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

Mengal, Kifayatullah LU ; Kor, Golara ; Siino, Valentina LU ; Buřič, Miloš ; Kozák, Pavel ; Levander, Fredrik LU and Niksirat, Hamid LU orcid (2023) In Developmental and Comparative Immunology 147.
Abstract

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... (More)

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 < 0.05, fold change>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.

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author
; ; ; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Clot proteomics, Decapods, Innate immunity, Protein
in
Developmental and Comparative Immunology
volume
147
article number
104760
publisher
Elsevier
external identifiers
  • pmid:37331675
  • scopus:85162154518
ISSN
0145-305X
DOI
10.1016/j.dci.2023.104760
language
English
LU publication?
yes
id
0f25f513-35f1-49db-8ecc-3b87ed32038f
date added to LUP
2023-09-04 10:41:32
date last changed
2024-04-20 02:27:42
@article{0f25f513-35f1-49db-8ecc-3b87ed32038f,
  abstract     = {{<p>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.</p>}},
  author       = {{Mengal, Kifayatullah and Kor, Golara and Siino, Valentina and Buřič, Miloš and Kozák, Pavel and Levander, Fredrik and Niksirat, Hamid}},
  issn         = {{0145-305X}},
  keywords     = {{Clot proteomics; Decapods; Innate immunity; Protein}},
  language     = {{eng}},
  publisher    = {{Elsevier}},
  series       = {{Developmental and Comparative Immunology}},
  title        = {{Quantification of proteomic profile changes in the hemolymph of crayfish during in vitro coagulation}},
  url          = {{http://dx.doi.org/10.1016/j.dci.2023.104760}},
  doi          = {{10.1016/j.dci.2023.104760}},
  volume       = {{147}},
  year         = {{2023}},
}