FRET-CLSM and double-labeling indirect immunofluorescence to detect close association of proteins in tissue sections

Laboratory Investigation

Volumn 86, Issue 8, 2006, Pages 853-864

  König, Peter ^a   Krasteva, Gabriela ^a   Tag, Claudia ^a   König, Inke R ^b   Arens, Christoph ^c   Kummer, Wolfgang ^a  

^a JUSTUS LIEBIG UNIVERSITY   (Germany)

^b UNIVERSITY OF LÜBECK   (Germany)

^c UNIVERSITY HOSPITAL GIESSEN   (Germany)

Author keywords

Caveolin; Double labeling immunohistochemistry; Fluorescence resonance energy transfer; FRET; Human material; Tissue sections

Indexed keywords

CAVEOLIN 1; CAVEOLIN 1ALPHA; CAVEOLIN 2; IMMUNOGLOBULIN F(AB) FRAGMENT; PROTEIN ANTIBODY; PROTEIN SUBUNIT; UNCLASSIFIED DRUG;

ANIMAL TISSUE; ANTIBODY LABELING; ARTICLE; CAVEOLA; CONFOCAL LASER MICROSCOPY; CONTROLLED STUDY; FEMALE; FLUORESCENCE; FLUORESCENCE RESONANCE ENERGY TRANSFER; GLOMUS TUMOR; HUMAN; HUMAN TISSUE; IMMUNOFLUORESCENCE TEST; INTERMETHOD COMPARISON; LABORATORY TEST; MALE; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; RAT; SIMULATION; TISSUE SECTION; VASCULAR ENDOTHELIUM;

ANIMALS; FEMALE; FLUORESCENCE RESONANCE ENERGY TRANSFER; FLUORESCENT ANTIBODY TECHNIQUE, INDIRECT; MALE; MICROSCOPY, CONFOCAL; PROTEIN BINDING; PROTEINS; RATS; RATS, WISTAR;

EID: 33746218260     PISSN: 00236837     EISSN: 15300307     Source Type: Journal    
DOI: 10.1038/labinvest.3700443     Document Type: Article

References (18)

1. Garini Y, Vermolen BJ, Young IT. From micro to nano: recent advances in high-resolution microscopy. Curr Opin Biotechnol 2005;16:3-12.
2. Jares-Erijman EA, Jovin TM. FRET imaging. Nat Biotechnol 2003;21:1387-1395.
3. Kenworthy AK. Imaging protein-protein interactions using fluorescence resonance energy transfer microscopy. Methods 2001;24:289-296.
4. Sharma N, Hewett J, Ozelius LJ, et al. A close association of torsinA and alpha-synuclein in Lewy bodies: a fluorescence resonance energy transfer study. Am J Pathol 2001;159:339-344.
5. Mills JD, Stone JR, Rubin DG, et al. Illuminating protein interactions in tissue using confocal and two-photon excitation fluorescent resonance energy transfer microscopy. J Biomed Opt 2003;8:347-356.
6. Razani B, Woodman SE, Lisanti MP. Caveolae: from cell biology to animal physiology. Pharmacol Rev 2002; 54:431-467.
7. Capozza F, Cohen AW, Cheung MW, et al. Muscle-specific interaction of caveolin isoforms: differential complex formation between caveolins in fibroblastic vs muscle cells. Am J Physiol Cell Physiol 2005;288: C677-C691.
8. Drab M, Verkade P, Elger M, et al. Loss of caveolae, vascular dysfunction, and pulmonary defects in caveolin-1 gene-disrupted mice. Science 2001;293: 2449-2452.
9. Dvorakova M, Lips KS, Brüggmann D, et al. Developmental changes in the expression of nicotinic acetylcholine receptor alpha-subunits in the rat heart. Cell Tissue Res 2005;319:201-209.
10. Brüggmann D, Lips KS, Pfeil U, et al. Rat arteries contain multiple nicotinic acetylcholine receptor alpha-subunits. Life Sci 2003;72:2095-2099.
11. Lips KS, Pfeil U, Kummer W. Coexpression of alpha 9 and alpha 10 nicotinic acetylcholine receptors in rat dorsal root ganglion neurons. Neuroscience 2002;115: 1-5.
12. Maurer WHL, Lehmacher W. Multiple comparisons in drug clinical trials and preclinical assays: a priori ordered hypothesis. In: Vollmar J (ed). Biometrie in der Chemisch-Pharmazeutischen Industrie. Fischer: Stuttgart, 1995, pp 3-18.
13. Hanley JA, McNeil BJ. The meaning and use of the area under a receiver operating characteristic (ROC) curve. Radiology 1982;143:29-36.
14. Lack EE. Pathology of Adrenal and Extra-Adrenal Paraganglia. W.B. Saunders: Philadelphia, USA, 1994.
15. Das K, Lewis RY, Scherer PE, et al. The membrane-spanning domains of caveolins-1 and -2 mediate the formation of caveolin hetero-oligomers. Implications for the assembly of caveolae membranes in vivo. J Biol Chem 1999;274:18721-18728.
16. Scherer PE, Lewis RY, Volonte D, et al. Cell-type and tissue-specific expression of caveolin-2. Caveolins 1 and 2 co-localize and form a stable hetero-oligomeric complex in vivo. J Biol Chem 1997; 272:29337-29346.
17. Sabanayagam CR, Eid JS, Meller A. Using fluorescence resonance energy transfer to measure distances along individual DNA molecules: corrections due to non-ideal transfer. J Chem Phys 2005;122:061103.
18. Harris LJ, Skaletsky E, McPherson A. Crystallographic structure of an intact IgG1 monoclonal antibody. J Mol Biol 1998;275:861-872.