메뉴 건너뛰기




Volumn 8, Issue 2, 1996, Pages 257-261

Analysis of cell-adhesion molecule interactions using surface plasmon resonance

Author keywords

[No Author keywords available]

Indexed keywords

CD2 ANTIGEN; CD22 ANTIGEN; CELL ADHESION MOLECULE; LECTIN; T LYMPHOCYTE ANTIGEN;

EID: 0029887430     PISSN: 09527915     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0952-7915(96)80065-3     Document Type: Article
Times cited : (86)

References (42)
  • 1
    • 0025182959 scopus 로고
    • Adhesion receptors of the immune system
    • Springer TA: Adhesion receptors of the immune system. Nature 1990, 346:425-434.
    • (1990) Nature , vol.346 , pp. 425-434
    • Springer, T.A.1
  • 3
    • 0027977974 scopus 로고
    • Transient intercellular adhesion: The importance of weak protein-protein interactions
    • Van der Merwe PA, Barclay AN: Transient intercellular adhesion: the importance of weak protein-protein interactions. Trends Biochem Sci 1994, 19:354-358. This study reviews published affinity and kinetic studies of CAMs, and illustrates that many CAM interactions are very weak.
    • (1994) Trends Biochem Sci , vol.19 , pp. 354-358
    • Van Der Merwe, P.A.1    Barclay, A.N.2
  • 5
    • 0028888183 scopus 로고
    • Detection and quantitation of biomolecular interactions with optical biosensors
    • Yeung D, Gill A, Maule CH, Davies RJ: Detection and quantitation of biomolecular interactions with optical biosensors. Trends Anal Chem 1995, 14:49-56. This review focuses on the IAsys instrument from Fisons (Cambridge, UK).
    • (1995) Trends Anal Chem , vol.14 , pp. 49-56
    • Yeung, D.1    Gill, A.2    Maule, C.H.3    Davies, R.J.4
  • 7
    • 14744291570 scopus 로고
    • Light, angles, action. Instruments for label-free, real-time monitoring of intermolecular interactions
    • Hodgson J: Light, angles, action. Instruments for label-free, real-time monitoring of intermolecular interactions. Biotechnology 1994, 12:31-35.
    • (1994) Biotechnology , vol.12 , pp. 31-35
    • Hodgson, J.1
  • 8
    • 0027486821 scopus 로고
    • Biochemical evidence for a homophilic interaction of the α3β1 integrin
    • Sriramarao P, Steffner P, Gehlsen KR: Biochemical evidence for a homophilic interaction of the α3β1 integrin. J Biol Chem 1993, 268:22036-22041.
    • (1993) J Biol Chem , vol.268 , pp. 22036-22041
    • Sriramarao, P.1    Steffner, P.2    Gehlsen, K.R.3
  • 9
    • 0028149335 scopus 로고
    • Binding of purified collagen receptors (α1β1, α2β1) and RGD-dependent integrins to laminins and laminin framents
    • Pfaff M, Göhring W, Brown JC, Timpl R: Binding of purified collagen receptors (α1β1, α2β1) and RGD-dependent integrins to laminins and laminin framents. Eur J Biochem 1994, 225:975-984.
    • (1994) Eur J Biochem , vol.225 , pp. 975-984
    • Pfaff, M.1    Göhring, W.2    Brown, J.C.3    Timpl, R.4
  • 10
    • 0028287889 scopus 로고
    • Interaction of immobilized recombinant mouse C-type macrophage lectin with glycopeptides and oligosaccharides
    • Yamamoto K, Ishida C, Shinohara Y, Hasegawa Y, Konami Y, Osawa T, Irimura T: Interaction of immobilized recombinant mouse C-type macrophage lectin with glycopeptides and oligosaccharides. Biochemistry 1994, 33:8159-8166.
    • (1994) Biochemistry , vol.33 , pp. 8159-8166
    • Yamamoto, K.1    Ishida, C.2    Shinohara, Y.3    Hasegawa, Y.4    Konami, Y.5    Osawa, T.6    Irimura, T.7
  • 11
    • 0028953265 scopus 로고
    • High affinity binding of Entamoeba histolytica lectin to polyvalent N-acetylgalactosaminides
    • Adler P, Wood SJ, Lee YC, Lee RT, Petri WA, Schnaar RL: High affinity binding of Entamoeba histolytica lectin to polyvalent N-acetylgalactosaminides. J Biol Chem 1995, 270:5164-5171.
    • (1995) J Biol Chem , vol.270 , pp. 5164-5171
    • Adler, P.1    Wood, S.J.2    Lee, Y.C.3    Lee, R.T.4    Petri, W.A.5    Schnaar, R.L.6
  • 12
    • 0029331504 scopus 로고
    • Characterization of the high affinity heparin binding site of the Alzheimer's disease βA4 amyloid precursor protein (APP) and its enhancement by zinc
    • Multhaup G, Mechler H, Masters CL: Characterization of the high affinity heparin binding site of the Alzheimer's disease βA4 amyloid precursor protein (APP) and its enhancement by zinc. J Mol Recog 1995, 8:247-257.
    • (1995) J Mol Recog , vol.8 , pp. 247-257
    • Multhaup, G.1    Mechler, H.2    Masters, C.L.3
  • 13
    • 0028986791 scopus 로고
    • 2+ suppresses cell adhesion to osteopontin by attenuating binding affinity for the integrin αvβ3
    • 2+ suppresses cell adhesion to osteopontin by attenuating binding affinity for the integrin αvβ3. J Biol Chem 1995, 270:9917-9925.
    • (1995) J Biol Chem , vol.270 , pp. 9917-9925
    • Hu, D.D.1    Hoyer, J.R.2    Smith, J.W.3
  • 14
    • 0028817807 scopus 로고
    • The amino-terminal immunoglobulin-like domain of sialoadhesin contains the sialic acid binding site: Comparison with CD22
    • Nath D, Van der Merwe PA, Kelm S, Bradfield P, Crocker PR: The amino-terminal immunoglobulin-like domain of sialoadhesin contains the sialic acid binding site: comparison with CD22. J Biol Chem 1995, 270:26184-26191. This paper illustrates one advantage of being able to analyze proteins without prior purification. One of the mutant proteins was active when analyzed before purification but was inactivated by the purification protocol.
    • (1995) J Biol Chem , vol.270 , pp. 26184-26191
    • Nath, D.1    Van Der Merwe, P.A.2    Kelm, S.3    Bradfield, P.4    Crocker, P.R.5
  • 15
    • 0027500841 scopus 로고
    • Affinity and kinetic analysis of the interaction of the cell-adhesion molecules rat CD2 and CD48
    • Van der Merwe PA, Brown MH, Davis SJ, Barclay AN: Affinity and kinetic analysis of the interaction of the cell-adhesion molecules rat CD2 and CD48. EMBO J 1993, 12:4945-4954.
    • (1993) EMBO J , vol.12 , pp. 4945-4954
    • Van Der Merwe, P.A.1    Brown, M.H.2    Davis, S.J.3    Barclay, A.N.4
  • 16
    • 0027730137 scopus 로고
    • Measuring very low affinity interactions between immunoglobulin superfamily cell-adhesion molecules
    • Van der Merwe PA, Brown MH, Davis SJ, Barclay AN: Measuring very low affinity interactions between immunoglobulin superfamily cell-adhesion molecules. Biochem Soc Trans 1993, 21:340S.
    • (1993) Biochem Soc Trans , vol.21
    • Van Der Merwe, P.A.1    Brown, M.H.2    Davis, S.J.3    Barclay, A.N.4
  • 18
    • 0029140842 scopus 로고
    • Topology of the CD2-CD48 cell-adhesion molecule complex: Implications for antigen recognition by T cells
    • Van der Merwe PA, McNamee PN, Davies EA, Barclay AN, Davis SJ: Topology of the CD2-CD48 cell-adhesion molecule complex: Implications for antigen recognition by T cells. Curr Biol 1995, 5:74-84. Illustrates how the BIAcore can be used to analyze mutant CAMs without prior purification.
    • (1995) Curr Biol , vol.5 , pp. 74-84
    • Van Der Merwe, P.A.1    McNamee, P.N.2    Davies, E.A.3    Barclay, A.N.4    Davis, S.J.5
  • 20
    • 0028907567 scopus 로고
    • Mutational analysis of the epitopes recognized by anti-(rat CD2) and anti-(rat CD48) monoclonal antibodies
    • Davis SJ, Davies EA, Van der Merwe PA: Mutational analysis of the epitopes recognized by anti-(rat CD2) and anti-(rat CD48) monoclonal antibodies. Biochem Soc Trans 1995, 23:188-194.
    • (1995) Biochem Soc Trans , vol.23 , pp. 188-194
    • Davis, S.J.1    Davies, E.A.2    Van Der Merwe, P.A.3
  • 22
    • 0029063466 scopus 로고
    • Kinetic and thermodynamics of virus binding to receptor. Studies with rhinovirus, intercellular adhesion molecule-1 (ICAM-1), and surface plasmon resonance
    • Casasnovas JM, Springer TA: Kinetic and thermodynamics of virus binding to receptor. Studies with rhinovirus, intercellular adhesion molecule-1 (ICAM-1), and surface plasmon resonance. J Biol Chem 1995, 270:13216-13224. It is shown that the interaction between ICAM-1 and rhinovirus has an unusually slow association rate constant The authors suggest that this may be because the ICAM-1 binding site resides in a depression on the viral surface. The authors estimate the binding enthalpy by varying the temperature, revealing that this interaction is endothermic.
    • (1995) J Biol Chem , vol.270 , pp. 13216-13224
    • Casasnovas, J.M.1    Springer, T.A.2
  • 23
    • 0026768221 scopus 로고
    • Detection of receptor-ligand interaction using surface plasmon resonance: Model studies employing the HIV-1 gp120/CD4 interaction
    • Brigham-Burke M, Edwards JR, O'Shannessy DJ: Detection of receptor-ligand interaction using surface plasmon resonance: model studies employing the HIV-1 gp120/CD4 interaction. Anal Biochem 1992, 205:125-131.
    • (1992) Anal Biochem , vol.205 , pp. 125-131
    • Brigham-Burke, M.1    Edwards, J.R.2    O'Shannessy, D.J.3
  • 24
    • 0029112274 scopus 로고
    • The α-glucosidase inhibitor N-butyldeoxynojirimycin inhibits human immunodeficiency virus entry at the level of post-CD4 binding
    • Fischer PB, Collin M, Karlsson GB, James W, Butters TD, Davis SJ, Gordon S, Dwek RA, Platt FM: The α-glucosidase inhibitor N-butyldeoxynojirimycin inhibits human immunodeficiency virus entry at the level of post-CD4 binding. J Virol 1995, 69:5791-5797.
    • (1995) J Virol , vol.69 , pp. 5791-5797
    • Fischer, P.B.1    Collin, M.2    Karlsson, G.B.3    James, W.4    Butters, T.D.5    Davis, S.J.6    Gordon, S.7    Dwek, R.A.8    Platt, F.M.9
  • 25
    • 0029022288 scopus 로고
    • Surface plasmon resonance detection and multi-sensing for direct monitoring of interactions involving low molecular weight analytes and for determination of low affinities
    • Karlsson R, Stȧhlberg R: Surface plasmon resonance detection and multi-sensing for direct monitoring of interactions involving low molecular weight analytes and for determination of low affinities. Anal Biochem 1995, 228:274-280. Demonstrates how the facility in the upgraded SPR instrument from Pharmacia (BIAcore 2000) for injecting samples through up to four flow cells in series is particularly useful for analyzing very low-affinity interactions.
    • (1995) Anal Biochem , vol.228 , pp. 274-280
    • Karlsson, R.1    Stahlberg, R.2
  • 26
    • 0029065020 scopus 로고
    • Effects of solute multivalence on the evaluation of binding constants by biosensor technology: Studies with concanavalin a and interleukin-6 as partitioning proteins
    • Kalinin NL, Ward LW, Winzor DJ: Effects of solute multivalence on the evaluation of binding constants by biosensor technology: studies with concanavalin A and interleukin-6 as partitioning proteins. Anal Biochem 1995, 228:238-244. The authors apply expressions developed for quantitative affinity chromatography of multivalent ligands in an attempt to estimate the monovalent affinity constant of concanavalin A. The approach makes several assumptions but the value obtained in this case agrees with other measurements.
    • (1995) Anal Biochem , vol.228 , pp. 238-244
    • Kalinin, N.L.1    Ward, L.W.2    Winzor, D.J.3
  • 27
    • 0011298312 scopus 로고
    • The kinetics of binding of peptide-MHC complexes to T-cell receptors: Application of surface plasmon resonance to a low-affinity measurement
    • Boniface JJ, Davis MM: The kinetics of binding of peptide-MHC complexes to T-cell receptors: application of surface plasmon resonance to a low-affinity measurement. Methods 1994, 6:168-176.
    • (1994) Methods , vol.6 , pp. 168-176
    • Boniface, J.J.1    Davis, M.M.2
  • 28
    • 0027901739 scopus 로고
    • Analytical ultracentrifugation and the genetic engineering of macromolecules
    • Harding SE: Analytical ultracentrifugation and the genetic engineering of macromolecules. Biotechnol Genet Eng Rev 1993, 11:317-356.
    • (1993) Biotechnol Genet Eng Rev , vol.11 , pp. 317-356
    • Harding, S.E.1
  • 29
    • 0029008438 scopus 로고
    • Stable chelating linkage for reversible immobilization of oligohistidine tagged proteins in the BIAcore surface plasmon resonance detector
    • Gershon PD, Khilko S: Stable chelating linkage for reversible immobilization of oligohistidine tagged proteins in the BIAcore surface plasmon resonance detector. J Immunol Methods 1995, 183:65-76.
    • (1995) J Immunol Methods , vol.183 , pp. 65-76
    • Gershon, P.D.1    Khilko, S.2
  • 32
    • 0028098788 scopus 로고
    • Characterization of glycoprotein oligosaccharides using surface plasmon resonance
    • ••].
    • (1994) Anal Biochem , vol.220 , pp. 303-307
    • Hutchinson, A.M.1
  • 33
    • 0027132013 scopus 로고
    • Comparison of a structural and a functional epitope
    • Cunningham BC, Wells JA: Comparison of a structural and a functional epitope. J Mol Biol 1993, 234:554-563.
    • (1993) J Mol Biol , vol.234 , pp. 554-563
    • Cunningham, B.C.1    Wells, J.A.2
  • 35
    • 0024356301 scopus 로고
    • Rapid measurement of binding constants and heats of binding using a new titration microcalorimeter
    • Wiseman T, Williston S, Brandts J, Lin L: Rapid measurement of binding constants and heats of binding using a new titration microcalorimeter. Anal Biochem 1989, 179:131-137.
    • (1989) Anal Biochem , vol.179 , pp. 131-137
    • Wiseman, T.1    Williston, S.2    Brandts, J.3    Lin, L.4
  • 36
    • 0028926048 scopus 로고
    • Protein-protein interactions: Methods for detection and analysis
    • Phizicky EM, Fields S: Protein-protein interactions: methods for detection and analysis. Microbiol Rev 1995, 59:94-123.
    • (1995) Microbiol Rev , vol.59 , pp. 94-123
    • Phizicky, E.M.1    Fields, S.2
  • 37
    • 0029056922 scopus 로고
    • Energetics of protein-protein interactions: Analysis of the barnase-barstar interface by single mutations and double mutant cycles
    • Schreiber G, Fersht AR: Energetics of protein-protein interactions: analysis of the barnase-barstar interface by single mutations and double mutant cycles. J Mol Biol 1995, 248:478-486.
    • (1995) J Mol Biol , vol.248 , pp. 478-486
    • Schreiber, G.1    Fersht, A.R.2
  • 38
    • 0002713383 scopus 로고
    • Ligand-protein binding affinities
    • Edited by Creighton TE. Oxford: IRL Press
    • Klotz IM: Ligand-protein binding affinities. In Protein Function -A Practical Approach. Edited by Creighton TE. Oxford: IRL Press; 1989:25-54.
    • (1989) Protein Function -A Practical Approach , pp. 25-54
    • Klotz, I.M.1
  • 39
    • 0027364840 scopus 로고
    • Direct evidence for two affinity states for lymphocyte function-associated antigen 1 on activated cells
    • Lollo BA, Chan KWH, Hanson EM, Moy VT, Brian AA: Direct evidence for two affinity states for lymphocyte function-associated antigen 1 on activated cells. J Biol Chem 1993, 268:21693-21700.
    • (1993) J Biol Chem , vol.268 , pp. 21693-21700
    • Lollo, B.A.1    Chan, K.W.H.2    Hanson, E.M.3    Moy, V.T.4    Brian, A.A.5
  • 42
    • 0029918134 scopus 로고    scopus 로고
    • Localization of the putative sialic acid binding site on the immunoglobulin superfamily cell surface molecule CD22
    • in press
    • Van der Merwe PA, Crocker P, Vincent M, Barclay AN, Kelm S: Localization of the putative sialic acid binding site on the immunoglobulin superfamily cell surface molecule CD22. J Biol Chem 1996, in press. The novel feature of this study is the in situ modification of the carbohydrate component of glycoproteins immobilized on the BIAcore sensor surface. Sialoconjugates were readily modified by injecting sialidases and sialotransferases over the sensor surface. In addition, this study provides another example of the usefulness of the BIAcore for the analysis of CAMs mutated by site-directed mutagenesis.
    • (1996) J Biol Chem
    • Van Der Merwe, P.A.1    Crocker, P.2    Vincent, M.3    Barclay, A.N.4    Kelm, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.