Evidence map›Paper›PMID 19397785›Full record

ArticleJournal of cellular and molecular medicine2009

Laminin isoforms in human embryonic stem cells: synthesis, receptor usage and growth support.

Sanna Vuoristo, Ismo Virtanen, Minna Takkunen, Jaan Palgi, Yamato Kikkawa, Patricia Rousselle, Kiyotoshi Sekiguchi, Timo Tuuri, Timo Otonkoski

Open access · bronzeAbstract read
In one paragraph

Article in Journal of cellular and molecular medicine, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

25 citing papers in PubMed, 50 citations in OpenAlex.

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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

9 authors at 4 institutions in 3 countries.

Sanna VuoristoBiomedicum Stem Cell Center, University of Helsinki, Helsinki, Finland.
Ismo VirtanenInstitute of Biomedicine/Anatomy, University of Helsinki, Helsinki, Finland.
Minna TakkunenInstitute of Biomedicine/Anatomy, University of Helsinki, Helsinki, Finland.
Jaan PalgiBiomedicum Stem Cell Center, University of Helsinki, Helsinki, Finland.
Yamato KikkawaLaboratory of Clinical Biochemistry, School of Pharmacy, Tokyo University of Pharmacy and Life Sciences, Hachioji, Tokyo, Japan.
Patricia RousselleInstitut de Biologie et Chimie des Protéines, Unité Mixte de Recherche, Institut Fédératif de Recherche BioSciences Lyon-Gerland, Lyon, France.
Kiyotoshi SekiguchiLaboratory of Extracellular Matrix Biochemistry, Institute for Protein Research, Osaka University, Suita, Osaka, Japan.
Timo TuuriBiomedicum Stem Cell Center, University of Helsinki, Helsinki, Finland.
Timo OtonkoskiBiomedicum Stem Cell Center, University of Helsinki, Helsinki, Finland.
University of Helsinki · FIInstitut de Biologie et de Chimie des Protéines · FRProtein Research Foundation · JPTokyo University of Pharmacy and Life Sciences · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

To reveal the functional intrinsic niche of human embryonic stem cells (hESC) we examined the production of basement membrane (BM) proteins and the presence of their receptors in feeder-free cell culture conditions. In addition, we investigated binding of hESCs to purified human BM proteins and identified the receptors mediating these contacts. Also, we tested whether purified human laminin (Lm) isoforms have a role in hESC self-renewal and growth in short-term cultures. The results show that hESCs synthesize Lm alpha(1) and Lm alpha(5) chains together with Lm beta(1) and gamma(1) chains suggesting the production of Lms-111 and -511 into the culture medium and deposits on cells. hESCs contain functionally important integrin (Int) subunits, Int beta(1), alpha(3), alpha(6), alpha(5), beta(5) and alpha(V), as well as the Lm alpha(5) receptor, Lutheran (Lu) glycoprotein and its truncated form, basal cell adhesion molecule (B-CAM). In cell adhesion experiments, Int beta(1) was crucial for adhesion to most of the purified human BM proteins. Lu/B-CAM mediated adhesion to Lm-511 together with Int alpha(3)beta(1), and was essential for the adhesion of hESCs to embryonic feeder cells. Adhesion to Lm-411 was mediated by Int alpha(6)beta(1). Lm-511 supported hESC growth in defined medium equally well as Matrigel. These results provide consequential information of the biological role of BM in hESCs, warranting further investigation of BM biology of human pluripotent stem cells.

Indexed as

Cells, CulturedCulture MediaEmbryonic Stem CellsFlow CytometryHumansImmunohistochemistryLamininProtein IsoformsReceptors, LamininReverse Transcriptase Polymerase Chain ReactionCulture MediaLamininProtein IsoformsReceptors, Laminin

Identifiers

PMID19397785
PMCPMC6529980
OpenAlexW2079745015

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.