiol. 70 (1993) 1669-1680
20. Sun H., Tsunenari T., Yau K.W., and Nathans J. The vitelliform macular dystrophy protein defines a new family of chloride channels. Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 4008-4013
21. Hartzell C., Putzier I., and Arreola J. Calcium-activated chloride channels. Annu. Rev. Physiol. 67 (2005) 719-758
22. R. Rosenthal, B. Bakall, T. Kinnick, N. Peachey, S. Wimmers, C. Wadelius, A. Marmorstein, O. Strauss, Expression of bestrophin-1, the product of the VMD2 gene, modulates voltage-dependent Ca2+ channels in retinal pigment epithelial cells. FASEB J. in press.
23. Qu Z., and Hartzell C. Determinants of anion permeation in the second transmembrane domain of the mouse bestrophin-2 chloride channel. J. Gen. Physiol. 124 (2004) 371-382
24. Qu Z., Fischmeister R., and Hartzell C. Mouse bestrophin-2 is a bona fide Cl(-) channel: identification of a residue important in anion binding and conduction. J. Gen. Physiol. 123 (2004) 327-340
25. Tsunenari T., Sun H., Williams J., Cahill H., Smallwood P., Yau K.W., and Nathans J. Structure-function analysis of the bestrophin family of anion channels. J. Biol. Chem. 278 (2003) 41114-41125
26. Qu Z., Wei R.W., Mann W., and Hartzell H.C. Two bestrophins cloned from Xenopus laevis oocytes express Ca(2+)-activated Cl(-) currents. J. Biol. Chem. 278 (2003) 49563-49572
27. Marmorstein L.Y., McLaughlin P.J., Stanton J.B., Yan L., Crabb J.W., and Marmorstein A.D. Bestrophin interacts physically and functionally with protein phosphatase 2A. J. Biol. Chem. 277 (2002) 30591-30597
28. West K.A., Yan L., Shadrach K., Sun J., Hasan A., Miyagi M., Crabb J.S., Hollyfield J.G., Marmorstein A.D., and Crabb J.W. Protein database, human retinal pigment epithelium. Mol, Cell Proteomics 2 (2003) 37-49
29. Laurent T.C., and Killander J. J. Chromatogr. 14 (1964) 317-330
30. Clarke S., and Smigel M.D. Size and shape of membrane protein-detergent complexes: hydrodynamic studies. Methods Enzymol. 172 (1989) 696-709
31. Martin R.G., and Ames B.N. A method for determining the sedimentation behavior of enzymes: application to protein mixtures. J. Biol. Chem. 236 (1961)
32. Goldberg A.F.X., and Molday R.S. Subunit composition of the peripherin/rds-rom-1 disk rim complex from rod photoreceptors: hydrodynamic evidence for a tetrameric quaternary structure. Biochemistry 35 (1996) 6144-6149
33. Sumner J.B., and Gralén N. The molecular weight of crystalline catalase. J. Biol. Chem. 125 (1938) 33-36
34. Aiyer R.A. Structural characterization of insulin receptors. I. Hydrodynamic properties of receptors from turkey erythrocytes. J. Biol. Chem. 258 (1983) 14992-14999
35. Clarke S. The size and detergent binding of membrane proteins. J. Biol. Chem. 250 (1975) 5459-5469
36. Marmorstein L.Y., McLaughlin P.J., Stanton J.B., Yan L., Crabb J.W., and Marmorstein A.D. Bestrophin interacts physically and functionally with protein phosphatase 2A. J. Biol. Chem. 277 (2002) 30591-30597
37. Rosenthal R., Bakall B., Kinnick T., Peachey N., Wimmers S., Wadelius C., Marmorstein A., and Strauss O. Expression of bestrophin-1, the product of the VMD2 gene, modulates voltage-dependent Ca2+ channels in retinal pigment epithelial cells. FASEB J. 20 (2006) 178-180
38. Marmorstein A.D., Stanton J.B., Yocom J., Bakall B., Schiavone M.T., Wadelius C., Marmorstein L.Y., and Peachey N.S. A model of best vitelliform macular dystrophy in rats. Invest. Ophthalmol. Vis. Sci. 45 (2004) 3733-3739
39. Strauss O., and Rosenthal R. Function of bestrophin. Ophthalmologe 102 (2005) 122-126
40. Stohr H., Marquardt A., Nanda I., Schmid M., and Weber B.H. Three novel human VMD2-like genes are members of the evolutionary highly conserved RFP-TM family. Eur. J. Hum. Genet. 10 (2002) 281-284
41. Sun H., Tsunenari T., Yau K.W., and Nathans J. The vitelliform macular dystrophy protein defines a new family of chloride channels. Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 4008-4013
42. Chabre M., and le Maire M. Monomeric G-protein-coupled receptor as a functional unit. Biochemistry 44 (2005) 9395-9403
43. Suda K., Filipek S., Palczewski K., Engel A., and Fotiadis D. The supramolecular structure of the GPCR rhodopsin in solution and native disc membranes. Mol. Membr. Biol. 21 (2004) 435-446