A style‐specific hydroxyproline‐rich glycoprotein with properties of both extensins and arabinogalactan proteins

Lind, Jan; Bacic, Antony; Clarke, Adrienne E.; Anderson, Marilyn A.

doi:10.1046/j.1365-313x.1994.6040491.x

Cited by 111 publications

(77 citation statements)

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“…(Goldraij et al, 2006). The 120-kD glycoprotein (120K), another SI modifier, is an abundant S-RNase-binding protein located in the N. alata transmitting tract (Lind et al, 1994(Lind et al, , 1996Cruz-Garcia et al, 2005) that also is required for S-specific pollen rejection . More recently, NaStEP (N. alta Stigma Expressed Protein) was identified as a proteinase inhibitor that is required for SI and also affects HT protein stability (Busot et al, 2008;Jiménez-Durán et al, 2013).…”

Section: S-rnase-based Simentioning

confidence: 99%

Pollen-Pistil Interactions and Their Role in Mate Selection

et al. 2016

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Section: S-rnase-based Simentioning

confidence: 99%

Pollen-Pistil Interactions and Their Role in Mate Selection

et al. 2016

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“…[40][41][42] TFMS is particularly useful for removing plant glycans that are not removed by enzymatic deglycosylation. 29) After TFMS treatment, the molecular weight changes of rrhGM-CSF and yrhGM-CSF were determined by SDS-PAGE.…”

Section: Resultsmentioning

confidence: 99%

The Glycosylation and in Vivo Stability of Human Granulocyte-Macrophage Colony-Stimulating Factor Produced in Rice Cells

Kim

Lee

Kim

et al. 2008

Biological & Pharmaceutical Bulletin

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Recombinant human granulocyte-macrophage colony-stimulating factor (rhGM-CSF) has been produced in several different cell types, and has different properties depending on the production process used. There has been no report of glycosylation ratio or of the role of glycans for plant cells-derived rhGM-CSF. We investigated the terminal sialylation of rhGM-CSF produced in rice cells (rrhGM-CSF) using lectins. Glycosylation ratios of rrhGM-CSF and yeast-derived rhGM-CSF (yrhGM-CSF) were evaluated by chemical deglycosylation. After intravenous administration to rats, the clearance rates of rrhGM-CSF and yrhGM-CSF as well as deglycosylated forms of them were evaluated. In vitro bioactivities of rrhGM-CSF and yrhGM-CSF were measured in dose-and time-dependent manners. Although rrhGM-CSF does not have terminal sialic acids, the glycosylation ratio was two-fold higher than that of yrhGM-CSF, and rrhGM-CSF sustained longer than yrhGM-CSF in the blood circulation. Moreover, yrhGM-CSF and rrhGM-CSF have almost same bioactivity via dose-and time-dependent manners. Deglycosylated rrhGM-CSF was cleared faster than native forms, while deglycosylated yrhGM-CSF and yrhGM-CSF were similarly cleared in blood circulation. These results suggest that the glycans on rrhGM-CSF are superior to the glycans on yrhGM-CSF in terms of in vivo stability.

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“…20,29,30) This property of TFMS is useful for determining the glycosylation ratio of uncharacterized glycoproteins. [31][32][33] TFMS is particularly useful for removing plant glycans that are not removed by enzymatic deglycosylation. 20) After TFMS treatment, the molecular weight changes of rrhCTLA4Ig and crhCTLA4Ig were determined by non-reducing and reducing SDS-PAGE (Fig.…”

Section: Resultsmentioning

confidence: 99%

The Glycosylation and Pharmacokinetics of CTLA4Ig Produced in Rice Cells

Kim

2007

Biological & Pharmaceutical Bulletin

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Cytotoxic T-lymphocyte antigen 4-immunoglobulin (CTLA4Ig) is soluble version of the T-cell transmembrane glycoprotein receptor CTLA-4; it is a recombinant chimeric fusion protein consisting of the extracellular domain of human CTLA-4 and the Fc region (hinge, CH2 and CH3) of human IgG.1) CTLA4Ig has demonstrated immunosuppressive activity and the ability to induce immune tolerance in several in vivo animal models.2) It is produced as a disulfidelinked dimer. Hence it is a ca. 100 kDa dimer under nonreducing conditions, and a ca. 50 kDa monomer under reducing conditions.3) It has two potential N-glycosylation sites (Asn 78, Asn 111) in the CTLA-4 portion 4) and one (Asn 297) in the Fc portion. 5) Recently recombinant CTLA4Ig produced in Chinese hamster ovary (CHO) cells was approved by the US Food and Drug Administration (FDA).6) CHO cell-derived recombinant human CTLA4Ig (crhCTLA4Ig) has a2,3-linked sialic acids, and the terminal sialic acids are important for its in vivo stability. 7) Recombinant CTLA4Ig has also been produced in rice cells. 6,8) Production in transgenic plants has low investment and operating costs, 9,10) and downstream processing has obvious economic advantages over traditional fermentation methods because recombinant proteins can be produced in plants at 2-10% of the cost of microbial fermentation systems and at 0.1% of the cost of mammalian cell culture. 11,12) N-Linked glycans in plants have a core substituted by two N-acetylglucosamine (GlcNAc) residues, as observed in mammals. However, plant N-glycans lack galactose and terminal sialic acids, and have plant-specific a1,3-fucose and b1,6-xylose residues.13) The lack of terminal sialic acids in plant cellderived glycoproteins has limited their use as therapeutic agents.13) However, recent reports of Shah et al. 14) and Takashima et al. 15) revealed a possible genetic and enzymatic basis for sialylation in plants and thus the potential for terminal sialylation of glycoproteins. However, there has been no report concerning the terminal sialylation of plant cell-derived glycoproteins. There have been few attempts to produce CTLA4Ig in prokaryotes, and there is therefore no information about the in vivo stability and molecular weight of nonglycosylated CTLA4Ig.In this study, we analyzed the terminal sialylation of rice cell-derived recombinant human CTLA4Ig (rrhCTLA4Ig). After chemical deglycosylation, we determined the molecular weight of non-glycosylated CTLA4Ig and the glycosylation ratios of rrhCTLA4Ig and crhCTLA4Ig. We also evaluated the pharmacokinetics of rrhCTLA4Ig and crhCTLA4Ig as well as of their deglycosylated forms after intravenous (i.v.) and subcutaneous (s.c.) administration to rats. MATERIALS AND METHODSProteins rrhCTLA4Ig was expressed and purified as described in Lee et al. 6) crhCTLA4Ig was used as a control in the chemical deglycosylation and pharmacokinetic experiments. In the previous report of Jung et al. 8) and Lee et al.,6) it is known that rrhCTLA4Ig and crhCTLA4Ig have similar in vitro immunosuppressive activit...

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A style‐specific hydroxyproline‐rich glycoprotein with properties of both extensins and arabinogalactan proteins

Cited by 111 publications

References 0 publications

Pollen-Pistil Interactions and Their Role in Mate Selection

Pollen-Pistil Interactions and Their Role in Mate Selection

The Glycosylation and in Vivo Stability of Human Granulocyte-Macrophage Colony-Stimulating Factor Produced in Rice Cells

The Glycosylation and Pharmacokinetics of CTLA4Ig Produced in Rice Cells

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