Quantification of proteomic profile changes in the hemolymph of crayfish during in vitro coagulation

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12520%2F23%3A43906382" target="_blank" >RIV/60076658:12520/23:43906382 - isvavai.cz</a>

Result on the web

<a href="https://doi.org/10.1016/j.dci.2023.104760" target="_blank" >https://doi.org/10.1016/j.dci.2023.104760</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.dci.2023.104760" target="_blank" >10.1016/j.dci.2023.104760</a>

Result language

angličtina

Original language name

Quantification of proteomic profile changes in the hemolymph of crayfish during in vitro coagulation

Original language description

Hemolymph is the circulatory fluid that fills the body cavity of crustaceans, analogous to blood in vertebrates. Hemolymph coagulation, similar to blood clotting in vertebrates, plays a crucial role in wound healing and innate immune responses. Despite extensive studies on the clotting process in crustaceans, no comparative quantitative analysis of the protein composition of non-clotted and clotted hemolymph in any decapod has been reported. In this study, we used label-free protein quantification with high-resolution mass spectrometry to identify the proteomic profile of hemolymph in crayfish and quantify significant changes in protein abundances between non-clotted and clotted hemolymph. Our analysis identified a total of two-hundred and nineteen proteins in both hemolymph groups. Furthermore, we discussed the potential functions of the top most high and low-abundant proteins in hemolymph proteomic profile. The quantity of most of the proteins was not significantly changed during coagulation between non-clotted and clotted hemolymph, which may indicate that clotting proteins are likely pre-synthesized, allowing for a swift coagulation response to injury. Four proteins still showed abundance differences (p &lt; 0.05, fold change&gt;2), including C-type lectin domain-containing proteins, Laminin A chain, Tropomyosin, and Reverse transcriptase domain-containing proteins. While the first three proteins were down-regulated, the last one was up-regulated. The down-regulation of structural and cytoskeletal proteins may affect the process of hemocyte degranulation needed for coagulation, while the up-regulation of an immune-related protein might be attributed to the phagocytosis ability of viable hemocytes during coagulation.

Czech name

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Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

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OECD FORD branch

30102 - Immunology

Project

—

Continuities

S - Specificky vyzkum na vysokych skolach

Publication year

2023

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Developmental and Comparative Immunology

ISSN

0145-305X

e-ISSN

1879-0089

Volume of the periodical

147

Issue of the periodical within the volume

neuvedeno

Country of publishing house

GB - UNITED KINGDOM

Number of pages

11

Pages from-to

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UT code for WoS article

001025875700001

EID of the result in the Scopus database

2-s2.0-85162154518