Evidence map›Paper›PMID 10092647›Full record

ArticleThe Journal of biological chemistry1999

Human pancreatic islets express mRNA species encoding two distinct catalytically active isoforms of group VI phospholipase A2 (iPLA2) that arise from an exon-skipping mechanism of alternative splicing of the transcript from the iPLA2 gene on chromosome 22q13.1.

Z Ma, X Wang, W Nowatzke, S Ramanadham, J Turk

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
7.6field-weighted citation impact, top 2% 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

49 citing papers in PubMed, 115 citations in OpenAlex.

  1. Article
  2. Association of Novel Pathogenic Variant (p. Ile366Asn) inInternational journal of molecular sciences · 2025
    Article
  3. The mechanism of allosteric regulation of calcium-independent phospholipase AProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  4. Differentiating human phospholipase ABiochimica et biophysica acta. Molecular and cell biology of lipids · 2024
    Article
  5. Article
  6. Review
  7. The natural history of infantile neuroaxonal dystrophy.Orphanet journal of rare diseases · 2020
    Article
  8. iPLABiochimica et biophysica acta. Molecular and cell biology of lipids · 2019
    Review
  9. Article
  10. Article
  11. Review
  12. Review of four major distinct types of human phospholipase AAdvances in biological regulation · 2018
    Review
  13. Review
  14. Membranes serve as allosteric activators of phospholipase A2, enabling it to extract, bind, and hydrolyze phospholipid substrates.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  15. Article
  16. Article
  17. Role of calcium-independent phospholipase A(2)β in human pancreatic islet β-cell apoptosis.American journal of physiology. Endocrinology and metabolism · 2012
    Article
  18. Article
  19. Article
  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

5 authors at 1 institution in 1 country.

Z MaMass Spectrometry Resource, Division of Endocrinology, Diabetes, and Metabolism, Department of Medicine, Washington University School of Medicine, St. Louis, Missouri 63110, USA.
X Wang
W Nowatzke
S Ramanadham
J Turk
Washington University in St. Louis · US

Funding

YOGA LIFESTYLE INTERVENTION REDUCES BLOOD PRESSURE IN HIV-INFECTED ADULTSP41RR000954 · NCRR · WASHINGTON UNIVERSITY · PI GROSS, MICHAEL L · 1985 to 2011
$16.0M
PHOSPHOLIPID-DERIVED MEDIATORS AND INSULIN SECRETIONR37DK034388 · NIDDK · WASHINGTON UNIVERSITY · PI TURK, JOHN W · 1993 to 2010
$4.9M
CALCIUM-INDEPENDENT PLA2BETA IN BETA-CELL APOPTOSISR01DK069455 · NIDDK · WASHINGTON UNIVERSITY · PI RAMANADHAM, SASANKA · 2004 to 2013
$2.7M
NCRR NIH HHS P41 RR000954NIDDK NIH HHS R01 DK069455NIDDK NIH HHS R37 DK034388NIDDK NIH HHS R37-DK-34388
6 · The paper itself

Abstract

An 85-kDa Group VI phospholipase A2 enzyme (iPLA2) that does not require Ca2+ for catalysis has recently been cloned from three rodent species. A homologous 88-kDa enzyme has been cloned from human B-lymphocyte lines that contains a 54-amino acid insert not present in the rodent enzymes, but human cells have not previously been observed to express catalytically active iPLA2 isoforms other than the 88-kDa protein. We have cloned cDNA species that encode two distinct iPLA2 isoforms from human pancreatic islet RNA and a human insulinoma cDNA library. One isoform is an 85-kDa protein (short isoform of human iPLA2 (SH-iPLA2)) and the other an 88-kDa protein (long isoform of human iPLA2 (LH-iPLA2)). Transcripts encoding both isoforms are also observed in human promonocytic U937 cells. Recombinant SH-iPLA2 and LH-iPLA2 are both catalytically active in the absence of Ca2+ and inhibited by a bromoenol lactone suicide substrate, but LH-iPLA2 is activated by ATP, whereas SH-iPLA2 is not. The human iPLA2 gene has been found to reside on chromosome 22 in region q13.1 and to contain 16 exons represented in the LH-iPLA2 transcript. Exon 8 is not represented in the SH-iPLA2 transcript, indicating that it arises by an exon-skipping mechanism of alternative splicing. The amino acid sequence encoded by exon 8 of the human iPLA2 gene is proline-rich and shares a consensus motif of PX5PX8HHPX12NX4Q with the proline-rich middle linker domains of the Smad proteins DAF-3 and Smad4. Expression of mRNA species encoding two active iPLA2 isoforms with distinguishable catalytic properties in two different types of human cells demonstrated here may have regulatory or functional implications about the roles of products of the iPLA2 gene in cell biologic processes.

Indexed as

Alternative SplicingChromosomes, Human, Pair 22ExonsAmino Acid SequenceBase SequenceCatalysisCell LineDNA, ComplementaryGroup VI Phospholipases A2HumansIn Situ Hybridization, FluorescenceIslets of LangerhansIsoenzymesMolecular Sequence DataPhospholipases APhospholipases A2DNA, ComplementaryGroup VI Phospholipases A2IsoenzymesPhospholipases APhospholipases A2PLA2G6 protein, humanRNA, Messenger

Identifiers

PMID10092647
PMCPMC3715997
OpenAlexW2013076235

What OpenQuestion holds

Texttitle and abstract
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.