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Volumn 434, Issue 1, 2013, Pages 124-130

Extracellular heat shock protein A9 is a novel interaction partner of podoplanin in oral squamous cell carcinoma cells

Author keywords

Heat shock protein A9 (HSPA9); Oral squamous cell carcinoma; Podoplanin; Podoplanin binding protein; Proteomics

Indexed keywords

HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN A9; PODOPLANIN; SMALL INTERFERING RNA; UNCLASSIFIED DRUG;

EID: 84876785521     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2013.03.057     Document Type: Article
Times cited : (25)

References (37)
  • 1
    • 0030796363 scopus 로고    scopus 로고
    • Podoplanin, novel 43-kd membrane protein of glomerular epithelial cells, is down-regulated in puromycin nephrosis
    • Breiteneder-Geleff S., Matsui K., Soleiman A., et al. Podoplanin, novel 43-kd membrane protein of glomerular epithelial cells, is down-regulated in puromycin nephrosis. Am. J. Pathol. 1997, 151:1141-1152.
    • (1997) Am. J. Pathol. , vol.151 , pp. 1141-1152
    • Breiteneder-Geleff, S.1    Matsui, K.2    Soleiman, A.3
  • 2
    • 33846605148 scopus 로고    scopus 로고
    • Lymphatic involvement in the histopathogenesis of mucous retention cyst
    • Kundu S., Cheng J., Maruyama S., et al. Lymphatic involvement in the histopathogenesis of mucous retention cyst. Pathol. Res. Pract. 2007, 203:89-97.
    • (2007) Pathol. Res. Pract. , vol.203 , pp. 89-97
    • Kundu, S.1    Cheng, J.2    Maruyama, S.3
  • 3
    • 79952989866 scopus 로고    scopus 로고
    • Expression of podoplanin in thymoma: its correlation with tumor invasion, nodal metastasis, and poor clinical outcome
    • Tateyama H., Sugiura H., Yamatani C., et al. Expression of podoplanin in thymoma: its correlation with tumor invasion, nodal metastasis, and poor clinical outcome. Hum. Pathol. 2011, 42:533-540.
    • (2011) Hum. Pathol. , vol.42 , pp. 533-540
    • Tateyama, H.1    Sugiura, H.2    Yamatani, C.3
  • 4
    • 33646880599 scopus 로고    scopus 로고
    • Podoplanin expression in primary central nervous system germ cell tumors: a useful histological marker for the diagnosis of germinoma
    • Mishima K., Kato Y., Kaneko M.K., et al. Podoplanin expression in primary central nervous system germ cell tumors: a useful histological marker for the diagnosis of germinoma. Acta Neuropathol. 2006, 111:563-568.
    • (2006) Acta Neuropathol. , vol.111 , pp. 563-568
    • Mishima, K.1    Kato, Y.2    Kaneko, M.K.3
  • 5
    • 24644506212 scopus 로고    scopus 로고
    • Enhanced expression of Aggrus (T1alpha/podoplanin), a platelet-aggregation-inducing factor in lung squamous cell carcinoma
    • Kato Y., Kaneko M., Sata M., et al. Enhanced expression of Aggrus (T1alpha/podoplanin), a platelet-aggregation-inducing factor in lung squamous cell carcinoma. Tumour. Biol. 2005, 26:195-200.
    • (2005) Tumour. Biol. , vol.26 , pp. 195-200
    • Kato, Y.1    Kaneko, M.2    Sata, M.3
  • 6
    • 79958063205 scopus 로고    scopus 로고
    • Enhanced expression of podoplanin in oral carcinomas in situ and squamous cell carcinomas
    • Funayama A., Cheng J., Maruyama S., et al. Enhanced expression of podoplanin in oral carcinomas in situ and squamous cell carcinomas. Pathobiology 2011, 78:171-180.
    • (2011) Pathobiology , vol.78 , pp. 171-180
    • Funayama, A.1    Cheng, J.2    Maruyama, S.3
  • 7
    • 84876811900 scopus 로고    scopus 로고
    • Cell adhesive function of podoplanin in oral squamous cell carcinoma
    • Tsuneki M., Yamazaki M., Maruyama S., et al. Cell adhesive function of podoplanin in oral squamous cell carcinoma. J. Oral. Biosci. 2011, 53:S125.
    • (2011) J. Oral. Biosci. , vol.53
    • Tsuneki, M.1    Yamazaki, M.2    Maruyama, S.3
  • 8
    • 84876082050 scopus 로고    scopus 로고
    • Podoplanin is a novel myoepithelial cell marker in pleomorphic adenoma and other salivary gland tumors with myoepithelial differentiation
    • Tsuneki M., Maruyama S., Yamazaki M., et al. Podoplanin is a novel myoepithelial cell marker in pleomorphic adenoma and other salivary gland tumors with myoepithelial differentiation. Virchows Arch 2013, 462:297-305.
    • (2013) Virchows Arch , vol.462 , pp. 297-305
    • Tsuneki, M.1    Maruyama, S.2    Yamazaki, M.3
  • 9
    • 84863406957 scopus 로고    scopus 로고
    • Podoplanin expression profiles characteristic of odontogenic tumor-specific tissue architectures
    • Tsuneki M., Maruyama S., Yamazaki M., et al. Podoplanin expression profiles characteristic of odontogenic tumor-specific tissue architectures. Pathol. Res. Pract. 2012, 208:140-146.
    • (2012) Pathol. Res. Pract. , vol.208 , pp. 140-146
    • Tsuneki, M.1    Maruyama, S.2    Yamazaki, M.3
  • 10
    • 33846257761 scopus 로고    scopus 로고
    • Functional glycosylation of human podoplanin: glycan structure of platelet aggregation-inducing factor
    • Kaneko M.K., Kato Y., Kameyama A., et al. Functional glycosylation of human podoplanin: glycan structure of platelet aggregation-inducing factor. FEBS. Lett. 2007, 581:331-336.
    • (2007) FEBS. Lett. , vol.581 , pp. 331-336
    • Kaneko, M.K.1    Kato, Y.2    Kameyama, A.3
  • 11
    • 34548843614 scopus 로고    scopus 로고
    • Involvement of the snake toxin receptor CLEC-2, in podoplanin-mediated platelet activation, by cancer cells
    • Suzuki-Inoue K., Kato Y., Inoue O., et al. Involvement of the snake toxin receptor CLEC-2, in podoplanin-mediated platelet activation, by cancer cells. J. Biol. Chem. 2007, 282:25993-26001.
    • (2007) J. Biol. Chem. , vol.282 , pp. 25993-26001
    • Suzuki-Inoue, K.1    Kato, Y.2    Inoue, O.3
  • 12
    • 67349234088 scopus 로고    scopus 로고
    • Galectin-8 interacts with podoplanin and modulates lymphatic endothelial cell functions
    • Cueni L.N., Detmar M. Galectin-8 interacts with podoplanin and modulates lymphatic endothelial cell functions. Exp. Cell. Res. 2009, 315:1715-1723.
    • (2009) Exp. Cell. Res. , vol.315 , pp. 1715-1723
    • Cueni, L.N.1    Detmar, M.2
  • 13
    • 78650452381 scopus 로고    scopus 로고
    • Podoplanin associates with CD44 to promote directional cell migration
    • Martin-Villar E., Fernandez-Munoz B., Parsons M., et al. Podoplanin associates with CD44 to promote directional cell migration. Mol. Biol. Cell. 2010, 21:4387-4399.
    • (2010) Mol. Biol. Cell. , vol.21 , pp. 4387-4399
    • Martin-Villar, E.1    Fernandez-Munoz, B.2    Parsons, M.3
  • 14
    • 0036666032 scopus 로고    scopus 로고
    • An Hsp70 family chaperone, mortalin/mthsp70/PBP74/Grp75: what, when, and where?
    • Wadhwa R., Taira K., Kaul S.C. An Hsp70 family chaperone, mortalin/mthsp70/PBP74/Grp75: what, when, and where?. Cell Stress Chaperones 2002, 7:309-316.
    • (2002) Cell Stress Chaperones , vol.7 , pp. 309-316
    • Wadhwa, R.1    Taira, K.2    Kaul, S.C.3
  • 15
    • 84867855446 scopus 로고    scopus 로고
    • Parenchymal-stromal switching for extracellular matrix production on invasion of oral squamous cell carcinoma
    • Metwaly H., Maruyama S., Yamazaki M., et al. Parenchymal-stromal switching for extracellular matrix production on invasion of oral squamous cell carcinoma. Hum. Pathol. 2012, 43:1973-1981.
    • (2012) Hum. Pathol. , vol.43 , pp. 1973-1981
    • Metwaly, H.1    Maruyama, S.2    Yamazaki, M.3
  • 16
    • 79957668546 scopus 로고    scopus 로고
    • Usage of electrostatic eliminator reduces human keratin contamination significantly in gel-based proteomics analysis
    • Xu B., Zhang Y., Zhao Z., et al. Usage of electrostatic eliminator reduces human keratin contamination significantly in gel-based proteomics analysis. J. Proteomics 2011, 74:1022-1029.
    • (2011) J. Proteomics , vol.74 , pp. 1022-1029
    • Xu, B.1    Zhang, Y.2    Zhao, Z.3
  • 18
    • 78650228956 scopus 로고    scopus 로고
    • Combined immunohistochemistry for the differential diagnosis of cystic jaw lesions: its practical use in surgical pathology
    • Tsuneki M., Yamazaki M., Cheng J., et al. Combined immunohistochemistry for the differential diagnosis of cystic jaw lesions: its practical use in surgical pathology. Histopathology 2010, 57:806-813.
    • (2010) Histopathology , vol.57 , pp. 806-813
    • Tsuneki, M.1    Yamazaki, M.2    Cheng, J.3
  • 19
    • 33751539322 scopus 로고    scopus 로고
    • Podoplanin binds ERM proteins to activate RhoA and promote epithelial-mesenchymal transition
    • Martin-Villar E., Megias D., Castel S., et al. Podoplanin binds ERM proteins to activate RhoA and promote epithelial-mesenchymal transition. J. Cell Sci. 2006, 119:4541-4553.
    • (2006) J. Cell Sci. , vol.119 , pp. 4541-4553
    • Martin-Villar, E.1    Megias, D.2    Castel, S.3
  • 20
    • 80052462264 scopus 로고    scopus 로고
    • Podoplanin is regulated by AP-1 and promotes platelet aggregation and cell migration in osteosarcoma
    • Kunita A., Kashima T.G., Ohazama A., et al. Podoplanin is regulated by AP-1 and promotes platelet aggregation and cell migration in osteosarcoma. Am. J. Pathol. 2011, 179:1041-1049.
    • (2011) Am. J. Pathol. , vol.179 , pp. 1041-1049
    • Kunita, A.1    Kashima, T.G.2    Ohazama, A.3
  • 21
    • 14644406264 scopus 로고    scopus 로고
    • Up-regulation of the lymphatic marker podoplanin, a mucin-type transmembrane glycoprotein, in human squamous cell carcinomas and germ cell tumors
    • Schacht V., Dadras S.S., Johnson L.A., et al. Up-regulation of the lymphatic marker podoplanin, a mucin-type transmembrane glycoprotein, in human squamous cell carcinomas and germ cell tumors. Am. J. Pathol. 2005, 166:913-921.
    • (2005) Am. J. Pathol. , vol.166 , pp. 913-921
    • Schacht, V.1    Dadras, S.S.2    Johnson, L.A.3
  • 22
    • 33746284520 scopus 로고    scopus 로고
    • Overexpression of podoplanin in oral cancer and its association with poor clinical outcome
    • Yuan P., Temam S., El-Naggar A., et al. Overexpression of podoplanin in oral cancer and its association with poor clinical outcome. Cancer 2006, 107:563-569.
    • (2006) Cancer , vol.107 , pp. 563-569
    • Yuan, P.1    Temam, S.2    El-Naggar, A.3
  • 23
    • 38649137242 scopus 로고    scopus 로고
    • Podoplanin: a novel marker for oral cancer risk in patients with oral premalignancy
    • Kawaguchi H., El-Naggar A.K., Papadimitrakopoulou V., et al. Podoplanin: a novel marker for oral cancer risk in patients with oral premalignancy. J. Clin. Oncol. 2008, 26:354-360.
    • (2008) J. Clin. Oncol. , vol.26 , pp. 354-360
    • Kawaguchi, H.1    El-Naggar, A.K.2    Papadimitrakopoulou, V.3
  • 24
    • 77952502329 scopus 로고    scopus 로고
    • Impact of podoplanin expression in oral squamous cell carcinoma: clinical and histopathologic correlations
    • Kreppel M., Scheer M., Drebber U., et al. Impact of podoplanin expression in oral squamous cell carcinoma: clinical and histopathologic correlations. Virchows Arch. 2010, 456:473-482.
    • (2010) Virchows Arch. , vol.456 , pp. 473-482
    • Kreppel, M.1    Scheer, M.2    Drebber, U.3
  • 25
    • 0842348931 scopus 로고    scopus 로고
    • Intraepithelial expression of perlecan, a basement membrane-type heparan sulfate proteoglycan reflects dysplastic changes of the oral mucosal epithelium
    • Ikarashi T., Ida-Yonemochi H., Ohshiro K., et al. Intraepithelial expression of perlecan, a basement membrane-type heparan sulfate proteoglycan reflects dysplastic changes of the oral mucosal epithelium. J. Oral Pathol. Med. 2004, 33:87-95.
    • (2004) J. Oral Pathol. Med. , vol.33 , pp. 87-95
    • Ikarashi, T.1    Ida-Yonemochi, H.2    Ohshiro, K.3
  • 26
    • 0027414085 scopus 로고
    • Identification of a novel member of mouse hsp70 family. Its association with cellular mortal phenotype
    • Wadhwa R., Kaul S.C., Ikawa Y., et al. Identification of a novel member of mouse hsp70 family. Its association with cellular mortal phenotype. J. Biol. Chem. 1993, 268:6615-6621.
    • (1993) J. Biol. Chem. , vol.268 , pp. 6615-6621
    • Wadhwa, R.1    Kaul, S.C.2    Ikawa, Y.3
  • 27
    • 0027263325 scopus 로고
    • Cloning of the gene encoding peptide-binding protein 74 shows that it is a new member of the heat shock protein 70 family
    • Domanico S.Z., Denagel D.C., Dahlseid J.N., et al. Cloning of the gene encoding peptide-binding protein 74 shows that it is a new member of the heat shock protein 70 family. Mol. Cell Biol. 1993, 13:3598-3610.
    • (1993) Mol. Cell Biol. , vol.13 , pp. 3598-3610
    • Domanico, S.Z.1    Denagel, D.C.2    Dahlseid, J.N.3
  • 28
    • 0028926541 scopus 로고
    • Cloning and subcellular localization of human mitochondrial hsp70
    • Bhattacharyya T., Karnezis A.N., Murphy S.P., et al. Cloning and subcellular localization of human mitochondrial hsp70. J. Biol. Chem. 1995, 270:1705-1710.
    • (1995) J. Biol. Chem. , vol.270 , pp. 1705-1710
    • Bhattacharyya, T.1    Karnezis, A.N.2    Murphy, S.P.3
  • 29
    • 0024380865 scopus 로고
    • Identification, characterization, and purification of two mammalian stress proteins present in mitochondria, grp 75, a member of the hsp 70 family and hsp 58, a homolog of the bacterial groEL protein
    • Mizzen L.A., Chang C., Garrels J.I., et al. Identification, characterization, and purification of two mammalian stress proteins present in mitochondria, grp 75, a member of the hsp 70 family and hsp 58, a homolog of the bacterial groEL protein. J. Biol. Chem. 1989, 264:20664-20675.
    • (1989) J. Biol. Chem. , vol.264 , pp. 20664-20675
    • Mizzen, L.A.1    Chang, C.2    Garrels, J.I.3
  • 30
    • 33646409045 scopus 로고    scopus 로고
    • Upregulation of mortalin/mthsp70/Grp75 contributes to human carcinogenesis
    • Wadhwa R., Takano S., Kaur K., et al. Upregulation of mortalin/mthsp70/Grp75 contributes to human carcinogenesis. Int. J. Cancer 2006, 118:2973-2980.
    • (2006) Int. J. Cancer , vol.118 , pp. 2973-2980
    • Wadhwa, R.1    Takano, S.2    Kaur, K.3
  • 31
    • 0031586587 scopus 로고    scopus 로고
    • Elevated levels of mortalin expression in human brain tumors
    • Takano S., Wadhwa R., Yoshii Y., et al. Elevated levels of mortalin expression in human brain tumors. Exp. Cell Res. 1997, 237:38-45.
    • (1997) Exp. Cell Res. , vol.237 , pp. 38-45
    • Takano, S.1    Wadhwa, R.2    Yoshii, Y.3
  • 32
    • 11144349225 scopus 로고    scopus 로고
    • Mortalin is over-expressed by colorectal adenocarcinomas and correlates with poor survival
    • Dundas S.R., Lawrie L.C., Rooney P.H., et al. Mortalin is over-expressed by colorectal adenocarcinomas and correlates with poor survival. J. Pathol. 2005, 205:74-81.
    • (2005) J. Pathol. , vol.205 , pp. 74-81
    • Dundas, S.R.1    Lawrie, L.C.2    Rooney, P.H.3
  • 33
    • 39749200037 scopus 로고    scopus 로고
    • Association of mortalin (HSPA9) with liver cancer metastasis and prediction for early tumor recurrence
    • Yi X., Luk J.M., Lee N.P., et al. Association of mortalin (HSPA9) with liver cancer metastasis and prediction for early tumor recurrence. Mol. Cell Proteomics 2008, 7:315-325.
    • (2008) Mol. Cell Proteomics , vol.7 , pp. 315-325
    • Yi, X.1    Luk, J.M.2    Lee, N.P.3
  • 34
    • 0031473848 scopus 로고    scopus 로고
    • Protein expression profiles in human breast ductal carcinoma and histologically normal tissue
    • Bini L., Magi B., Marzocchi B., et al. Protein expression profiles in human breast ductal carcinoma and histologically normal tissue. Electrophoresis 1997, 18:2832-2841.
    • (1997) Electrophoresis , vol.18 , pp. 2832-2841
    • Bini, L.1    Magi, B.2    Marzocchi, B.3
  • 35
    • 34848889680 scopus 로고    scopus 로고
    • Mechanisms for Hsp70 secretion: crossing membranes without a leader
    • Mambula S.S., Stevenson M.A., Ogawa K., et al. Mechanisms for Hsp70 secretion: crossing membranes without a leader. Methods 2007, 43:168-175.
    • (2007) Methods , vol.43 , pp. 168-175
    • Mambula, S.S.1    Stevenson, M.A.2    Ogawa, K.3
  • 36
    • 33750570923 scopus 로고    scopus 로고
    • Heat shock protein 70 is secreted from tumor cells by a nonclassical pathway involving lysosomal endosomes
    • Mambula S.S., Calderwood S.K. Heat shock protein 70 is secreted from tumor cells by a nonclassical pathway involving lysosomal endosomes. J. Immunol. 2006, 177:7849-7857.
    • (2006) J. Immunol. , vol.177 , pp. 7849-7857
    • Mambula, S.S.1    Calderwood, S.K.2
  • 37
    • 34848859541 scopus 로고    scopus 로고
    • Heat shock protein 70 (Hsp70): membrane location, export and immunological relevance
    • Multhoff G. Heat shock protein 70 (Hsp70): membrane location, export and immunological relevance. Methods 2007, 43:229-237.
    • (2007) Methods , vol.43 , pp. 229-237
    • Multhoff, G.1


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