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Volumn 15, Issue 5, 1996, Pages 349-357

Structural and cell-adhesive properties of three recombinant fragments derived from perlecan domain III

Author keywords

Basement membranes; Cell adhesion; Protein modules; Proteoglycan; Recombinant production

Indexed keywords

INTEGRIN; LAMININ; PERLECAN; PROTEOGLYCAN; RECOMBINANT PROTEIN;

EID: 0030298061     PISSN: 0945053X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0945-053X(96)90138-9     Document Type: Article
Times cited : (31)

References (29)
  • 1
    • 0024559992 scopus 로고
    • Cell attachment properties of collagen type VI and Arg-Gly-Asp dependent binding to its α2(VI) and α3(VI) chains
    • Aumailley M., Mann K., von der Mark H., Timpl R. Cell attachment properties of collagen type VI and Arg-Gly-Asp dependent binding to its α2(VI) and α3(VI) chains. Exp. Cell Res. 181:1989;463-474.
    • (1989) Exp. Cell Res. , vol.181 , pp. 463-474
    • Aumailley, M.1    Mann, K.2    Von Der Mark, H.3    Timpl, R.4
  • 4
    • 0026703151 scopus 로고
    • Basement membrane heparan sulfate proteoglycan binds to laminin by its heparan sulfate chains and to nidogen by sites in the protein core
    • Bartaglia C., Mayer U., Aumailley M., Timpl R. Basement membrane heparan sulfate proteoglycan binds to laminin by its heparan sulfate chains and to nidogen by sites in the protein core. Eur. J. Biochem. 208:1992;359-366.
    • (1992) Eur. J. Biochem. , vol.208 , pp. 359-366
    • Bartaglia, C.1    Mayer, U.2    Aumailley, M.3    Timpl, R.4
  • 5
    • 0027324217 scopus 로고
    • Structural basis of β1 integrin-mediated cell adhesion to a large heparan sulphate proteoglycan from basement membranes
    • Battaglia C., Aumailley M., Mann K., Mayer C., Timpl R. Structural basis of β1 integrin-mediated cell adhesion to a large heparan sulphate proteoglycan from basement membranes. Eur. J. Cell Biol. 61:1993;92-99.
    • (1993) Eur. J. Cell Biol. , vol.61 , pp. 92-99
    • Battaglia, C.1    Aumailley, M.2    Mann, K.3    Mayer, C.4    Timpl, R.5
  • 6
    • 0027050807 scopus 로고
    • The refined 1.9-Å X-ray crystal structure of D-Phe-Pro-Arg chloromethylketone-inhibited human α-thrombin: Structure analysis, overall structure, electrostatic properties, detailed active-site geometry and structure-function relationships
    • Bode W., Turk D., Karshinkov A. The refined 1.9-Å X-ray crystal structure of D-Phe-Pro-Arg chloromethylketone-inhibited human α-thrombin: structure analysis, overall structure, electrostatic properties, detailed active-site geometry and structure-function relationships. Protein Sci. 1:1992;426-471.
    • (1992) Protein Sci. , vol.1 , pp. 426-471
    • Bode, W.1    Turk, D.2    Karshinkov, A.3
  • 7
    • 0028815498 scopus 로고
    • Recombinant domain III of perlecan promotes cell attachment through its RGDS sequence
    • Chakravarti S., Horchar T., Jefferson B., Laurie G.W., Hassell J.R. Recombinant domain III of perlecan promotes cell attachment through its RGDS sequence. J. Biol. Chem. 270:1995;404-409.
    • (1995) J. Biol. Chem. , vol.270 , pp. 404-409
    • Chakravarti, S.1    Horchar, T.2    Jefferson, B.3    Laurie, G.W.4    Hassell, J.R.5
  • 8
    • 0028978690 scopus 로고
    • Antibody mapping and tissue localization of globular and cysteine-rich regions of perlecan domain III
    • Couchman J.R., Ljubimov A.V., Sthaman M., Horchar T., Hassell J.R. Antibody mapping and tissue localization of globular and cysteine-rich regions of perlecan domain III. J. Histochem. Cytochem. 43:1995;955-963.
    • (1995) J. Histochem. Cytochem. , vol.43 , pp. 955-963
    • Couchman, J.R.1    Ljubimov, A.V.2    Sthaman, M.3    Horchar, T.4    Hassell, J.R.5
  • 9
    • 0024413453 scopus 로고
    • EGF-like domains in extracellular matrix proteins: Localized signals for growth and differentiation?
    • Engel J. EGF-like domains in extracellular matrix proteins: localized signals for growth and differentiation? FEBS Lett. 251:1989;1-7.
    • (1989) FEBS Lett. , vol.251 , pp. 1-7
    • Engel, J.1
  • 10
    • 0023587128 scopus 로고
    • Electron microscopy and other physical methods for the characterization of extracellular matrix components: Laminin, fibronectin, collagen IV, collagen VI and proteoglycans
    • Engel J., Furthmayr H. Electron microscopy and other physical methods for the characterization of extracellular matrix components: laminin, fibronectin, collagen IV, collagen VI and proteoglycans. Meth. Enzymol. 145:1987;3-78.
    • (1987) Meth. Enzymol. , vol.145 , pp. 3-78
    • Engel, J.1    Furthmayr, H.2
  • 11
    • 0025950577 scopus 로고
    • Localization of a major nidogen-binding site to domain III of laminin B2 chain
    • Gerl M., Mann K., Aumailley M., Timpl R. Localization of a major nidogen-binding site to domain III of laminin B2 chain. Eur. J. Biochem. 202:1991;167-174.
    • (1991) Eur. J. Biochem. , vol.202 , pp. 167-174
    • Gerl, M.1    Mann, K.2    Aumailley, M.3    Timpl, R.4
  • 12
    • 0026463887 scopus 로고
    • Endothelial cells interact with the core protein of basement membrane perlecan through β1 and β3 integrins: An adhesion modulated by glycosaminoglycan
    • Hayashi K., Madri J.A., Yurchenco P.D. Endothelial cells interact with the core protein of basement membrane perlecan through β1 and β3 integrins: an adhesion modulated by glycosaminoglycan. J. Cell Biol. 199:1992;945-959.
    • (1992) J. Cell Biol. , vol.199 , pp. 945-959
    • Hayashi, K.1    Madri, J.A.2    Yurchenco, P.D.3
  • 13
    • 0028102255 scopus 로고
    • The biology of perlecan: The multifaceted heparan sulphate proteoglycan of basement membranes and pericellular matrices
    • Iozzo R., Cohen I.R., Grässel S., Murdoch A.D. The biology of perlecan: the multifaceted heparan sulphate proteoglycan of basement membranes and pericellular matrices. Biochem. J. 302:1994;625-639.
    • (1994) Biochem. J. , vol.302 , pp. 625-639
    • Iozzo, R.1    Cohen, I.R.2    Grässel, S.3    Murdoch, A.D.4
  • 14
    • 0026500541 scopus 로고
    • Human basement membrane heparan sulfate proteoglycan core protein: A 467 kD protein containing multiple domains resembling elements of the low density lipoprotein receptor, laminin, neural cell adhesion molecules and epidermal growth factor
    • Kallunki P., Tryggvason K. Human basement membrane heparan sulfate proteoglycan core protein: A 467 kD protein containing multiple domains resembling elements of the low density lipoprotein receptor, laminin, neural cell adhesion molecules and epidermal growth factor. J. Cell Biol. 116:1992;559-571.
    • (1992) J. Cell Biol. , vol.116 , pp. 559-571
    • Kallunki, P.1    Tryggvason, K.2
  • 15
    • 0023923198 scopus 로고
    • Visualization of the large heparan sulfate proteoglycan from basement membrane
    • Laurie G.W., Inoue S., Bing J.T., Hassell J.R. Visualization of the large heparan sulfate proteoglycan from basement membrane. Am. J. Anat. 181:1988;320-326.
    • (1988) Am. J. Anat. , vol.181 , pp. 320-326
    • Laurie, G.W.1    Inoue, S.2    Bing, J.T.3    Hassell, J.R.4
  • 16
  • 17
    • 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., Iozzo R.V. 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. 267:1992;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
  • 18
    • 0025858265 scopus 로고
    • Recombinant expression and properties of the human calcium-binding extracellular matrix protein BM-40
    • Nischrt R., Pottgiesser J., Krieg T., Mayer U., Aumailley M., Timpl R. Recombinant expression and properties of the human calcium-binding extracellular matrix protein BM-40. Eur. J. Biochem. 200:1991;529-536.
    • (1991) Eur. J. Biochem. , vol.200 , pp. 529-536
    • Nischrt, R.1    Pottgiesser, J.2    Krieg, T.3    Mayer, U.4    Aumailley, M.5    Timpl, R.6
  • 19
    • 0026317977 scopus 로고
    • The complete sequence of perlecan, a basement membrane heparan sulfate proteoglycan, reveals extensive similarity with laminin A chain, LDL-receptor and N-CAM
    • Noonan D.M., Fulle A., Valente P., Cai S., Horigan E., Sasaki M., Yamada Y., Hassell J.R. The complete sequence of perlecan, a basement membrane heparan sulfate proteoglycan, reveals extensive similarity with laminin A chain, LDL-receptor and N-CAM. J. Biol. Chem. 266:1991;22939-22947.
    • (1991) J. Biol. Chem. , vol.266 , pp. 22939-22947
    • Noonan, D.M.1    Fulle, A.2    Valente, P.3    Cai, S.4    Horigan, E.5    Sasaki, M.6    Yamada, Y.7    Hassell, J.R.8
  • 20
    • 0023660965 scopus 로고
    • Structure of low density heparan sulfate proteoglycan isolated from a mouse tumor basemenet membrane
    • Paulson M., Yurchenco P.D., Ruben G.C., Engel J., Timpl R. Structure of low density heparan sulfate proteoglycan isolated from a mouse tumor basemenet membrane. J. Mol. Biol. 197:1987;297-313.
    • (1987) J. Mol. Biol. , vol.197 , pp. 297-313
    • Paulson, M.1    Yurchenco, P.D.2    Ruben, G.C.3    Engel, J.4    Timpl, R.5
  • 21
    • 0028149335 scopus 로고
    • Binding of purified collagen receptors (α1β1, α2β1) and RGD-dependent integrins to laminins and laminin fragments
    • Pfaff M., Göhring W., Brown J.C., Timpl R. Binding of purified collagen receptors (α1β1, α2β1) and RGD-dependent integrins to laminins and laminin fragments. Eur. J. Biochem. 225:1994;975-984.
    • (1994) Eur. J. Biochem. , vol.225 , pp. 975-984
    • Pfaff, M.1    Göhring, W.2    Brown, J.C.3    Timpl, R.4
  • 22
    • 0029087888 scopus 로고
    • Integrin-binding and cell-adhesion studies of fibulins reveal a particular affinity for αIIbβ3
    • Pfaff M., Sasaki T., Tangemann K., Chu M.-L., Timpl R. Integrin-binding and cell-adhesion studies of fibulins reveal a particular affinity for αIIbβ3. Exp. Cell Res. 219:1995;87-92.
    • (1995) Exp. Cell Res. , vol.219 , pp. 87-92
    • Pfaff, M.1    Sasaki, T.2    Tangemann, K.3    Chu, M.-L.4    Timpl, R.5
  • 23
    • 0029867570 scopus 로고    scopus 로고
    • Cell adhesion and integrin binding to recombinant human fibrillin-1
    • Pfaff M., Reinhardt D.P., Sakai L.Y., Timpl R. Cell adhesion and integrin binding to recombinant human fibrillin-1. FEBS Lett. 384:1996;247-250.
    • (1996) FEBS Lett. , vol.384 , pp. 247-250
    • Pfaff, M.1    Reinhardt, D.P.2    Sakai, L.Y.3    Timpl, R.4
  • 24
    • 0029115899 scopus 로고
    • Structural properties of recombinant domain III-3 of perlecan containing a globular domain inserted into an epidermal-growth-factor-like motif
    • Schulze B., Mann K., Battistutta R., Wiedemann H., Timpl R. Structural properties of recombinant domain III-3 of perlecan containing a globular domain inserted into an epidermal-growth-factor-like motif. Eur. J. Biochem. 213:1995;551-556.
    • (1995) Eur. J. Biochem. , vol.213 , pp. 551-556
    • Schulze, B.1    Mann, K.2    Battistutta, R.3    Wiedemann, H.4    Timpl, R.5
  • 25
    • 0029984696 scopus 로고    scopus 로고
    • Structural and functional analysis of the globular domain IVa of the laminin α1 chain and its impact on an adjacent RGD site
    • Schulze B., Mann K., Pöschl E., Yamada Y., Timpl R. Structural and functional analysis of the globular domain IVa of the laminin α1 chain and its impact on an adjacent RGD site. Biochem. J. 314:1996;847-851.
    • (1996) Biochem. J. , vol.314 , pp. 847-851
    • Schulze, B.1    Mann, K.2    Pöschl, E.3    Yamada, Y.4    Timpl, R.5
  • 26
    • 0029967684 scopus 로고    scopus 로고
    • Crystal structure of three consecutive laminin-type epidermal growth factor-like (LE) modules of laminin γ1 chain harboring the nidogen binding site
    • Stetefeld J., Mayer U., Timpl R., Huber R. Crystal structure of three consecutive laminin-type epidermal growth factor-like (LE) modules of laminin γ1 chain harboring the nidogen binding site. J. Mol. Biol. 257:1996;644-657.
    • (1996) J. Mol. Biol. , vol.257 , pp. 644-657
    • Stetefeld, J.1    Mayer, U.2    Timpl, R.3    Huber, R.4
  • 27
    • 0029132269 scopus 로고
    • Perlecan is a component of cartilage matrix and promotes chondrocyte attachment
    • Sundar Raj N., Fite D., Ledbetter S., Chakravarti S., Hassell J.R. Perlecan is a component of cartilage matrix and promotes chondrocyte attachment. J. Cell Sci. 108:1995;2663-2672.
    • (1995) J. Cell Sci. , vol.108 , pp. 2663-2672
    • Sundar Raj, N.1    Fite, D.2    Ledbetter, S.3    Chakravarti, S.4    Hassell, J.R.5
  • 28
    • 0020011438 scopus 로고
    • Antibodies to collagens and procollagens
    • Timpl R. Antibodies to collagens and procollagens. Meth. Enzymol. 82:1982;472-498.
    • (1982) Meth. Enzymol. , vol.82 , pp. 472-498
    • Timpl, R.1
  • 29
    • 0027151901 scopus 로고
    • Proteoglycans of basement membranes
    • Timpl R. Proteoglycans of basement membranes. Experientia. 49:1993;417-428.
    • (1993) Experientia , vol.49 , pp. 417-428
    • Timpl, R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.