Evidence map›Paper›PMID 40106538›Full record

ArticleBiology open2025

Insights into Octopus maya cathepsins from metatranscriptome and genome: structure evolutionary relationships and functional role prediction in digestive processes.

Daisy Pineda-Suazo, Francisco Guillén-Chable, Wendy Itzel Escobedo-Hinojosa, Clara E Galindo-Sánchez, Carlos Rosas

Abstract read
In one paragraph

Article in Biology open, 2025. 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
–field-weighted citation impact
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.

  1. Tissue-Specific Gene Expression of Digestive Tract Glands inAnimals : an open access journal from MDPI · 2025
    Article
  2. 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.

Daisy Pineda-SuazoUnidad Multidisciplinaria de Docencia e Investigación, Facultad de Ciencias UNAM, Puerto de abrigo s/n Sisal, Mpio, Hunucmá, Yucatán 97356, México.ORCID 0000-0002-8939-0687
Francisco Guillén-ChableUnidad Multidisciplinaria de Docencia e Investigación, Facultad de Ciencias UNAM, Puerto de abrigo s/n Sisal, Mpio, Hunucmá, Yucatán 97356, México.ORCID 0000-0003-2238-8467
Wendy Itzel Escobedo-HinojosaUnidad de Química en Sisal, Facultad de Química, Universidad Nacional Autónoma de México, Puerto de abrigo s/n, Sisal, Yucatán 97356, México.
Clara E Galindo-SánchezDepartamento de Biotecnología Marina, Laboratorio de Genómica Funcional, CICESE, Ensenada, Baja California 22860, México.
Carlos RosasUnidad Multidisciplinaria de Docencia e Investigación, Facultad de Ciencias UNAM, Puerto de abrigo s/n Sisal, Mpio, Hunucmá, Yucatán 97356, México.ORCID 0000-0002-1301-7368

Funding

Direccion General de Asuntos del Personal Academico, Universidad Nacional Autonoma de Mexico IN203022Secretaria de Ciencia, Humanidades, tecnologia e Innovacion (Mexico) PRONAII-2024-70Universidad Nacional Autónoma de México IN203022
6 · The paper itself

Abstract

Physiological response to feeding is crucial for various production factors such as feed catabolism and growth. Despite growing significance in red Octopus maya aquaculture, large-scale commercial production is limited by not sufficiently knowing their nutritional needs, especially their digestive physiology. Since this species is carnivorous, one of the main feeding aspects is directed to protein digestion, but its enzymatic digestive repertoire has not been studied yet at genomic and transcriptomic levels. This study searched for protease enzymes encoded in O. maya genome and expressed in the transcriptome, allowing an initial annotation of genes involved in protein catabolism; 117 amino acid sequences related to 'octopus digestive enzymes' were retrieved from 66 available-species' genomes in the NCBI database, coding for cathepsins, papilins, and metalloproteases. Homology analysis identified 36 homologous sequences from O. maya transcriptome and three from its genome. Phylogenetic analysis grouped 37 of 39 sequences into 11 of 14 main clades, offering new insights into the evolutionary relationships and functional roles of these proteases. Phylogenetic and motif analyses resulted in selecting 19 amino acid O. maya sequences using multiple sequence alignment that were used to generate three-dimensional protein models. The obtained models revealed a diverse structural architecture among 16 modelled cathepsins; however, their catalytic potential to fully clarify their role in protein hydrolysis and cellular processes remains to be determined. Foundational data provides insights into biochemistry and physiology behind O. maya protein digestion. Further complementation of these results with enzymatic characterization of the identified proteases should allow for improved diet formulation in order to foster this species aquaculture.

Indexed as

CathepsinsDigestionEvolution, MolecularGenomeOctopodiformesTranscriptomeAmino Acid SequenceAnimalsComputational BiologyGene Expression ProfilingModels, MolecularPhylogenySequence AlignmentCathepsinsCathepsinDigestive physiologyGenomeMetatranscriptomeOctopus maya

Identifiers

PMID40106538
PMCPMC12032550

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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.