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Phenoloxidases from black tiger shrimp (Penaeus monodon): gene expression and activity distribution in different tissues
In this study, the expression of four reference genes ( β-actin , EF1-α , GAPDH , and SubF0 ), two prophenoloxidase genes ( proPO1 and proPO2 ), and the distribution of phenoloxidase (PO) activity in eight tissues (carapace, cuticle, hemolymph, hepatopancreas, muscle, pereiopods, pleopods, and uro...
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Published in: | Aquaculture international 2023-06, Vol.31 (3), p.1423-1437 |
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Main Authors: | , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: |
In this study, the expression of four reference genes (
β-actin
,
EF1-α
,
GAPDH
, and
SubF0
), two prophenoloxidase genes (
proPO1
and
proPO2
), and the distribution of phenoloxidase (PO) activity in eight tissues (carapace, cuticle, hemolymph, hepatopancreas, muscle, pereiopods, pleopods, and uropods) of black tiger shrimp (
Penaeus monodon
) were evaluated. According to the geNorm and NormFinder algorithms, the most stable reference gene or the best combinations of reference genes for the evaluation of
proPO1
and
proPO2
expression are
SubF0
for cuticle, muscle, and uropods,
EF1-α
for hemolymph and pereiopods,
EF1-α
+
SubF0
for carapace,
β-actin
+
SubF0
for hepatopancreas, and
β-actin
+
GAPDH
for pleopods. In the hemolymph and uropods,
proPO1
expression was significantly stronger than that of
proPO2
(433 and 5 times higher, respectively). However, in hepatopancreas,
proPO2
expression was significantly stronger than
proPO1
(36 times higher). Trypsin cleaves the proPO zymogen into active PO in most of the studied tissues, except hepatopancreas. PO activity (units/mg protein) following trypsin activation varied among the tissues in the following order: uropods > hemolymph > pleopods > pereiopods > hepatopancreas > carapace > cuticle > muscle. The results indicate that
proPO1
is dominant in hemolymph, whereas
proPO2
is dominant in hepatopancreas. Altogether, these results contribute to the elucidation of the phenoloxidase function in
P. monodon
. |
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ISSN: | 0967-6120 1573-143X |
DOI: | 10.1007/s10499-022-01033-z |