메뉴 건너뛰기




Volumn 310, Issue 10, 2016, Pages F1123-F1135

N-sulfation of heparan sulfate is critical for syndecan-4-mediated podocyte cell-matrix interactions

Author keywords

Glycosaminoglycans; Heparan sulfate; Podocyte; Proteoglycans; Syndecan

Indexed keywords

ALPHA ACTININ 4; FOCAL ADHESION KINASE; GLYCOSAMINOGLYCAN; HEPARAN SULFATE; NEPHRIN; PROTEIN KINASE C ALPHA; PROTEOGLYCAN; SULFOTRANSFERASE; SYNAPTOPODIN; SYNDECAN 4; VERY LATE ACTIVATION ANTIGEN 5; VINCULIN; ACTININ; ACTN4 PROTEIN, MOUSE; HEPARITIN SULFOTRANSFERASE; SDC4 PROTEIN, MOUSE;

EID: 84984614267     PISSN: 1931857X     EISSN: 15221466     Source Type: Journal    
DOI: 10.1152/ajprenal.00603.2015     Document Type: Article
Times cited : (11)

References (55)
  • 1
    • 84867424399 scopus 로고    scopus 로고
    • Transmembrane and extracellular domains of syndecan-1 have distinct functions in regulating lung epithelial migration andadhesion
    • Altemeier WA, Schlesinger SY, Buell CA, Brauer R, Rapraeger AC, Parks WC, Chen P. Transmembrane and extracellular domains of syndecan-1 have distinct functions in regulating lung epithelial migration and adhesion. J Biol Chem 287: 34927-34935, 2012
    • (2012) J Biol Chem , vol.287 , pp. 34927-34935
    • Altemeier, W.A.1    Schlesinger, S.Y.2    Buell, C.A.3    Brauer, R.4    Rapraeger, A.C.5    Parks, W.C.6    Chen, P.7
  • 2
    • 84867411149 scopus 로고    scopus 로고
    • Syndecan-1 controls cell migration by activating Rap1 to regulate focaladhesion disassembly
    • Altemeier WA, Schlesinger SY, Buell CA, Parks WC, Chen P. Syndecan-1 controls cell migration by activating Rap1 to regulate focal adhesion disassembly. J Cell Sci 125: 5188-5195, 2012
    • (2012) J Cell Sci , vol.125 , pp. 5188-5195
    • Altemeier, W.A.1    Schlesinger, S.Y.2    Buell, C.A.3    Parks, W.C.4    Chen, P.5
  • 3
    • 35648978998 scopus 로고    scopus 로고
    • Structure and mechanics ofintegrin-based cell adhesion
    • Arnaout MA, Goodman SL, Xiong JP. Structure and mechanics of integrin-based cell adhesion. Curr Opin Cell Biol 19: 495-507, 2007
    • (2007) Curr Opin Cell Biol , vol.19 , pp. 495-507
    • Arnaout, M.A.1    Goodman, S.L.2    Xiong, J.P.3
  • 5
    • 0020132520 scopus 로고
    • 35S-glycosaminoglycanand 35S-glycopeptide metabolism by diabetic glomeruli and aorta
    • Brown DM, Klein DJ, Michael AF, Oegema TR. 35S-glycosaminoglycan and 35S-glycopeptide metabolism by diabetic glomeruli and aorta. Diabetes 31: 418-425, 1982
    • (1982) Diabetes , vol.31 , pp. 418-425
    • Brown, D.M.1    Klein, D.J.2    Michael, A.F.3    Oegema, T.R.4
  • 6
    • 0024584913 scopus 로고
    • Molecular modeling of protein-glycosaminoglycaninteractions
    • Cardin AD, Weintraub HJ. Molecular modeling of protein-glycosaminoglycan interactions. Arteriosclerosis 9: 21-32, 1989
    • (1989) Arteriosclerosis , vol.9 , pp. 21-32
    • Cardin, A.D.1    Weintraub, H.J.2
  • 7
    • 68749110934 scopus 로고    scopus 로고
    • MMP7shedding of syndecan-1 facilitates re-epithelialization by affecting α2β1integrin activation
    • Chen P, Abacherli LE, Nadler ST, Wang Y, Li Q, Parks WC. MMP7 shedding of syndecan-1 facilitates re-epithelialization by affecting α2β1 integrin activation. PloS One 4: e6565, 2009
    • (2009) Plos One , vol.4
    • Chen, P.1    Abacherli, L.E.2    Nadler, S.T.3    Wang, Y.4    Li, Q.5    Parks, W.C.6
  • 10
    • 51249107328 scopus 로고    scopus 로고
    • Theoligomeric status of syndecan-4 regulates syndecan-4 interaction withalpha-actinin
    • Choi Y, Kim S, Lee J, Ko SG, Lee W, Han IO, Woods A, Oh ES. The oligomeric status of syndecan-4 regulates syndecan-4 interaction with alpha-actinin. Eur J Cell Biol 87: 807-815, 2008
    • (2008) Eur J Cell Biol , vol.87 , pp. 807-815
    • Choi, Y.1    Kim, S.2    Lee, J.3    Ko, S.G.4    Lee, W.5    Han, I.O.6    Woods, A.7    Oh, E.S.8
  • 11
    • 0024202717 scopus 로고
    • Undersulfation of glomerular basementmembrane heparan sulfate in experimental diabetes and lack of correctionwith aldose reductase inhibition
    • Cohen MP, Klepser H, Wu VY. Undersulfation of glomerular basement membrane heparan sulfate in experimental diabetes and lack of correction with aldose reductase inhibition. Diabetes 37: 1324-1327, 1988
    • (1988) Diabetes , vol.37 , pp. 1324-1327
    • Cohen, M.P.1    Klepser, H.2    Wu, V.Y.3
  • 12
    • 0019730380 scopus 로고
    • [35S]sulfate incorporation into glomerular basementmembrane glycosaminoglycans is decreased in experimental diabetes
    • Cohen MP, Surma ML. [35S]sulfate incorporation into glomerular basement membrane glycosaminoglycans is decreased in experimental diabetes. J Lab Clin Med 98: 715-722, 1981
    • (1981) J Lab Clin Med , vol.98 , pp. 715-722
    • Cohen, M.P.1    Surma, M.L.2
  • 15
    • 0020469810 scopus 로고
    • Comparative distribution oflaminin, type IV collagen, and fibronectin in the rat glomerulus
    • Courtoy PJ, Timpl R, Farquhar MG. Comparative distribution of laminin, type IV collagen, and fibronectin in the rat glomerulus. J Histochem Cytochem 30: 874-886, 1982
    • (1982) J Histochemcytochem , vol.30 , pp. 874-886
    • Courtoy, P.J.1    Timpl, R.2    Farquhar, M.G.3
  • 16
    • 0032722310 scopus 로고    scopus 로고
    • Syndecan-4 core protein is sufficient for the assembly of focal adhesions andactin stress fibers
    • Echtermeyer F, Baciu PC, Saoncella S, Ge Y, Goetinck PF. Syndecan-4 core protein is sufficient for the assembly of focal adhesions and actin stress fibers. J Cell Sci 112, Pt 20: 3433-3441, 1999
    • (1999) J Cell Sci , vol.112 , pp. 3433-3441
    • Echtermeyer, F.1    Baciu, P.C.2    Saoncella, S.3    Ge, Y.4    Goetinck, P.F.5
  • 17
    • 0035997376 scopus 로고    scopus 로고
    • Order out of chaos: Assembly of ligand binding sitesin heparan sulfate
    • Esko JD, Selleck SB. Order out of chaos: assembly of ligand binding sites in heparan sulfate. Annu Rev Biochem 71: 435-471, 2002
    • (2002) Annu Rev Biochem , vol.71 , pp. 435-471
    • Esko, J.D.1    Selleck, S.B.2
  • 19
    • 0037470045 scopus 로고    scopus 로고
    • Syndecan-4 associates withalpha-actinin
    • Greene DK, Tumova S, Couchman JR. Syndecan-4 associates with alpha-actinin. J Biol Chem 278: 7617-7623, 2003
    • (2003) J Biol Chem , vol.278 , pp. 7617-7623
    • Greene, D.K.1    Tumova, S.2    Couchman, J.R.3
  • 20
    • 77956260099 scopus 로고    scopus 로고
    • Heparansulfate domain organization and sulfation modulate FGF-induced cellsignaling
    • Jastrebova N, Vanwildemeersch M, Lindahl U, Spillmann D. Heparan sulfate domain organization and sulfation modulate FGF-induced cell signaling. J Biol Chem 285: 26842-26851, 2010
    • (2010) J Biol Chem , vol.285 , pp. 26842-26851
    • Jastrebova, N.1    Vanwildemeersch, M.2    Lindahl, U.3    Spillmann, D.4
  • 22
    • 12344264662 scopus 로고    scopus 로고
    • Localization of transgenes and genotyping ofH-2kb-tsA58 transgenic mice
    • Kern G, Flucher BE. Localization of transgenes and genotyping of H-2kb-tsA58 transgenic mice. Biotechniques 38: 38, 40, 42, 2005
    • (2005) Biotechniques 38 , vol.38 , Issue.40
    • Kern, G.1    Flucher, B.E.2
  • 23
    • 1642545636 scopus 로고    scopus 로고
    • Syndecan-4regulates localization, activity and stability of protein kinase C-alpha
    • Keum E, Kim Y, Kim J, Kwon S, Lim Y, Han I, Oh ES. Syndecan-4 regulates localization, activity and stability of protein kinase C-alpha. Biochem J 378: 1007-1014, 2004
    • (2004) Biochem J , vol.378 , pp. 1007-1014
    • Keum, E.1    Kim, Y.2    Kim, J.3    Kwon, S.4    Lim, Y.5    Han, I.6    Oh, E.S.7
  • 24
    • 0026522633 scopus 로고
    • Inhibition of glomerular glucosaminyl N-deacetylasein diabetic rats
    • Kofoed-Enevoldsen A. Inhibition of glomerular glucosaminyl N-deacetylase in diabetic rats. Kidney Int 41: 763-767, 1992
    • (1992) Kidney Int , vol.41 , pp. 763-767
    • Kofoed-Enevoldsen, A.1
  • 25
    • 0027468332 scopus 로고
    • Diabetes mellitus inducedinhibition of glucosaminyl N-deacetylase: Effect of short-term blood glucosecontrol in diabetic rats
    • Kofoed-Enevoldsen A, Noonan D, Deckert T. Diabetes mellitus induced inhibition of glucosaminyl N-deacetylase: effect of short-term blood glucose control in diabetic rats. Diabetologia 36: 310-315, 1993
    • (1993) Diabetologia , vol.36 , pp. 310-315
    • Kofoed-Enevoldsen, A.1    Noonan, D.2    Deckert, T.3
  • 26
    • 0027233469 scopus 로고
    • GlucosaminylN-deacetylase in cultured fibroblasts; comparison of patients with andwithout diabetic nephropathy, and identification of a possible mechanismfor diabetes-induced N-deacetylase inhibition
    • Kofoed-Enevoldsen A, Petersen JS, Deckert T. Glucosaminyl N-deacetylase in cultured fibroblasts; comparison of patients with and without diabetic nephropathy, and identification of a possible mechanism for diabetes-induced N-deacetylase inhibition. Diabetologia 36: 536-540, 1993
    • (1993) Diabetologia , vol.36 , pp. 536-540
    • Kofoed-Enevoldsen, A.1    Petersen, J.S.2    Deckert, T.3
  • 27
    • 33746614761 scopus 로고    scopus 로고
    • Interactions between heparansulfate and proteins: The concept of specificity
    • Kreuger J, Spillmann D, Li J, Lindahl U. Interactions between heparan sulfate and proteins: the concept of specificity. J Cell Biol 174: 323-327, 2006
    • (2006) J Cell Biol , vol.174 , pp. 323-327
    • Kreuger, J.1    Spillmann, D.2    Li, J.3    Lindahl, U.4
  • 30
    • 54949157675 scopus 로고    scopus 로고
    • Defining human diabeticnephropathy on the molecular level: Integration of transcriptomic profileswith biological knowledge
    • Martini S, Eichinger F, Nair V, Kretzler M. Defining human diabetic nephropathy on the molecular level: integration of transcriptomic profiles with biological knowledge. Rev Endocr Metab Disord 9: 267-274, 2008
    • (2008) Rev Endocr Metab Disord , vol.9 , pp. 267-274
    • Martini, S.1    Eichinger, F.2    Nair, V.3    Kretzler, M.4
  • 31
    • 84856017650 scopus 로고    scopus 로고
    • The glomerular basementmembrane as a model system to study the bioactivity of heparan sulfateglycosaminoglycans
    • McCarthy KJ, Wassenhove-McCarthy DJ. The glomerular basement membrane as a model system to study the bioactivity of heparan sulfate glycosaminoglycans. Microsc Microanal 18: 3-21, 2012
    • (2012) Microsc Microanal , vol.18 , pp. 3-21
    • McCarthy, K.J.1    Wassenhove-McCarthy, D.J.2
  • 33
    • 0018691968 scopus 로고
    • Localization of fibronectin withinthe renal glomerulus and its production by cultured glomerular cells
    • Oberley TD, Mosher DF, Mills MD. Localization of fibronectin within the renal glomerulus and its production by cultured glomerular cells. Am J Pathol 96: 651-662, 1979
    • (1979) Amj Pathol , vol.96 , pp. 651-662
    • Oberley, T.D.1    Mosher, D.F.2    Mills, M.D.3
  • 34
    • 0030911243 scopus 로고    scopus 로고
    • Multimerization of the cytoplasmicdomain of syndecan-4 is required for its ability to activate protein kinaseC
    • Oh ES, Woods A, Couchman JR. Multimerization of the cytoplasmic domain of syndecan-4 is required for its ability to activate protein kinase C. J Biol Chem 272: 11805-11811, 1997
    • (1997) J Biol Chem , vol.272 , pp. 11805-11811
    • Oh, E.S.1    Woods, A.2    Couchman, J.R.3
  • 35
  • 36
    • 0015894129 scopus 로고
    • The alkaline cleavage and borohydridereduction of cartilage proteoglycan
    • Robinson HC, Hopwood JJ. The alkaline cleavage and borohydride reduction of cartilage proteoglycan. Biochem J 133: 457-470, 1973
    • (1973) Biochem J , vol.133 , pp. 457-470
    • Robinson, H.C.1    Hopwood, J.J.2
  • 37
    • 84875702158 scopus 로고    scopus 로고
    • Cell-matrix adhesion of podocytes in physiologyand disease
    • Sachs N, Sonnenberg A. Cell-matrix adhesion of podocytes in physiology and disease. Nat Rev Nephrol 9: 200-210, 2013
    • (2013) Nat Rev Nephrol , vol.9 , pp. 200-210
    • Sachs, N.1    Sonnenberg, A.2
  • 40
  • 41
    • 0017189425 scopus 로고
    • Formation of anhydrosugars in the chemicaldepolymerization of heparin
    • Shively JE, Conrad HE. Formation of anhydrosugars in the chemical depolymerization of heparin. Biochemistry 15: 3932-3942, 1976
    • (1976) Biochemistry , vol.15 , pp. 3932-3942
    • Shively, J.E.1    Conrad, H.E.2
  • 42
    • 84895908406 scopus 로고    scopus 로고
    • Podocyte-specific deletion of NDST1, a keyenzyme in the sulfation of heparan sulfate glycosaminoglycans, leads toabnormalities in podocyte organization in vivo
    • Sugar T, Wassenhove-McCarthy DJ, Esko JD, van Kuppevelt TH, Holzman L, McCarthy KJ. Podocyte-specific deletion of NDST1, a key enzyme in the sulfation of heparan sulfate glycosaminoglycans, leads to abnormalities in podocyte organization in vivo. Kidney Int 85: 307-318, 2014
    • (2014) Kidney Int , vol.85 , pp. 307-318
    • Sugar, T.1    Wassenhove-McCarthy, D.J.2    Esko, J.D.3    Van Kuppevelt, T.H.4    Holzman, L.5    McCarthy, K.J.6
  • 43
    • 0036733653 scopus 로고    scopus 로고
    • A new method for large scaleisolation of kidney glomeruli from mice
    • Takemoto M, Asker N, Gerhardt H. A new method for large scale isolation of kidney glomeruli from mice. Am J Pathol 161: 799-805, 2002
    • (2002) Am J Pathol , vol.161 , pp. 799-805
    • Takemoto, M.1    Asker, N.2    Gerhardt, H.3
  • 44
    • 33646167686 scopus 로고    scopus 로고
    • 3-O-sulfated oligosaccharidestructures are recognized by anti-heparan sulfate antibody HS4C3
    • Ten Dam GB, Kurup S, van de Westerlo EM. 3-O-sulfated oligosaccharide structures are recognized by anti-heparan sulfate antibody HS4C3. J Biol Chem 281: 4654-4662, 2006
    • (2006) J Biol Chem , vol.281 , pp. 4654-4662
    • Ten Dam, G.B.1    Kurup, S.2    Van De Westerlo, E.M.3
  • 46
    • 0037205432 scopus 로고    scopus 로고
    • Clustering induces redistribution of syndecan-4 core protein into raft membrane domains
    • Tkachenko E, Simons M. Clustering induces redistribution of syndecan-4 core protein into raft membrane domains. J Biol Chem 277: 19946-19951, 2002
    • (2002) J Biol Chem , vol.277 , pp. 19946-19951
    • Tkachenko, E.1    Simons, M.2
  • 48
    • 35348904935 scopus 로고    scopus 로고
    • The structure and function ofthe endothelial glycocalyx layer
    • Weinbaum S, Tarbell JM, Damiano ER. The structure and function of the endothelial glycocalyx layer. Annu Rev Biomed Eng 9: 121-167, 2007
    • (2007) Annu Rev Biomed Eng , vol.9 , pp. 121-167
    • Weinbaum, S.1    Tarbell, J.M.2    Damiano, E.R.3
  • 49
    • 0037031817 scopus 로고    scopus 로고
    • Syndecan-4 modulates focaladhesion kinase phosphorylation
    • Wilcox-Adelman S, Denhez F, Goetinck P. Syndecan-4 modulates focal adhesion kinase phosphorylation. J Biol Chem 277: 32970-32977, 2002
    • (2002) J Biol Chem , vol.277 , pp. 32970-32977
    • Wilcox-Adelman, S.1    Denhez, F.2    Goetinck, P.3
  • 50
    • 0035052095 scopus 로고    scopus 로고
    • Syndecans: Transmembrane modulators of adhesion and matrixassembly
    • Woods A. Syndecans: transmembrane modulators of adhesion and matrix assembly. J Clin Invest 107: 935-941, 2001
    • (2001) J Clin Invest , vol.107 , pp. 935-941
    • Woods, A.1
  • 51
    • 0028213641 scopus 로고
    • Syndecan 4 heparan sulfate proteoglycan is aselectively enriched and widespread focal adhesion component
    • Woods A, Couchman JR. Syndecan 4 heparan sulfate proteoglycan is a selectively enriched and widespread focal adhesion component. Mol Biol Cell 5: 183-192, 1994
    • (1994) Mol Biolcell , vol.5 , pp. 183-192
    • Woods, A.1    Couchman, J.R.2
  • 52
    • 0027315260 scopus 로고
    • A syntheticpeptide from the COOH-terminal heparin-binding domain of fibronectinpromotes focal adhesion formation
    • Woods A, McCarthy JB, Furcht LT, Couchman JR. A synthetic peptide from the COOH-terminal heparin-binding domain of fibronectin promotes focal adhesion formation. Mol Biol Cell 4: 605-613, 1993
    • (1993) Mol Biol Cell , vol.4 , pp. 605-613
    • Woods, A.1    McCarthy, J.B.2    Furcht, L.T.3    Couchman, J.R.4
  • 53
    • 0033562989 scopus 로고    scopus 로고
    • Syndecan-4 is expressed by B lineage lymphocytes and can transmita signal for formation of dendritic processes
    • Yamashita Y, Oritani K, Miyoshi EK, Wall R, Bernfield M, Kincade PW. Syndecan-4 is expressed by B lineage lymphocytes and can transmit a signal for formation of dendritic processes. J Immunol 162: 5940-5948, 1999
    • (1999) J Immunol , vol.162 , pp. 5940-5948
    • Yamashita, Y.1    Oritani, K.2    Miyoshi, E.K.3    Wall, R.4    Bernfield, M.5    Kincade, P.W.6
  • 54
    • 0037630415 scopus 로고    scopus 로고
    • Heparan sulfateregulates targeting of syndecan-1 to a functional domain on the cellsurface
    • Yang Y, Borset M, Langford JK, Sanderson RD. Heparan sulfate regulates targeting of syndecan-1 to a functional domain on the cell surface. J Biol Chem 278: 12888-12893, 2003
    • (2003) J Biol Chem , vol.278 , pp. 12888-12893
    • Yang, Y.1    Borset, M.2    Langford, J.K.3    Sanderson, R.D.4
  • 55
    • 0036196378 scopus 로고    scopus 로고
    • Influence of highglucose concentrations on the expression of glycosaminoglycans andN-deacetylase/N-sulphotransferase mRNA in cultured skin fibroblastsfrom diabetic patients with or without nephropathy
    • Yard B, Feng Y, Keller H, Mall C, van Der Woude F. Influence of high glucose concentrations on the expression of glycosaminoglycans and N-deacetylase/N-sulphotransferase mRNA in cultured skin fibroblasts from diabetic patients with or without nephropathy. Nephrol Dial Transplant 17: 386-391, 2002
    • (2002) Nephrol Dial Transplant , vol.17 , pp. 386-391
    • Yard, B.1    Feng, Y.2    Keller, H.3    Mall, C.4    Van Der Woude, F.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.