Evidence map›Paper›PMID 19948721›Full record

ArticleThe Journal of biological chemistry2010

S-nitrosylation at cysteine 498 of c-Src tyrosine kinase regulates nitric oxide-mediated cell invasion.

Mohammad Aminur Rahman, Takeshi Senga, Satoko Ito, Toshinori Hyodo, Hitoki Hasegawa, Michinari Hamaguchi

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed
5.4field-weighted citation impact, top 4% 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

60 citing papers in PubMed, 105 citations in OpenAlex.

  1. Review
  2. Review
  3. Emerging Roles of YES1 in Cancer: The Putative Target in Drug Resistance.International journal of molecular sciences · 2024
    Review
  4. Article
  5. Article
  6. Targeting Nitric Oxide: Say NO to Metastasis.Clinical cancer research : an official journal of the American Association for Cancer Research · 2023
    Review
  7. Review
  8. Review
  9. Review
  10. Article
  11. S-Nitrosylation in Tumor Microenvironment.International journal of molecular sciences · 2021
    Review
  12. Review
  13. Review
  14. Nitric Oxide and S-Nitrosylation in Cancers: Emphasis on Breast Cancer.Breast cancer : basic and clinical research · 2020
    Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Computational Structural Biology ofFrontiers in oncology · 2018
    Review
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.

Mohammad Aminur RahmanFrom the Division of Cancer Biology, Nagoya University School of Medicine, Nagoya 466-8550, Japan.
Takeshi SengaFrom the Division of Cancer Biology, Nagoya University School of Medicine, Nagoya 466-8550, Japan. Electronic address: tsenga@med.nagoya-u.ac.jp.
Satoko ItoFrom the Division of Cancer Biology, Nagoya University School of Medicine, Nagoya 466-8550, Japan.
Toshinori HyodoFrom the Division of Cancer Biology, Nagoya University School of Medicine, Nagoya 466-8550, Japan.
Hitoki HasegawaFrom the Division of Cancer Biology, Nagoya University School of Medicine, Nagoya 466-8550, Japan.
Michinari HamaguchiFrom the Division of Cancer Biology, Nagoya University School of Medicine, Nagoya 466-8550, Japan. Electronic address: mhamagu@med.nagoya-u.ac.jp.
Nagoya University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nitric oxide (NO) plays a pivotal role in tumorigenesis, particularly with relation to cancer cell invasion and metastasis. NO can reversibly couple to cysteine thiols to form an S-nitrosothiol, which regulates the enzymatic activities of target proteins. c-Src is a tyrosine kinase that promotes cancer cell invasion and metastasis. Interestingly, c-Src can be activated by NO stimulation. However, mechanisms by which NO stimulates Src kinase activity have not been elucidated. We report here that NO causes S-nitrosylation of c-Src at cysteine 498 (Cys(498)) to stimulate its kinase activity. Cys(498) is conserved among Src family kinases, and Cys(506) of c-Yes, which corresponds to Cys(498) of c-Src, was also important for the NO-mediated activation of c-Yes. Estrogens may work synergistically with NO to induce the proliferation and migration of many kinds of breast cancer cells. For example, beta-estradiol induces the expression of endothelial nitric synthase and production of NO in MCF7 cells. We found that activation of c-Src in MCF7 cells by beta-estradiol stimulation was mediated by the S-nitrosylation of Cys(498). In addition, we report that disruption of E-cadherin junctions and enhancement of cell invasion by beta-estradiol stimulation was mediated by NO-dependent activation of c-Src. These results identify a novel signaling pathway that links NO and Src family kinases to cancer cell invasion and metastasis.

Indexed as

Cell MovementAmino Acid SequenceAnimalsBlotting, WesternCadherinsCell AdhesionCell Line, TumorCells, CulturedCysteineEstradiolHumansMiceMice, KnockoutMicroscopy, FluorescenceMolecular Sequence DataMutationCadherinsCysteineEstradiolFyn protein, mouseNitric OxideNitric Oxide DonorsProto-Oncogene Proteins c-fynProto-Oncogene Proteins c-yesS-Nitroso-N-Acetylpenicillaminesrc-Family KinasesYes1 protein, mouse

Identifiers

PMID19948721
PMCPMC2823522
OpenAlexW2036730547

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.