메뉴 건너뛰기




Volumn 24, Issue 4, 2006, Pages 251-261

Integrins in the ovary

Author keywords

Cancer; Fertilization; Integrin signaling; Oocyte; Ovarian follicles

Indexed keywords

ACTIN; ADAM PROTEIN; INTEGRIN; UNCLASSIFIED DRUG;

EID: 33748645915     PISSN: 15268004     EISSN: None     Source Type: Journal    
DOI: 10.1055/s-2006-948554     Document Type: Review
Times cited : (27)

References (117)
  • 1
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: Bidirectional, allosteric signaling machines
    • Hynes RO. Integrins: bidirectional, allosteric signaling machines. Cell 2002;110:673-687
    • (2002) Cell , vol.110 , pp. 673-687
    • Hynes, R.O.1
  • 3
  • 4
    • 0034912430 scopus 로고    scopus 로고
    • All in the family: Primary megakaryocytes for studies of platelet alphaIIbbeta3 signaling
    • Shattil SJ, Leavitt AD. All in the family: primary megakaryocytes for studies of platelet alphaIIbbeta3 signaling. Thromb Haemost 2001;86:259-265
    • (2001) Thromb Haemost , vol.86 , pp. 259-265
    • Shattil, S.J.1    Leavitt, A.D.2
  • 5
    • 0029671374 scopus 로고    scopus 로고
    • Beta 1D integrin displaces the beta 1A isoform in striated muscles: Localization at junctional structures and signaling potential in nonmuscle cells
    • Belkin AM, Zhidkova NI, Balzac F, et al. Beta 1D integrin displaces the beta 1A isoform in striated muscles: localization at junctional structures and signaling potential in nonmuscle cells. J Cell Biol 1996;132:211-226
    • (1996) J Cell Biol , vol.132 , pp. 211-226
    • Belkin, A.M.1    Zhidkova, N.I.2    Balzac, F.3
  • 6
    • 0025183918 scopus 로고
    • Changes in keratinocyte adhesion during terminal differentiation: Reduction in fibronectin binding precedes alpha 5 beta 1 integrin loss from the cell surface
    • Adams JC, Watt FM. Changes in keratinocyte adhesion during terminal differentiation: reduction in fibronectin binding precedes alpha 5 beta 1 integrin loss from the cell surface. Cell 1990;63:425-435
    • (1990) Cell , vol.63 , pp. 425-435
    • Adams, J.C.1    Watt, F.M.2
  • 7
    • 0028362876 scopus 로고
    • Requirement of vascular integrin alpha v beta 3 for angiogenesis
    • Brooks PC, Clark RA, Cheresh DA. Requirement of vascular integrin alpha v beta 3 for angiogenesis. Science 1994;264:569-571
    • (1994) Science , vol.264 , pp. 569-571
    • Brooks, P.C.1    Clark, R.A.2    Cheresh, D.A.3
  • 9
    • 0142026204 scopus 로고    scopus 로고
    • Therapeutic antagonists and conformational regulation of integrin function
    • Shimaoka M, Springer TA. Therapeutic antagonists and conformational regulation of integrin function. Nat Rev Drug Discov 2003;2:703-716
    • (2003) Nat Rev Drug Discov , vol.2 , pp. 703-716
    • Shimaoka, M.1    Springer, T.A.2
  • 10
    • 1442331993 scopus 로고    scopus 로고
    • Integrin activation
    • Calderwood DA. Integrin activation. J Cell Sci 2004;117:657-666
    • (2004) J Cell Sci , vol.117 , pp. 657-666
    • Calderwood, D.A.1
  • 12
    • 0033824065 scopus 로고    scopus 로고
    • Avidity regulation of integrins: The driving force in leukocyte adhesion
    • van Kooyk Y, Figdor CG. Avidity regulation of integrins: the driving force in leukocyte adhesion. Curr Opin Cell Biol 2000;12:542-547
    • (2000) Curr Opin Cell Biol , vol.12 , pp. 542-547
    • Van Kooyk, Y.1    Figdor, C.G.2
  • 14
    • 0023185957 scopus 로고
    • The platelet fibrinogen receptor: An immunogold-surface replica study of agonist-induced ligand binding and receptor clustering
    • Isenberg WM, McEver RP, Phillips DR, Shuman MA, Bainton DF. The platelet fibrinogen receptor: an immunogold-surface replica study of agonist-induced ligand binding and receptor clustering. J Cell Biol 1987;104:1655-1663
    • (1987) J Cell Biol , vol.104 , pp. 1655-1663
    • Isenberg, W.M.1    McEver, R.P.2    Phillips, D.R.3    Shuman, M.A.4    Bainton, D.F.5
  • 15
    • 0030611604 scopus 로고    scopus 로고
    • Integrin alphaIIb beta3 reconstituted into lipid bilayers is nonclustered in its activated state but clusters after fibrinogen binding
    • Erb EM, Tangemann K, Bohrmann B, Muller B, Engel J. Integrin alphaIIb beta3 reconstituted into lipid bilayers is nonclustered in its activated state but clusters after fibrinogen binding. Biochemistry 1997;36:7395-7402
    • (1997) Biochemistry , vol.36 , pp. 7395-7402
    • Erb, E.M.1    Tangemann, K.2    Bohrmann, B.3    Muller, B.4    Engel, J.5
  • 16
    • 0038644597 scopus 로고    scopus 로고
    • Activation of integrin alphaIIbbeta3 by modulation of transmembrane helix associations
    • Li R, Mitra N, Gratkowski H, et al. Activation of integrin alphaIIbbeta3 by modulation of transmembrane helix associations. Science 2003;300:795-798
    • (2003) Science , vol.300 , pp. 795-798
    • Li, R.1    Mitra, N.2    Gratkowski, H.3
  • 17
    • 0035850669 scopus 로고    scopus 로고
    • Crystal structure of the extracellular segment of integrin alpha Vbeta3
    • Xiong JP, Stehle T, Diefenbach B, et al. Crystal structure of the extracellular segment of integrin alpha Vbeta3. Science 2001;294:339-345
    • (2001) Science , vol.294 , pp. 339-345
    • Xiong, J.P.1    Stehle, T.2    Diefenbach, B.3
  • 18
    • 0037023363 scopus 로고    scopus 로고
    • Crystal structure of the extracellular segment of integrin alpha Vbeta3 in complex with an Arg-Gly-Asp ligand
    • Xiong JP, Stehle T, Zhang R, et al. Crystal structure of the extracellular segment of integrin alpha Vbeta3 in complex with an Arg-Gly-Asp ligand. Science 2002;296:151-155
    • (2002) Science , vol.296 , pp. 151-155
    • Xiong, J.P.1    Stehle, T.2    Zhang, R.3
  • 19
    • 8544259562 scopus 로고    scopus 로고
    • Structural basis for allostery in integrins and binding to fibrinogen-mimetic therapeutics
    • Xiao T, Takagi J, Coller BS, Wang JH, Springer TA. Structural basis for allostery in integrins and binding to fibrinogen-mimetic therapeutics. Nature 2004;432:59-67
    • (2004) Nature , vol.432 , pp. 59-67
    • Xiao, T.1    Takagi, J.2    Coller, B.S.3    Wang, J.H.4    Springer, T.A.5
  • 21
    • 0037428080 scopus 로고    scopus 로고
    • Structures of the alpha L I domain and its complex with ICAM-1 reveal a shape-shifting pathway for integrin regulation
    • Shimaoka M, Xiao T, Liu JH, et al. Structures of the alpha L I domain and its complex with ICAM-1 reveal a shape-shifting pathway for integrin regulation. Cell 2003;112:99-111
    • (2003) Cell , vol.112 , pp. 99-111
    • Shimaoka, M.1    Xiao, T.2    Liu, J.H.3
  • 22
  • 23
    • 0042739086 scopus 로고    scopus 로고
    • New insights into the structural basis of integrin activation
    • Xiong JP, Stehle T, Goodman SL, Arnaout MA. New insights into the structural basis of integrin activation. Blood 2003;102:1155-1159
    • (2003) Blood , vol.102 , pp. 1155-1159
    • Xiong, J.P.1    Stehle, T.2    Goodman, S.L.3    Arnaout, M.A.4
  • 25
    • 0036220127 scopus 로고    scopus 로고
    • Cysteine-rich module structure reveals a fulcrum for integrin rearrangement upon activation
    • Beglova N, Blacklow SC, Takagi J, Springer TA. Cysteine-rich module structure reveals a fulcrum for integrin rearrangement upon activation. Nat Struct Biol 2002;9:282-287
    • (2002) Nat Struct Biol , vol.9 , pp. 282-287
    • Beglova, N.1    Blacklow, S.C.2    Takagi, J.3    Springer, T.A.4
  • 26
    • 0037031906 scopus 로고    scopus 로고
    • Global conformational rearrangements in integrin extracellular domains in outside-in and inside-out signaling
    • Takagi J, Petre BM, Walz T, Springer TA. Global conformational rearrangements in integrin extracellular domains in outside-in and inside-out signaling. Cell 2002;110:599-611
    • (2002) Cell , vol.110 , pp. 599-611
    • Takagi, J.1    Petre, B.M.2    Walz, T.3    Springer, T.A.4
  • 27
    • 0141625303 scopus 로고    scopus 로고
    • Structure of integrin alpha5beta1 in complex with fibronectin
    • Takagi J, Strokovich K, Springer TA, Walz T. Structure of integrin alpha5beta1 in complex with fibronectin. EMBO J 2003;22:4607-4615
    • (2003) EMBO J , vol.22 , pp. 4607-4615
    • Takagi, J.1    Strokovich, K.2    Springer, T.A.3    Walz, T.4
  • 28
    • 0037418254 scopus 로고    scopus 로고
    • Stabilizing the open conformation of the integrin headpiece with a glycan wedge increases affinity for ligand
    • Luo BH, Springer TA, Takagi J. Stabilizing the open conformation of the integrin headpiece with a glycan wedge increases affinity for ligand. Proc Natl Acad Sci USA 2003;100:2403-2408
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 2403-2408
    • Luo, B.H.1    Springer, T.A.2    Takagi, J.3
  • 29
    • 3042602113 scopus 로고    scopus 로고
    • Allosteric beta1 integrin antibodies that stabilize the low affinity state by preventing the swing-out of the hybrid domain
    • Luo BH, Strokovich K, Walz T, Springer TA, Takagi J. Allosteric beta1 integrin antibodies that stabilize the low affinity state by preventing the swing-out of the hybrid domain. J Biol Chem 2004;279:27466-27471
    • (2004) J Biol Chem , vol.279 , pp. 27466-27471
    • Luo, B.H.1    Strokovich, K.2    Walz, T.3    Springer, T.A.4    Takagi, J.5
  • 30
    • 0037131270 scopus 로고    scopus 로고
    • Agonist-specific structural rearrangements of integrin alpha IIbbeta 3. Confirmation of the bent conformation in platelets at rest and after activation
    • Calzada MJ, Alvarez MV, Gonzalez-Rodriguez J. Agonist-specific structural rearrangements of integrin alpha IIbbeta 3. Confirmation of the bent conformation in platelets at rest and after activation. J Biol Chem 2002;277:39899-39908
    • (2002) J Biol Chem , vol.277 , pp. 39899-39908
    • Calzada, M.J.1    Alvarez, M.V.2    Gonzalez-Rodriguez, J.3
  • 31
    • 16844381981 scopus 로고    scopus 로고
    • Three-dimensional EM structure of the ectodomain of integrin {alpha}V{beta}3 in a complex with fibronectin
    • Adair BD, Xiong JP, Maddock C, Goodman SL, Arnaout MA, Yeager M. Three-dimensional EM structure of the ectodomain of integrin {alpha}V{beta}3 in a complex with fibronectin. J Cell Biol 2005;168:1109-1118
    • (2005) J Cell Biol , vol.168 , pp. 1109-1118
    • Adair, B.D.1    Xiong, J.P.2    Maddock, C.3    Goodman, S.L.4    Arnaout, M.A.5    Yeager, M.6
  • 32
    • 0037195164 scopus 로고    scopus 로고
    • Three-dimensional model of the human platelet integrin alpha IIbbeta 3 based on electron cryomicroscopy and x-ray crystallography
    • Adair BD, Yeager M. Three-dimensional model of the human platelet integrin alpha IIbbeta 3 based on electron cryomicroscopy and x-ray crystallography. Proc Natl Acad Sci USA 2002;99:14059-14064
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 14059-14064
    • Adair, B.D.1    Yeager, M.2
  • 33
    • 0033962672 scopus 로고    scopus 로고
    • Focal adhesions-the cytoskeletal connection
    • Critchley DR. Focal adhesions-the cytoskeletal connection. Curr Opin Cell Biol 2000;12:133-139
    • (2000) Curr Opin Cell Biol , vol.12 , pp. 133-139
    • Critchley, D.R.1
  • 34
    • 0034725593 scopus 로고    scopus 로고
    • Integrins and actin filaments: Reciprocal regulation of cell adhesion and signaling
    • Calderwood DA, Shattil SJ, Ginsberg MH. Integrins and actin filaments: reciprocal regulation of cell adhesion and signaling. J Biol Chem 2000;275:22607-22610
    • (2000) J Biol Chem , vol.275 , pp. 22607-22610
    • Calderwood, D.A.1    Shattil, S.J.2    Ginsberg, M.H.3
  • 35
    • 0033731119 scopus 로고    scopus 로고
    • Integrin cytoplasmic domain-binding proteins
    • Liu S, Calderwood DA, Ginsberg MH. Integrin cytoplasmic domain-binding proteins. J Cell Sci 2000;113(pt 20):3563-3571
    • (2000) J Cell Sci , vol.113 , Issue.PART 20 , pp. 3563-3571
    • Liu, S.1    Calderwood, D.A.2    Ginsberg, M.H.3
  • 36
    • 0037904987 scopus 로고    scopus 로고
    • The integrin-actin connection, an eternal love affair
    • Brakebusch C, Fassler R. The integrin-actin connection, an eternal love affair. EMBO J 2003;22:2324-2333
    • (2003) EMBO J , vol.22 , pp. 2324-2333
    • Brakebusch, C.1    Fassler, R.2
  • 37
    • 0035516140 scopus 로고    scopus 로고
    • Transmembrane crosstalk between the extracellular matrix-cytoskeleton crosstalk
    • Geiger B, Bershadsky A, Pankov R, Yamada KM. Transmembrane crosstalk between the extracellular matrix-cytoskeleton crosstalk. Nat Rev Mol Cell Biol 2001;2:793-805
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 793-805
    • Geiger, B.1    Bershadsky, A.2    Pankov, R.3    Yamada, K.M.4
  • 38
    • 0141865705 scopus 로고    scopus 로고
    • Talin binding to integrin beta tails: A final common step in integrin activation
    • Tadokoro S, Shattil SJ, Eto K, et al. Talin binding to integrin beta tails: a final common step in integrin activation. Science 2003;302:103-106
    • (2003) Science , vol.302 , pp. 103-106
    • Tadokoro, S.1    Shattil, S.J.2    Eto, K.3
  • 40
    • 0036796781 scopus 로고    scopus 로고
    • Get a ligand, get a life: Integrins, signaling and cell survival
    • Stupack DG, Cheresh DA. Get a ligand, get a life: integrins, signaling and cell survival. J Cell Sci 2002;115:3729-3738
    • (2002) J Cell Sci , vol.115 , pp. 3729-3738
    • Stupack, D.G.1    Cheresh, D.A.2
  • 41
    • 0036229694 scopus 로고    scopus 로고
    • Networks and crosstalk: Integrin signalling spreads
    • Schwartz MA, Ginsberg MH. Networks and crosstalk: integrin signalling spreads. Nat Cell Biol 2002;4:E65-E68
    • (2002) Nat Cell Biol , vol.4
    • Schwartz, M.A.1    Ginsberg, M.H.2
  • 42
    • 0037484137 scopus 로고    scopus 로고
    • Coupling membrane protrusion and cell adhesion
    • DeMali KA, Burridge K. Coupling membrane protrusion and cell adhesion. J Cell Sci 2003;116:2389-2397
    • (2003) J Cell Sci , vol.116 , pp. 2389-2397
    • DeMali, K.A.1    Burridge, K.2
  • 44
    • 3543013755 scopus 로고    scopus 로고
    • A novel basal lamina matrix of the stratified epithelium of the ovarian follicle
    • Irving-Rodgers HF, Harland ML, Rodgers RJ. A novel basal lamina matrix of the stratified epithelium of the ovarian follicle. Matrix Biol 2004;23:207-217
    • (2004) Matrix Biol , vol.23 , pp. 207-217
    • Irving-Rodgers, H.F.1    Harland, M.L.2    Rodgers, R.J.3
  • 45
    • 0344758479 scopus 로고    scopus 로고
    • Mouse primordial germ cells lacking beta1 integrins enter the germline but fail to migrate normally to the gonads
    • Anderson R, Fassler R, Georges-Labouesse E, et al. Mouse primordial germ cells lacking beta1 integrins enter the germline but fail to migrate normally to the gonads. Development 1999;126:1655-1664
    • (1999) Development , vol.126 , pp. 1655-1664
    • Anderson, R.1    Fassler, R.2    Georges-Labouesse, E.3
  • 46
    • 0032146870 scopus 로고    scopus 로고
    • Timing of gene expression and oolemma localization of mouse alpha6 and beta1 integrin subunits during oogenesis
    • Zuccotti M, Giorgi Rossi P, Fiorillo E, Garagna S, Forabosco A, Redi CA. Timing of gene expression and oolemma localization of mouse alpha6 and beta1 integrin subunits during oogenesis. Dev Biol 1998;200:27-34
    • (1998) Dev Biol , vol.200 , pp. 27-34
    • Zuccotti, M.1    Giorgi Rossi, P.2    Fiorillo, E.3    Garagna, S.4    Forabosco, A.5    Redi, C.A.6
  • 47
    • 0029812099 scopus 로고    scopus 로고
    • Expression of integrins in marmoset (Callithrix jacchus) ovary during folliculogenesis
    • Giebel J, de Souza P, Rune GM. Expression of integrins in marmoset (Callithrix jacchus) ovary during folliculogenesis. Tissue Cell 1996;28:379-385
    • (1996) Tissue Cell , vol.28 , pp. 379-385
    • Giebel, J.1    De Souza, P.2    Rune, G.M.3
  • 48
    • 20944441191 scopus 로고    scopus 로고
    • Identification of genes expressed in primate primordial oocytes
    • Arraztoa JA, Zhou J, Marcu D, et al. Identification of genes expressed in primate primordial oocytes. Hum Reprod 2005;20:476-483
    • (2005) Hum Reprod , vol.20 , pp. 476-483
    • Arraztoa, J.A.1    Zhou, J.2    Marcu, D.3
  • 50
    • 4544299291 scopus 로고    scopus 로고
    • Expression of integrin fraction and adhesion molecules on human granulosa cells and its relation with oocyte maturity and follicular steroidogenesis
    • Clavero A, Castilla JA, Martinez L, Mendoza N, Fontes J, Maldonado V. Expression of integrin fraction and adhesion molecules on human granulosa cells and its relation with oocyte maturity and follicular steroidogenesis. J Assist Reprod Genet 2004;21:187-195
    • (2004) J Assist Reprod Genet , vol.21 , pp. 187-195
    • Clavero, A.1    Castilla, J.A.2    Martinez, L.3    Mendoza, N.4    Fontes, J.5    Maldonado, V.6
  • 51
    • 0036007211 scopus 로고    scopus 로고
    • Laminin-alpha6beta1 integrin interaction enhances survival and proliferation and modulates steroidogenesis of ovine granulosa cells
    • Le Bellego F, Pisselet C, Huet C, Monget P, Monniaux D. Laminin-alpha6beta1 integrin interaction enhances survival and proliferation and modulates steroidogenesis of ovine granulosa cells. J Endocrinol 2002;172:45-59
    • (2002) J Endocrinol , vol.172 , pp. 45-59
    • Le Bellego, F.1    Pisselet, C.2    Huet, C.3    Monget, P.4    Monniaux, D.5
  • 52
    • 0028971081 scopus 로고
    • Integrin alpha 6 is a differentiation antigen of human granulosa cells
    • Honda T, Fujiwara H, Ueda M, Maeda M, Mori T. Integrin alpha 6 is a differentiation antigen of human granulosa cells. J Clin Endocrinol Metab 1995;80:2899-2905
    • (1995) J Clin Endocrinol Metab , vol.80 , pp. 2899-2905
    • Honda, T.1    Fujiwara, H.2    Ueda, M.3    Maeda, M.4    Mori, T.5
  • 53
    • 0029112186 scopus 로고
    • A porcine homolog of human integrin alpha 6 is a differentiation antigen of granulosa cells
    • Fujiwara H, Ueda M, Takakura K, Mori T, Maeda M. A porcine homolog of human integrin alpha 6 is a differentiation antigen of granulosa cells. Biol Reprod 1995;53:407-417
    • (1995) Biol Reprod , vol.53 , pp. 407-417
    • Fujiwara, H.1    Ueda, M.2    Takakura, K.3    Mori, T.4    Maeda, M.5
  • 54
  • 55
    • 0030696297 scopus 로고    scopus 로고
    • Relationship between expression of integrins and granulosa cell apoptosis in ovarian follicles of the marmoset (Callithrix jacchus)
    • Giebel J, Rune GM. Relationship between expression of integrins and granulosa cell apoptosis in ovarian follicles of the marmoset (Callithrix jacchus). Tissue Cell 1997;29:525-531
    • (1997) Tissue Cell , vol.29 , pp. 525-531
    • Giebel, J.1    Rune, G.M.2
  • 57
    • 0028986319 scopus 로고
    • Alpha 6 subunit of integrins in the development and sex differentiation of the mouse ovary
    • Frojdman K, Pelliniemi LJ. Alpha 6 subunit of integrins in the development and sex differentiation of the mouse ovary. Dev Dyn 1995;202:397-404
    • (1995) Dev Dyn , vol.202 , pp. 397-404
    • Frojdman, K.1    Pelliniemi, L.J.2
  • 58
    • 0027371908 scopus 로고
    • Embryonic mesodermal defects in alpha 5 integrin-deficient mice
    • Yang JT, Rayburn H, Hynes RO. Embryonic mesodermal defects in alpha 5 integrin-deficient mice. Development 1993;119:1093-1105
    • (1993) Development , vol.119 , pp. 1093-1105
    • Yang, J.T.1    Rayburn, H.2    Hynes, R.O.3
  • 59
    • 0034721888 scopus 로고    scopus 로고
    • Regulation of integrin alpha vbeta 3-mediated endothelial cell migration and angiogenesis by integrin alpha5beta1 and protein kinase A
    • Kim S, Harris M, Varner JA. Regulation of integrin alpha vbeta 3-mediated endothelial cell migration and angiogenesis by integrin alpha5beta1 and protein kinase A. J Biol Chem 2000;275:33920-33928
    • (2000) J Biol Chem , vol.275 , pp. 33920-33928
    • Kim, S.1    Harris, M.2    Varner, J.A.3
  • 60
    • 1042301376 scopus 로고    scopus 로고
    • The homeobox transcription factor Hox D3 promotes integrin alpha5beta1 expression and function during angiogenesis
    • Boudreau NJ, Varner JA. The homeobox transcription factor Hox D3 promotes integrin alpha5beta1 expression and function during angiogenesis. J Biol Chem 2004;279:4862-4868
    • (2004) J Biol Chem , vol.279 , pp. 4862-4868
    • Boudreau, N.J.1    Varner, J.A.2
  • 61
    • 0012077872 scopus 로고
    • Permissive effect of the extracellular matrix on cell proliferation in vitro
    • Gospodarowicz D, Delgado D, Vlodavsky I. Permissive effect of the extracellular matrix on cell proliferation in vitro. Proc Natl Acad Sci USA 1980;77:4094-4098
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 4094-4098
    • Gospodarowicz, D.1    Delgado, D.2    Vlodavsky, I.3
  • 62
    • 0031036949 scopus 로고    scopus 로고
    • Differential effect of components of the extracellular matrix on differentiation and apoptosis
    • Aharoni D, Meiri I, Atzmon R, Vlodavsky I, Amsterdam A. Differential effect of components of the extracellular matrix on differentiation and apoptosis. Curr Biol 1997;7:43-51
    • (1997) Curr Biol , vol.7 , pp. 43-51
    • Aharoni, D.1    Meiri, I.2    Atzmon, R.3    Vlodavsky, I.4    Amsterdam, A.5
  • 63
    • 0035011914 scopus 로고    scopus 로고
    • Extracellular matrix regulates ovine granulosa cell survival, proliferation and steroidogenesis: Relationships between cell shape and function
    • Huet C, Pisselet C, Mandon-Pepin B, Monget P, Monniaux D. Extracellular matrix regulates ovine granulosa cell survival, proliferation and steroidogenesis: relationships between cell shape and function. J Endocrinol 2001;169:347-360
    • (2001) J Endocrinol , vol.169 , pp. 347-360
    • Huet, C.1    Pisselet, C.2    Mandon-Pepin, B.3    Monget, P.4    Monniaux, D.5
  • 64
    • 27444445952 scopus 로고    scopus 로고
    • Cytoskeleton reorganization mediates alpha6beta1 integrin-associated actions of laminin on proliferation and survival, but not on steroidogenesis of ovine granulosa cells
    • Le Bellego F, Fabre S, Pisselet C, Monniaux D. Cytoskeleton reorganization mediates alpha6beta1 integrin-associated actions of laminin on proliferation and survival, but not on steroidogenesis of ovine granulosa cells. Reprod Biol Endocrinol 2005;3:19. Available at: www.nbej. com/content/3/1/29
    • (2005) Reprod Biol Endocrinol , vol.3 , pp. 19
    • Le Bellego, F.1    Fabre, S.2    Pisselet, C.3    Monniaux, D.4
  • 65
    • 0017339672 scopus 로고
    • The porcine ovarian follicle. II. Electron microscopic study of surface features of granulosa cells at different stages of development
    • Chang SC, Anderson W, Lewis JC, Ryan RJ, Kang YK. The porcine ovarian follicle. II. Electron microscopic study of surface features of granulosa cells at different stages of development. Biol Reprod 1977;16:349-357
    • (1977) Biol Reprod , vol.16 , pp. 349-357
    • Chang, S.C.1    Anderson, W.2    Lewis, J.C.3    Ryan, R.J.4    Kang, Y.K.5
  • 66
    • 0021823616 scopus 로고
    • The distribution of actin in sheep ovaries
    • Cran DG, Musk L. The distribution of actin in sheep ovaries. J Exp Zool 1985;235:375-380
    • (1985) J Exp Zool , vol.235 , pp. 375-380
    • Cran, D.G.1    Musk, L.2
  • 67
    • 0014265733 scopus 로고
    • Morphology of the membrana granulosa of the ovarian follicle
    • Lipner H, Cross NL. Morphology of the membrana granulosa of the ovarian follicle. Endocrinology 1968;82:638-641
    • (1968) Endocrinology , vol.82 , pp. 638-641
    • Lipner, H.1    Cross, N.L.2
  • 69
    • 11144223232 scopus 로고    scopus 로고
    • Conversion of mechanical force into biochemical signaling
    • Han B, Bai XH, Lodyga M, et al. Conversion of mechanical force into biochemical signaling. J Biol Chem 2004;279:54793-54801
    • (2004) J Biol Chem , vol.279 , pp. 54793-54801
    • Han, B.1    Bai, X.H.2    Lodyga, M.3
  • 70
    • 0012796190 scopus 로고    scopus 로고
    • How structural networks influence cellular information processing networks
    • Ingber DE, Tensegrity II. How structural networks influence cellular information processing networks. J Cell Sci 2003;116:1397-1408
    • (2003) J Cell Sci , vol.116 , pp. 1397-1408
    • Ingber, D.E.1    Tensegrity, I.I.2
  • 71
    • 2942707853 scopus 로고    scopus 로고
    • Role of RhoA, mDia, and ROCK in cell shape-dependent control of the Skp2-p27kip1 pathway and the G1/S transition
    • Mammoto A, Huang S, Moore K, Oh P, Ingber DE. Role of RhoA, mDia, and ROCK in cell shape-dependent control of the Skp2-p27kip1 pathway and the G1/S transition. J Biol Chem 2004;279:26323-26330
    • (2004) J Biol Chem , vol.279 , pp. 26323-26330
    • Mammoto, A.1    Huang, S.2    Moore, K.3    Oh, P.4    Ingber, D.E.5
  • 72
    • 0028335948 scopus 로고
    • Anchorage dependence, integrins, and apoptosis
    • Ruoslahti E, Reed JC. Anchorage dependence, integrins, and apoptosis. Cell 1994;77:477-478
    • (1994) Cell , vol.77 , pp. 477-478
    • Ruoslahti, E.1    Reed, J.C.2
  • 73
    • 0020603001 scopus 로고
    • Developmental changes in the ovarian follicular basal lamina detected by immunofluorescence and electron microscopy
    • Bagavandoss P, Midgley AR Jr, Wicha M. Developmental changes in the ovarian follicular basal lamina detected by immunofluorescence and electron microscopy. J Histochem Cytochem 1983;31:633-640
    • (1983) J Histochem Cytochem , vol.31 , pp. 633-640
    • Bagavandoss, P.1    Midgley Jr., A.R.2    Wicha, M.3
  • 74
    • 0030895217 scopus 로고    scopus 로고
    • Changes in extracellular matrix components and steroidogenic enzymes during growth and atresia of antral ovarian follicles in the sheep
    • Huet C, Monget P, Pisselet C, Monniaux D. Changes in extracellular matrix components and steroidogenic enzymes during growth and atresia of antral ovarian follicles in the sheep. Biol Reprod 1997;56:1025-1034
    • (1997) Biol Reprod , vol.56 , pp. 1025-1034
    • Huet, C.1    Monget, P.2    Pisselet, C.3    Monniaux, D.4
  • 75
    • 0029971764 scopus 로고    scopus 로고
    • Proteolytic activity is involved in changes in intrafollicular insulin-like growth factor-binding protein levels during growth and atresia of ovine ovarian follicles
    • Besnard N, Pisselet C, Zapf J, Hornebeck W, Monniaux D, Monget P. Proteolytic activity is involved in changes in intrafollicular insulin-like growth factor-binding protein levels during growth and atresia of ovine ovarian follicles. Endocrinology 1996;137:1599-1607
    • (1996) Endocrinology , vol.137 , pp. 1599-1607
    • Besnard, N.1    Pisselet, C.2    Zapf, J.3    Hornebeck, W.4    Monniaux, D.5    Monget, P.6
  • 76
    • 0033558815 scopus 로고    scopus 로고
    • Laminin 5 promotes activation and apoptosis of the T cells expressing alpha3-beta1 integrin
    • Sato K, Katagiri K, Hattori S, et al. Laminin 5 promotes activation and apoptosis of the T cells expressing alpha3-beta1 integrin. Exp Cell Res 1999;247:451-460
    • (1999) Exp Cell Res , vol.247 , pp. 451-460
    • Sato, K.1    Katagiri, K.2    Hattori, S.3
  • 77
    • 0035851921 scopus 로고    scopus 로고
    • Suppression of p53 function in normal human mammary epithelial cells increases sensitivity to extracellular matrix-induced apoptosis
    • Seewaldt VL, Mrozek K, Sigle R, et al. Suppression of p53 function in normal human mammary epithelial cells increases sensitivity to extracellular matrix-induced apoptosis. J Cell Biol 2001;155:471-486
    • (2001) J Cell Biol , vol.155 , pp. 471-486
    • Seewaldt, V.L.1    Mrozek, K.2    Sigle, R.3
  • 78
    • 0027232013 scopus 로고
    • Culture of human preovulatory granulosa cells: Effect of extracellular matrix on steroidogenesis
    • Bussenot I, Ferre G, Azoulay-Barjonet C, Murgo C, Vieitez G, Parinaud J. Culture of human preovulatory granulosa cells: effect of extracellular matrix on steroidogenesis. Biol Cell 1993;77:181-186
    • (1993) Biol Cell , vol.77 , pp. 181-186
    • Bussenot, I.1    Ferre, G.2    Azoulay-Barjonet, C.3    Murgo, C.4    Vieitez, G.5    Parinaud, J.6
  • 79
    • 0023814785 scopus 로고
    • Culture of granulosa cells in collagen gels: The influence of cell shape on steroidogenesis
    • Carnegie JA, Byard R, Dardick I, Tsang BK. Culture of granulosa cells in collagen gels: the influence of cell shape on steroidogenesis. Biol Reprod 1988;38:881-890
    • (1988) Biol Reprod , vol.38 , pp. 881-890
    • Carnegie, J.A.1    Byard, R.2    Dardick, I.3    Tsang, B.K.4
  • 80
    • 0024166135 scopus 로고
    • Collagen matrix influences the morphologic features and steroid secretion of human granulosa cells
    • Ben-Rafael Z, Benadiva CA, Mastroianni L Jr, et al. Collagen matrix influences the morphologic features and steroid secretion of human granulosa cells. Am J Obstet Gynecol 1988;159:1570-1574
    • (1988) Am J Obstet Gynecol , vol.159 , pp. 1570-1574
    • Ben-Rafael, Z.1    Benadiva, C.A.2    Mastroianni Jr., L.3
  • 81
    • 0028932548 scopus 로고
    • A cell adhesion receptor antiserum abolishes, whereas laminin and fibronectin glycoprotein components of extracellular matrix promote, luteinization of cultured rat granulosa cells
    • Aten RF, Kolodecik TR, Behrman HR. A cell adhesion receptor antiserum abolishes, whereas laminin and fibronectin glycoprotein components of extracellular matrix promote, luteinization of cultured rat granulosa cells. Endocrinology 1995;136:1753-1758
    • (1995) Endocrinology , vol.136 , pp. 1753-1758
    • Aten, R.F.1    Kolodecik, T.R.2    Behrman, H.R.3
  • 82
    • 0029916065 scopus 로고    scopus 로고
    • Adhesion proteins increase cellular attachment, follicle-stimulating hormone receptors, and progesterone production in cultured porcine granulosa cells
    • Sites CK, Kessel B, LaBarbera AR. Adhesion proteins increase cellular attachment, follicle-stimulating hormone receptors, and progesterone production in cultured porcine granulosa cells. Proc Soc Exp Biol Med 1996;212:78-83
    • (1996) Proc Soc Exp Biol Med , vol.212 , pp. 78-83
    • Sites, C.K.1    Kessel, B.2    Labarbera, A.R.3
  • 83
    • 0030856519 scopus 로고    scopus 로고
    • Laminin suppresses progesterone production by human luteinizing granulosa cells via interaction with integrin alpha 6 beta 1
    • Fujiwara H, Honda T, Ueda M, et al. Laminin suppresses progesterone production by human luteinizing granulosa cells via interaction with integrin alpha 6 beta 1. J Clin Endocrinol Metab 1997;82:2122-2128
    • (1997) J Clin Endocrinol Metab , vol.82 , pp. 2122-2128
    • Fujiwara, H.1    Honda, T.2    Ueda, M.3
  • 84
    • 1842843786 scopus 로고    scopus 로고
    • The mechanism of sperm-oocyte fusion in mammals
    • Kaji K, Kudo A. The mechanism of sperm-oocyte fusion in mammals. Reproduction 2004;127:423-429
    • (2004) Reproduction , vol.127 , pp. 423-429
    • Kaji, K.1    Kudo, A.2
  • 85
    • 0031593926 scopus 로고    scopus 로고
    • Distribution of alpha3, alpha5 and alpha(v) integrin subunits in mature and immature human oocytes
    • Capmany G, Mart M, Santalo J, Bolton VN. Distribution of alpha3, alpha5 and alpha(v) integrin subunits in mature and immature human oocytes. Mol Hum Reprod 1998;4:951-956
    • (1998) Mol Hum Reprod , vol.4 , pp. 951-956
    • Capmany, G.1    Mart, M.2    Santalo, J.3    Bolton, V.N.4
  • 86
    • 28544442231 scopus 로고    scopus 로고
    • Cyclic FEE peptide increases human gamete fusion and potentiates its RGD-induced inhibition
    • Ziyyat A, Naud-Barriant N, Barraud-Lange V, et al. Cyclic FEE peptide increases human gamete fusion and potentiates its RGD-induced inhibition. Hum Reprod 2005;20:3452-3458
    • (2005) Hum Reprod , vol.20 , pp. 3452-3458
    • Ziyyat, A.1    Naud-Barriant, N.2    Barraud-Lange, V.3
  • 87
    • 0027496522 scopus 로고
    • Mammalian oocytes exhibit specific recognition of the RGD (Arg-Gly-Asp) tripeptide and express oolemmal integrins
    • Fusi FM, Vignali M, Gailit J, Bronson RA. Mammalian oocytes exhibit specific recognition of the RGD (Arg-Gly-Asp) tripeptide and express oolemmal integrins. Mol Reprod Dev 1993;36:212-219
    • (1993) Mol Reprod Dev , vol.36 , pp. 212-219
    • Fusi, F.M.1    Vignali, M.2    Gailit, J.3    Bronson, R.A.4
  • 88
    • 0032782655 scopus 로고    scopus 로고
    • Mediation of sperm-egg fusion: Evidence that mouse egg alpha6beta1 integrin is the receptor for sperm fertilin beta
    • Chen H, Sampson NS. Mediation of sperm-egg fusion: evidence that mouse egg alpha6beta1 integrin is the receptor for sperm fertilin beta. Chem Biol 1999;6:1-10
    • (1999) Chem Biol , vol.6 , pp. 1-10
    • Chen, H.1    Sampson, N.S.2
  • 89
    • 0034914182 scopus 로고    scopus 로고
    • Fertilin beta and other ADAMs as integrin ligands: Insights into cell adhesion and fertilization
    • Evans JP. Fertilin beta and other ADAMs as integrin ligands: insights into cell adhesion and fertilization. Bioessays 2001;23:628-639
    • (2001) Bioessays , vol.23 , pp. 628-639
    • Evans, J.P.1
  • 90
    • 0029047919 scopus 로고
    • Mouse egg integrin alpha 6 beta 1 functions as a sperm receptor
    • Almeida EA, Huovila AP, Sutherland AE, et al. Mouse egg integrin alpha 6 beta 1 functions as a sperm receptor. Cell 1995;81:1095-1104
    • (1995) Cell , vol.81 , pp. 1095-1104
    • Almeida, E.A.1    Huovila, A.P.2    Sutherland, A.E.3
  • 91
    • 0037124066 scopus 로고    scopus 로고
    • Functional classification of ADAMs based on a conserved motif for binding to integrin alpha 9beta 1: Implications for sperm-egg binding and other cell interactions
    • Eto K, Huet C, Tarui T, et al. Functional classification of ADAMs based on a conserved motif for binding to integrin alpha 9beta 1: implications for sperm-egg binding and other cell interactions. J Biol Chem 2002;277:17804-17810
    • (2002) J Biol Chem , vol.277 , pp. 17804-17810
    • Eto, K.1    Huet, C.2    Tarui, T.3
  • 92
    • 0036197618 scopus 로고    scopus 로고
    • Analysis of the roles of RGD-binding integrins, alpha(4)/alpha(9) integrins, alpha(6) integrins, and CD9 in the interaction of the fertilin beta (ADAM2) disintegrin domain with the mouse egg membrane
    • Zhu X, Evans JP. Analysis of the roles of RGD-binding integrins, alpha(4)/alpha(9) integrins, alpha(6) integrins, and CD9 in the interaction of the fertilin beta (ADAM2) disintegrin domain with the mouse egg membrane. Biol Reprod 2002;66:1193-1202
    • (2002) Biol Reprod , vol.66 , pp. 1193-1202
    • Zhu, X.1    Evans, J.P.2
  • 93
    • 0037442567 scopus 로고    scopus 로고
    • None of the integrins known to be present on the mouse egg or to be ADAM receptors are essential for sperm-egg binding and fusion
    • He ZY, Brakebusch C, Fassler R, Kreidberg JA, Primakoff P, Myles DG. None of the integrins known to be present on the mouse egg or to be ADAM receptors are essential for sperm-egg binding and fusion. Dev Biol 2003;254:226-237
    • (2003) Dev Biol , vol.254 , pp. 226-237
    • He, Z.Y.1    Brakebusch, C.2    Fassler, R.3    Kreidberg, J.A.4    Primakoff, P.5    Myles, D.G.6
  • 94
    • 1542397146 scopus 로고    scopus 로고
    • Integrins are not involved in the process of human sperm-oolemmal fusion
    • Sengoku K, Takuma N, Miyamoto T, Horikawa M, Ishikawa M. Integrins are not involved in the process of human sperm-oolemmal fusion. Hum Reprod 2004;19:639-644
    • (2004) Hum Reprod , vol.19 , pp. 639-644
    • Sengoku, K.1    Takuma, N.2    Miyamoto, T.3    Horikawa, M.4    Ishikawa, M.5
  • 95
    • 0036152857 scopus 로고    scopus 로고
    • Enhanced pathological angiogenesis in mice lacking beta3 integrin or beta3 and beta5 integrins
    • Reynolds LE, Wyder L, Lively JC, et al. Enhanced pathological angiogenesis in mice lacking beta3 integrin or beta3 and beta5 integrins. Nat Med 2002;8:27-34
    • (2002) Nat Med , vol.8 , pp. 27-34
    • Reynolds, L.E.1    Wyder, L.2    Lively, J.C.3
  • 96
    • 0036156813 scopus 로고    scopus 로고
    • Integrin indecision
    • Carmeliet P. Integrin indecision. Nat Med 2002;8:14-16
    • (2002) Nat Med , vol.8 , pp. 14-16
    • Carmeliet, P.1
  • 98
    • 1642349298 scopus 로고    scopus 로고
    • Germline stem cells and follicular renewal in the postnatal mammalian ovary
    • Johnson J, Canning J, Kaneko T, Pru JK, Tilly JL. Germline stem cells and follicular renewal in the postnatal mammalian ovary. Nature 2004;428:145-150
    • (2004) Nature , vol.428 , pp. 145-150
    • Johnson, J.1    Canning, J.2    Kaneko, T.3    Pru, J.K.4    Tilly, J.L.5
  • 99
    • 1242271192 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha-induced matrix proteolytic enzyme production and basement membrane remodeling by human ovarian surface epithelial cells: Molecular basis linking ovulation and cancer risk
    • Yang WL, Godwin AK, Xu XX. Tumor necrosis factor-alpha-induced matrix proteolytic enzyme production and basement membrane remodeling by human ovarian surface epithelial cells: molecular basis linking ovulation and cancer risk. Cancer Res 2004;64:1534-1540
    • (2004) Cancer Res , vol.64 , pp. 1534-1540
    • Yang, W.L.1    Godwin, A.K.2    Xu, X.X.3
  • 100
    • 0032749677 scopus 로고    scopus 로고
    • Hormonal control of urokinase plasminogen activator secretion by sheep ovarian surface epithelial cells
    • Murdoch J, Van Kirk EA, Murdoch WJ. Hormonal control of urokinase plasminogen activator secretion by sheep ovarian surface epithelial cells. Biol Reprod 1999;61:1487-1491
    • (1999) Biol Reprod , vol.61 , pp. 1487-1491
    • Murdoch, J.1    Van Kirk, E.A.2    Murdoch, W.J.3
  • 101
    • 32644470154 scopus 로고    scopus 로고
    • MMPS and TIMPS in ovarian physiology and pathophysiology
    • Goldman S, Shalev E. MMPS and TIMPS in ovarian physiology and pathophysiology. Front Biosci 2004;9:2474-2483
    • (2004) Front Biosci , vol.9 , pp. 2474-2483
    • Goldman, S.1    Shalev, E.2
  • 102
    • 0029915884 scopus 로고    scopus 로고
    • Expression of alpha 6 and beta 4 integrins in serous ovarian carcinoma correlates with expression of the basement membrane protein laminin
    • Skubitz AP, Bast RC Jr, Wayner EA, Letourneau PC, Wilke MS. Expression of alpha 6 and beta 4 integrins in serous ovarian carcinoma correlates with expression of the basement membrane protein laminin. Am J Pathol 1996;148:1445-1461
    • (1996) Am J Pathol , vol.148 , pp. 1445-1461
    • Skubitz, A.P.1    Bast Jr., R.C.2    Wayner, E.A.3    Letourneau, P.C.4    Wilke, M.S.5
  • 103
    • 0030221156 scopus 로고    scopus 로고
    • Expression and localization of alpha v integrins and their ligand vitronectin in normal ovarian epithelium and in ovarian carcinoma
    • Carreiras F, Denoux Y, Staedel C, Lehmann M, Sichel F, Gauduchon P. Expression and localization of alpha v integrins and their ligand vitronectin in normal ovarian epithelium and in ovarian carcinoma. Gynecol Oncol 1996;62:260-267
    • (1996) Gynecol Oncol , vol.62 , pp. 260-267
    • Carreiras, F.1    Denoux, Y.2    Staedel, C.3    Lehmann, M.4    Sichel, F.5    Gauduchon, P.6
  • 104
    • 0036007394 scopus 로고    scopus 로고
    • Association between alphavbeta6 integrin expression, elevated p42/44 kDa MAPK, and plasminogen-dependent matrix degradation in ovarian cancer
    • Ahmed N, Pansino F, Baker M, Rice G, Quinn M. Association between alphavbeta6 integrin expression, elevated p42/44 kDa MAPK, and plasminogen-dependent matrix degradation in ovarian cancer. J Cell Biochem 2002;84:675-686
    • (2002) J Cell Biochem , vol.84 , pp. 675-686
    • Ahmed, N.1    Pansino, F.2    Baker, M.3    Rice, G.4    Quinn, M.5
  • 105
    • 18144404647 scopus 로고    scopus 로고
    • Expression of alpha V-associated integrin beta subunits in epithelial ovarian cancer and its relation to prognosis in patients treated with platinum-based regimens
    • Maubant S, Cruet-Hennequart S, Dutoit S, et al. Expression of alpha V-associated integrin beta subunits in epithelial ovarian cancer and its relation to prognosis in patients treated with platinum-based regimens. J Mol Histol 2005;36:119-129
    • (2005) J Mol Histol , vol.36 , pp. 119-129
    • Maubant, S.1    Cruet-Hennequart, S.2    Dutoit, S.3
  • 106
    • 0030842795 scopus 로고    scopus 로고
    • Plasminogen activators, integrins, and the coordinated regulation of cell adhesion and migration
    • Chapman HA. Plasminogen activators, integrins, and the coordinated regulation of cell adhesion and migration. Curr Opin Cell Biol 1997;9:714-724
    • (1997) Curr Opin Cell Biol , vol.9 , pp. 714-724
    • Chapman, H.A.1
  • 107
    • 0034923326 scopus 로고    scopus 로고
    • Protease crosstalk with integrins: The urokinase receptor paradigm
    • Chapman HA, Wei Y. Protease crosstalk with integrins: the urokinase receptor paradigm. Thromb Haemost 2001;86:124-129
    • (2001) Thromb Haemost , vol.86 , pp. 124-129
    • Chapman, H.A.1    Wei, Y.2
  • 108
    • 0028243591 scopus 로고
    • Coordinate expression of urinary-type plasminogen activator and its receptor accompanies malignant transformation of the ovarian surface epithelium
    • Young TN, Rodriguez GC, Moser TL, Bast RC Jr, Pizzo SV, Stack MS. Coordinate expression of urinary-type plasminogen activator and its receptor accompanies malignant transformation of the ovarian surface epithelium. Am J Obstet Gynecol 1994;170:1285-1296
    • (1994) Am J Obstet Gynecol , vol.170 , pp. 1285-1296
    • Young, T.N.1    Rodriguez, G.C.2    Moser, T.L.3    Bast Jr., R.C.4    Pizzo, S.V.5    Stack, M.S.6
  • 109
    • 0038643516 scopus 로고    scopus 로고
    • Urokinase receptor and integrin interactions
    • Kugler MC, Wei Y, Chapman HA. Urokinase receptor and integrin interactions. Curr Pharm Des 2003;9:1565-1574
    • (2003) Curr Pharm Des , vol.9 , pp. 1565-1574
    • Kugler, M.C.1    Wei, Y.2    Chapman, H.A.3
  • 110
    • 13444274458 scopus 로고    scopus 로고
    • Regulation of alpha5beta1 integrin conformation and function by urokinase receptor binding
    • Wei Y, Czekay RP, Robillard L, et al. Regulation of alpha5beta1 integrin conformation and function by urokinase receptor binding. J Cell Biol 2005;168:501-511
    • (2005) J Cell Biol , vol.168 , pp. 501-511
    • Wei, Y.1    Czekay, R.P.2    Robillard, L.3
  • 111
    • 19944375775 scopus 로고    scopus 로고
    • ADAM15 decreases integrin alphavbeta3/vitronectin-mediated ovarian cancer cell adhesion and motility in an RGD-dependent fashion
    • Beck V, Herold H, Benge A, et al. ADAM15 decreases integrin alphavbeta3/vitronectin-mediated ovarian cancer cell adhesion and motility in an RGD-dependent fashion. Int J Biochem Cell Biol 2005;37:590-603
    • (2005) Int J Biochem Cell Biol , vol.37 , pp. 590-603
    • Beck, V.1    Herold, H.2    Benge, A.3
  • 112
    • 0034640885 scopus 로고    scopus 로고
    • Normal fertilization occurs with eggs lacking the integrin alpha6beta1 and is CD9-dependent
    • Miller BJ, Georges-Labouesse E, Primakoff P, Myles DG. Normal fertilization occurs with eggs lacking the integrin alpha6beta1 and is CD9-dependent. J Cell Biol 2000;149:1289-1296
    • (2000) J Cell Biol , vol.149 , pp. 1289-1296
    • Miller, B.J.1    Georges-Labouesse, E.2    Primakoff, P.3    Myles, D.G.4
  • 113
    • 0030589587 scopus 로고    scopus 로고
    • Targeted mutations in cell adhesion genes: What have we learned from them?
    • Hynes RO. Targeted mutations in cell adhesion genes: what have we learned from them? Dev Biol 1996;180:402-412
    • (1996) Dev Biol , vol.180 , pp. 402-412
    • Hynes, R.O.1
  • 114
    • 0033570076 scopus 로고    scopus 로고
    • Overexpression of focal adhesion kinase, a protein tyrosine kinase, in ovarian carcinoma
    • Judson PL, He X, Cance WG. Van Le L. Overexpression of focal adhesion kinase, a protein tyrosine kinase, in ovarian carcinoma. Cancer 1999;86:1551-1556
    • (1999) Cancer , vol.86 , pp. 1551-1556
    • Judson, P.L.1    He, X.2    Cance, W.G.3    Van Le, L.4
  • 115
    • 4644315256 scopus 로고    scopus 로고
    • Biological significance of focal adhesion kinase in ovarian cancer: Role in migration and invasion
    • Sood AK, Coffin JE, Schneider GB, et al. Biological significance of focal adhesion kinase in ovarian cancer: role in migration and invasion. Am J Pathol 2004;165:1087-1095
    • (2004) Am J Pathol , vol.165 , pp. 1087-1095
    • Sood, A.K.1    Coffin, J.E.2    Schneider, G.B.3
  • 116
    • 0034954054 scopus 로고    scopus 로고
    • Fibronectin activates matrix metalloproteinase-9 secretion via the MEK1-MAPK and the PI3K-Akt pathways in ovarian cancer cells
    • Thant AA, Nawa A, Kikkawa F, et al. Fibronectin activates matrix metalloproteinase-9 secretion via the MEK1-MAPK and the PI3K-Akt pathways in ovarian cancer cells. Clin Exp Metastasis 2000;18:423-428
    • (2000) Clin Exp Metastasis , vol.18 , pp. 423-428
    • Thant, A.A.1    Nawa, A.2    Kikkawa, F.3
  • 117
    • 0141995796 scopus 로고    scopus 로고
    • Integrin-linked kinase expression increases with ovarian tumour grade and is sustained by peritoneal tumour fluid
    • Ahmed N, Riley C, Oliva K, Stutt E, Rice GE, Quinn MA. Integrin-linked kinase expression increases with ovarian tumour grade and is sustained by peritoneal tumour fluid. J Pathol 2003;201:229-237
    • (2003) J Pathol , vol.201 , pp. 229-237
    • Ahmed, N.1    Riley, C.2    Oliva, K.3    Stutt, E.4    Rice, G.E.5    Quinn, M.A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.