Preparation of cell membranes for high resolution imaging by AFM

Ultramicroscopy

Volumn 110, Issue 4, 2010, Pages 305-312

  Wang, Hongda ^a   Hao, Xian ^a,b   Shan, Yuping ^a,b   Jiang, Junguang ^a   Cai, Mingjun ^a   Shang, Xin ^a  

^a CHANGCHUN INSTITUTE OF APPLIED CHEMISTRY   (China)

^b UNIVERSITY OF CHINESE ACADEMY OF SCIENCES   (China)

Author keywords

Cell membranes; In situ AFM; Single molecule

Indexed keywords

AFM; FREE LIPIDS; HIGH RESOLUTION IMAGE; HIGH-RESOLUTION IMAGING; IN-SITU; INNER MEMBRANES; MEMBRANE MODELS; MICA SURFACES; OUTER MEMBRANE; PNGASE F; RED BLOOD CELL; SAMPLE PREPARATION; SINGLE MOLECULE; TRANS-MEMBRANE PROTEINS; TRYPSIN DIGESTION;

ATOMIC FORCE MICROSCOPY; BLOOD; CELL MEMBRANES; FLEXIBLE STRUCTURES; HEMOGLOBIN OXYGEN SATURATION; MEMBRANE STRUCTURES; MICA; OLIGOSACCHARIDES; PROTEINS; SILICATE MINERALS;

CYTOLOGY;

OLIGOSACCHARIDE; TRYPSIN;

ARTICLE; ATOMIC FORCE MICROSCOPY; CELL ELONGATION; CELL MEMBRANE; CELL SHAPE; CELL STRUCTURE; CELL SURFACE; CONTROLLED STUDY; ERYTHROCYTE MEMBRANE; HUMAN; HUMAN CELL; IMAGE ANALYSIS; LIPID BILAYER; PARTICLE SIZE; PROTEIN LOCALIZATION; SAMPLING; SURFACE PROPERTY;

CELL MEMBRANE; CYTOLOGICAL TECHNIQUES; ERYTHROCYTE MEMBRANE; HUMANS; IMAGE PROCESSING, COMPUTER-ASSISTED; MICROSCOPY, ATOMIC FORCE;

EID: 77649180583     PISSN: 03043991     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ultramic.2009.12.014     Document Type: Article

References (51)

1. Singer S.J., and Nicolson G.L. The fluid mosaic model of the structure of cell membranes. Science 175 (1972) 720-730
2. Simons K., and Ikonen E. Functional rafts in cell membranes. Nature 387 (1997) 569-572
3. Nichols B. Cell biology: without a raft. Nature 436 (2005) 638-639
4. Douglass A., and Vale R. Single-molecule microscopy reveals plasma membrane microdomains created by protein-protein networks that exclude or trap signaling molecules in T cells. Cell 121 (2005) 937-950
5. Schuz G.J., Kada G., Pastushenko V.P., and Schindler H. Properties of lipid microdomains in a muscle cell membrane visualized by single molecule microscopy. EMBO J. 19 (2000) 892-901
6. Edidin M. Lipids on the frontier: a century of cell-membrane bilayers. Nat. Rev. Mol. Cell Biol. 4 (2003) 414-418
7. Engelman D.M. Membranes are more mosaic than fluid. Nature 438 (2005) 578-580
8. Richter G.W., and Scarpelli D.G. Cell Membranes: Biological and Pathological Aspects (1971), Waverly Press Inc. pp. 145-174
9. Han W., Lindsay S., Dlakic M., Harrington R., and Kinked D. Nature 386 (1997) 563
10. Jena B.P. Cell secretion machinery: studies using the AFM. Ultramicroscopy 106 (2006) 663-669
11. Schillers H. Imaging CFTR in its native environment. Pflugers Arch. 456 (2008) 163-177
12. Rinker S., Ke Y., Liu Y., Chhabra R., Yan H., and Self-assembled D. nanostructures for distance-dependent multivalent ligand-protein binding. Nat. Nanotechnol. 3 (2008) 418-422
13. Cui X.D., Primak A., Zarate X., Tomfohr J., Sankey O.F., Moore A.L., Moore T.A., Gust D., Harris G., and Lindsay S.M. Reproducible measurement of single-molecule conductivity. Science 294 (2001) 571-574
14. Xu B.Q., and Tao N.J. Measurement of single molecule conductance by repeated formation of molecular junctions. Science 301 (2003) 1221-1223
15. Brujic J., Hermans R.I., Walther K.A., and Fernandez J.M. Single-molecule force spectroscopy reveals signatures of glassy dynamics in the energy landscape of ubiquitin. Nat. Phys. 2 (2006) 282-286
16. Hinterdorfer P., and Dufrene Y.F. Detection and localization of single molecular recognition events using atomic force microscopy. Nat. Methods 3 (2006) 347-355
17. Peng Q., and Li H.B. Atomic force microscopy reveals parallel mechanical unfolding pathways of T4 lysozyme: evidence for a kinetic partitioning mechanism. Proc. Natl. Acad. Sci. USA 105 (2008) 1885-1890
18. Ke Y.G., Lindsay S., Chang Y., Liu Y., and Yan H. Self-assembled water-soluble nucleic acid probe tiles for label-free RNA hybridization assays. Science 319 (2008) 180-183
19. Kienberger F., Mueller H., Pastushenko V., and Hinterdorfer P. Following single antibody binding to purple membranes in real time. EMBO Rep. 5 (2004) 579-583
20. Tang J.L., Ebner A., Badelt-Lichtblau H., Vollenkle C., Rankl C., Kraxberger B., Leitner M., Wildling L., Gruber H.J., Sleytr U.B., Ilk N., and Hinterdorfer P. Recognition imaging and highly ordered molecular templating of bacterial S-layer nanoarrays containing affinity-tags. Nano Lett. 8 (2008) 4312-4319
21. Raess B.U., and Tunnicliff G. The Red Cell Membrane: A Model for Solute Transport (1989), The Humana Press Inc. p. 3-17
22. Lyubchenko Y., Shlyakhtenko L., Harrington R., Oden P., and Lindsay S. Atomic force microscopy of long DNA-imaging in air and under water. Proc. Natl. Acad. Sci. USA 90 (1993) 2137-2140
23. Lange T., Jungmann P., Haberle J., Falk S., Duebbers A., Bruns R., Ebner A., Hinterdorfer P., Oberleithner H., and Schillers H. Reduced number of CFTR molecules in erythrocyte plasma membrane of cystic fibrosis patients. Mol. Membr. Biol. 23 (2006) 317-323
24. Lohr D., Bash R., Wang H., Yodh J., and Lindsay S. Using atomic force microscopy to study chromatin structure and nucleosome remodeling. Methods 41 (2007) 333-341
25. Johnson S.J., Bayerl T.M., McDermott D.C., Adam G.W., Rennie A.R., Thomas R.K., and Sackmann E. Structure of an adsorbed dimyristoylphosphatidylcholine bilayer measured with specular reflection of neutrons. Biophys. J. 59 (1991) 289-294
26. + ATPases in quasi-native cell membranes. Nano Lett. 9 (2009) 4489-4493
27. Plummer T.H., Elder J.H., Alexander S., Phelan A.W., and Tarentino A.L. Demonstration of peptide: N-glycosidase F activity in endo-beta-N-acetylglucosaminidase F preparations. J. Biol. Chem. 259 (1984) 10700-10704
28. Triplett R.B., and Carraway K.L. Proteolytic digestion of erythrocytes, resealed ghosts, and isolated membranes. Biochemistry 11 (1972) 2897-2903
29. Stroh C., Wang H., Bash R., Ashcroft B., Nelson J., Gruber H., Lohr D., Lindsay S.M., and Hinterdorfer P. Single-molecule recognition imaging-microscopy. Proc. Natl. Acad. Sci. USA 101 (2004) 12503-12507
30. Wang H., Bash R., Yodh J.G., Hager G., Lindsay S.M., and Lohr D. Using atomic force microscopy to study nucleosome remodeling on individual nucleosomal arrays in situ. Biophys. J. 87 (2004) 1964-1971
31. Wang H., Bash R., Lindsay S.M., and Lohr D. Solution AFM studies of human Swi-Snf and its interactions with MMTV DNA and chromatin. Biophys. J. 89 (2005) 3386-3398
32. Radmacher M., Fritz M., Hansma H.G., and Hansma P.K. Direct observation of enzyme-activity with the atomic-force microscope. Science 265 (1994) 1577-1579
33. Sadava D.E. Cell Biology: Organelle Structure and Function (1993), Jones and Bartlett Publishers, Inc. p. 7
34. Jain M.K. Introduction to Biological Membranes (1988), John Wiley & Sons, Inc. p. 46
35. Elgsaeter A., Stokke B.T., Mikkelsen A., and Branton D. The molecular basis of erythrocyte shape. Science 234 (1986) 1217-1223
36. Weinstein R.S. The Red Blood Cell (1974), Academic Press Inc., New York
37. Voet D., Voet J., and Pratt C.W. Fundamentals of Biochemistry Upgrade (2002), John Wiley & Sons, Inc. p. 247
38. Bloom F. A Textbook of Histology. 12th ed. (1994), Chapman and Hall, New York
39. Drickamer L.K. Fragmentation of the 95,000-dalton transmembrane polypeptide in human erythrocyte membranes. J. Biol. Chem. 251 (1976) 5115-5123
40. 2+-ATPase of the sarcoplasmic reticulum. Annu. Rev. Biochem. 73 (2004) 269-292
41. Azurmendi H.F., Martin-Pastor M., and Bush C.A. Conformational studies of Lewis X and Lewis A trisaccharides using NMR residual dipolar couplings. Bio Polymers 63 (2002) 89-98
42. Reynolds M., Fuchs A., Lindhorst T.K., and Perez S. The hydration features of carbohydrate determinants of Lewis antigens. Mol. Simul. 34 (2008) 447-460
43. Hricovini M. Structural aspects of carbohydrates and the relation with their biological properties. Curr. Med. Chem. 11 (2004) 2565-2583
44. Bush C.A., Yan Z.Y., and Rao B.N.N. Conformational energy calculations and proton nuclear overhauser enhancements reveal a unique conformation for blood group-a oligosaccharides. J. Am. Chem. Soc. 108 (1986) 6168-6173
45. 3. Eur. J. Biochem. 259 (1999) 295-303
46. Perez S., MouhousRiou N., Nifantev N.E., Tsvetkov Y.E., Bachet B., and Imberty A. Crystal and molecular structure of a histo-blood group antigen involved in cell adhesion: the Lewis x trisaccharide. Glycobiology 6 (1996) 537-542
47. Bechinger B. Biophysical investigations of membrane perturbations by polypeptides using solid-state NMR spectroscopy (review). Mol. Membr. Biol. 17 (2000) 135-142
48. Vogt T.C.B., and Bechinger B. The interactions of histidine-containing amphipathic helical peptide antibiotics with lipid bilayers-the effects of charges and pH. J. Biol. Chem. 274 (1999) 29115-29121
49. Bechinger B., Zasloff M., and Opella S.J. Structure and orientation of the antibiotic peptide magainin in membranes by solid-state nuclear magnetic resonance spectroscopy. Protein Sci. 2 (1993) 2077-2084
50. Mani R., Cady S., Tang M., Waring A., Lehrer R., and Hong M. Membrane-dependent oligomeric structure and pore formation of a beta-hairpin antimicrobial peptide in lipid bilayers from solid-state NMR. Proc. Natl. Acad. Sci. USA 103 (2006) 16242-16247
51. Durell S.R., Raghunathan G., and Guy H.R. Modeling the ion channel structure of cecropin. Biophys. J. 63 (1992) 1623-1631