Effects of Yariv phenylglycosides onRosa cell suspensions: Evidence for the involvement of arabinogalactan-proteins in cell proliferation

Serpe, Marcelo D.; Nothnagel, Eugene A.

doi:10.1007/bf02411560

Cited by 171 publications

(175 citation statements)

References 51 publications

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“…5) The -glucosyl Yariv reagent (-Yariv), 6) which has specific interaction with and inhibits the functions of AGPs, has been used to elucidate the functions of AGPs. -Yariv induces inhibition of cell division, 7) cell elongation, [8][9][10] cell proliferation, 11) and GA signal transduction. 12) In spite of the above-mentioned importance of AGPs, their definitive biological function(s) remain elusive, since neither the antibodies for immuno-staining experiments nor -Yariv for functional disturbance are specific to any single AGP.…”

mentioning

confidence: 99%

AtFLA11, a Fasciclin-Like Arabinogalactan-Protein, Specifically Localized in Screlenchyma Cells

Ito

Suzuki

Miyamoto

et al. 2005

Bioscience, Biotechnology, and Biochemistry

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confidence: 99%

AtFLA11, a Fasciclin-Like Arabinogalactan-Protein, Specifically Localized in Screlenchyma Cells

Ito

Suzuki

Miyamoto

et al. 2005

Bioscience, Biotechnology, and Biochemistry

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“…Another perturbation approach of growing popularity involves use of (␤-D-Glc) 3 Yariv phenylglycoside, a synthetic molecule that binds and precipitates AGPs. Experiments in which (␤-D-Glc) 3 has been applied to living plants or cells have yielded evidence of AGP action in cell proliferation (11), cell expansion (12,13), somatic embryogenesis (14), pollen tube growth (15), and cell death (16).…”

mentioning

confidence: 99%

Presence of a Glycosylphosphatidylinositol Lipid Anchor on Rose Arabinogalactan Proteins

Svetek¹,

Yadav

Nothnagel

1999

Journal of Biological Chemistry

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135

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Arabinogalactan proteins constitute a class of plant cell surface proteoglycans with widespread occurrence and suggested functions in various aspects of plant growth and development, including cell proliferation, expansion, marking, and death. Previous investigations of subcellular fractions from suspension-cultured cells of "Paul's Scarlet" rose (Rosa sp.) have revealed extensive structural similarity between some soluble arabinogalactan proteins from the cell wall space and some plasma membrane-associated arabinogalactan proteins, thus inspiring the present investigation of the mechanism through which these inherently water-soluble molecules are held on the plasma membrane. Several lines of evidence gained through a combination of methods including reversed-phase chromatography, treatment with phosphatidylinositol-specific phospholipase C, and chemical structural analysis now show that some rose arabinogalactan proteins carry a ceramide class glycosylphosphatidylinositol lipid anchor. The predominant form of the ceramide is composed of tetracosanoic acid and 4-hydroxysphinganine. Plasma membrane vesicles readily shed arabinogalactan proteins by an inherent mechanism that appears to involve a phospholipase. This finding has significance toward understanding the biosynthesis, localization, and function of arabinogalactan proteins and toward stimulating other studies that may expand the currently very short list of higher plant proteins found to carry such membrane lipid anchors.

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“…For example, Y(␤-Glc) 3 have inhibited the proliferation of suspension-cultured rose (Rosa spp.) cells, which suggested that AGPs function in cell division (Serpe and Nothnagel, 1994). The involvement of AGPs in the phytohormone function has also been suggested by the observation that Y(␤-Glc) 3 inhibited GA-promoted induction of ␣-amylase in barley (Hordeum vulgare) aleurone protoplasts (Suzuki et al, 2002).…”

mentioning

confidence: 90%

“…In addition, Y(␤-Glc) 3 has been used to disrupt the AGP function in living systems and has provided insight into the role of AGPs in planta (Serpe and Nothnagel, 1994;Jauh and Lord, 1996;Willats and Knox, 1996;Langan and Nothnagel, 1997). For example, Y(␤-Glc) 3 have inhibited the proliferation of suspension-cultured rose (Rosa spp.)…”

mentioning

confidence: 99%

CsAGP1, a Gibberellin-Responsive Gene from Cucumber Hypocotyls, Encodes a Classical Arabinogalactan Protein and Is Involved in Stem Elongation

et al. 2003

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Fluorescence differential display was used to isolate the gibberellin (GA)-responsive gene, CsAGP1, from cucumber (Cucumis sativus) hypocotyls. A sequence analysis of CsAGP1 indicated that the gene putatively encodes a "classical" arabinogalactan protein (AGP) in cucumber. Transgenic tobacco (Nicotiana tabacum) plants overexpressing CsAGP1 under the control of the cauliflower mosaic virus 35S promoter produced a Y(␤Glc) 3 -reactive proteoglycan in addition to AGPs present in wild-type tobacco plants. Immuno-dot blotting of the product, using anti-AGP antibodies, showed that the CsAGP1 protein had the AGP epitopes common to AGP families. The transcription level of CsAGP1 in cucumber hypocotyls increased in response not only to GA but also to indole-3-acetic acid. Although CsAGP1 is expressed in most vegetative tissues of cucumber, including the shoot apices and roots, the GA treatment resulted in an increase in the mRNA level of CsAGP1 only in the upper part of the hypocotyls. Y(␤Glc) 3 , which selectively binds AGPs, inhibited the hormone-promoted elongation of cucumber seedling hypocotyls. Transgenic plants ectopically expressing CsAGP1 showed a taller stature and earlier flowering than the wild-type plants. These observations suggest that CsAGP1 is involved in stem elongation.

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Effects of Yariv phenylglycosides onRosa cell suspensions: Evidence for the involvement of arabinogalactan-proteins in cell proliferation

Cited by 171 publications

References 51 publications

AtFLA11, a Fasciclin-Like Arabinogalactan-Protein, Specifically Localized in Screlenchyma Cells

AtFLA11, a Fasciclin-Like Arabinogalactan-Protein, Specifically Localized in Screlenchyma Cells

Presence of a Glycosylphosphatidylinositol Lipid Anchor on Rose Arabinogalactan Proteins

CsAGP1, a Gibberellin-Responsive Gene from Cucumber Hypocotyls, Encodes a Classical Arabinogalactan Protein and Is Involved in Stem Elongation

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