Evidence map›Paper›PMID 29140689›Full record

ArticleBiochemistry2017

Tissue Inhibitor of Metalloprotease-2 (TIMP-2): Bioprocess Development, Physicochemical, Biochemical, and Biological Characterization of Highly Expressed Recombinant Protein.

Anandã Chowdhury, Robert Brinson, Beiyang Wei, William G Stetler-Stevenson

Open access · greenAbstract readEvaluation Study
In one paragraph

Article in Biochemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed, 1 pooled it
0.6field-weighted citation impact, top 35% 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

14 citing papers in PubMed, 1 synthesis or guideline pooled it, 25 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Observational
  4. bioRxiv : the preprint server for biology · 2023
    Article
  5. Tissue inhibitors of metalloproteinases are proteolytic targets of matrix metalloproteinase 9.Matrix biology : journal of the International Society for Matrix Biology · 2023
    Article
  6. Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Review
  12. Article
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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

4 authors at 2 institutions in 1 country.

Anandã ChowdhuryRadiation Oncology Branch, Center for Cancer Research, National Cancer Institute , Bethesda, Maryland 20892, United States.ORCID http://orcid.org/0000-0002-2016-3697
Robert BrinsonInstitute for Bioscience and Biotechnology Research, National Institute of Standards and Technology and University of Maryland , 9600 Gudelsky Drive, Rockville, Maryland 20850, United States.
Beiyang WeiRadiation Oncology Branch, Center for Cancer Research, National Cancer Institute , Bethesda, Maryland 20892, United States.
William G Stetler-StevensonRadiation Oncology Branch, Center for Cancer Research, National Cancer Institute , Bethesda, Maryland 20892, United States.ORCID http://orcid.org/0000-0002-5500-5808
National Cancer Institute · USNational Institute of Standards and Technology · US

Funding

Preclinical development of TIMP-2 as a biologic therapy for cancerZIABC011204 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI STETLER-STEVENSON, WILLIAM · 2009 to 2024
$14.5M
The Role of TIMPs in Cell Growth, Tumor Progression and MetastasisZIASC009179 · NCI · DIVISION OF CLINICAL SCIENCES - NCI · PI STETLER-STEVENSON, WILLIAM · 2009 to 2024
$9.7M
Tissue Inhibitors of Metalloproteinases: Regulation of CZ01SC009179 · SC · DIVISION OF CLINICAL SCIENCES - NCI · PI STETLER-STEVENSON, WILLIAM G · 1996 to 2008
$3.4M
Intramural NIH HHS Z01 SC009179
6 · The paper itself

Abstract

Tissue inhibitor of metalloprotease-2 (TIMP-2) is a secreted 21 kDa multifunctional protein first described as an endogenous inhibitor of matrix metalloproteinases (MMPs) that prevents breakdown of the extracellular matrix often observed in chronic diseases. TIMP-2 diminishes the level of growth factor-mediated cell proliferation in vitro, as well as neoangiogenesis and tumor growth in vivo independent of its MMP inhibitory activity. These physiological properties make TIMP-2 an excellent candidate for further preclinical development as a biologic therapy of cancer. Here we present a straightforward bioprocessing methodology that yields >35 mg/L recombinant human TIMP-2 6XHis-tagged protein (rhTIMP-2) from suspension cultures of HEK-293-F cells. Enhanced rhTIMP-2-6XHis yields were achieved by optimization of both TIMP-2 cDNA codon sequence and cell culture conditions. Using a two-step chromatographic process, we achieved >95% purity with minimal processing losses. Purified rhTIMP-2-6XHis was free of mouse antigen contamination. Circular dichroism spectroscopy indicated a well-folded rhTIMP-2-6XHis that is highly stable and refractory to pH changes. Two-dimensional heteronuclear single-quantum coherence nuclear magnetic resonance of full length rhTIMP-2-6XHis also indicated a monodisperse, well-folded protein preparation. Purified rhTIMP-2-6XHis inhibited MMP-2 enzymatic activity in a dose-dependent fashion with an IC

Indexed as

AnimalsCell ProliferationHEK293 CellsHumansMiceNeoplasmsProtein EngineeringProtein FoldingRecombinant ProteinsTissue Inhibitor of Metalloproteinase-2Recombinant ProteinsTIMP2 protein, humanTissue Inhibitor of Metalloproteinase-2

Identifiers

PMID29140689
PMCPMC6322544
OpenAlexW2770283545

What OpenQuestion holds

Textmetadata
LicenceTDM
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.