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Volumn 288, Issue 5, 2013, Pages 3289-3304

Mast cells produce novel shorter forms of perlecan that contain functional endorepellin a role in angiogenesis and wound healing

Author keywords

[No Author keywords available]

Indexed keywords

ANGIOGENESIS; C-TERMINAL REGIONS; DOMAIN SPECIFIC; ENDOREPELLIN; EXTRACELLULAR; GROWTH FACTOR; HEPARAN SULFATES; HUMAN MAST CELLS; INTEGRINS; MAST CELLS; MUCOSAL TISSUES; N-TERMINAL SEQUENCING; PERLECAN; PROTEIN CORE; PROTEOGLYCANS; WOUND HEALING;

EID: 84873289627     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.387811     Document Type: Article
Times cited : (53)

References (59)
  • 1
    • 23044444804 scopus 로고    scopus 로고
    • Heparan sulfate. A complex polymer charged with biological activity
    • Whitelock, J. M., and Iozzo, R. V. (2005) Heparan sulfate. A complex polymer charged with biological activity. Chem. Rev. 105, 2745-2764
    • (2005) Chem. Rev. , vol.105 , pp. 2745-2764
    • Whitelock, J.M.1    Iozzo, R.V.2
  • 2
    • 0035656258 scopus 로고    scopus 로고
    • Electrophoretic, biosensor, and bioactivity analyses of perlecans of different cellular origins
    • Knox, S., Melrose, J., and Whitelock, J. (2001) Electrophoretic, biosensor, and bioactivity analyses of perlecans of different cellular origins. Proteomics 1, 1534-1541
    • (2001) Proteomics , vol.1 , pp. 1534-1541
    • Knox, S.1    Melrose, J.2    Whitelock, J.3
  • 5
    • 0034629170 scopus 로고    scopus 로고
    • The protein core of the proteoglycan perlecan binds specifically to fibroblast growth factor-7
    • Mongiat, M., Taylor, K., Otto, J., Aho, S., Uitto, J., Whitelock, J. M., and Iozzo, R. V. (2000) The protein core of the proteoglycan perlecan binds specifically to fibroblast growth factor-7. J. Biol. Chem. 275, 7095-7100
    • (2000) J. Biol. Chem. , vol.275 , pp. 7095-7100
    • Mongiat, M.1    Taylor, K.2    Otto, J.3    Aho, S.4    Uitto, J.5    Whitelock, J.M.6    Iozzo, R.V.7
  • 6
    • 36148980833 scopus 로고    scopus 로고
    • The core protein of growth plate perlecan binds FGF-18 and alters its mitogenic effect on chondrocytes
    • Smith, S. M., West, L. A., and Hassell, J. R. (2007) The core protein of growth plate perlecan binds FGF-18 and alters its mitogenic effect on chondrocytes. Arch. Biochem. Biophys. 468, 244-251
    • (2007) Arch. Biochem. Biophys. , vol.468 , pp. 244-251
    • Smith, S.M.1    West, L.A.2    Hassell, J.R.3
  • 8
    • 79960400832 scopus 로고    scopus 로고
    • Endorepellin, the angiostatic module of perlecan, interacts with both the α2β1 integrin and vascular endothelial growth factor receptor 2 (VEGFR2). A dual receptor antagonism
    • Goyal, A., Pal, N., Concannon, M., Paul, M., Doran, M., Poluzzi, C, Sekiguchi, K., Whitelock, J. M., Neill, T., and Iozzo, R. V. (2011) Endorepellin, the angiostatic module of perlecan, interacts with both the α2β1 integrin and vascular endothelial growth factor receptor 2 (VEGFR2). A dual receptor antagonism. J. Biol. Chem. 286, 25947-25962
    • (2011) J. Biol. Chem. , vol.286 , pp. 25947-25962
    • Goyal, A.1    Pal, N.2    Concannon, M.3    Paul, M.4    Doran, M.5    Poluzzi, C.6    Sekiguchi, K.7    Whitelock, J.M.8    Neill, T.9    Iozzo, R.V.10
  • 9
    • 2542478053 scopus 로고    scopus 로고
    • Wound healing. An overview of acute, fibrotic and delayed healing
    • Diegelmann, R. F., and Evans, M. C. (2004) Wound healing. An overview of acute, fibrotic and delayed healing. Front. Biosci. 9, 283-289
    • (2004) Front. Biosci. , vol.9 , pp. 283-289
    • Diegelmann, R.F.1    Evans, M.C.2
  • 10
    • 0021907874 scopus 로고
    • Increased dermal mast cell populations in progressive systemic sclerosis. A link in chronic fibrosis?
    • Hawkins, R. A., Claman, H. N., Clark, R. A., and Steigerwald, J. C. (1985) Increased dermal mast cell populations in progressive systemic sclerosis. A link in chronic fibrosis? Ann. Intern. Med. 102, 182-186
    • (1985) Ann. Intern. Med. , vol.102 , pp. 182-186
    • Hawkins, R.A.1    Claman, H.N.2    Clark, R.A.3    Steigerwald, J.C.4
  • 11
    • 26844514867 scopus 로고    scopus 로고
    • Degranulating mast cells in fibrotic regions of human tumors and evidence that mast cell heparin interferes with the growth of tumor cells through a mechanism involving fibroblasts
    • Samoszuk, M., Kanakubo, E., and Chan, J. K. (2005) Degranulating mast cells in fibrotic regions of human tumors and evidence that mast cell heparin interferes with the growth of tumor cells through a mechanism involving fibroblasts. BMC Cancer 5, 121
    • (2005) BMC Cancer , vol.5 , pp. 121
    • Samoszuk, M.1    Kanakubo, E.2    Chan, J.K.3
  • 12
    • 0021748808 scopus 로고
    • Mast cell heterogeneity and hyperplasia in bleomycin-induced pulmonary fibrosis of rats
    • Goto, T., Befus, D., Low, R., and Bienenstock, J. (1984) Mast cell heterogeneity and hyperplasia in bleomycin-induced pulmonary fibrosis of rats. Am. Rev. Respir. Dis. 130, 797-802
    • (1984) Am. Rev. Respir. Dis. , vol.130 , pp. 797-802
    • Goto, T.1    Befus, D.2    Low, R.3    Bienenstock, J.4
  • 13
    • 0032938967 scopus 로고    scopus 로고
    • Mast cells and their mediators in cutaneous wound healing. Active participants or innocent bystanders?
    • Artuc, M., Hermes, B., Steckelings, U. M., Grützkau, A., and Henz, B. M. (1999) Mast cells and their mediators in cutaneous wound healing. Active participants or innocent bystanders? Exp. Dermatol. 8, 1-16
    • (1999) Exp. Dermatol. , vol.8 , pp. 1-16
    • Artuc, M.1    Hermes, B.2    Steckelings, U.M.3    Grützkau, A.4    Henz, B.M.5
  • 14
    • 34147144149 scopus 로고    scopus 로고
    • Serglycin proteoglycan is required for secretory granule integrity in mucosal mast cells
    • Braga, T., Grujic, M., Lukinius, A., Hellman, L., Abrink, M., and Pejler, G. (2007) Serglycin proteoglycan is required for secretory granule integrity in mucosal mast cells. Biochem. J. 403, 49-57
    • (2007) Biochem. J. , vol.403 , pp. 49-57
    • Braga, T.1    Grujic, M.2    Lukinius, A.3    Hellman, L.4    Abrink, M.5    Pejler, G.6
  • 15
    • 77649144115 scopus 로고    scopus 로고
    • The role of mast cells in wound healing
    • Ng, M. F. (2010) The Role of Mast Cells in Wound Healing. Int Wound J. 7, 55-61
    • (2010) Int Wound J. , vol.7 , pp. 55-61
    • Ng, M.F.1
  • 16
    • 0025974625 scopus 로고
    • Murine mast cells synthesize basement membrane components. A potential role in early fibrosis
    • Thompson, H. L., Burbelo, P. D., Gabriel, G., Yamada, Y., and Metcalfe, D. D. (1991) Murine mast cells synthesize basement membrane components. A potential role in early fibrosis. J. Clin. Invest. 87, 619-623
    • (1991) J. Clin. Invest. , vol.87 , pp. 619-623
    • Thompson, H.L.1    Burbelo, P.D.2    Gabriel, G.3    Yamada, Y.4    Metcalfe, D.D.5
  • 17
    • 68449097464 scopus 로고    scopus 로고
    • RBL-2H3 cells are an imprecise model for mast cell mediator release
    • Passante, E., Ehrhardt, C, Sheridan, H., and Frankish, N. (2009) RBL-2H3 cells are an imprecise model for mast cell mediator release. Inflamm. Res. 58, 611-618
    • (2009) Inflamm. Res. , vol.58 , pp. 611-618
    • Passante, E.1    Ehrhardt, C.2    Sheridan, H.3    Frankish, N.4
  • 18
    • 79961126296 scopus 로고    scopus 로고
    • Human lung mast cells modulate the functions of airway smooth muscle cells in asthma
    • Alkhouri, H, Hollins, F., Moir, L. M., Brightling, C. E., Armour, C. L., and Hughes, J. M. (2011) Human lung mast cells modulate the functions of airway smooth muscle cells in asthma. Allergy 66, 1231-1241
    • (2011) Allergy , vol.66 , pp. 1231-1241
    • Alkhouri, H.1    Hollins, F.2    Moir, L.M.3    Brightling, C.E.4    Armour, C.L.5    Hughes, J.M.6
  • 20
    • 0020529209 scopus 로고
    • Identification of a monoclonal antibody that specifically recognized corneal and skeletal keratan sulfate. Monoclonal antibodies to cartilage proteoglycan
    • Caterson, B., Christner, J. E., and Baker, J. R. (1983) Identification of a monoclonal antibody that specifically recognized corneal and skeletal keratan sulfate. Monoclonal antibodies to cartilage proteoglycan. J. Biol. Chem. 258, 8848-8854
    • (1983) J. Biol. Chem. , vol.258 , pp. 8848-8854
    • Caterson, B.1    Christner, J.E.2    Baker, J.R.3
  • 22
    • 0032893101 scopus 로고    scopus 로고
    • Human perlecan immuno-purified from different endothelial cell sources has different adhesive properties for vascular cells
    • Whitelock, J. M., Graham, L. D., Melrose, J., Murdoch, A. D., Iozzo, R. V., and Underwood, P. A. (1999) Human perlecan immuno-purified from different endothelial cell sources has different adhesive properties for vascular cells. Matrix Biol. 18, 163-178
    • (1999) Matrix Biol. , vol.18 , pp. 163-178
    • Whitelock, J.M.1    Graham, L.D.2    Melrose, J.3    Murdoch, A.D.4    Iozzo, R.V.5    Underwood, P.A.6
  • 23
    • 0037177869 scopus 로고    scopus 로고
    • Not all perlecans are created equal. Interactions with fibroblast growth factor (FGF) 2 and FGF receptors
    • Knox, S., Merry, C., Stringer, S., Melrose, J., and Whitelock, J. (2002) Not all perlecans are created equal. Interactions with fibroblast growth factor (FGF) 2 and FGF receptors. J. Biol. Chem. 277, 14657-14665
    • (2002) J. Biol. Chem. , vol.277 , pp. 14657-14665
    • Knox, S.1    Merry, C.2    Stringer, S.3    Melrose, J.4    Whitelock, J.5
  • 24
    • 0029094503 scopus 로고
    • Packaging of proteases and proteoglycans in the granules of mast cells and other hematopoietic cells. A cluster of histidines on mouse mast cell protease 7 regulates its binding to heparin serglycin proteoglycans
    • Matsumoto, R., Sali, A., Ghildyal, N., Karplus, M., and Stevens, R. L. (1995) Packaging of proteases and proteoglycans in the granules of mast cells and other hematopoietic cells. A cluster of histidines on mouse mast cell protease 7 regulates its binding to heparin serglycin proteoglycans. J. Biol. Chem. 270, 19524-19531
    • (1995) J. Biol. Chem. , vol.270 , pp. 19524-19531
    • Matsumoto, R.1    Sali, A.2    Ghildyal, N.3    Karplus, M.4    Stevens, R.L.5
  • 25
    • 33750036078 scopus 로고    scopus 로고
    • A role for serglycin proteoglycan in granular retention and processing of mast cell secretory granule components
    • Henningsson, F., Hergeth, S., Cortelius, R., Abrink, M., and Pejler, G. (2006) A role for serglycin proteoglycan in granular retention and processing of mast cell secretory granule components. FEBS J. 273, 4901-4912
    • (2006) FEBS J. , vol.273 , pp. 4901-4912
    • Henningsson, F.1    Hergeth, S.2    Cortelius, R.3    Abrink, M.4    Pejler, G.5
  • 26
    • 73349108467 scopus 로고    scopus 로고
    • Mast cell differentiation and activation is closely linked to expression of genes coding for the serglycin proteoglycan core protein and a distinct set of chondroitin sulfate and heparin sulfotransferases
    • Duelli, A., Rönnberg, E., Waern, I., Ringvall, M., Kolset, S. O., and Pejler, G. (2009) Mast cell differentiation and activation is closely linked to expression of genes coding for the serglycin proteoglycan core protein and a distinct set of chondroitin sulfate and heparin sulfotransferases. J. Immunol. 183, 7073-7083
    • (2009) J. Immunol. , vol.183 , pp. 7073-7083
    • Duelli, A.1    Rönnberg, E.2    Waern, I.3    Ringvall, M.4    Kolset, S.O.5    Pejler, G.6
  • 27
    • 0023894336 scopus 로고
    • Isolation and characterization of a cDNA that encodes the peptide core of the secretory granule proteoglycan of human promyelocytic leukemia HL-60 cells
    • Stevens, R. L., Avraham, S., Gartner, M. C., Bruns, G. A., Austen, K. F., and Weis, J. H. (1988) Isolation and characterization of a cDNA that encodes the peptide core of the secretory granule proteoglycan of human promyelocytic leukemia HL-60 cells. J. Biol. Chem. 263, 7287-7291
    • (1988) J. Biol. Chem. , vol.263 , pp. 7287-7291
    • Stevens, R.L.1    Avraham, S.2    Gartner, M.C.3    Bruns, G.A.4    Austen, K.F.5    Weis, J.H.6
  • 28
    • 0023923997 scopus 로고
    • Identification of chondroitin sulfate E in human lung mast cells
    • Thompson, H. L., Schulman, E. S., and Metcalfe, D. D. (1988) Identification of chondroitin sulfate E in human lung mast cells. J. Immunol. 140, 2708-2713
    • (1988) J. Immunol. , vol.140 , pp. 2708-2713
    • Thompson, H.L.1    Schulman, E.S.2    Metcalfe, D.D.3
  • 30
    • 0022973971 scopus 로고
    • Secretory granules of heparin-containing rat serosal mast cells also possess highly sulfated chondroitin sulfate proteoglycans
    • Katz, H. R., Austen, K. F., Caterson, B., and Stevens, R. L. (1986) Secretory granules of heparin-containing rat serosal mast cells also possess highly sulfated chondroitin sulfate proteoglycans. J. Biol. Chem. 261, 13393-13396
    • (1986) J. Biol. Chem. , vol.261 , pp. 13393-13396
    • Katz, H.R.1    Austen, K.F.2    Caterson, B.3    Stevens, R.L.4
  • 31
    • 0022235738 scopus 로고
    • Purification and characterization of protease-resistant secretory granule proteoglycans containing chondroitin sulfate di-B and heparin-like glycosaminoglycans from rat basophilic leukemia cells
    • Seldin, D. C., Austen, K. F., and Stevens, R. L. (1985) Purification and characterization of protease-resistant secretory granule proteoglycans containing chondroitin sulfate di-B and heparin-like glycosaminoglycans from rat basophilic leukemia cells. J. Biol. Chem. 260, 11131-11139
    • (1985) J. Biol. Chem. , vol.260 , pp. 11131-11139
    • Seldin, D.C.1    Austen, K.F.2    Stevens, R.L.3
  • 32
    • 0242393804 scopus 로고
    • Coculture of interleukin 3-dependent mouse mast cells with fibroblasts results in a phenotypic change of the mast cells
    • Levi-Schaffer, F., Austen, K. F., Gravallese, P. M., and Stevens, R. L. (1986) Coculture of interleukin 3-dependent mouse mast cells with fibroblasts results in a phenotypic change of the mast cells. Proc. Natl. Acad. Sci. U. S. A. 83, 6485-6488
    • (1986) Proc. Natl. Acad. Sci. U. S. A. , vol.83 , pp. 6485-6488
    • Levi-Schaffer, F.1    Austen, K.F.2    Gravallese, P.M.3    Stevens, R.L.4
  • 33
    • 0028158005 scopus 로고
    • Widespread expression ofperlecan proteoglycanin basement membranes and extracellular matrices of human tissues as detected by a novel monoclonal antibody against domain III and by in situ hybridization
    • Murdoch, A. D., Liu, B., Schwarting, R., Tuan, R. S., and Iozzo, R. V. (1994) Widespread expression ofperlecan proteoglycanin basement membranes and extracellular matrices of human tissues as detected by a novel monoclonal antibody against domain III and by in situ hybridization. J. Histochem. Cytochem. 42, 239-249
    • (1994) J. Histochem. Cytochem. , vol.42 , pp. 239-249
    • Murdoch, A.D.1    Liu, B.2    Schwarting, R.3    Tuan, R.S.4    Iozzo, R.V.5
  • 34
    • 0028978690 scopus 로고
    • Antibody mapping and tissue localization of globular and cysteine-rich regions of perlecan domain III
    • Couchman, J. R., Ljubimov, A. V., Sthanam, M., Horchar, T., and Hassell, J. R. (1995) Antibody mapping and tissue localization of globular and cysteine-rich regions of perlecan domain III. J. Histochem. Cytochem. 43, 955-963
    • (1995) J. Histochem. Cytochem. , vol.43 , pp. 955-963
    • Couchman, J.R.1    Ljubimov, A.V.2    Sthanam, M.3    Horchar, T.4    Hassell, J.R.5
  • 35
    • 33845997777 scopus 로고    scopus 로고
    • The structure, location, and function of perlecan, a prominent pericellular proteoglycan of fetal, postnatal, and mature hyaline cartilages
    • Melrose, J., Roughley, P., Knox, S., Smith, S., Lord, M., and Whitelock, J. (2006) The structure, location, and function of perlecan, a prominent pericellular proteoglycan of fetal, postnatal, and mature hyaline cartilages. J. Biol. Chem. 281, 36905-36914
    • (2006) J. Biol. Chem. , vol.281 , pp. 36905-36914
    • Melrose, J.1    Roughley, P.2    Knox, S.3    Smith, S.4    Lord, M.5    Whitelock, J.6
  • 36
    • 33745040051 scopus 로고    scopus 로고
    • Changes in perlecan during chondrocyte differentiation in the fetal bovine rib growth plate
    • West, L., Govindraj, P., Koob, T. J., and Hassell, J. R. (2006) Changes in perlecan during chondrocyte differentiation in the fetal bovine rib growth plate. J. Orthop. Res. 24, 1317-1326
    • (2006) J. Orthop. Res. , vol.24 , pp. 1317-1326
    • West, L.1    Govindraj, P.2    Koob, T.J.3    Hassell, J.R.4
  • 37
    • 0029876376 scopus 로고    scopus 로고
    • The degradation of human endothelial cell-derived perlecan, and release of bound bFGF, by stromelysin, plasmin and heparanases
    • Whitelock, J. M., Murdoch, A. D., Iozzo, R. V., and Underwood, P. A. (1996) The degradation of human endothelial cell-derived perlecan, and release of bound bFGF, by stromelysin, plasmin and heparanases. J. Biol. Chem. 271, 10079-10086
    • (1996) J. Biol. Chem. , vol.271 , pp. 10079-10086
    • Whitelock, J.M.1    Murdoch, A.D.2    Iozzo, R.V.3    Underwood, P.A.4
  • 38
    • 14844299756 scopus 로고    scopus 로고
    • BMP-1/Tolloid-like metalloproteases process endorepellin, the angiostatic C-terminal fragment of perlecan
    • Gonzalez, E. M., Reed, C. C., Bix, G., Fu, J., Zhang, Y., Gopalakrishnan, B., Greenspan, D. S., and Iozzo, R. V. (2005) BMP-1/Tolloid-like metalloproteases process endorepellin, the angiostatic C-terminal fragment of perlecan. J. Biol. Chem. 280, 7080-7087
    • (2005) J. Biol. Chem. , vol.280 , pp. 7080-7087
    • Gonzalez, E.M.1    Reed, C.C.2    Bix, G.3    Fu, J.4    Zhang, Y.5    Gopalakrishnan, B.6    Greenspan, D.S.7    Iozzo, R.V.8
  • 40
    • 0030606329 scopus 로고    scopus 로고
    • Purification and characterization of perlecan fragment in urine of end-stage renal failure patients
    • Oda, O., Shinzato, T., Ohbayashi, K., Takai, I., Kunimatsu, M., Maeda, K., and Yamanaka, N. (1996) Purification and characterization of perlecan fragment in urine of end-stage renal failure patients. Clin. Chim. Acta 255, 119-132
    • (1996) Clin. Chim. Acta , vol.255 , pp. 119-132
    • Oda, O.1    Shinzato, T.2    Ohbayashi, K.3    Takai, I.4    Kunimatsu, M.5    Maeda, K.6    Yamanaka, N.7
  • 41
    • 84858771289 scopus 로고    scopus 로고
    • A fragment of the LG3 peptide of endorepellin is present in the urine of physically active mining workers. A potential marker of physical activity
    • Parker, T. J., Sampson, D. L., Broszczak, D., Chng, Y. L., Carter, S. L., Leavesley, D. I., Parker, A. W., and Upton, Z. (2012) A fragment of the LG3 peptide of endorepellin is present in the urine of physically active mining workers. A potential marker of physical activity. PLoS One 7, e33714
    • (2012) PLoS One , vol.7
    • Parker, T.J.1    Sampson, D.L.2    Broszczak, D.3    Chng, Y.L.4    Carter, S.L.5    Leavesley, D.I.6    Parker, A.W.7    Upton, Z.8
  • 42
    • 38949128498 scopus 로고    scopus 로고
    • Identification of circulating endorepellin LG3 fragment. Potential use as a serological biomarker for breast cancer proteomics
    • Chang, J. W., Kang, U. B., Kim, D. H., Yi, J. K., Lee, J. W., Noh, D. Y., Lee, C., and Yu, M. H. (2008) Identification of circulating endorepellin LG3 fragment. Potential use as a serological biomarker for breast cancer proteomics. Clin. Appl. 2, 23-32
    • (2008) Clin. Appl. , vol.2 , pp. 23-32
    • Chang, J.W.1    Kang, U.B.2    Kim, D.H.3    Yi, J.K.4    Lee, J.W.5    Noh, D.Y.6    Lee, C.7    Yu, M.H.8
  • 44
    • 34247330149 scopus 로고    scopus 로고
    • Endorepellin, the C-terminal angiostatic module of perlecan, enhances collagen-platelet responses via the alpha2beta1-integrin receptor
    • Bix, G., Iozzo, R. A., Woodall, B., Burrows, M., McQuillan, A., Campbell, S., Fields, G. B., and Iozzo, R. V. (2007) Endorepellin, the C-terminal angiostatic module of perlecan, enhances collagen-platelet responses via the alpha2beta1-integrin receptor. Blood 109, 3745-3748
    • (2007) Blood , vol.109 , pp. 3745-3748
    • Bix, G.1    Iozzo, R.A.2    Woodall, B.3    Burrows, M.4    McQuillan, A.5    Campbell, S.6    Fields, G.B.7    Iozzo, R.V.8
  • 46
    • 33750057983 scopus 로고    scopus 로고
    • Perlecan proteolysis induces an α2β1 integrin-and Src family kinase-dependent anti-apoptotic pathway in fibroblasts in the absence of focal adhesion kinase activation
    • Laplante, P., Raymond, M. A., Labelle, A., Abe, J., Iozzo, R. V., and Hebert, M. J. (2006) Perlecan proteolysis induces an α2β1 integrin-and Src family kinase-dependent anti-apoptotic pathway in fibroblasts in the absence of focal adhesion kinase activation. J. Biol. Chem. 281, 30383-30392
    • (2006) J. Biol. Chem. , vol.281 , pp. 30383-30392
    • Laplante, P.1    Raymond, M.A.2    Labelle, A.3    Abe, J.4    Iozzo, R.V.5    Hebert, M.J.6
  • 47
    • 77950972617 scopus 로고    scopus 로고
    • Epidermal growth factor and perlecan fragments produced by apoptotic endothelial cells co-ordinately activate ERK1/2-dependent antiapoptotic pathways in mesenchymal stem cells
    • Soulez, M., Sirois, I., Brassard, N., Raymond, M. A., Nicodeme, F., Noiseux, N., Durocher, Y., Pshezhetsky, A. V., and Hebert, M. J. (2010) Epidermal growth factor and perlecan fragments produced by apoptotic endothelial cells co-ordinately activate ERK1/2-dependent antiapoptotic pathways in mesenchymal stem cells. Stem Cells 28, 810-820
    • (2010) Stem Cells , vol.28 , pp. 810-820
    • Soulez, M.1    Sirois, I.2    Brassard, N.3    Raymond, M.A.4    Nicodeme, F.5    Noiseux, N.6    Durocher, Y.7    Pshezhetsky, A.V.8    Hebert, M.J.9
  • 49
    • 0027373292 scopus 로고
    • Structural characterization of the complete human perlecan gene and its promoter
    • Cohen, I. R., Grassel, S., Murdoch, A. D., and Iozzo, R. V. (1993) Structural characterization of the complete human perlecan gene and its promoter. Proc. Natl. Acad. Sci. U. S. A. 90, 10404-10408
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 10404-10408
    • Cohen, I.R.1    Grassel, S.2    Murdoch, A.D.3    Iozzo, R.V.4
  • 50
    • 0026758187 scopus 로고
    • Primary structure of the human heparan sulfate proteoglycan from basement membrane (HSPG2/perlecan). A chimeric molecule with multiple domains homologous to the low density lipoprotein receptor, laminin, neural cell adhesion molecules, and epidermal growth factor
    • Murdoch, A. D., Dodge, G. R., Cohen, I., Tuan, R. S., and Iozzo, R. V. (1992) Primary structure of the human heparan sulfate proteoglycan from basement membrane (HSPG2/perlecan). A chimeric molecule with multiple domains homologous to the low density lipoprotein receptor, laminin, neural cell adhesion molecules, and epidermal growth factor. J. Biol. Chem. 267, 8544-8557
    • (1992) J. Biol. Chem. , vol.267 , pp. 8544-8557
    • Murdoch, A.D.1    Dodge, G.R.2    Cohen, I.3    Tuan, R.S.4    Iozzo, R.V.5
  • 51
    • 0031054689 scopus 로고    scopus 로고
    • Structural and functional characterization of the human perlecan gene promoter. Transcriptional activation by transforming growth factor-β via a nuclear factor 1-binding element
    • Iozzo, R. V., Pillarisetti, J., Sharma, B., Murdoch, A. D., Danielson, K. G., Uitto, J., and Mauviel, A. (1997) Structural and functional characterization of the human perlecan gene promoter. Transcriptional activation by transforming growth factor-β via a nuclear factor 1-binding element. J. Biol. Chem. 272, 5219-5228
    • (1997) J. Biol. Chem. , vol.272 , pp. 5219-5228
    • Iozzo, R.V.1    Pillarisetti, J.2    Sharma, B.3    Murdoch, A.D.4    Danielson, K.G.5    Uitto, J.6    Mauviel, A.7
  • 52
    • 0029948299 scopus 로고    scopus 로고
    • A proteoglycan that activates fibroblast growth factors during early neuronal development is a perlecan variant
    • Joseph, S. J., Ford, M. D., Barth, C, Portbury, S., Bartlett, P. F., Nurcombe, V., and Greferath, U. (1996) A proteoglycan that activates fibroblast growth factors during early neuronal development is a perlecan variant. Development 122, 3443-3452
    • (1996) Development , vol.122 , pp. 3443-3452
    • Joseph, S.J.1    Ford, M.D.2    Barth, C.3    Portbury, S.4    Bartlett, P.F.5    Nurcombe, V.6    Greferath, U.7
  • 53
    • 0032849672 scopus 로고    scopus 로고
    • Complex patterns of alternative splicing mediate the spatial and temporal distribution of perlecan/UNC-52 in Caenorhabditis elegans
    • Mullen, G. P., Rogalski, T. M., Bush, J. A., Gorji, P. R., and Moerman, D. G. (1999) Complex patterns of alternative splicing mediate the spatial and temporal distribution of perlecan/UNC-52 in Caenorhabditis elegans. Mol. Biol. Cell. 10, 3205-3221
    • (1999) Mol. Biol. Cell. , vol.10 , pp. 3205-3221
    • Mullen, G.P.1    Rogalski, T.M.2    Bush, J.A.3    Gorji, P.R.4    Moerman, D.G.5
  • 54
    • 0029942984 scopus 로고    scopus 로고
    • The mec-8 gene of C. elegans encodes a protein with two RNA recognition motifs and regulates alternative splicing of unc-52 transcripts
    • Lundquist, E. A., Herman, R. K., Rogalski, T. M., Mullen, G. P., Moerman, D. G., and Shaw, J. E. (1996) The mec-8 gene of C. elegans encodes a protein with two RNA recognition motifs and regulates alternative splicing of unc-52 transcripts. Development 122, 1601-1610
    • (1996) Development , vol.122 , pp. 1601-1610
    • Lundquist, E.A.1    Herman, R.K.2    Rogalski, T.M.3    Mullen, G.P.4    Moerman, D.G.5    Shaw, J.E.6
  • 55
    • 0034947727 scopus 로고    scopus 로고
    • Analysis of smu-1, a gene that regulates the alternative splicing of unc-52 pre-mRNA in Caenorhabditis elegans
    • Spike, C. A., Shaw, J. E., and Herman, R. K. (2001) Analysis of smu-1, a gene that regulates the alternative splicing of unc-52 pre-mRNA in Caenorhabditis elegans. Mol. Cell. Biol. 21, 4985-4995
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 4985-4995
    • Spike, C.A.1    Shaw, J.E.2    Herman, R.K.3
  • 56
    • 3242740095 scopus 로고    scopus 로고
    • SMU-2 and SMU-1, Caenorhabditis elegans homologs of mammalian spliceosome-associated proteins RED and fSAP57, work together to affect splice site choice
    • Spartz, A. K., Herman, R. K., and Shaw, J. E. (2004) SMU-2 and SMU-1, Caenorhabditis elegans homologs of mammalian spliceosome-associated proteins RED and fSAP57, work together to affect splice site choice. Mol. Cell. Biol. 24, 6811-6823
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 6811-6823
    • Spartz, A.K.1    Herman, R.K.2    Shaw, J.E.3
  • 57
    • 0035100624 scopus 로고    scopus 로고
    • Co-cultured human mast cells stimulate fibroblast-mediated contraction of collagen gels
    • Sköld, C. M., Ohkuni, Y., Liu, X. D., Numerof, R., and Rennard, S. I. (2001) Co-cultured human mast cells stimulate fibroblast-mediated contraction of collagen gels. Inflammation 25, 47-51
    • (2001) Inflammation , vol.25 , pp. 47-51
    • Sköld, C.M.1    Ohkuni, Y.2    Liu, X.D.3    Numerof, R.4    Rennard, S.I.5
  • 59
    • 0037423391 scopus 로고    scopus 로고
    • Endorepellin, a novel inhibitor of angiogenesis derived from the C terminus of perlecan
    • Mongiat, M., Sweeney, S. M., San Antonio, J. D., Fu, J., and Iozzo, R. V. (2003) Endorepellin, a novel inhibitor of angiogenesis derived from the C terminus of perlecan. J. Biol. Chem. 278, 4238-4249
    • (2003) J. Biol. Chem. , vol.278 , pp. 4238-4249
    • Mongiat, M.1    Sweeney, S.M.2    San Antonio, J.D.3    Fu, J.4    Iozzo, R.V.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.