Evidence map›Paper›PMID 16632592›Full record

ArticlePlant physiology2006

The intracellular fate of a recombinant protein is tissue dependent.

Georgia Drakakaki, Sylvain Marcel, Elsa Arcalis, Friedrich Altmann, Pablo Gonzalez-Melendi, Rainer Fischer, Paul Christou, Eva Stoger

Open access · bronzeAbstract read
In one paragraph

Article in Plant physiology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
9.6field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

30 citing papers in PubMed, 83 citations in OpenAlex.

  1. Cell Biology Methods to Study Recombinant Proteins in Seeds.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  2. Review
  3. Glyco-Engineering of Plant-Based Expression Systems.Advances in biochemical engineering/biotechnology · 2021
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 4 institutions in 2 countries.

Georgia DrakakakiInstitute for Molecular Biotechnology, Biology VII, Aachen University, 52074 Aachen, Germany.
Sylvain Marcel
Elsa Arcalis
Friedrich Altmann
Pablo Gonzalez-Melendi
Rainer Fischer
Paul Christou
Eva Stoger
Universitat de Lleida · ESBOKU University · ATCentro de Investigaciones Biológicas Margarita Salas · ESConsejo Superior de Investigaciones Científicas · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Recombinant proteins directed to the secretory pathway in plants require a signal peptide for entry into the endoplasmic reticulum. In the absence of further targeting information, such proteins are generally secreted via the default pathway to the apoplast. This has been well documented in protoplasts and leaf tissue, but the trafficking of recombinant proteins in seeds and other storage tissues has rarely been investigated. We used Aspergillus niger phytase as a model glycoprotein to compare the intracellular fate of a recombinant protein in the leaves and seeds of rice (Oryza sativa). Using fluorescence and electron microscopy we showed that the recombinant protein was efficiently secreted from leaf cells as expected. In contrast, within endosperm cells it was retained in endoplasmic reticulum-derived prolamin bodies and protein storage vacuoles. Consistent with our immunolocalization data, the phytase produced in endosperm cells possessed oligomannose and vacuolar-type N-glycans [Man(3)(Xyl)(Fuc)GlcNAc(2)], whereas the phytase produced in leaves contained predominantly secretion-type N-glycans [GlcNAc(2)Man(3)(Xyl)(Fuc)GlcNAc(2)]. The latter could not be detected in preparations of the endosperm-derived phytase. Our results show that the intracellular deposition and modification of a recombinant protein is tissue dependent.

Indexed as

6-PhytaseBase SequenceDNA PrimersEndoplasmic ReticulumIn Situ HybridizationMicroscopy, ElectronMicroscopy, FluorescenceMolecular WeightOryzaPlant LeavesPlant ProteinsPlants, Genetically ModifiedRecombinant ProteinsRNA, MessengerSeeds6-PhytaseDNA PrimersPlant ProteinsRecombinant ProteinsRNA, Messenger

Identifiers

PMID16632592
PMCPMC1475444
OpenAlexW2112722344

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.