Evidence map›Paper›PMID 22539347›Full record

ArticleThe Journal of biological chemistry2012

Characterization of gut-associated cathepsin D hemoglobinase from tick Ixodes ricinus (IrCD1).

Daniel Sojka, Zdenek Franta, Helena Frantová, Pavla Bartosová, Martin Horn, Jana Váchová, Anthony J O'Donoghue, Alegra A Eroy-Reveles, Charles S Craik, Giselle M Knudsen and 4 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

21 citing papers in PubMed, 44 citations in OpenAlex.

  1. Article
  2. Article
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  4. The biotechnological potential of proteases from hematophagous arthropod vectors.Frontiers in cellular and infection microbiology · 2023
    Article
  5. Article
  6. Article
  7. Mialostatin, a Novel Midgut Cystatin fromInternational journal of molecular sciences · 2021
    Article
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  14. Review
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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

14 authors at 5 institutions in 2 countries.

Daniel SojkaFrom the Institute of Parasitology, Biology Centre of the Academy of Sciences of the Czech Republic, České Budějovice, CZ 370 05, Czech Republic.
Zdenek Franta
Helena Frantová
Pavla Bartosová
Martin Horn
Jana Váchová
Anthony J O'Donoghue
Alegra A Eroy-Reveles
Charles S Craik
Giselle M Knudsen
Conor R Caffrey
James H McKerrow
Michael Mares
Petr Kopácek
University of California, San Francisco · USInstitute of Parasitology · CZCzech Academy of Sciences · CZCzech Academy of Sciences, Biology Centre · CZCzech Academy of Sciences, Institute of Organic Chemistry and Biochemistry · CZ

Funding

UCSF IRACDA Scholars ProgramK12GM081266 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI Raymond M. Esquerra, HOLLY A. INGRAHAM · 2007 to 2026
$19.4M
Bio-Organic Biomedical Mass Spectromy ResourceP41GM103481 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI BURLINGAME, ALMA L · 2012 to 2015
$6.4M
NIGMS NIH HHS K12 GM081266NIGMS NIH HHS P41 GM103481
6 · The paper itself

Abstract

To identify the gut-associated tick aspartic hemoglobinase, this work focuses on the functional diversity of multiple Ixodes ricinus cathepsin D forms (IrCDs). Out of three encoding genes representing Ixodes scapularis genome paralogs, IrCD1 is the most distinct enzyme with a shortened propeptide region and a unique pattern of predicted post-translational modifications. IrCD1 gene transcription is induced by tick feeding and is restricted to the gut tissue. The hemoglobinolytic role of IrCD1 was further supported by immunolocalization of IrCD1 in the vesicles of tick gut cells. Properties of recombinantly expressed rIrCD1 are consistent with the endo-lysosomal environment because the zymogen is autoactivated and remains optimally active in acidic conditions. Hemoglobin cleavage pattern of rIrCD1 is identical to that produced by the native enzyme. The preference for hydrophobic residues at the P1 and P1' position was confirmed by screening a novel synthetic tetradecapeptidyl substrate library. Outside the S1-S1' regions, rIrCD1 tolerates most amino acids but displays a preference for tyrosine at P3 and alanine at P2'. Further analysis of the cleavage site location within the peptide substrate indicated that IrCD1 is a true endopeptidase. The role in hemoglobinolysis was verified with RNAi knockdown of IrCD1 that decreased gut extract cathepsin D activity by >90%. IrCD1 was newly characterized as a unique hemoglobinolytic cathepsin D contributing to the complex intestinal proteolytic network of mainly cysteine peptidases in ticks.

Indexed as

AnimalsArthropod ProteinsCathepsin DGenomeHemoglobinsIntestinesIxodesProtein Processing, Post-TranslationalRecombinant ProteinsTranscription, GeneticArthropod ProteinsCathepsin DHemoglobinsRecombinant Proteins

Identifiers

PMID22539347
PMCPMC3375538
OpenAlexW2042126350

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.