Evidence map›Paper›PMID 18174176›Full record

ArticleThe Journal of biological chemistry2008

Osteopontin regulates actin cytoskeleton and contributes to cell proliferation in primary erythroblasts.

Jeong-Ah Kang, Ying Zhou, Tahlia L Weis, Hui Liu, Jodie Ulaszek, Nilesh Satgurunathan, Li Zhou, Koen van Besien, John Crispino, Amit Verma and 2 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.6field-weighted citation impact, top 12% 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

28 citing papers in PubMed, 48 citations in OpenAlex.

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  12. Reduced DOCK4 expression leads to erythroid dysplasia in myelodysplastic syndromes.Proceedings of the National Academy of Sciences of the United States of America · 2015
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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

12 authors at 3 institutions in 1 country.

Jeong-Ah KangDepartment of Medicine, University of Chicago, Chicago, Illinois 60637, USA.
Ying Zhou
Tahlia L Weis
Hui Liu
Jodie Ulaszek
Nilesh Satgurunathan
Li Zhou
Koen van Besien
John Crispino
Amit Verma
Philip S Low
Amittha Wickrema
University of Chicago · USAlbert Einstein College of Medicine · USPurdue University West Lafayette · US

Funding

Studies of Erythrocyte Membrane StructureR01GM024417 · NIGMS · PURDUE UNIVERSITY WEST LAFAYETTE · PI LOW, PHILIP STEWART · 1985 to 2020
$5.4M
BIOPHYS STUD OF PROTEINS, NUCLEIC ACIDS, AND VIRUSEST32GM008296 · NIGMS · PURDUE UNIVERSITY WEST LAFAYETTE · PI STAUFFACHER, CYNTHIA VIANNE · 1989 to 2012
$2.2M
p38 MAPK--Therapeutic target in Myelodysplastic syndromeR01HL082946 · NHLBI · ALBERT EINSTEIN COL OF MED YESHIVA UNIV · PI VERMA, AMIT K. · 2005 to 2009
$1.7M
Transcriptional Regulation of Myeloma Cell GrowthR01CA098550 · NCI · UNIVERSITY OF CHICAGO · PI WICKREMA, AMITTHA · 2004 to 2008
$1.2M
NCI NIH HHS R01 CA098550NHLBI NIH HHS HL082946NHLBI NIH HHS R01 HL082946NIGMS NIH HHS R01 GM024417NIGMS NIH HHS T32 GM008296NIGMS NIH HHS T32-GM008296-17
6 · The paper itself

Abstract

Erythropoietin and stem cell factor are the key cytokines that regulate early stages of erythroid differentiation. However, it remains undetermined whether additional cytokines also play a role in the differentiation program. Here, we report that osteopontin (OPN) is highly expressed and secreted by erythroblasts during differentiation. We also demonstrate that OPN-deficient human and mouse erythroblasts exhibit defects in F-actin filaments, and addition of exogenous OPN to OPN-deficient erythroblasts restored the F-actin filaments in these cells. Furthermore, our studies demonstrate that OPN contributes to erythroblast proliferation. OPN knock-out male mice exhibit lower hematocrit and hemoglobin levels compared with their wild-type counterparts. We also show that OPN mediates phosphorylation or activation of multiple proteins including Rac-1 GTPase and the actin-binding protein, adducin, in human erythroblasts. In addition, we show that the OPN effects include regulation of intracellular calcium in human erythroblasts. Finally, we demonstrate that human erythroblasts express CD44 and integrins beta1 and alpha4, three known receptors for OPN, and that the integrin beta1 receptor is involved in transmitting the proliferative signal. Together these results provide evidence for signal transduction by OPN and contribution to multiple functions during the erythroid differentiation program in human and mouse.

Indexed as

Gene Expression RegulationActinsAnimalsCell DifferentiationCell ProliferationCytoskeletonErythrocytesHumansHyaluronan ReceptorsIntegrin alpha4Integrin beta1MaleMiceMice, KnockoutModels, BiologicalOsteopontinActinsHyaluronan ReceptorsIntegrin alpha4Integrin beta1OsteopontinStem Cell Factor

Identifiers

PMID18174176
PMCPMC3385928
OpenAlexW2038658082

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.