Evidence map›Paper›PMID 9371713›Full record

ArticleThe Biochemical journal1997

Characterization of five different proteins produced by alternatively spliced mRNAs from the human cAMP-specific phosphodiesterase PDE4D gene.

G B Bolger, S Erdogan, R E Jones, K Loughney, G Scotland, R Hoffmann, I Wilkinson, C Farrell, M D Houslay

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The Biochemical journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed
5.3field-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

62 citing papers in PubMed, 185 citations in OpenAlex.

  1. Review
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  3. Review
  4. Article
  5. Interaction betweenExperimental biology and medicine (Maywood, N.J.) · 2019
    Article
  6. Small-molecule allosteric activators of PDE4 long form cyclic AMP phosphodiesterases.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  7. Article
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  16. Article
  17. Review
  18. Exome sequencing identifies PDE4D mutations in acrodysostosis.American journal of human genetics · 2012
    Article
  19. Article
  20. Article

2 more citing papers are in PubMed but not listed here.

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 2 countries.

G B BolgerDepartment of Veterans Affairs Medical Center, 151M, and Huntsman Cancer Institute, Department of Oncologic Sciences and Department of Medicine (Hematology/Oncology) University of Utah Health Sciences Center, Salt Lake City, UT 84148, USA.
S Erdogan
R E Jones
K Loughney
G Scotland
R Hoffmann
I Wilkinson
C Farrell
M D Houslay
University of Glasgow · GBEKOS Corporation · USHuntsman Cancer Institute · US

Funding

UTAH REGIONAL CANCER CENTERP30CA042014 · NCI · UTAH STATE HIGHER EDUCATION SYSTEM--UNIVERSITY OF UTAH · PI KATHARINE S ULLMAN · 1986 to 2026
$72.6M
NCI NIH HHS 5-PO-CA42014Wellcome Trust
6 · The paper itself

Abstract

We have isolated and characterized complete cDNAs for two isoforms (HSPDE4D4 and HSPDE4A5) encoded by the human PDE4D gene, one of four genes that encode cAMP-specific rolipram-inhibited 3',5'-cyclic nucleotide phosphodiesterases (type IVPDEs; PDE4 family). The HSPDE4D4 and HSPDE4D5 cDNAs encode proteins of 810 and 746 amino acids respectively. A comparison of the nucleotide sequences of these two cDNAs with those encoding the three other human PDE4D proteins (HSPDE4D1, HSPDE4D2 and HSPDE4D3) demonstrates that each corresponding mRNA transcript has a unique region of sequence at or near its 5'-end, consistent with alternative mRNA splicing. Transient expression of the five cDNAs in monkey COS-7 cells produced proteins of apparent molecular mass under denaturing conditions of 68, 68, 95, 119 and 105 kDa for isoforms HSPDE4D1-5 respectively. Immunoblotting of human cell lines and rat brain demonstrated the presence of species that co-migrated with the proteins produced in COS-7 cells. COS-cell-expressed and native HSPDE4D1 and HSPDE4D2 were found to exist only in the cytosol, whereas HSPDE4D3, HSPDE4D4 and HSPDE4D5 were found in both cytosolic and particulate fractions. The IC50 values for the selective PDE4 inhibitor rolipram for the cytosolic forms of the five enzymes were similar (0.05-0.14 microM), whereas they were 2-7-fold higher for the particulate forms of HSPDE4D3 and HSPDE4D5 (0.32 and 0.59 microM respectively), than for the corresponding cytosolic forms. Our data indicate that the N-terminal regions of the HSPDE4D3, HSPDE4D4 and HSPDE4D5 proteins, which are derived from alternatively spliced regions of their mRNAs, are important in determining their subcellular localization, activity and differential sensitivity to inhibitors.

Indexed as

Alternative Splicing3',5'-Cyclic-AMP PhosphodiesterasesAmino Acid SequenceCell CompartmentationCloning, MolecularCyclic AMPCyclic Nucleotide Phosphodiesterases, Type 3Cyclic Nucleotide Phosphodiesterases, Type 4CytosolDNA, ComplementaryHeLa CellsHumansIsoenzymesMolecular Sequence DataPhosphodiesterase InhibitorsPyrrolidinones3',5'-Cyclic-AMP PhosphodiesterasesCyclic AMPCyclic Nucleotide Phosphodiesterases, Type 3Cyclic Nucleotide Phosphodiesterases, Type 4DNA, ComplementaryIsoenzymesPDE4D protein, humanPhosphodiesterase InhibitorsPyrrolidinonesRNA, MessengerRolipram

Identifiers

PMID9371713
PMCPMC1218953
OpenAlexW1959359615

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.