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Volumn 51, Issue 4, 2007, Pages 499-508

Increased cytoplasmic level of migfilin is associated with higher grades of human leiomyosarcoma

Author keywords

Cell matrix adhesion; Kindlin; Leiomyosarcoma; Mig 2; Migfilin; Tissue microarray

Indexed keywords

MIGFILIN; SCLEROPROTEIN; UNCLASSIFIED DRUG;

EID: 34548707077     PISSN: 03090167     EISSN: 13652559     Source Type: Journal    
DOI: 10.1111/j.1365-2559.2007.02791.x     Document Type: Article
Times cited : (20)

References (29)
  • 1
    • 0002748003 scopus 로고    scopus 로고
    • Leiomyosarcoma
    • In. Weis, S.W., Goldblum, J.R. eds. Mosby, St Louis:
    • Enzinger F, Weis SW. Leiomyosarcoma. In Weis SW, Goldblum JR eds. Soft tissue tumors, 4th edn. Mosby, St Louis : 2001 724 748.
    • (2001) Soft Tissue Tumors, 4th Edn. , pp. 724-748
    • Enzinger, F.1    Weis, S.W.2
  • 3
    • 0037531733 scopus 로고    scopus 로고
    • Gene expression analysis of human soft tissue leiomyosarcomas
    • Ren B, Yu YP, Jing L et al. Gene expression analysis of human soft tissue leiomyosarcomas. Hum. Pathol. 2003 34 549 558.
    • (2003) Hum. Pathol. , vol.34 , pp. 549-558
    • Ren, B.1    Yu, Y.P.2    Jing, L.3
  • 4
    • 25144434380 scopus 로고    scopus 로고
    • Assembly and signaling of the cell-extracellular matrix adhesion complexes
    • Sepulveda J, Gkretsi V, Wu C. Assembly and signaling of the cell-extracellular matrix adhesion complexes. Curr. Top. Dev. Biol. 2005 68 183 225.
    • (2005) Curr. Top. Dev. Biol. , vol.68 , pp. 183-225
    • Sepulveda, J.1    Gkretsi, V.2    Wu, C.3
  • 5
    • 0036228744 scopus 로고    scopus 로고
    • Intercellular adhesion, signalling and the cytoskeleton
    • Jamora C, Fuchs E. Intercellular adhesion, signalling and the cytoskeleton. Nat. Cell. Biol. 2002 4 E101 108.
    • (2002) Nat. Cell. Biol. , vol.4
    • Jamora, C.1    Fuchs, E.2
  • 7
    • 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. JBiol. Chem. 2000 275 22607 22610.
    • (2000) JBiol. Chem. , vol.275 , pp. 22607-22610
    • Calderwood, D.A.1    Shattil, S.J.2    Ginsberg, M.H.3
  • 9
    • 7944233251 scopus 로고    scopus 로고
    • The interplay between Src and integrins in normal and tumor biology
    • Playford MP, Schaller MD. The interplay between Src and integrins in normal and tumor biology. Oncogene 2004 23 7928 7946.
    • (2004) Oncogene , vol.23 , pp. 7928-7946
    • Playford, M.P.1    Schaller, M.D.2
  • 10
    • 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
  • 11
    • 0034631954 scopus 로고    scopus 로고
    • UNC112. a new regulator of cell-extracellular matrix adhesions?
    • Schaller MD. UNC112. A new regulator of cell-extracellular matrix adhesions? JCell Biol. 2000 150 F9 F11.
    • (2000) JCell Biol. , vol.150
    • Schaller, M.D.1
  • 12
    • 0034632070 scopus 로고    scopus 로고
    • The UNC-112 gene in Caenorhabditis elegans encodes a novel component of cell-matrix adhesion structures required for integrin localization in the muscle cell membrane
    • Rogalski TM, Mullen GP, Gilbert MM, Williams BD, Moerman DG. The UNC-112 gene in Caenorhabditis elegans encodes a novel component of cell-matrix adhesion structures required for integrin localization in the muscle cell membrane. JCell Biol. 2000 150 253 264.
    • (2000) JCell Biol. , vol.150 , pp. 253-264
    • Rogalski, T.M.1    Mullen, G.P.2    Gilbert, M.M.3    Williams, B.D.4    Moerman, D.G.5
  • 13
    • 0037418837 scopus 로고    scopus 로고
    • Migfilin and Mig-2 link focal adhesions to filamin and the actin cytoskeleton and function in cell shape modulation
    • Tu Y, Wu S, Shi X, Chen K, Wu C. Migfilin and Mig-2 link focal adhesions to filamin and the actin cytoskeleton and function in cell shape modulation. Cell 2003 113 37 47.
    • (2003) Cell , vol.113 , pp. 37-47
    • Tu, Y.1    Wu, S.2    Shi, X.3    Chen, K.4    Wu, C.5
  • 14
    • 0037451891 scopus 로고    scopus 로고
    • URP1: A member of a novel family of PH and FERM domain-containing membrane-associated proteins is significantly over-expressed in lung and colon carcinomas
    • Weinstein EJ, Bourner M, Head R, Zakeri H, Bauer C, Mazzarella R. URP1: a member of a novel family of PH and FERM domain-containing membrane-associated proteins is significantly over-expressed in lung and colon carcinomas. Biochim. Biophys. Acta 2003 1637 207 216.
    • (2003) Biochim. Biophys. Acta , vol.1637 , pp. 207-216
    • Weinstein, E.J.1    Bourner, M.2    Head, R.3    Zakeri, H.4    Bauer, C.5    Mazzarella, R.6
  • 15
    • 1342346591 scopus 로고    scopus 로고
    • The Kindler syndrome protein is regulated by transforming growth factor-beta and involved in integrin-mediated adhesion
    • Kloeker S, Major MB, Calderwood DA, Ginsberg MH, Jones DA, Beckerle MC. The Kindler syndrome protein is regulated by transforming growth factor-beta and involved in integrin-mediated adhesion. JBiol. Chem. 2004 279 6824 6833.
    • (2004) JBiol. Chem. , vol.279 , pp. 6824-6833
    • Kloeker, S.1    Major, M.B.2    Calderwood, D.A.3    Ginsberg, M.H.4    Jones, D.A.5    Beckerle, M.C.6
  • 16
    • 0038389789 scopus 로고    scopus 로고
    • Loss of kindlin-1, a human homolog of the Caenorhabditis elegans actin-extracellular-matrix linker protein UNC-112, causes Kindler syndrome
    • Siegel DH, Ashton GH, Penagos HG et al. Loss of kindlin-1, a human homolog of the Caenorhabditis elegans actin-extracellular-matrix linker protein UNC-112, causes Kindler syndrome. Am. J. Hum. Genet. 2003 73 174 187.
    • (2003) Am. J. Hum. Genet. , vol.73 , pp. 174-187
    • Siegel, D.H.1    Ashton, G.H.2    Penagos, H.G.3
  • 17
    • 0242515916 scopus 로고    scopus 로고
    • Identification of mutations in a new gene encoding a FERM family protein with a pleckstrin homology domain in Kindler syndrome
    • Jobard F, Bouadjar B, Caux F et al. Identification of mutations in a new gene encoding a FERM family protein with a pleckstrin homology domain in Kindler syndrome. Hum. Mol. Genet. 2003 12 925 935.
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 925-935
    • Jobard, F.1    Bouadjar, B.2    Caux, F.3
  • 18
    • 0024309209 scopus 로고
    • Poikiloderma of Theresa Kindler: Report of a case with ultrastructural study, and review of the literature
    • Hovnanian A, Blanchet-Bardon C, de Prost Y. Poikiloderma of Theresa Kindler: report of a case with ultrastructural study, and review of the literature. Pediatr. Dermatol. 1989 6 82 90.
    • (1989) Pediatr. Dermatol. , vol.6 , pp. 82-90
    • Hovnanian, A.1    Blanchet-Bardon, C.2    De Prost, Y.3
  • 20
    • 0030461569 scopus 로고    scopus 로고
    • Kindler syndrome. Clinical and ultrastructural findings
    • Haber RM, Hanna WM. Kindler syndrome. Clinical and ultrastructural findings. Arch. Dermatol. 1996 132 1487 1490.
    • (1996) Arch. Dermatol. , vol.132 , pp. 1487-1490
    • Haber, R.M.1    Hanna, W.M.2
  • 21
    • 0842288224 scopus 로고    scopus 로고
    • A novel LIM protein Cal promotes cardiac differentiation by association with CSX/NKX2-5
    • Akazawa H, Kudoh S, Mochizuki N et al. A novel LIM protein Cal promotes cardiac differentiation by association with CSX/NKX2-5. JCell Biol. 2004 164 195 405.
    • (2004) JCell Biol. , vol.164 , pp. 195-405
    • Akazawa, H.1    Kudoh, S.2    Mochizuki, N.3
  • 22
    • 14944370105 scopus 로고    scopus 로고
    • Migfilin and its binding partners: From cell biology to human diseases
    • Wu C. Migfilin and its binding partners: from cell biology to human diseases. JCell Sci. 2005 118 659 664.
    • (2005) JCell Sci. , vol.118 , pp. 659-664
    • Wu, C.1
  • 23
    • 14944346911 scopus 로고    scopus 로고
    • Physical and functional association of migfilin with cell-cell adhesions
    • Gkretsi V, Zhang Y, Tu Y et al. Physical and functional association of migfilin with cell-cell adhesions. JCell Sci. 2005 118 697 710.
    • (2005) JCell Sci. , vol.118 , pp. 697-710
    • Gkretsi, V.1    Zhang, Y.2    Tu, Y.3
  • 24
    • 0035972170 scopus 로고    scopus 로고
    • A new focal adhesion protein that interacts with integrin-linked kinase and regulates cell adhesion and spreading
    • Tu Y, Huang Y, Zhang Y, Hua Y, Wu C. A new focal adhesion protein that interacts with integrin-linked kinase and regulates cell adhesion and spreading. JCell Biol. 2001 153 585 598.
    • (2001) JCell Biol. , vol.153 , pp. 585-598
    • Tu, Y.1    Huang, Y.2    Zhang, Y.3    Hua, Y.4    Wu, C.5
  • 25
    • 0033378656 scopus 로고    scopus 로고
    • Integrin-linked kinase is localized to cell-matrix focal adhesions but not cell-cell adhesion sites and the focal adhesion localization of integrin-linked kinase is regulated by the PINCH-binding ANK repeats
    • Li F, Zhang Y, Wu C. Integrin-linked kinase is localized to cell-matrix focal adhesions but not cell-cell adhesion sites and the focal adhesion localization of integrin-linked kinase is regulated by the PINCH-binding ANK repeats. JCell Sci. 1999 112 4589 4599.
    • (1999) JCell Sci. , vol.112 , pp. 4589-4599
    • Li, F.1    Zhang, Y.2    Wu, C.3
  • 26
    • 0038581169 scopus 로고    scopus 로고
    • Changing neighbours, changing behaviour: Cell adhesion molecule-mediated signalling during tumour progression
    • Christofori G. Changing neighbours, changing behaviour: cell adhesion molecule-mediated signalling during tumour progression. EMBO J. 2003 22 2318 2323.
    • (2003) EMBO J. , vol.22 , pp. 2318-2323
    • Christofori, G.1
  • 27
    • 0034089127 scopus 로고    scopus 로고
    • Low E-cadherin expression in bladder cancer at the transcriptional and protein level provides prognostic information
    • Popov Z, Gil-Diez de Medina S, Lefrere-Belda M-A et al. Low E-cadherin expression in bladder cancer at the transcriptional and protein level provides prognostic information. Br. J. Cancer 2000 83 209 214.
    • (2000) Br. J. Cancer , vol.83 , pp. 209-214
    • Popov, Z.1    Gil-Diez De Medina, S.2    Lefrere-Belda, M.-A.3
  • 28
    • 33744951973 scopus 로고    scopus 로고
    • Migfilin interacts with vasodilator-stimulated phosphoprotein (VASP) and regulates VASP localization to cell-matrix adhesions and migration
    • Zhang Y, Tu Y, Gkretsi V, Wu C. Migfilin interacts with vasodilator-stimulated phosphoprotein (VASP) and regulates VASP localization to cell-matrix adhesions and migration. JBiol. Chem. 2006 281 12397 12407.
    • (2006) JBiol. Chem. , vol.281 , pp. 12397-12407
    • Zhang, Y.1    Tu, Y.2    Gkretsi, V.3    Wu, C.4
  • 29
    • 1642499129 scopus 로고    scopus 로고
    • Expression of the mitogen-inducible gene-2 (mig-2) is elevated in human uterine leiomyomas but not in leiomyosarcomas
    • Kato K, Shiozawa T, Mitsushita J et al. Expression of the mitogen-inducible gene-2 (mig-2) is elevated in human uterine leiomyomas but not in leiomyosarcomas. Hum. Pathol. 2004 35 55 60.
    • (2004) Hum. Pathol. , vol.35 , pp. 55-60
    • Kato, K.1    Shiozawa, T.2    Mitsushita, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.