Evidence map›Paper›PMID 31630284›Full record

ArticleClinical & experimental metastasis2020

Selective loss of phosphoserine aminotransferase 1 (PSAT1) suppresses migration, invasion, and experimental metastasis in triple negative breast cancer.

Stephanie Metcalf, Susan Dougherty, Traci Kruer, Nazarul Hasan, Rumeysa Biyik-Sit, Lindsey Reynolds, Brian F Clem

Abstract read
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In one paragraph

Article in Clinical & experimental metastasis, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

36 citing papers in PubMed, 72 citations in OpenAlex.

  1. Regulation of PSAT1 and PHGDH by m6A in endocrine-resistant breast cancer cells.Biochimica et biophysica acta. Molecular basis of disease · 2026
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  11. Review
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  14. Overexpression of Phosphoserine Aminotransferase (Plants (Basel, Switzerland) · 2024
    Article
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  16. Article
  17. Article
  18. Review
  19. 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

7 authors at 1 institution in 1 country.

Stephanie MetcalfDepartment of Biochemistry and Molecular Genetics, University of Louisville, Louisville, KY, USA.
Susan DoughertyDepartment of Biochemistry and Molecular Genetics, University of Louisville, Louisville, KY, USA.
Traci KruerDepartment of Biochemistry and Molecular Genetics, University of Louisville, Louisville, KY, USA.
Nazarul HasanDepartment of Biochemistry and Molecular Genetics, University of Louisville, Louisville, KY, USA.
Rumeysa Biyik-SitDepartment of Biochemistry and Molecular Genetics, University of Louisville, Louisville, KY, USA.
Lindsey ReynoldsDepartment of Biochemistry and Molecular Genetics, University of Louisville, Louisville, KY, USA.
Brian F ClemDepartment of Biochemistry and Molecular Genetics, University of Louisville, Louisville, KY, USA. bfclem01@louisville.edu.ORCID http://orcid.org/0000-0002-9082-8914
University of Louisville · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Breast cancer is the second leading cause of cancer-related deaths among women and 90% of these mortalities can be attributed to progression to metastatic disease. In particular, triple negative breast cancer (TNBC) is extremely aggressive and frequently metastasizes to multiple organs. As TNBCs are categorized by their lack of hormone receptors, these tumors are very heterogeneous and are immune to most targeted therapies. Metabolic changes are observed in the majority of TNBC and a large proportion upregulate enzymes within the serine synthesis pathway, including phosphoserine aminotransferase 1 (PSAT1). In this report, we investigate the role of PSAT1 in migration and invasion potential in a subset of TNBC cell types. We found that the expression of PSAT1 increases with TNBC clinical grade. We also demonstrate that suppression of PSAT1 or phosphoglycerate dehydrogenase (PHGDH) does not negatively impact cell proliferation in TNBC cells that are not dependent on de novo serine synthesis. However, we observed that suppression of PSAT1 specifically alters the F-actin cytoskeletal arrangement and morphology in these TNBC cell lines. In addition, suppression of PSAT1 inhibits motility and migration in these TNBC cell lines, which is not recapitulated upon loss of PHGDH. PSAT1 silencing also reduced the number of lung tumor nodules in a model of experimental metastasis; yet did not decrease anchorage-independent growth. Together, these results suggest that PSAT1 functions to drive migratory potential in promoting metastasis in select TNBC cells independent of its role in serine synthesis.

Indexed as

AnimalsBreastCell Line, TumorCell MovementCell ProliferationFemaleGene Expression Regulation, NeoplasticGene Knockdown TechniquesHumansLungLung NeoplasmsMiceNeoplasm GradingNeoplasm InvasivenessPhosphoglycerate DehydrogenaseRNA, Small InterferingPhosphoglycerate Dehydrogenasephosphoserine aminotransferaseRNA, Small InterferingTransaminasesMetastasisPSAT1Serine synthesisTriple negative breast cancer

Identifiers

PMID31630284
OpenAlexW2981044279

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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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.