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C-reactive protein (CRP) and serum amyloid P (SAP) play essential roles in the phagocytic cell-mediated innate immune response of mammals. In-depth studies into CRP and SAP have been completed in mammals; however, such studies, particularly those relating to the functions of CRP and SAP, are rare in fish species. In this study, a homolog of CRP/SAP (BpCRP/SAP) was identified in mudskipper (Boleophthalmus pectinirostris), which had the typical characteristics of a fish short pentraxin protein. Phylogenetic tree analysis revealed that BpCRP/SAP was most closely related to mudskipper CRP/SAP-l3. BpCRP/SAP transcripts were detected in all tested tissues, with the highest level observed in the liver; transcripts in the immune tissues and protein expression in the serum were induced in response to Edwardsiella tarda infection. The active recombinant BpCRP/SAP (rBpCRP/SAP) was able to augment the mRNA expression of pro-inflammatory cytokines and attenuate the mRNA expression of anti-inflammatory cytokines in monocytes/macrophages (MO/MΦ). In addition, phagocytosis and bacterial killing of E. tarda by mudskipper MO/MΦ were boosted by rBpCRP/SAP stimulation. rBpCRP/SAP also promoted M1-type MO/MΦ polarization, but inhibited M2-type polarization. In conclusion, the present research describes the pro-inflammatory function of BpCRP/SAP in mudskipper against E. tarda infection.
This article was published in the following journal.
Name: Fish & shellfish immunology
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Amyloid P component is a small, non-fibrillar glycoprotein found in normal serum and in all amyloid deposits. It has a pentagonal (pentaxin) structure. It is an acute phase protein, modulates immunologic responses, inhibits ELASTASE, and has been suggested as an indicator of LIVER DISEASE.
A type of extracellularly deposited substance composed of an amyloid protein and additional components including HEPARAN SULFATE PROTEOGLYCAN; LAMININ; COLLAGEN TYPE IV; SERUM AMYLOID P-COMPONENT; and APOLIPOPROTEINS E which together form characteristic amyloid fibrils. The core of amyloid fibrils is formed by the stacking of overlapping beta-pleated sheet domains of the amyloid protein. There are many different amyloid proteins that have been found forming the core of the fibrils in vivo. However, amyloid can be formed from any protein that exposes beta-pleated strand conformations during unfolding or refolding. A common characteristic of amyloid is the ability to bind such dyes as CONGO RED and thioflavine.
Proteins that form the core of amyloid fibrils. For example, the core of amyloid A is formed from amyloid A protein, also known as serum amyloid A protein or SAA protein.
An ACUTE PHASE REACTION protein present in low concentrations in normal sera, but found at higher concentrations in sera of older persons and in patients with AMYLOIDOSIS. It is the circulating precusor of amyloid A protein, which is found deposited in AA type AMYLOID FIBRILS.
Endopeptidases that are specific for AMYLOID PROTEIN PRECURSOR. Three secretase subtypes referred to as alpha, beta, and gamma have been identified based upon the region of amyloid protein precursor they cleave.
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