Journal Article

Integrin-Like Proteins in the Pollen Tube: Detection, Localization and Function

Ying Sun, Hong Qian, Xiao-dong Xu, Ye Han, Long-fei Yen and Da-ye Sun

in Plant and Cell Physiology

Published on behalf of Japanese Society of Plant Physiologists

Volume 41, issue 10, pages 1136-1142
Published in print October 2000 | ISSN: 0032-0781
Published online October 2000 | e-ISSN: 1471-9053 | DOI: http://dx.doi.org/10.1093/pcp/pcd039
Integrin-Like Proteins in the Pollen Tube: Detection, Localization and Function

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The distribution of integrin-like proteins in the pollen tube was examined by immunofluorescent labeling and western blotting techniques using antibodies against human placenta integrin vitronectin receptor (VnR), and αV, β3 and β1 integrin subunits. Pseudocolor-coded confocal images showed intense immunostaining within 10 and 5 µm of the tip of the pollen tube in Lilium davidii and Nicotiana tabacum respectively. In both segments the site near the plasma membrane was labeled. Western blotting analyses revealed cross-reaction of anti-β3, anti-αV and anti-VnR with the proteins in the plasma membrane preparation of L. davidii and Hemerocallis citrina pollen tube. These studies provide evidence for the first time that the integrin-like protein is present in pollen tubes, and it may be mainly composed of αV and β3 subunits in lily pollen tubes. In a functional assay, neither anti-VnR antibody nor the Arg-Gly-Asp-Ser tetrapeptide inhibited pollen tube growth of N. tabacum in vitro, but both of them depressed tube growth on the stigma and in style under quasi in vivo culture conditions. The integrin-like proteins localized in the tip and periphery of the pollen tube appeared to play roles in growth of the pollen tube tip and interaction with the extracellular matrix of the style.

Keywords: Key words: Immunochemical detection/localization — Integrin-like protein (subunits) — Pollen tube — Tip growth.; Abbreviations: BK medium, Brewback and Kwack medium; ECM, extracellular matrix; FITC, fluorescein isothiocyanate; PM, plasma membrane; RGDS, Arg-Gly-Asp-Ser; RGES, Arg-Gly-Glu-Ser; Vn, vitronectin; VnR, vitronectin receptor.

Journal Article.  4354 words.  Illustrated.

Subjects: Biochemistry ; Molecular and Cell Biology ; Plant Sciences and Forestry

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