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Role of a vitronectin-like molecule in embryo adhesion of the brown alga Fucus.
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| Zeitschriftentitel: | Proceedings of the National Academy of Sciences |
|---|---|
| Personen und Körperschaften: | , , |
| In: | Proceedings of the National Academy of Sciences, 89, 1992, 8, S. 3644-3648 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Proceedings of the National Academy of Sciences
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| Schlagwörter: |
| author_facet |
Wagner, V T Brian, L Quatrano, R S Wagner, V T Brian, L Quatrano, R S |
|---|---|
| author |
Wagner, V T Brian, L Quatrano, R S |
| spellingShingle |
Wagner, V T Brian, L Quatrano, R S Proceedings of the National Academy of Sciences Role of a vitronectin-like molecule in embryo adhesion of the brown alga Fucus. Multidisciplinary |
| author_sort |
wagner, v t |
| spelling |
Wagner, V T Brian, L Quatrano, R S 0027-8424 1091-6490 Proceedings of the National Academy of Sciences Multidisciplinary http://dx.doi.org/10.1073/pnas.89.8.3644 <jats:p>The rhizoid cell of the two-celled embryo of the brown alga Fucus is structurally and functionally differentiated from the thallus cell. The rhizoid cell is highly polar and transports directionally components of the cell wall to its elongating tip, which attaches the developing embryo to the substratum. Polyclonal antibodies to human vitronectin (Vn) recognize a vitronectin-like glycoprotein (Vn-F) in extracts of zygotes and two-celled embryos of Fucus, with a molecular mass (approximately 62 kDa) similar to that of human Vn. The specificity of the immunological cross-reactivity of Vn-F to rabbit polyclonal antibodies made to human Vn is demonstrated by competition experiments using pure human Vn and monospecific antibodies generated toward Vn-F. Vn-F possesses affinities for glass and heparin that are identical to those of human Vn. Immunolocalization and subcellular fractionation results demonstrate that Vn-F is localized first in the cytoplasm of the zygote, which is followed by the polar transport of Vn-F to its exclusive localization in the cell wall of the elongating rhizoid tip. Vn does not localize to the rhizoid tip under culture conditions that prevent two-celled embryos from attaching. Furthermore, an adhesion assay demonstrates that two-celled Fucus embryos do not adhere to the substratum in the presence of the Vn antibody, suggesting that the Vn-F in this brown alga not only possesses structural similarity to mammalian Vn but may also have a similar functional role in adhesion. The presence of Vn-F in brown algae suggests a high degree of evolutionary conservation of its structural and functional characteristics.</jats:p> Role of a vitronectin-like molecule in embryo adhesion of the brown alga Fucus. Proceedings of the National Academy of Sciences |
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| title |
Role of a vitronectin-like molecule in embryo adhesion of the brown alga Fucus. |
| title_unstemmed |
Role of a vitronectin-like molecule in embryo adhesion of the brown alga Fucus. |
| title_full |
Role of a vitronectin-like molecule in embryo adhesion of the brown alga Fucus. |
| title_fullStr |
Role of a vitronectin-like molecule in embryo adhesion of the brown alga Fucus. |
| title_full_unstemmed |
Role of a vitronectin-like molecule in embryo adhesion of the brown alga Fucus. |
| title_short |
Role of a vitronectin-like molecule in embryo adhesion of the brown alga Fucus. |
| title_sort |
role of a vitronectin-like molecule in embryo adhesion of the brown alga fucus. |
| topic |
Multidisciplinary |
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http://dx.doi.org/10.1073/pnas.89.8.3644 |
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1992 |
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3644-3648 |
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<jats:p>The rhizoid cell of the two-celled embryo of the brown alga Fucus is structurally and functionally differentiated from the thallus cell. The rhizoid cell is highly polar and transports directionally components of the cell wall to its elongating tip, which attaches the developing embryo to the substratum. Polyclonal antibodies to human vitronectin (Vn) recognize a vitronectin-like glycoprotein (Vn-F) in extracts of zygotes and two-celled embryos of Fucus, with a molecular mass (approximately 62 kDa) similar to that of human Vn. The specificity of the immunological cross-reactivity of Vn-F to rabbit polyclonal antibodies made to human Vn is demonstrated by competition experiments using pure human Vn and monospecific antibodies generated toward Vn-F. Vn-F possesses affinities for glass and heparin that are identical to those of human Vn. Immunolocalization and subcellular fractionation results demonstrate that Vn-F is localized first in the cytoplasm of the zygote, which is followed by the polar transport of Vn-F to its exclusive localization in the cell wall of the elongating rhizoid tip. Vn does not localize to the rhizoid tip under culture conditions that prevent two-celled embryos from attaching. Furthermore, an adhesion assay demonstrates that two-celled Fucus embryos do not adhere to the substratum in the presence of the Vn antibody, suggesting that the Vn-F in this brown alga not only possesses structural similarity to mammalian Vn but may also have a similar functional role in adhesion. The presence of Vn-F in brown algae suggests a high degree of evolutionary conservation of its structural and functional characteristics.</jats:p> |
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| description | <jats:p>The rhizoid cell of the two-celled embryo of the brown alga Fucus is structurally and functionally differentiated from the thallus cell. The rhizoid cell is highly polar and transports directionally components of the cell wall to its elongating tip, which attaches the developing embryo to the substratum. Polyclonal antibodies to human vitronectin (Vn) recognize a vitronectin-like glycoprotein (Vn-F) in extracts of zygotes and two-celled embryos of Fucus, with a molecular mass (approximately 62 kDa) similar to that of human Vn. The specificity of the immunological cross-reactivity of Vn-F to rabbit polyclonal antibodies made to human Vn is demonstrated by competition experiments using pure human Vn and monospecific antibodies generated toward Vn-F. Vn-F possesses affinities for glass and heparin that are identical to those of human Vn. Immunolocalization and subcellular fractionation results demonstrate that Vn-F is localized first in the cytoplasm of the zygote, which is followed by the polar transport of Vn-F to its exclusive localization in the cell wall of the elongating rhizoid tip. Vn does not localize to the rhizoid tip under culture conditions that prevent two-celled embryos from attaching. Furthermore, an adhesion assay demonstrates that two-celled Fucus embryos do not adhere to the substratum in the presence of the Vn antibody, suggesting that the Vn-F in this brown alga not only possesses structural similarity to mammalian Vn but may also have a similar functional role in adhesion. The presence of Vn-F in brown algae suggests a high degree of evolutionary conservation of its structural and functional characteristics.</jats:p> |
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| spelling | Wagner, V T Brian, L Quatrano, R S 0027-8424 1091-6490 Proceedings of the National Academy of Sciences Multidisciplinary http://dx.doi.org/10.1073/pnas.89.8.3644 <jats:p>The rhizoid cell of the two-celled embryo of the brown alga Fucus is structurally and functionally differentiated from the thallus cell. The rhizoid cell is highly polar and transports directionally components of the cell wall to its elongating tip, which attaches the developing embryo to the substratum. Polyclonal antibodies to human vitronectin (Vn) recognize a vitronectin-like glycoprotein (Vn-F) in extracts of zygotes and two-celled embryos of Fucus, with a molecular mass (approximately 62 kDa) similar to that of human Vn. The specificity of the immunological cross-reactivity of Vn-F to rabbit polyclonal antibodies made to human Vn is demonstrated by competition experiments using pure human Vn and monospecific antibodies generated toward Vn-F. Vn-F possesses affinities for glass and heparin that are identical to those of human Vn. Immunolocalization and subcellular fractionation results demonstrate that Vn-F is localized first in the cytoplasm of the zygote, which is followed by the polar transport of Vn-F to its exclusive localization in the cell wall of the elongating rhizoid tip. Vn does not localize to the rhizoid tip under culture conditions that prevent two-celled embryos from attaching. Furthermore, an adhesion assay demonstrates that two-celled Fucus embryos do not adhere to the substratum in the presence of the Vn antibody, suggesting that the Vn-F in this brown alga not only possesses structural similarity to mammalian Vn but may also have a similar functional role in adhesion. The presence of Vn-F in brown algae suggests a high degree of evolutionary conservation of its structural and functional characteristics.</jats:p> Role of a vitronectin-like molecule in embryo adhesion of the brown alga Fucus. Proceedings of the National Academy of Sciences |
| spellingShingle | Wagner, V T, Brian, L, Quatrano, R S, Proceedings of the National Academy of Sciences, Role of a vitronectin-like molecule in embryo adhesion of the brown alga Fucus., Multidisciplinary |
| title | Role of a vitronectin-like molecule in embryo adhesion of the brown alga Fucus. |
| title_full | Role of a vitronectin-like molecule in embryo adhesion of the brown alga Fucus. |
| title_fullStr | Role of a vitronectin-like molecule in embryo adhesion of the brown alga Fucus. |
| title_full_unstemmed | Role of a vitronectin-like molecule in embryo adhesion of the brown alga Fucus. |
| title_short | Role of a vitronectin-like molecule in embryo adhesion of the brown alga Fucus. |
| title_sort | role of a vitronectin-like molecule in embryo adhesion of the brown alga fucus. |
| title_unstemmed | Role of a vitronectin-like molecule in embryo adhesion of the brown alga Fucus. |
| topic | Multidisciplinary |
| url | http://dx.doi.org/10.1073/pnas.89.8.3644 |