Evidence map›Paper›PMID 22908220›Full record

ArticleThe Journal of biological chemistry2012

Polysialylation of the synaptic cell adhesion molecule 1 (SynCAM 1) depends exclusively on the polysialyltransferase ST8SiaII in vivo.

Manuela Rollenhagen, Sarah Kuckuck, Christina Ulm, Maike Hartmann, Sebastian P Galuska, Rudolf Geyer, Hildegard Geyer, Martina Mühlenhoff

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.6field-weighted citation impact, top 19% 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

19 citing papers in PubMed, 44 citations in OpenAlex.

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  9. Polysialylation at Early Stages of Oligodendrocyte Differentiation Promotes Myelin Repair.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2017
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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 2 institutions in 1 country.

Manuela RollenhagenInstitute of Cellular Chemistry, Hannover Medical School, 30625 Hannover, Germany.
Sarah KuckuckInstitute of Cellular Chemistry, Hannover Medical School, 30625 Hannover, Germany.
Christina UlmInstitute of Biochemistry, Faculty of Medicine, University of Giessen, 35392 Giessen, Germany.
Maike HartmannInstitute of Cellular Chemistry, Hannover Medical School, 30625 Hannover, Germany.
Sebastian P GaluskaInstitute of Biochemistry, Faculty of Medicine, University of Giessen, 35392 Giessen, Germany.
Rudolf GeyerInstitute of Biochemistry, Faculty of Medicine, University of Giessen, 35392 Giessen, Germany.
Hildegard GeyerInstitute of Biochemistry, Faculty of Medicine, University of Giessen, 35392 Giessen, Germany.
Martina MühlenhoffInstitute of Cellular Chemistry, Hannover Medical School, 30625 Hannover, Germany. Electronic address: muehlenhoff.martina@mh-hannover.de.
Medizinische Hochschule Hannover · DEUniversity of Giessen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Polysialic acid is a unique carbohydrate polymer specifically attached to a limited number of glycoproteins. Among them is synaptic cell adhesion molecule 1 (SynCAM 1), a member of the immunoglobulin (Ig) superfamily composed of three extracellular Ig-like domains. Polysialylation of SynCAM 1 is cell type-specific and was exclusively found in NG2 cells, a class of multifunctional progenitor cells that form specialized synapses with neurons. Here, we studied the molecular requirements for SynCAM 1 polysialylation. Analysis of mice lacking one of the two polysialyltransferases, ST8SiaII or ST8SiaIV, revealed that polysialylation of SynCAM 1 is exclusively mediated by ST8SiaII throughout postnatal brain development. Alternative splicing of the three variable exons 8a, 8b, and 8c can theoretically give rise to eight transmembrane isoforms of SynCAM 1. We detected seven transcript variants in the developing mouse brain, including three variants containing exon 8c, which was so far regarded as a cryptic exon in mice. Polysialylation of SynCAM 1 was restricted to four isoforms in perinatal brain. However, cell culture experiments demonstrated that all transmembrane isoforms of SynCAM 1 can be polysialylated by ST8SiaII. Moreover, analysis of domain deletion constructs revealed that Ig1, which harbors the polysialylation site, is not sufficient as an acceptor for ST8SiaII. The minimal polypeptide required for polysialylation contained Ig1 and Ig2, suggesting an important role for Ig2 as a docking site for ST8SiaII.

Indexed as

Alternative SplicingAnimalsBase SequenceBrainCell Adhesion Molecule-1Cell Adhesion MoleculesCell LineImmunoglobulinsMiceMice, KnockoutMolecular Sequence DataNerve Tissue ProteinsNeural Stem CellsNeuronsProtein IsoformsSialyltransferasesCadm1 protein, mouseCell Adhesion Molecule-1Cell Adhesion MoleculesCMP-N-acetylneuraminate-poly-alpha-2,8-sialosyl sialyltransferaseImmunoglobulinsNerve Tissue ProteinsProtein IsoformsSialyltransferases

Identifiers

PMID22908220
PMCPMC3471733
OpenAlexW2039974348

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.