Evidence map›Paper›PMID 20807762›Full record

ArticleThe Journal of biological chemistry2010

Regulated secretion of acid sphingomyelinase: implications for selectivity of ceramide formation.

Russell W Jenkins, Daniel Canals, Jolanta Idkowiak-Baldys, Fabio Simbari, Patrick Roddy, David M Perry, Kazuyuki Kitatani, Chiara Luberto, Yusuf A Hannun

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
3.7field-weighted citation impact, top 6% 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, 111 citations in OpenAlex.

  1. Article
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  7. Review
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  12. Review
  13. Ceramide signaling in the gut.Molecular and cellular endocrinology · 2022
    Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Involvement of Ceramide Metabolism in Cerebral Ischemia.Frontiers in molecular biosciences · 2022
    Review
  19. Review
  20. Article
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

9 authors at 3 institutions in 3 countries.

Russell W JenkinsDepartment of Biochemistry and Molecular Biology, Medical University of South Carolina, Charleston, South Carolina 29425, USA.
Daniel Canals
Jolanta Idkowiak-Baldys
Fabio Simbari
Patrick Roddy
David M Perry
Kazuyuki Kitatani
Chiara Luberto
Yusuf A Hannun
Medical University of South Carolina · USInstitute of Advanced Chemistry of Catalonia · ESTottori University Hospital · JP

Funding

Translational Science Laboratory Shared ResourceP30CA138313 · NCI · MEDICAL UNIVERSITY OF SOUTH CAROLINA · PI RAYMOND N. DUBOIS · 2009 to 2026
$42.7M
Sphingolipids in Cancer Therapy and AngiogenesisP01CA097132 · NCI · STATE UNIVERSITY NEW YORK STONY BROOK · PI Daniel Canals · 2003 to 2026
$30.8M
TRAINING PROGRAM FOR MEDICAL SCIENTISTST32GM008716 · NIGMS · MEDICAL UNIVERSITY OF SOUTH CAROLINA · PI DEMORE, NANCY · 1999 to 2024
$9.3M
NCI NIH HHS 1P30 CA138313-01NCI NIH HHS P01 CA097132NCI NIH HHS P01CA97132NCI NIH HHS P30 CA138313NIGMS NIH HHS GM08716NIGMS NIH HHS T32 GM008716
6 · The paper itself

Abstract

The acid sphingomyelinase (aSMase) gene gives rise to two distinct enzymes, lysosomal sphingomyelinase (L-SMase) and secretory sphingomyelinase (S-SMase), via differential trafficking of a common protein precursor. However, the regulation of S-SMase and its role in cytokine-induced ceramide formation remain ill defined. To determine the role of S-SMase in cellular sphingolipid metabolism, MCF7 breast carcinoma cells stably transfected with V5-aSMase(WT) were treated with inflammatory cytokines. Interleukin-1β and tumor necrosis factor-α induced a time- and dose-dependent increase in S-SMase secretion and activity, coincident with selective elevations in cellular C(16)-ceramide. To establish a role for S-SMase, we utilized a mutant of aSMase (S508A) that is shown to retain L-SMase activity, but is defective in secretion. MCF7 expressing V5-aSMase(WT) exhibited increased S-SMase and L-SMase activity, as well as elevated cellular levels of specific long-chain and very long-chain ceramide species relative to vector control MCF7. Interestingly, elevated levels of only certain very long-chain ceramides were evident in V5-aSMase(S508A) MCF7. Secretion of the S508A mutant was also defective in response to IL-1β, as was the regulated generation of C(16)-ceramide. Taken together, these data support a crucial role for Ser(508) in the regulation of S-SMase secretion, and they suggest distinct metabolic roles for S-SMase and L-SMase.

Indexed as

Amino Acid SubstitutionBlotting, WesternCell Line, TumorCeramidesDose-Response Relationship, DrugExtracellular SpaceHEK293 CellsHumansInterleukin-1betaIntracellular SpaceLysosomesMutationReverse Transcriptase Polymerase Chain ReactionSerineSphingomyelin PhosphodiesteraseTime FactorsCeramidesInterleukin-1betaSerineSMPD1 protein, humanSphingomyelin PhosphodiesteraseTumor Necrosis Factor-alpha

Identifiers

PMID20807762
PMCPMC2975195
OpenAlexW2020466852

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.