The roles of serine protease, intracellular and extracellular phenoloxidase in activation of prophenoloxidase system, and characterization of phenoloxidase from shrimp haemocytes induced by lipopolysaccharide or dopamine

Peng Xie; Luqing Pan; Wujie Xu; Feng Yue

doi:10.1007/s00343-013-2236-6

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The roles of serine protease, intracellular and extracellular phenoloxidase in activation of prophenoloxidase system, and characterization of phenoloxidase from shrimp haemocytes induced by lipopolysaccharide or dopamine

OriginalPaper | Updated：2023-05-16

- The roles of serine protease, intracellular and extracellular phenoloxidase in activation of prophenoloxidase system, and characterization of phenoloxidase from shrimp haemocytes induced by lipopolysaccharide or dopamine
- The roles of serine protease, intracellular and extracellular phenoloxidase in activation of prophenoloxidase system, and characterization of phenoloxidase from shrimp haemocytes induced by lipopolysaccharide or dopamine
- 海洋湖沼学报（英文） 2013年31卷第5期页码：1018-1027
- Affiliations：
  
  1. Feed Science Institute Zhejiang University
  2. Key Laboratory of Mariculture Ministry of Education Ocean University of China
- Author bio：
- Funds：
  
  Supported by the New Century Excellent Talents in University (No. NCET-06-0597) and Introducing Talents of Discipline of Universities (111 Project) (No. B08049)
- DOI：10.1007/s00343-013-2236-6
  中图分类号：
- 网络首发：2013-09-07，
  
  纸质出版：2013
- Accepted：
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The roles of serine protease, intracellular and extracellular phenoloxidase in activation of prophenoloxidase system, and characterization of phenoloxidase from shrimp haemocytes induced by lipopolysaccharide or dopamine[J]. 海洋湖沼学报（英文）, 2013,31(5):1018-1027.

Xie, P., Pan, L., Xu, W. et al. The roles of serine protease, intracellular and extracellular phenoloxidase in activation of prophenoloxidase system, and characterization of phenoloxidase from shrimp haemocytes induced by lipopolysaccharide or dopamine., Chin. J. Ocean. Limnol. 31, 1018–1027 (2013). https://doi.org/10.1007/s00343-013-2236-6
The roles of serine protease, intracellular and extracellular phenoloxidase in activation of prophenoloxidase system, and characterization of phenoloxidase from shrimp haemocytes induced by lipopolysaccharide or dopamine[J]. 海洋湖沼学报（英文）, 2013,31(5):1018-1027. DOI： 10.1007/s00343-013-2236-6.

Xie, P., Pan, L., Xu, W. et al. The roles of serine protease, intracellular and extracellular phenoloxidase in activation of prophenoloxidase system, and characterization of phenoloxidase from shrimp haemocytes induced by lipopolysaccharide or dopamine., Chin. J. Ocean. Limnol. 31, 1018–1027 (2013). https://doi.org/10.1007/s00343-013-2236-6 DOI：

摘要

Abstract

We investigated the effects of lipopolysaccharide (LPS) and dopamine (DA) on the activation of the prophenoloxidase (proPO) system of Litopenaeus vannamei. LPS and DA were shown with a negative dose-dependent effect on hyalne cells (HC)

semi-granular cells (SGC)

large granular cells (LGC)

and total haemocyte count (THC). When haemocytes were treated with LPS or DA

serine proteinase activity and intracellular phenoloxidase (PO) activity were significantly reduced

but extracellular PO activity increased significantly. These findings indicated that the reduction in haemocyte counts was mainly because of the degranulation and activation of the proPO system from semi-granule and large granule cells. The PKC inhibitor

chelerythrine

and the TPK inhibitor

genistein

had an inhibitory effect on extracellular PO activity

while serine proteinase and intracellular PO activity increased. This suggests that the LPS and DA induce the activation of proPO in haemocytes via PKC and TPK-related signaling pathways

but serine proteinase may be activated only by PKC

as the genistein effects were not statistically significant. Electrophoresis analysis revealed that POs induced by LPS or DA have the same molecular mass and high diphenolase activity. Two PO bands at 526 kDa and 272 kDa were observed in PAGE

while in the haemocyte lysate supernatant (HLS)

only a 272-kDa band was observed. This band was resolved after SDS-PAGE under non-reducing and reducing conditions into two groups of POs

166 kDa and 126 kDa

and 78.1 kDa and 73.6 kDa

respectively

suggesting that PO in L. vannamei is an oligomer

which may have different compositions intra- and extracellularly.

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references

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