Evidence map›Paper›PMID 30610619›Full record

ArticleGenes & genomics2019

Identification and expression pattern of a new digestive invertebrate-type lysozyme from the earthworm.

Yun-Sang Yu, Ju-Young Lee, Ji-Won Woo, Jin-Se Kim, Yoon-Hwan Bae, Sung-Jin Cho, Soon Cheol Park

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Article in Genes & genomics, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.6field-weighted citation impact, top 29% 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

2 citing papers in PubMed, 8 citations in OpenAlex.

  1. Article
  2. Trophic Position of the White Worm (International journal of molecular sciences · 2024
    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

7 authors at 4 institutions in 1 country.

Yun-Sang YuSchool of Biological Sciences, Chungbuk National University, Cheongju, Chungbuk, 362-763, Republic of Korea.
Ju-Young LeeDepartment of Biomedical Engineering, College of Medical Convergence, Catholic Kwandong University, Gangneung, Republic of Korea.
Ji-Won WooDepartment of Life Sciences, Chung-Ang University, 221 Heukseok-dong, Dongjak-gu, Seoul, 156-756, Republic of Korea.
Jin-Se KimSchool of Biological Sciences, Chungbuk National University, Cheongju, Chungbuk, 362-763, Republic of Korea.
Yoon-Hwan BaeDivision of Life Sciences & Chemistry, Daejin University, Pocheon, Republic of Korea.
Sung-Jin ChoSchool of Biological Sciences, Chungbuk National University, Cheongju, Chungbuk, 362-763, Republic of Korea. sjchobio@cbnu.ac.kr.
Soon Cheol ParkDepartment of Life Sciences, Chung-Ang University, 221 Heukseok-dong, Dongjak-gu, Seoul, 156-756, Republic of Korea. scpark@cau.ac.kr.
Chungbuk National University · KRChung-Ang University · KRCatholic Kwandong University · KRDaejin University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundThe invertebrate type (i-type) lysozyme not showing a clear homology with the known types of lysozyme was first demonstrated from a marine bivalve, conch and earthworm by N-terminal sequence. An i-type lysozyme isolated from the earthworm found to be up-regulated upon bacterial challenge, suggesting this lysozyme to function as an inducible immune factor. However, information on the i-type lysozyme related with digestive function is very limited in the earthworm.

objectiveThe objective of this study is to investigate the molecular characteristics and function of the new i-type lysozyme from the earthworm.

methodsTo identify a new i-type lysozyme, multiple amino acid sequence alignment and phylogenetic analyses were employed. Its mRNA expression pattern was observed by fluorescent in situ hybridization (FISH).

resultsA new i-type lysozyme (Ea-iLys) from an earthworm, Eisenia andrei with the open reading frame of 678 bp (226 amino acid residues) appeared to comprise conserved 14 cysteine residues for disulfide bridges and amino acid residues for the enzyme activities of lysozyme and isopeptidase, of which mRNA expression is mainly localized in the lining of midgut epithelium. No significant expression signal was detected in immune competent sites such as chloragogue tissue, typhlosole region, body coelom and muscle layers.

conclusionOur results suggest that this enzyme primarily acts as a digestive enzyme rather than an innate immune factor.

Indexed as

AnimalsIntestinal MucosaMuramidaseMuscle, SkeletalOligochaetaMuramidaseDigestionEarthwormExpression patternInvertebrate-type lysozyme

Identifiers

PMID30610619
OpenAlexW2907345497

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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.