메뉴 건너뛰기




Volumn 112, Issue 14, 1999, Pages 2335-2345

Integrin α and β subunit contribution to the kinetic properties of α2β1 collagen receptors on human keratinocytes analyzed under hydrodynamic conditions

Author keywords

Adhesion; Flow chamber; Integrin; Keratinocyte; Kinetic parameter; Monoclonal antibody; Structure function relationship

Indexed keywords

COLLAGEN TYPE 1; INTEGRIN; KALININ; MONOCLONAL ANTIBODY; SELECTIN;

EID: 0032772471     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (19)

References (43)
  • 1
    • 0028910904 scopus 로고
    • Lifetime of the P-selectin-carbohydrate bond and its response to tensile force in hydrodynamic flow
    • Alon, R., Hammer, D. A. and Springer, T. A. (1995). Lifetime of the P-selectin-carbohydrate bond and its response to tensile force in hydrodynamic flow. Nature 374, 539-542.
    • (1995) Nature , vol.374 , pp. 539-542
    • Alon, R.1    Hammer, D.A.2    Springer, T.A.3
  • 2
    • 0027158161 scopus 로고
    • Epidermal growth factor and insulin-like growth factor I enhance keratinocyte migration
    • Ando, Y. and Jensen, P. J. (1993). Epidermal growth factor and insulin-like growth factor I enhance keratinocyte migration. J. Invest. Dermatol. 100, 633-639.
    • (1993) J. Invest. Dermatol. , vol.100 , pp. 633-639
    • Ando, Y.1    Jensen, P.J.2
  • 3
    • 0018101150 scopus 로고
    • Models for the specific adhesion of cells to cells
    • Bell, G. I. (1978). Models for the specific adhesion of cells to cells. Science 200, 618-627.
    • (1978) Science , vol.200 , pp. 618-627
    • Bell, G.I.1
  • 4
    • 0029062047 scopus 로고
    • Energetics of leucocyte integrin activation
    • Cai, T.-Q. and Wright, S. D. (1995). Energetics of leucocyte integrin activation. J. Biol. Chem. 270, 14358-14365.
    • (1995) J. Biol. Chem. , vol.270 , pp. 14358-14365
    • Cai, T.-Q.1    Wright, S.D.2
  • 5
    • 0030612224 scopus 로고    scopus 로고
    • The integrin α1 A-domain is a ligand binding site for collagens and laminin
    • Calderwood, D. A., Tuckwell, D. S., Eble, J., Kühn, K. and Humphries, M. J. (1997). The integrin α1 A-domain is a ligand binding site for collagens and laminin. J. Biol. Chem. 272, 12311-12317.
    • (1997) J. Biol. Chem. , vol.272 , pp. 12311-12317
    • Calderwood, D.A.1    Tuckwell, D.S.2    Eble, J.3    Kühn, K.4    Humphries, M.J.5
  • 6
    • 0030916713 scopus 로고    scopus 로고
    • Crystal structure of ICAM-2 reveals a distinctive integrin recognition surface
    • Casasnovas, J. M., Springer, T. M., Liu, J.-H., Harrisson, S. C. and Wang, J.-H. (1997). Crystal structure of ICAM-2 reveals a distinctive integrin recognition surface. Nature 387, 312-315.
    • (1997) Nature , vol.387 , pp. 312-315
    • Casasnovas, J.M.1    Springer, T.M.2    Liu, J.-H.3    Harrisson, S.C.4    Wang, J.-H.5
  • 7
    • 0029786892 scopus 로고    scopus 로고
    • Ligand binding to integrin αIIbβ3 is dependent on a MIDAS-like domain in the β3 subunit
    • Collins Tozer, E., Liddington, R. C., Sutcliffe, M. J., Smeeton, A. H. and Loftus, J. C. (1996). Ligand binding to integrin αIIbβ3 is dependent on a MIDAS-like domain in the β3 subunit. J. Biol. Chem. 271, 21978-21984.
    • (1996) J. Biol. Chem. , vol.271 , pp. 21978-21984
    • Collins Tozer, E.1    Liddington, R.C.2    Sutcliffe, M.J.3    Smeeton, A.H.4    Loftus, J.C.5
  • 9
    • 0027530684 scopus 로고
    • The I domain is a major recognition site on the leucocyte integrin Mac-1 (CD11b/CD18) for four distinct adhesion ligands
    • Diamond, M. S., Garcia-Aguilar, J., Bickford, J. K., Corbi, A. L. and Springer, T. A. (1993). The I domain is a major recognition site on the leucocyte integrin Mac-1 (CD11b/CD18) for four distinct adhesion ligands. J. Cell Biol. 120, 1031-1043.
    • (1993) J. Cell Biol. , vol.120 , pp. 1031-1043
    • Diamond, M.S.1    Garcia-Aguilar, J.2    Bickford, J.K.3    Corbi, A.L.4    Springer, T.A.5
  • 10
    • 0027395041 scopus 로고
    • Affinity modulation of integrin alpha 5 beta 1: Regulation of the functional response by soluble fibronectin
    • Faull, R. J., Kovach, N. L., Harlan, J. M. and Ginsberg, M. H. (1993). Affinity modulation of integrin alpha 5 beta 1: regulation of the functional response by soluble fibronectin. J. Cell Biol. 121, 155-162.
    • (1993) J. Cell Biol. , vol.121 , pp. 155-162
    • Faull, R.J.1    Kovach, N.L.2    Harlan, J.M.3    Ginsberg, M.H.4
  • 11
    • 0031022629 scopus 로고    scopus 로고
    • Functional relevance during lymphocyte migration and cellular localization of activated β1 integrins
    • Gomez, M., Luque, A., del, Pozo, M. A., Hogg, N., Sànchez-Madrid, F. and Cabanas, C. (1997). Functional relevance during lymphocyte migration and cellular localization of activated β1 integrins. Eur. J. Immunol. 27, 8-16.
    • (1997) Eur. J. Immunol. , vol.27 , pp. 8-16
    • Gomez, M.1    Luque, A.2    Del Pozo, M.A.3    Hogg, N.4    Sànchez-Madrid, F.5    Cabanas, C.6
  • 12
    • 0029796131 scopus 로고    scopus 로고
    • Identifying the putative metal ion-dependent adhesion site in the β2 (CD18) subunit required for αLβ2 and αMβ2 ligand interactions
    • Goodman, T. G. and Bjat, M. L. (1996). Identifying the putative metal ion-dependent adhesion site in the β2 (CD18) subunit required for αLβ2 and αMβ2 ligand interactions. J. Biol. Chem. 271, 23729-23736.
    • (1996) J. Biol. Chem. , vol.271 , pp. 23729-23736
    • Goodman, T.G.1    Bjat, M.L.2
  • 13
    • 0023405068 scopus 로고
    • A dynamical model for receptor-mediated cell adhesion to surfaces
    • Hammer, D. A. and Lauffenburger, D. A. (1987). A dynamical model for receptor-mediated cell adhesion to surfaces. Biophys. J. 52, 35-57.
    • (1987) Biophys. J. , vol.52 , pp. 35-57
    • Hammer, D.A.1    Lauffenburger, D.A.2
  • 14
    • 0029664968 scopus 로고    scopus 로고
    • 2+ binding site on the beta3 integrins that regulates the dissociation rate for RGD
    • 2+ binding site on the beta3 integrins that regulates the dissociation rate for RGD J. Biol. Chem. 276, 21745-21751.
    • (1996) J. Biol. Chem. , vol.276 , pp. 21745-21751
    • Hu, D.D.1    Barbas C.F. III2    Smith, J.W.3
  • 15
    • 0023666065 scopus 로고
    • Integrins: A family of cell surface receptors
    • Hynes, R. O. (1987). Integrins: a family of cell surface receptors. Cell 48, 549-554.
    • (1987) Cell , vol.48 , pp. 549-554
    • Hynes, R.O.1
  • 16
    • 0026770377 scopus 로고
    • Integrins: Versatility, modulation, and signaling in cell adhesion
    • Hynes, R. O. (1992). Integrins: versatility, modulation, and signaling in cell adhesion. Cell 69, 11-25.
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.O.1
  • 17
    • 0030788570 scopus 로고    scopus 로고
    • Multiple loop structures critical for ligand binding of the integrin alpha-4 subunit in the upper face of the beta-propeller model
    • Irie, A., Kamata, T. and Takada, Y. (1997). multiple loop structures critical for ligand binding of the integrin alpha-4 subunit in the upper face of the beta-propeller model. Proc. Nat. Acad Sci. USA 94, 7198-7203.
    • (1997) Proc. Nat. Acad Sci. USA , vol.94 , pp. 7198-7203
    • Irie, A.1    Kamata, T.2    Takada, Y.3
  • 18
    • 0028984448 scopus 로고
    • Vascular cell adhesion molecule (VCAM)-Ig fusion protein defines distinct affinity states of the very late antigen-4 (VLA-4) receptor
    • Jakubowski, A., Rosa, M. D., Bixler, S., Lobb, R. and Burkly, R. C. (1995). Vascular cell adhesion molecule (VCAM)-Ig fusion protein defines distinct affinity states of the very late antigen-4 (VLA-4) receptor. Cell Adhes. Commun. 3, 131-142.
    • (1995) Cell Adhes. Commun. , vol.3 , pp. 131-142
    • Jakubowski, A.1    Rosa, M.D.2    Bixler, S.3    Lobb, R.4    Burkly, R.C.5
  • 19
    • 0028225987 scopus 로고
    • Identification of putative ligand binding site within I domain of integrin alpha 2 beta 1
    • Kamata, T., Puzon, W. and Takada, Y. (1994). Identification of putative ligand binding site within I domain of integrin alpha 2 beta 1. J. Biol. Chem. 269, 9659-9663.
    • (1994) J. Biol. Chem. , vol.269 , pp. 9659-9663
    • Kamata, T.1    Puzon, W.2    Takada, Y.3
  • 21
    • 0027268377 scopus 로고
    • Interaction of type IV collagen with isolated alpha 1 beta 1 and alpha 2 beta 1
    • Kern, A., Eble, J., Golbik, R. and Kühn, K. (1993). Interaction of type IV collagen with isolated alpha 1 beta 1 and alpha 2 beta 1. Eur. J. Biochem. 215, 151-159.
    • (1993) Eur. J. Biochem. , vol.215 , pp. 151-159
    • Kern, A.1    Eble, J.2    Golbik, R.3    Kühn, K.4
  • 22
    • 0027933588 scopus 로고
    • The role of the I-domain in ligand binding of the human integrin alpha 1 beta 1
    • Kern, A., Briesewitz, R., Bank, I. and Marcantonio, E. E. (1994). The role of the I-domain in ligand binding of the human integrin alpha 1 beta 1. J. Biol. Chem. 269, 22811-22816.
    • (1994) J. Biol. Chem. , vol.269 , pp. 22811-22816
    • Kern, A.1    Briesewitz, R.2    Bank, I.3    Marcantonio, E.E.4
  • 23
    • 0025854524 scopus 로고
    • Leukocytes roll on a selectin at physiologic flow rates: Distinction from and prerequisite for adhesion through inlegrins
    • Lawrence, M. B. and Springer, T. A. (1991). Leukocytes roll on a selectin at physiologic flow rates: distinction from and prerequisite for adhesion through inlegrins. Cell 65, 859-873.
    • (1991) Cell , vol.65 , pp. 859-873
    • Lawrence, M.B.1    Springer, T.A.2
  • 24
    • 0028986196 scopus 로고
    • Crystal structure of the A domain from the alpha subunit of integrin CR3 (CD11b/CD18)
    • Lee, J. O., Rieu, P., Arnaout, M. A. and Liddington, R. (1995). Crystal structure of the A domain from the alpha subunit of integrin CR3 (CD11b/CD18). Cell 80, 631-638.
    • (1995) Cell , vol.80 , pp. 631-638
    • Lee, J.O.1    Rieu, P.2    Arnaout, M.A.3    Liddington, R.4
  • 25
    • 0031569914 scopus 로고    scopus 로고
    • New insights into integrin-ligand interaction
    • Loftus, J. C. and Liddington, R. C. (1997). New insights into integrin-ligand interaction. J. Clin. Invest. 99, 2302-2306.
    • (1997) J. Clin. Invest. , vol.99 , pp. 2302-2306
    • Loftus, J.C.1    Liddington, R.C.2
  • 26
    • 0027364840 scopus 로고
    • Direct evidence of two affinity states for lymphocyte function-associated antigen I on activated T cells
    • Lollo, B. A., Chan, K. W., Hanson, E. M., Moy, V. T. and Brian, A. A. (1993). Direct evidence of two affinity states for lymphocyte function-associated antigen I on activated T cells. J. Biol. Chem. 268, 21693-21700.
    • (1993) J. Biol. Chem. , vol.268 , pp. 21693-21700
    • Lollo, B.A.1    Chan, K.W.2    Hanson, E.M.3    Moy, V.T.4    Brian, A.A.5
  • 27
    • 0031964440 scopus 로고    scopus 로고
    • Dual regulation of ligand binding by CD11b I domain. Inhibition of intercellular adhesion and monocyte procoagulant activity by factor X-derived peptide
    • Mesri, M., Plescia, J. and Altieri, D. C. (1998). Dual regulation of ligand binding by CD11b I domain. Inhibition of intercellular adhesion and monocyte procoagulant activity by factor X-derived peptide. J. Biol. Chem. 273, 744-748.
    • (1998) J. Biol. Chem. , vol.273 , pp. 744-748
    • Mesri, M.1    Plescia, J.2    Altieri, D.C.3
  • 28
    • 0029969086 scopus 로고    scopus 로고
    • Getting integrins into shape/recent insights into how integrin activity is regulated by conformational changes
    • Mould, P. A. (1996). Getting integrins into shape/recent insights into how integrin activity is regulated by conformational changes. J. Cell Sci. 109, 2613-2618.
    • (1996) J. Cell Sci. , vol.109 , pp. 2613-2618
    • Mould, P.A.1
  • 29
    • 0030798854 scopus 로고    scopus 로고
    • Defining the topology of integrin α5β1-fibronectin interactions using inhibitory anti-α5 and anti-β1 antibodies
    • Mould, P. A., Askari, J. A., Aota, S.-i., Yamada, K. M., Irie, A., Takada, Y., Mardon, H. J. and Humphries, M. J. (1997). Defining the topology of integrin α5β1-fibronectin interactions using inhibitory anti-α5 and anti-β1 antibodies. J. Biol. Chem. 272, 17283-17292.
    • (1997) J. Biol. Chem. , vol.272 , pp. 17283-17292
    • Mould, P.A.1    Askari, J.A.2    Aota, S.-I.3    Yamada, K.M.4    Irie, A.5    Takada, Y.6    Mardon, H.J.7    Humphries, M.J.8
  • 31
    • 0028260522 scopus 로고
    • Dynamic adhesion of CD8-positive cells to antibody coated surfaces: The initial step is independent of microfilaments and intracellular domains of cell-binding molecules
    • Pierres, A., Tissot, O., Malissen, B. and Bongrand, P. (1994). Dynamic adhesion of CD8-positive cells to antibody coated surfaces: the initial step is independent of microfilaments and intracellular domains of cell-binding molecules. J. Cell Biol. 125, 945-953.
    • (1994) J. Cell Biol. , vol.125 , pp. 945-953
    • Pierres, A.1    Tissot, O.2    Malissen, B.3    Bongrand, P.4
  • 32
    • 0028842502 scopus 로고
    • Measuring the lifetime of bonds made between surface-linked molecules
    • Pierres, A., Benoliel, A. M. and Bongrand, P. (1995). Measuring the lifetime of bonds made between surface-linked molecules. J. Biol. Chem. 270, 26586-26592.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26586-26592
    • Pierres, A.1    Benoliel, A.M.2    Bongrand, P.3
  • 33
    • 0030448942 scopus 로고    scopus 로고
    • Determination of the lifetime and force dependence of interactions of single bonds formation between surface-attached CD2 and CD 48 adhesion molecules
    • Pierres, A., Benoliel, A. M., Bongrand, P. and van der Merwe, P. A. (1996). Determination of the lifetime and force dependence of interactions of single bonds formation between surface-attached CD2 and CD 48 adhesion molecules. Proc. Nat. Acad Sci. USA 93, 15114-15118.
    • (1996) Proc. Nat. Acad Sci. USA , vol.93 , pp. 15114-15118
    • Pierres, A.1    Benoliel, A.M.2    Bongrand, P.3    Van Der Merwe, P.A.4
  • 34
    • 0031055273 scopus 로고    scopus 로고
    • The dependence of the association-rate of surface-attached adhesion molecules CD2 and CD 48 molecules on separation distance
    • Pierres, A., Benoliel, A. M., Bongrand, P. and van der Merwe, P. A. (1997). The dependence of the association-rate of surface-attached adhesion molecules CD2 and CD 48 molecules on separation distance. FEBS Lett. 403, 239-244.
    • (1997) FEBS Lett. , vol.403 , pp. 239-244
    • Pierres, A.1    Benoliel, A.M.2    Bongrand, P.3    Van Der Merwe, P.A.4
  • 35
    • 0031686131 scopus 로고    scopus 로고
    • Studying receptor-mediated cell adhesion at the single molecule level
    • Pierres, A., Benoliel, A. M. and Bongrand, P. (1998a). Studying receptor-mediated cell adhesion at the single molecule level. Cell Adhes. Commun. 5, 375-385.
    • (1998) Cell Adhes. Commun. , vol.5 , pp. 375-385
    • Pierres, A.1    Benoliel, A.M.2    Bongrand, P.3
  • 37
    • 0029786408 scopus 로고    scopus 로고
    • Critical residues for ligand binding in an I domain-like structure of the integrin β1 subunit
    • Puzon-McLaughlin, W. and Takada, Y. (1996). Critical residues for ligand binding in an I domain-like structure of the integrin β1 subunit. J. Biol. Chem. 271, 20438-20443.
    • (1996) J. Biol. Chem. , vol.271 , pp. 20438-20443
    • Puzon-McLaughlin, W.1    Takada, Y.2
  • 38
    • 0028294842 scopus 로고
    • Kalinin is more efficient than laminin in promoting adhesion of primary keratinocytes and some other cell lines and has a different requirement for integrin receptors
    • Rousselle, P. and Aumailley, M. (1994). Kalinin is more efficient than laminin in promoting adhesion of primary keratinocytes and some other cell lines and has a different requirement for integrin receptors. J. Cell Biol. 125, 205-214.
    • (1994) J. Cell Biol. , vol.125 , pp. 205-214
    • Rousselle, P.1    Aumailley, M.2
  • 39
    • 0031013031 scopus 로고    scopus 로고
    • Folding of the N-terminal, ligand-binding region of integrin alpha-subunit into a propeller domain
    • Springer, T. A. (1997). folding of the N-terminal, ligand-binding region of integrin alpha-subunit into a propeller domain. Proc. Nat. Acad. Sci. USA 94, 65-72.
    • (1997) Proc. Nat. Acad. Sci. USA , vol.94 , pp. 65-72
    • Springer, T.A.1
  • 40
    • 0028281362 scopus 로고
    • Integrin LFA-1 alpha subunit contains an ICAM-1 binding site in domains V an VI
    • Stanley, P., Bates, P. A., Harvey, J., Bennett, R. I. and Hogg, N. (1994). Integrin LFA-1 alpha subunit contains an ICAM-1 binding site in domains V an VI. EMBO J. 13, 1790-1798.
    • (1994) EMBO J. , vol.13 , pp. 1790-1798
    • Stanley, P.1    Bates, P.A.2    Harvey, J.3    Bennett, R.I.4    Hogg, N.5
  • 41
    • 0027248518 scopus 로고
    • Identification of a regulatory region of integrin β1 subunit using activating and inhibiting antibodies
    • Takada, Y. and Puzon, W. (1993). Identification of a regulatory region of integrin β1 subunit using activating and inhibiting antibodies. J. Biol. Chem. 268, 17597-17601.
    • (1993) J. Biol. Chem. , vol.268 , pp. 17597-17601
    • Takada, Y.1    Puzon, W.2
  • 42
    • 0030856555 scopus 로고    scopus 로고
    • Changing ligand binding specificities of αvβ3 and αvβ1 integrins by swapping a short diverse sequence of the β subunit
    • Takagi, J., Kamata, T., Meredith, J., Puzon-McLaughlin, W. and Takada, Y. (1997). Changing ligand binding specificities of αvβ3 and αvβ1 integrins by swapping a short diverse sequence of the β subunit. J. Biol. Chem. 272, 19794-19800.,
    • (1997) J. Biol. Chem. , vol.272 , pp. 19794-19800
    • Takagi, J.1    Kamata, T.2    Meredith, J.3    Puzon-McLaughlin, W.4    Takada, Y.5
  • 43
    • 0025831838 scopus 로고
    • Cellular interactions: Out of equilibrium
    • Williams, A. F. (1991). Cellular interactions: out of equilibrium. Nature 352, 473-474.
    • (1991) Nature , vol.352 , pp. 473-474
    • Williams, A.F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.