Endothelial cells adhere to the RGD domain and the fibrinogen-like terminal knob of tenascin

P. Joshi; C.Y. Chung; I. Aukhil; H.P. Erickson

Summary

We have found that endothelial cells adhere much more strongly than fibroblasts to domains of tenascin and fibronectin. Endothelial cells adhered weakly, without spreading, to bacterial expression proteins corresponding to the tenth fibronectin type III (FN-III) domain of fibronectin, which contains the RGD. A larger fibronectin protein, containing this domain and the three amino-terminal ‘synergy’ domains gave strong adhesion and spreading. Two widely separated domains of tenascin gave adhesion. The third FN-III domain, TNfn3, which contains an RGD sequence in human and chicken tenascin, gave very strong adhesion and spreading of endothelial cells when tested as an isolated domain. Larger segments containing TNfn3 and the adjacent TNfn2 gave weaker adhesion, probably because the RGD sequence is partially blocked. Adhesion to this domain required divalent cations, was exquisitely sensitive to soluble GRGDSP peptide, and was blocked by antisera to the integrin alpha v beta 3. The second tenascin adhesion domain was the fibrinogen-like C-terminal knob, TNfbg. Cells adhered to but did not spread on this domain. This adhesion required divalent cations and was also sensitive to GRGDSP peptide, so it may be mediated by an integrin receptor. We have explored a range of conditions for preparing the adhesion substratum, and our results may resolve the controversy over whether tenascin can act as a substratum adhesion molecule. When coated for short times (1-2 hours) on plastic, tenascin had no adhesion activity, in contrast to fibronectin and the expression proteins, which gave strong adhesion under these conditions. When coated for longer times (12-24 hours) on plastic, the tenascin substratum supported good adhesion, but not spreading, of endothelial cells. Tenascin coated on nitrocellulose gave substantially stronger adhesion than on plastic, but still required long coating times for maximal activity. Adhesion of endothelial cells to native TN was inhibited by GRDGSP peptide. The cell adhesion activity demonstrates the presence on endothelial cells of tenascin receptors, which may play a supportive role in angiogenesis, in the structure of blood vessels, or in binding tenascin to the cell surface to elicit or enhance a signalling function.

REFERENCES

1. Aota S.,
2. Nagai T. and
3. Yamada K. M.
(1991). Characterization of regions of fibronectin besides the arginine-glycine-aspartic acid sequence required for adhesive function of the cell-binding domain using site-directed mutagenesis. J. Biol. Chem 266, 15938–15943
OpenUrl Abstract/FREE Full Text
1. Aukhil I.,
2. Joshi P.,
3. Yan Y. Z. and
4. Erickson H. P.
(1993). Cell-and heparin-binding domains of the hexabrachion arm identified by tenascin expression proteins. J. Biol. Chem 268, 2542–2553
OpenUrl Abstract/FREE Full Text
1. Aukhil I.,
2. Slemp C. A.,
3. Lightner V. A.,
4. Nishimura K.,
5. Briscoe G. and
6. Erickson H. P.
(1990). Purification of hexabrachion (tenascin) from cell culture conditioned medium, and separation from a cell adhesion factor. Matrix 10, 98–111
OpenUrl CrossRef PubMed Web of Science
1. Bourdon M. A. and
2. Ruoslahti E.
(1989). Tenascin mediates cell attachment through an RGD-dependent receptor. J. Cell Biol 108, 1149–1155
OpenUrl Abstract/FREE Full Text
1. Cheng Y.-F.,
2. Clyman R. I.,
3. Enenstein J.,
4. Waleh N.,
5. Pytela R. and
6. Kramer R. H.
(1991). The integrin complexv 3participates in the adhesion of microvascular endothelial cells to fibronectin. Exp. Cell Res 194, 69–77
OpenUrl CrossRef PubMed Web of Science
1. Chiquet M.,
2. Vrucinic-Filipi N.,
3. Schenk S.,
4. Beck K. and
5. Chiquet-Ehrismann R.
(1991). Isolation of chick tenascin variants and fragments. A C-terminal heparin-binding fragment produced by cleavage of the extra domain from the largest subunit splicing variant. Eur. J. Biochem 199, 379–388
OpenUrl PubMed Web of Science
1. Chiquet-Ehrismann R.,
2. Kalla P.,
3. Pearson C. A.,
4. Beck K. and
5. Chiquet M.
(1988). Tenascin interferes with fibronectin action. Cell 53, 383–390
OpenUrl CrossRef PubMed Web of Science
1. Erickson H. P. and
2. Bourdon M. A.
(1989). Tenascin: an extracellularmatrix protein prominent in specialized embryonic tissues and tumors. Annu. Rev. Cell Biol 5, 71–92
OpenUrl CrossRef Web of Science
1. Erickson H. P. and
2. Taylor H. C.
(1987). Hexabrachion proteins in embryonic chicken tissues and human tumors. J. Cell Biol 105, 1387–1394
OpenUrl Abstract/FREE Full Text
1. Friedlander D. R.,
2. Hoffman S. and
3. Edelman G. M.
(1988). Functional mapping of cytotactin: Proteolytic fragments active in cell-substratum adhesion. J. Cell Biol 107, 2329–2340
OpenUrl Abstract/FREE Full Text
1. Greenwood F. C.,
2. Hunter W. M. and
3. Glover J. S.
(1963). The preparation of 131 I-labelled human growth hormone of high specific radioactivity. Biochem. J 89, 114–123
OpenUrl FREE Full Text
1. Grinspan J. B.,
2. Mueller S. N. and
3. Levine E. M.
(1983). Bovine endothelial cells transformed in vitro by benzo(a)pyrene. J. Cell. Physiol 114, 328–338
OpenUrl CrossRef PubMed Web of Science
1. Hynes R. O.
(1992). Integrins: Versatility, modulation, and signaling in cell adhesion. Cell 69, 11–25
OpenUrl CrossRef PubMed Web of Science
1. Kimizuka F.,
2. Ohdate Y.,
3. Kawase Y.,
4. Shimojo T.,
5. Taguchi Y.,
6. Hashino K.,
7. Goto S.,
8. Hashi H.,
9. Kato I.,
10. Sekiguchi K. and
11. Titani K.
(1991). Role of type III homology repeats in cell adhesive function within the cell-binding domain of fibronectin. J. Biol. Chem 266, 3045–3051
OpenUrl Abstract/FREE Full Text
1. Leahy D. J.,
2. Hendrickson W. A.,
3. Aukhil I. and
4. Erickson H. P.
(1992). Structure of a fibronectin type III domain from tenascin phased by MAD analysis of the selenomethionyl protein. Science 258, 987–991
OpenUrl Abstract/FREE Full Text
1. Lightner V. A. and
2. Erickson H. P.
(1990). Binding of hexabrachion (tenascin) to the extracellular matrix and substratum and its effect on cell adhesion. J. Cell Sci 95, 263–277
OpenUrl Abstract/FREE Full Text
1. Loeser R. F. and
2. Wallin R.
(1992). Cell adhesion to matrix Gla protein and its inhibition by an Arg-Gly-Asp-containing peptide. J. Biol. Chem 267, 9459–9462
OpenUrl Abstract/FREE Full Text
1. Lotz M. M.,
2. Burdsal C. A.,
3. Erickson H. P. and
4. McClay D. R.
(1989). Cell adhesion to fibronectin and tenascin: quantitative measurements of initial binding and subsequent strengthening response. J. Cell Biol 109, 1795–1805
OpenUrl Abstract/FREE Full Text
1. Mackie E. J.,
2. Thesleff I. and
3. Chiquet-Ehrismann R.
(1987). Tenascin is associated with chondrogenic and osteogenic differentiation in vivo and promotes chondrogenesis in vitro. J. Cell Biol 105, 2569–2579
OpenUrl Abstract/FREE Full Text
1. Maier J. A. M.,
2. Rusnati M.,
3. Ragnotti G. and
4. Presta M.
(1990). Characterization of a M r20,000 basic fibroblast growth factor-like protein secreted by normal and transformed fetal bovine aortic endothelial cells. Exp. Cell Res 186, 354–361
OpenUrl CrossRef PubMed
1. Main A. L.,
2. Harvey T. S.,
3. Baron M.,
4. Boyd J. and
5. Campbell I. D.
(1992). The three-dimensional structure of the tenth type III module of fibronectin: An insight into RGD-mediated interactions. Cell 71, 671–678
OpenUrl CrossRef PubMed Web of Science
1. Massia S. P. and
2. Hubbell J. A.
(1991). An RGD spacing of 440 nm is sufficient for integrinv 3-mediated fibroblast spreading and 140 nm for focal contact and stress fiber formation. J. Cell Biol 114, 1089–1100
OpenUrl Abstract/FREE Full Text
1. Murphy-Ullrich J. E.,
2. Lightner V. A.,
3. Aukhil I.,
4. Yan Y. Z.,
5. Erickson H. P. and
6. Höök M.
(1991). Focal adhesion integrity is downregulated by the alternatively spliced domain of human tenascin. J. Cell Biol 115, 1127–1136
OpenUrl Abstract/FREE Full Text
1. Nishi T.,
2. Weinstein J.,
3. Gillespie W. M. and
4. Paulson J. C.
(1991). Complete primary structure of porcine tenascin. Detection of tenascin transcripts in adult submaxillary glands. Eur. J. Biochem 202, 643–648
OpenUrl PubMed
1. Nörenberg U.,
2. Wille H.,
3. Wolff J. M.,
4. Frank R. and
5. Rathjen F. G.
(1992). The chicken neural extracellular matrix molecule restrictin: Similarity with EGF-, fibronectin type III-, and fibrinogen-like motifs. Neuron 8, 849–863
OpenUrl CrossRef PubMed Web of Science
1. Onda H.,
2. Poulin M. L.,
3. Tassava R. A. and
4. Chiu I.-M.
(1991). Characterization of a newt tenascin cDNA and localization of tenascin mRNA during newt limb regeneration by in situ hybridization. Dev. Biol 148, 219–232
OpenUrl CrossRef PubMed
1. Pierschbacher M. D. and
2. Ruoslahti E.
(1984). Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule. Nature 309, 30–33
OpenUrl CrossRef PubMed Web of Science
1. Pierschbacher M. D. and
2. Ruoslahti E.
(1987). Influence of stereochemistry of the sequence Arg-Gly-Asp-Xaa on binding specificity in cell adhesion. J. Biol. Chem 262, 17294–17298
OpenUrl Abstract/FREE Full Text
1. Prieto A. L.,
2. Andersson-Fisone C. and
3. Crossin K. L.
(1992). 400Characterization of multiple adhesive and counteradhesive domains in the extracellular matrix protein cytotactin. J. Cell Biol 119, 663–678
OpenUrl Abstract/FREE Full Text
1. Saga Y.,
2. Tsukamoto T.,
3. Jing N.,
4. Kusakabe M. and
5. Sakakura T.
(1991). Murine tenascin: cDNA cloning, structure and temporal expression of isoforms. Gene 104, 177–185
OpenUrl CrossRef PubMed
1. Saga Y.,
2. Yagi T.,
3. Ikawa Y.,
4. Sakakura T. and
5. Aizawa S.
(1992). Mice develop normally without tenascin. Genes Dev 6, 1821–1831
OpenUrl Abstract/FREE Full Text
1. Saginati M.,
2. Siri A.,
3. Balza E.,
4. Ponassi M. and
5. Zardi L.
(1992). A simple procedure for tenascin purification. Eur. J. Biochem 2, 545–549
OpenUrl
1. Spring J.,
2. Beck K. and
3. Chiquet-Ehrismann R.
(1989). Two contrary functions of tenascin: dissection of the active site by recombinant tenascin fragments. Cell 59, 325–334
OpenUrl CrossRef PubMed Web of Science
1. Sriramarao P.,
2. Mendler M. and
3. Bourdon M. A.
(1993). Endothelial cell attachment and spreading on human tenascin is mediated by alpha2-beta1 and alphaV-beta3 integrins. J. Cell Sci.
1. Weller A.,
2. Beck S. and
3. Ekblom P.
(1991). Amino acid sequence of mouse tenascin and differential expression of two tenascin isoforms during embryogenesis. J. Cell Biol 112, 355–362
OpenUrl Abstract/FREE Full Text

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[1] Aota S.,
Nagai T. and
Yamada K. M.
(1991). Characterization of regions of fibronectin besides the arginine-glycine-aspartic acid sequence required for adhesive function of the cell-binding domain using site-directed mutagenesis. J. Biol. Chem 266, 15938–15943
OpenUrl Abstract/FREE Full Text

[2] Aota S.,

[3] Nagai T. and

[4] Yamada K. M.

[5] Aukhil I.,
Joshi P.,
Yan Y. Z. and
Erickson H. P.
(1993). Cell-and heparin-binding domains of the hexabrachion arm identified by tenascin expression proteins. J. Biol. Chem 268, 2542–2553
OpenUrl Abstract/FREE Full Text

[6] Aukhil I.,

[7] Joshi P.,

[8] Yan Y. Z. and

[9] Erickson H. P.

[10] Aukhil I.,
Slemp C. A.,
Lightner V. A.,
Nishimura K.,
Briscoe G. and
Erickson H. P.
(1990). Purification of hexabrachion (tenascin) from cell culture conditioned medium, and separation from a cell adhesion factor. Matrix 10, 98–111
OpenUrl CrossRef PubMed Web of Science

[11] Aukhil I.,

[12] Slemp C. A.,

[13] Lightner V. A.,

[14] Nishimura K.,

[15] Briscoe G. and

[16] Erickson H. P.

[17] Bourdon M. A. and
Ruoslahti E.
(1989). Tenascin mediates cell attachment through an RGD-dependent receptor. J. Cell Biol 108, 1149–1155
OpenUrl Abstract/FREE Full Text

[18] Bourdon M. A. and

[19] Ruoslahti E.

[20] Cheng Y.-F.,
Clyman R. I.,
Enenstein J.,
Waleh N.,
Pytela R. and
Kramer R. H.
(1991). The integrin complexv 3participates in the adhesion of microvascular endothelial cells to fibronectin. Exp. Cell Res 194, 69–77
OpenUrl CrossRef PubMed Web of Science

[21] Cheng Y.-F.,

[22] Clyman R. I.,

[23] Enenstein J.,

[24] Waleh N.,

[25] Pytela R. and

[26] Kramer R. H.

[27] Chiquet M.,
Vrucinic-Filipi N.,
Schenk S.,
Beck K. and
Chiquet-Ehrismann R.
(1991). Isolation of chick tenascin variants and fragments. A C-terminal heparin-binding fragment produced by cleavage of the extra domain from the largest subunit splicing variant. Eur. J. Biochem 199, 379–388
OpenUrl PubMed Web of Science

[28] Chiquet M.,

[29] Vrucinic-Filipi N.,

[30] Schenk S.,

[31] Beck K. and

[32] Chiquet-Ehrismann R.

[33] Chiquet-Ehrismann R.,
Kalla P.,
Pearson C. A.,
Beck K. and
Chiquet M.
(1988). Tenascin interferes with fibronectin action. Cell 53, 383–390
OpenUrl CrossRef PubMed Web of Science

[34] Chiquet-Ehrismann R.,

[35] Kalla P.,

[36] Pearson C. A.,

[37] Beck K. and

[38] Chiquet M.

[39] Erickson H. P. and
Bourdon M. A.
(1989). Tenascin: an extracellularmatrix protein prominent in specialized embryonic tissues and tumors. Annu. Rev. Cell Biol 5, 71–92
OpenUrl CrossRef Web of Science

[40] Erickson H. P. and

[41] Bourdon M. A.

[42] Erickson H. P. and
Taylor H. C.
(1987). Hexabrachion proteins in embryonic chicken tissues and human tumors. J. Cell Biol 105, 1387–1394
OpenUrl Abstract/FREE Full Text

[43] Erickson H. P. and

[44] Taylor H. C.

[45] Friedlander D. R.,
Hoffman S. and
Edelman G. M.
(1988). Functional mapping of cytotactin: Proteolytic fragments active in cell-substratum adhesion. J. Cell Biol 107, 2329–2340
OpenUrl Abstract/FREE Full Text

[46] Friedlander D. R.,

[47] Hoffman S. and

[48] Edelman G. M.

[49] Greenwood F. C.,
Hunter W. M. and
Glover J. S.
(1963). The preparation of 131 I-labelled human growth hormone of high specific radioactivity. Biochem. J 89, 114–123
OpenUrl FREE Full Text

[50] Greenwood F. C.,

[51] Hunter W. M. and

[52] Glover J. S.

[53] Grinspan J. B.,
Mueller S. N. and
Levine E. M.
(1983). Bovine endothelial cells transformed in vitro by benzo(a)pyrene. J. Cell. Physiol 114, 328–338
OpenUrl CrossRef PubMed Web of Science

[54] Grinspan J. B.,

[55] Mueller S. N. and

[56] Levine E. M.

[57] Hynes R. O.
(1992). Integrins: Versatility, modulation, and signaling in cell adhesion. Cell 69, 11–25
OpenUrl CrossRef PubMed Web of Science

[58] Hynes R. O.

[59] Kimizuka F.,
Ohdate Y.,
Kawase Y.,
Shimojo T.,
Taguchi Y.,
Hashino K.,
Goto S.,
Hashi H.,
Kato I.,
Sekiguchi K. and
Titani K.
(1991). Role of type III homology repeats in cell adhesive function within the cell-binding domain of fibronectin. J. Biol. Chem 266, 3045–3051
OpenUrl Abstract/FREE Full Text

[60] Kimizuka F.,

[61] Ohdate Y.,

[62] Kawase Y.,

[63] Shimojo T.,

[64] Taguchi Y.,

[65] Hashino K.,

[66] Goto S.,

[67] Hashi H.,

[68] Kato I.,

[69] Sekiguchi K. and

[70] Titani K.

[71] Leahy D. J.,
Hendrickson W. A.,
Aukhil I. and
Erickson H. P.
(1992). Structure of a fibronectin type III domain from tenascin phased by MAD analysis of the selenomethionyl protein. Science 258, 987–991
OpenUrl Abstract/FREE Full Text

[72] Leahy D. J.,

[73] Hendrickson W. A.,

[74] Aukhil I. and

[75] Erickson H. P.

[76] Lightner V. A. and
Erickson H. P.
(1990). Binding of hexabrachion (tenascin) to the extracellular matrix and substratum and its effect on cell adhesion. J. Cell Sci 95, 263–277
OpenUrl Abstract/FREE Full Text

[77] Lightner V. A. and

[78] Erickson H. P.

[79] Loeser R. F. and
Wallin R.
(1992). Cell adhesion to matrix Gla protein and its inhibition by an Arg-Gly-Asp-containing peptide. J. Biol. Chem 267, 9459–9462
OpenUrl Abstract/FREE Full Text

[80] Loeser R. F. and

[81] Wallin R.

[82] Lotz M. M.,
Burdsal C. A.,
Erickson H. P. and
McClay D. R.
(1989). Cell adhesion to fibronectin and tenascin: quantitative measurements of initial binding and subsequent strengthening response. J. Cell Biol 109, 1795–1805
OpenUrl Abstract/FREE Full Text

[83] Lotz M. M.,

[84] Burdsal C. A.,

[85] Erickson H. P. and

[86] McClay D. R.

[87] Mackie E. J.,
Thesleff I. and
Chiquet-Ehrismann R.
(1987). Tenascin is associated with chondrogenic and osteogenic differentiation in vivo and promotes chondrogenesis in vitro. J. Cell Biol 105, 2569–2579
OpenUrl Abstract/FREE Full Text

[88] Mackie E. J.,

[89] Thesleff I. and

[90] Chiquet-Ehrismann R.

[91] Maier J. A. M.,
Rusnati M.,
Ragnotti G. and
Presta M.
(1990). Characterization of a M r20,000 basic fibroblast growth factor-like protein secreted by normal and transformed fetal bovine aortic endothelial cells. Exp. Cell Res 186, 354–361
OpenUrl CrossRef PubMed

[92] Maier J. A. M.,

[93] Rusnati M.,

[94] Ragnotti G. and

[95] Presta M.

[96] Main A. L.,
Harvey T. S.,
Baron M.,
Boyd J. and
Campbell I. D.
(1992). The three-dimensional structure of the tenth type III module of fibronectin: An insight into RGD-mediated interactions. Cell 71, 671–678
OpenUrl CrossRef PubMed Web of Science

[97] Main A. L.,

[98] Harvey T. S.,

[99] Baron M.,

[100] Boyd J. and

[101] Campbell I. D.

[102] Massia S. P. and
Hubbell J. A.
(1991). An RGD spacing of 440 nm is sufficient for integrinv 3-mediated fibroblast spreading and 140 nm for focal contact and stress fiber formation. J. Cell Biol 114, 1089–1100
OpenUrl Abstract/FREE Full Text

[103] Massia S. P. and

[104] Hubbell J. A.

[105] Murphy-Ullrich J. E.,
Lightner V. A.,
Aukhil I.,
Yan Y. Z.,
Erickson H. P. and
Höök M.
(1991). Focal adhesion integrity is downregulated by the alternatively spliced domain of human tenascin. J. Cell Biol 115, 1127–1136
OpenUrl Abstract/FREE Full Text

[106] Murphy-Ullrich J. E.,

[107] Lightner V. A.,

[108] Aukhil I.,

[109] Yan Y. Z.,

[110] Erickson H. P. and

[111] Höök M.

[112] Nishi T.,
Weinstein J.,
Gillespie W. M. and
Paulson J. C.
(1991). Complete primary structure of porcine tenascin. Detection of tenascin transcripts in adult submaxillary glands. Eur. J. Biochem 202, 643–648
OpenUrl PubMed

[113] Nishi T.,

[114] Weinstein J.,

[115] Gillespie W. M. and

[116] Paulson J. C.

[117] Nörenberg U.,
Wille H.,
Wolff J. M.,
Frank R. and
Rathjen F. G.
(1992). The chicken neural extracellular matrix molecule restrictin: Similarity with EGF-, fibronectin type III-, and fibrinogen-like motifs. Neuron 8, 849–863
OpenUrl CrossRef PubMed Web of Science

[118] Nörenberg U.,

[119] Wille H.,

[120] Wolff J. M.,

[121] Frank R. and

[122] Rathjen F. G.

[123] Onda H.,
Poulin M. L.,
Tassava R. A. and
Chiu I.-M.
(1991). Characterization of a newt tenascin cDNA and localization of tenascin mRNA during newt limb regeneration by in situ hybridization. Dev. Biol 148, 219–232
OpenUrl CrossRef PubMed

[124] Onda H.,

[125] Poulin M. L.,

[126] Tassava R. A. and

[127] Chiu I.-M.

[128] Pierschbacher M. D. and
Ruoslahti E.
(1984). Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule. Nature 309, 30–33
OpenUrl CrossRef PubMed Web of Science

[129] Pierschbacher M. D. and

[130] Ruoslahti E.

[131] Pierschbacher M. D. and
Ruoslahti E.
(1987). Influence of stereochemistry of the sequence Arg-Gly-Asp-Xaa on binding specificity in cell adhesion. J. Biol. Chem 262, 17294–17298
OpenUrl Abstract/FREE Full Text

[132] Pierschbacher M. D. and

[133] Ruoslahti E.

[134] Prieto A. L.,
Andersson-Fisone C. and
Crossin K. L.
(1992). 400Characterization of multiple adhesive and counteradhesive domains in the extracellular matrix protein cytotactin. J. Cell Biol 119, 663–678
OpenUrl Abstract/FREE Full Text

[135] Prieto A. L.,

[136] Andersson-Fisone C. and

[137] Crossin K. L.

[138] Saga Y.,
Tsukamoto T.,
Jing N.,
Kusakabe M. and
Sakakura T.
(1991). Murine tenascin: cDNA cloning, structure and temporal expression of isoforms. Gene 104, 177–185
OpenUrl CrossRef PubMed

[139] Saga Y.,

[140] Tsukamoto T.,

[141] Jing N.,

[142] Kusakabe M. and

[143] Sakakura T.

[144] Saga Y.,
Yagi T.,
Ikawa Y.,
Sakakura T. and
Aizawa S.
(1992). Mice develop normally without tenascin. Genes Dev 6, 1821–1831
OpenUrl Abstract/FREE Full Text

[145] Saga Y.,

[146] Yagi T.,

[147] Ikawa Y.,

[148] Sakakura T. and

[149] Aizawa S.

[150] Saginati M.,
Siri A.,
Balza E.,
Ponassi M. and
Zardi L.
(1992). A simple procedure for tenascin purification. Eur. J. Biochem 2, 545–549
OpenUrl

[151] Saginati M.,

[152] Siri A.,

[153] Balza E.,

[154] Ponassi M. and

[155] Zardi L.

[156] Spring J.,
Beck K. and
Chiquet-Ehrismann R.
(1989). Two contrary functions of tenascin: dissection of the active site by recombinant tenascin fragments. Cell 59, 325–334
OpenUrl CrossRef PubMed Web of Science

[157] Spring J.,

[158] Beck K. and

[159] Chiquet-Ehrismann R.

[160] Sriramarao P.,
Mendler M. and
Bourdon M. A.
(1993). Endothelial cell attachment and spreading on human tenascin is mediated by alpha2-beta1 and alphaV-beta3 integrins. J. Cell Sci.

[161] Sriramarao P.,

[162] Mendler M. and

[163] Bourdon M. A.

[164] Weller A.,
Beck S. and
Ekblom P.
(1991). Amino acid sequence of mouse tenascin and differential expression of two tenascin isoforms during embryogenesis. J. Cell Biol 112, 355–362
OpenUrl Abstract/FREE Full Text

[165] Weller A.,

[166] Beck S. and

[167] Ekblom P.

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New funding scheme supports sustainable events

Read & Publish participation continues to grow

Cell scientist to watch: Romain Levayer

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Summary

REFERENCES

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Cited by...

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Other journals from The Company of Biologists

Introducing FocalPlane’s new Community Manager, Esperanza Agullo-Pascual

New funding scheme supports sustainable events

Read & Publish participation continues to grow

Cell scientist to watch: Romain Levayer

Live lactating mammary tissue

JCS and COVID-19