Evidence map›Paper›PMID 24489995›Full record

ArticleAmerican journal of translational research2014

Nuclear localization of catalytically active MMP-2 in endothelial cells and neurons.

Satyesh K Sinha, Kamlesh Asotra, Hiroyasu Uzui, Santosh Nagwani, Vivek Mishra, Tripathi B Rajavashisth

Open access · greenAbstract read
In one paragraph

Article in American journal of translational research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.8field-weighted citation impact, top 30% 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

11 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Article
  3. Novel Roles of MT1-MMP and MMP-2: Beyond the Extracellular Milieu.International journal of molecular sciences · 2022
    Review
  4. Article
  5. Article
  6. Review
  7. Review
  8. 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

6 authors at 1 institution in 1 country.

Satyesh K SinhaCardiometabolic Research Unit, Division of Endocrinology, Metabolism and Molecular Medicine, Charles R. Drew University of Medicine and Science Los Angeles, CA, USA.
Kamlesh AsotraCedars-Sinai Medical Center Los Angeles, California.
Hiroyasu UzuiCedars-Sinai Medical Center Los Angeles, California.
Santosh NagwaniMolecular Biology Unit, Institute of Medical Sciences, Banaras Hindu University Varanasi, India.
Vivek MishraMolecular Biology Unit, Institute of Medical Sciences, Banaras Hindu University Varanasi, India.
Tripathi B RajavashisthCardiometabolic Research Unit, Division of Endocrinology, Metabolism and Molecular Medicine, Charles R. Drew University of Medicine and Science Los Angeles, CA, USA ; Molecular Biology Unit, Institute of Medical Sciences, Banaras Hindu University Varanasi, India ; Omics Biotechnology, Inc. Lawndale, CA, USA.
Cedars-Sinai Medical Center · US

Funding

Sustaining Faculty Development & Community EngagementS21MD000103 · NIMHD · CHARLES R. DREW UNIVERSITY OF MED &SCI · PI CARLISLE, DAVID M · 2001 to 2015
$73.9M
Workshop for Junior Biostatisticians in Health ResearchU54MD007598 · NIMHD · CHARLES R. DREW UNIVERSITY OF MED & SCI · PI Piwen Wang · 2012 to 2026
$60.0M
ROLE OF M-CSF IN THE PATHOGENESIS OF ATHEROSCLEROSISR01HL051980 · NHLBI · CEDARS-SINAI MEDICAL CENTER · PI RAJAVASHISTH, TRIPATHI BYASMUNI · 2001 to 2004
$1.2M
M CSF AND THE PATHOGENESIS OF ATHEROSCLEROSISR29HL051980 · NHLBI · LA BIOMED RES INST/ HARBOR UCLA MED CTR · PI RAJAVASHISTH, TRIPATHI BYASMUNI · 1995 to 1998
–
NHLBI NIH HHS R01 HL051980NHLBI NIH HHS R29 HL051980NIMHD NIH HHS S21 MD000103NIMHD NIH HHS U54 MD007598
6 · The paper itself

Abstract

From microscopic organelles and sub-cellular domains to the level of whole tissues, organs, and body parts, living organisms must continuously maintain and renovate structural components. Matrix metalloproteinases (MMPs) comprise a family of over two dozen Zn-dependent endopeptidases thought to be primary effectors of extracellular tissue renewal and remodeling processes. Endogenous inhibitors, particularly the tissue inhibitors of MMPs (TIMPs), counteract MMP-2 proteolytic activity, but also participate in conversion of several pro-MMPs to proteolytically active forms. Numerous pathologies are characterized by imbalances in activities of MMPs relative to TIMPs. MMPs are synthesized and stored in cytoplasmic domains prior to secretion or expression in cell surface-associated form. Several proteases have been identified in cell nuclei, but their functions, regulation, and substrates remain largely unknown. Here we showed that the catalytically active gelatinase MMP-2 is expressed in nuclei of endothelial cells and neurons, but not in glial or Schwannoma cell lines, in a pattern resembling nuclear speckles, and colocalizes with TIMP-1.

Indexed as

catalytically active MMP-2endothelial cellsneuronsNuclear localization

Identifiers

PMID24489995
PMCPMC3902226
OpenAlexW47498231

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.