Evidence map›Paper›PMID 25059665›Full record

ArticleThe Journal of biological chemistry2014

Binding of tissue-type plasminogen activator to the glucose-regulated protein 78 (GRP78) modulates plasminogen activation and promotes human neuroblastoma cell proliferation in vitro.

Mario Gonzalez-Gronow, Cristian Farias Gomez, Gustaaf G de Ridder, Rupa Ray, Salvatore V Pizzo

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.4field-weighted citation impact, top 22% 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

9 citing papers in PubMed, 18 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

5 authors at 2 institutions in 2 countries.

Mario Gonzalez-GronowFrom the Department of Biological Sciences, Laboratory of Environmental Neurotoxicology Faculty of Medicine, Universidad Católica del Norte, Coquimbo 1781421, Chile and the Department of Pathology, Duke University, Medical Center, Durham, North Carolina 27710 gonza002@mc.duke.edu.
Cristian Farias GomezFrom the Department of Biological Sciences, Laboratory of Environmental Neurotoxicology Faculty of Medicine, Universidad Católica del Norte, Coquimbo 1781421, Chile and.
Gustaaf G de Ridderthe Department of Pathology, Duke University, Medical Center, Durham, North Carolina 27710.
Rupa Raythe Department of Pathology, Duke University, Medical Center, Durham, North Carolina 27710.
Salvatore V Pizzothe Department of Pathology, Duke University, Medical Center, Durham, North Carolina 27710.
Duke University · USUniversidad Católica del Norte · CL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The glucose-regulated protein 78 (GRP78) is a plasminogen (Pg) receptor on the cell surface. In this study, we demonstrate that GRP78 also binds the tissue-type plasminogen activator (t-PA), which results in a decrease in K(m) and an increase in the V(max) for both its amidolytic activity and activation of its substrate, Pg. This results in accelerated Pg activation when GRP78, t-PA, and Pg are bound together. The increase in t-PA activity is the result of a mechanism involving a t-PA lysine-dependent binding site in the GRP78 amino acid sequence (98)LIGRTWNDPSVQQDIKFL(115). We found that GRP78 is expressed on the surface of neuroblastoma SK-N-SH cells where it is co-localized with the voltage-dependent anion channel (VDAC), which is also a t-PA-binding protein in these cells. We demonstrate that both Pg and t-PA serve as a bridge between GRP78 and VDAC bringing them together to facilitate Pg activation. t-PA induces SK-N-SH cell proliferation via binding to GRP78 on the cell surface. Furthermore, Pg binding to the COOH-terminal region of GRP78 stimulates cell proliferation via its microplasminogen domain. This study confirms previous findings from our laboratory showing that GRP78 acts as a growth factor-like receptor and that its association with t-PA, Pg, and VDAC on the cell surface may be part of a system controlling cell growth.

Indexed as

Cell ProliferationAmidohydrolasesAmino Acid SequenceCell Line, TumorCell MembraneEndoplasmic Reticulum Chaperone BiPEnzyme ActivationHeat-Shock ProteinsHumansImmunoblottingKineticsMicroscopy, FluorescenceMolecular Sequence DataNeuroblastomaPlasminogenProtein BindingAmidohydrolasesEndoplasmic Reticulum Chaperone BiPHeat-Shock ProteinsHSPA5 protein, humanPlasminogenTissue Plasminogen ActivatorVoltage-Dependent Anion ChannelsBrainBrain PhysiologyCell ProliferationGRP78KineticsNeurochemistryPg ActivationProtein Foldingt-PA

Identifiers

PMID25059665
PMCPMC4155680
OpenAlexW2014705302

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.