Evidence map›Paper›PMID 20624920›Full record

ArticleThe Journal of biological chemistry2010

Analysis of mutually exclusive alternatively spliced serpin-1 isoforms and identification of serpin-1 proteinase complexes in Manduca sexta hemolymph.

Emily J Ragan, Chunju An, Celeste T Yang, Michael R Kanost

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 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.0field-weighted citation impact, top 24% 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

16 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Serpins in arthropod biology.Seminars in cell & developmental biology · 2017
    Review
  7. Article
  8. 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

4 authors at 1 institution in 1 country.

Emily J RaganDepartment of Biochemistry, Kansas State University, Manhattan, Kansas 66506, USA.
Chunju An
Celeste T Yang
Michael R Kanost
Kansas State University · US

Funding

UNDERGRADUATE RESEARCH AND TRAININGP20RR016464 · NCRR · UNIVERSITY OF NEVADA RENO · PI REIBER, CARL · 2001 to 2011
$30.3M
Supplement 2 to promote diversity in health related res.: protease systems in insR37GM041247 · NIGMS · KANSAS STATE UNIVERSITY · PI KANOST, MICHAEL R · 2011 to 2020
$3.8M
SERINE PROTEINASE INHIBITORS IN INSECTSR01GM041247 · NIGMS · KANSAS STATE UNIVERSITY · PI KANOST, MICHAEL R · 1994 to 2010
$3.1M
UAB Biostatistics Pre-doctoral Training ProgramT32HL079888 · NHLBI · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI ALLISON, DAVID B, CUTTER, GARY R · 2005 to 2014
$2.3M
SERINE PROTEINASE INHIBITORS IN INSECTSR29GM041247 · NIGMS · UNIVERSITY OF ARIZONA · PI KANOST, MICHAEL R. · 1989 to 1993
–
NCRR NIH HHS P20 RR016464NHLBI NIH HHS T32 HL079888NIGMS NIH HHS GM41247NIGMS NIH HHS R01 GM041247NIGMS NIH HHS R37 GM041247
6 · The paper itself

Abstract

Mutually exclusive alternative splicing produces transcripts for 12 serpin-1 isoforms in Manduca sexta that differ only in the region encoding the carboxyl-terminal 36-40-amino acid residues. This variable region includes the reactive center loop, which determines the inhibitory selectivity of the serpin. We investigated mRNA levels of individual serpin-1 isoforms by quantitative PCR. The 12 isoforms were expressed at similar levels in hemocytes, but in fat body isoform B mRNA was present at significantly higher levels than isoforms C, D, E, F, G, J, K, and Z. To investigate the presence of individual serpin-1 isoforms in plasma we used immunoaffinity purification of serpin-1 isoforms from M. sexta plasma, followed by two-dimensional PAGE and identification of protein spots by digestion with a series of proteinases and analysis of the resulting peptides by MALDI-TOF/TOF. We identified nine of the 12 serpin-1 isoforms and, through analysis of putative serpin-1-proteinase complexes, identified three endogenous M. sexta proteinase targets of serpin-1. Our results suggest that M. sexta serpin-1 isoforms A, E, and J can inhibit hemolymph proteinase 8, which activates the cytokine spätzle. At least one isoform of serpin-1 can inhibit hemocyte proteinase 1, another M. sexta blood proteinase. In addition, a complex of serpin-1K in a complex with M. sexta midgut chymotrypsin was identified, suggesting serpin-1 isoforms may also function to protect insect tissues from digestive proteinases that may leak into the hemocoel.

Indexed as

Alternative SplicingAmino Acid SequenceAnimalsElectrophoresis, Gel, Two-DimensionalHemolymphInsect ProteinsManducaMolecular Sequence DataPolymerase Chain ReactionProtein IsoformsProtein Structure, SecondarySequence Homology, Amino AcidSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationInsect ProteinsProtein Isoforms

Identifiers

PMID20624920
PMCPMC2937995
OpenAlexW2081404840

What OpenQuestion holds

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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.