Skip to main content

Advertisement

SpringerLink
Log in

Molecular Cloning and Functional Analysis of Secretory Phospholipase A2 from Apostichopus japonicus

  • Original Article
  • Published:
Biochemical Genetics Aims and scope Submit manuscript

Abstract

Secretory phospholipase A2 (sPLA2) plays important roles in phospholipid metabolism, skin barrier maintenance, immune response and other processes in organisms. sPLA2 of sea cucumber A. japonicus (AjPLA2) has not yet been reported. This study successfully amplified the AjPLA2 sequence. The total cDNA of AjPLA2 is 931 bp, including a 480 bp ORF that encodes 159 amino acids. The AjPLA2 protein includes a 16-aa signal peptide, a 5-aa precursor peptide and a 138-aa mature peptide. Homologous alignment showed that AjPLA2 and the sPLA2s from starfish have the typical domains of the Group IB sPLA2. And additional amino acid sequences were found around the β-Wing, which is different from the Group IB sPLA2. These results showed that AjPLA2 and sPLA2s from starfish all belong to a new group in the Group I sPLA2 family. AjPLA2 is widely distributed in sea cucumber tissues. The functional analysis also showed that AjPLA2 was upregulated in the intestine by feeding. When the body wall was damaged, it was significantly upregulated around the wound. And the expression levels of AjPLA2 were significantly increased in V. splendens-infected sea cucumbers. The results indicated that AjPLA2 plays roles in the sea cucumber immunologic process. Combined with the upregulation of unsaturated fatty acids (PUFAs) content in A. japonicus, it demonstrated that AjPLA2 could participate in the immune of A. japonicus by hydrolyzing phospholipid and releasing PUFAs. This study had a solid foundation for the further research of AjPLA2 gene function in vivo, development and application of AjPLA2 protein.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Fig. 1
Fig. 2
Fig. 3
Fig. 4
Fig. 5
Fig. 6
Fig. 7
Fig. 8

Similar content being viewed by others

References

  • Alvarez Y, Valera I, Municio C, Hugo E, Padrón F, Blanco L, Rodríguez M, Fernández N, Crespo MS (2010) Eicosanoids in the innate immune response: TLR and non-TLR routes. Mediators Inflamm 2010:201929

    Article  PubMed  PubMed Central  Google Scholar 

  • Arni RK, Ward RJ (1996) Phospholipase A2—a structural review. Toxicon 34(8):827–841

    Article  CAS  PubMed  Google Scholar 

  • Chang YQ, Ding J, Song J (2004) The biology research and cultivation of sea cucumber and sea urchins. Marine Publishing Company, pp 1–4

    Google Scholar 

  • Chen LY, Liang B (2000) Progress on Phospholipase A2. Foreign Med Sci 20(6):473–476

    Google Scholar 

  • Clark JD, Lin LL, Kriz RW, Ramesha CS, Sultzman LA, Lin AY, Milona N, Knopf JL (1991) A novel arachidonic acid-selective cytosolic PLA2 contains a Ca2+-dependent translocation domain with homology to PKC and GAP. Cell 65(6):1043–1051

    Article  CAS  PubMed  Google Scholar 

  • Condrea E, De Vries A (1965) Venom phospholipase A: a review. Toxicon 2(4):261–273

    Article  CAS  PubMed  Google Scholar 

  • Dennis EA, Cao J, Hsu YH, Magrioti V, Kokotos G (2011) Phospholipase A2 enzymes: physical structure, biological function, disease implication, chemical inhibition and therapeutic intervention. Chem Rev 111(10):6130–6185

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  • Harizi H, Corcuff JB, Gualde N (2008) Arachidonic-acid-derived eicosanoids: roles in biology and immunopathology. Trends Mol Med 14(10):461–469

    Article  CAS  PubMed  Google Scholar 

  • Hatakeyama T, Higashi E, Nakagawa H (2015) cDNA cloning and expression of Contractin A, a phospholipase A2-like protein from the globiferous pedicellariae of the venomous sea urchin Toxopneustes pileolus. Toxicon 108:46–52

    Article  CAS  PubMed  Google Scholar 

  • Hauck CR, Borisova M, Muenzner P (2012) Exploitation of integrin function by pathogenic microbes. Curr Opin Cell Biol 24:637–644

    Article  CAS  PubMed  Google Scholar 

  • Ibrahim F, Widhyastuti N, Savitri IKE, Sahlan M, Wijanarko A (2013) Antibacterial investigated of phospholipase A2 from the spines venom of crown of thorns starfish Acanthaster planci. Int J Pharm Bio Sci 4(2):1–5

    Google Scholar 

  • Ilic D, Bollinger JM, Gelb M, Mauro TM (2014) sPLA2 and the epidermal barrier. Biochim Biophys Acta (BBA): Mol Cell Biol Lipids 1841(3):416–421

    Article  CAS  Google Scholar 

  • Kim JO, Chakrabarti BK, Guha-Niyogi A, Louder MK, Mascola JR, Ganesh L, Nabel GJ (2007) Lysis of human immunodeficiency virus type 1 by a specific secreted human phospholipase A2. J Virol 81(3):1444–1450

    Article  CAS  PubMed  Google Scholar 

  • Koduri RS, Grönroos JO, Laine VJO, Calvez CL, Lambeau G, Nevalainen TJ, Gelb MH (2002) Bactericidal properties of human and murine groups I, II, V, X, and XII secreted phospholipases A2. J Biol Chem 277(8):5849–5857

    Article  CAS  PubMed  Google Scholar 

  • Krizaj I (2014) Roles of secreted phospholipases A2 in the mammalian immune system. Protein Pept Lett 21(12):1201–1208

    Article  CAS  PubMed  Google Scholar 

  • Li C, Xing X, Qi HQ, Liu Y, Jian FJ, Wang JH (2022) The arachidonic acid and its metabolism pathway play important roles for Apostichopus japonicus infected by Vibrio splendens. Fish Shellfish Immunol 125:152–160

    Article  CAS  PubMed  Google Scholar 

  • Lindquist S, Hernell O (2010) Lipid digestion and absorption in early life: an update. Curr Opin Clin Nutr Metab Care 13(3):314–320

    Article  CAS  PubMed  Google Scholar 

  • McIntosh JM, Ghomashchi F, Gelb MH, Dooley DJ, Stoehr SJ, Giordani AB, Naisbitt SR, Olivera BM (1995) Conodipine-M, a novel phospholipase A2 isolated from the venom of the marine snail Conus magus. J Biol Chem 270(8):3518–3526

    Article  CAS  PubMed  Google Scholar 

  • Mitsuishi M, Masuda S, Kudo I, Murakami M (2007) Human group III phospholipase A2 suppresses adenovirus infection into host cells: evidence that group III, V and X phospholipase A2s act on distinct cellular phospholipid molecular species. Biochim Biophys Acta (BBA): Mol Cell Biol Lipids 1771(11):1389–1396

    Article  CAS  Google Scholar 

  • Murakami M, Taketomi Y, Girard C, Yamamoto K, Lambeau G (2010) Emerging roles of secreted phospholipase A2 enzymes: lessons from transgenic and knockout mice. Biochimie 92(6):561–582

    Article  CAS  PubMed  Google Scholar 

  • Nevalainen TJ, Peuravuori HJ, Quinn RJ, Llewellyn LE, Benzie JAH, Fenner PJ, Winkel KD (2004a) Phospholipase A2 in cnidaria. Comp Biochem Physiol b: Biochem Mol Biol 139(4):731–735

    Article  PubMed  Google Scholar 

  • Nevalainen TJ, Quinn RJ, Hooper JNA (2004b) Phospholipase A2 in porifera. Comp Biochem Physiol b: Biochem Mol Biol 137(3):413–420

    Article  PubMed  Google Scholar 

  • Ota E, Nagai H, Nagashima Y, Shiomi K (2006) Molecular cloning of two toxic phospholipases A2 from the crown-of-thorns starfish Acanthaster planci venom. Comp Biochem Physiol b: Biochem Mol Biol 143(1):54–60

    Article  PubMed  Google Scholar 

  • Palm NW, Rosenstein RK, Yu S, Schenten DD, Florsheim E (2013) Bee venom phospholipase A2 induces a primary type 2 response that is dependent on the receptor ST2 and confers protective immunity. Immunity 39(5):976–985

    Article  CAS  PubMed  Google Scholar 

  • Seilhamer JJ, Pruzanski W, Vadas P, Plant S, Miller JA, Kloss J, Johnson LK (1989) Cloning and recombinant expression of phospholipase A2 present in rheumatoid arthritic synovial fluid. J Biol Chem 264(10):5335–5338

    Article  CAS  PubMed  Google Scholar 

  • Snitko Y, Han SK, Lee BI, Cho W (1999) Differential interfacial and substrate binding modes of mammalian pancreatic phospholipases A2: a comparison among human, bovine, and porcine enzymes. Biochemistry 38(24):7803–7810

    Article  CAS  PubMed  Google Scholar 

  • Vatanparast M, Ahmed S, Herrero S, Kim Y (2018) A non-venomous sPLA2 of a lepidopteran insect: its physiological functions in development and immunity. Dev Comp Immunol 89:83–92

    Article  CAS  PubMed  Google Scholar 

  • Yang YP, Liang ZQ, Gu ZL, Qin ZH (2005) The research progress of cobra venom secretory phospholipase A2. Chin Pharmacol Bull 21(9):1045–1048

    CAS  Google Scholar 

  • Zhang PJ, Li CH, Zhang P, Jin CH, Pan DD, Bao YB (2014) iTRAQ-based proteomics reveals novel members involved in pathogen challenge in sea cucumber Apostichopus japonicas. PLoS ONE 9:e100492

    Article  ADS  PubMed  PubMed Central  Google Scholar 

Download references

Funding

This work was supported by the Natural Science Foundation of Liaoning Province (2021-MS-302), the scientific research fund project of Liaoning Provincial Department of Education (LJKZ0520) and the Scientific Research Fund Project of Education Department of Liaoning Province (LJKZZ20220060).

Author information

Author notes

  1. Cheng Li and Lili Yang have contributed equally to the manuscript.

Authors and Affiliations

  1. Department of Biotechnology, School of Biological Engineering, Dalian Polytechnic University, Dalian, 116034, Liaoning Province, People’s Republic of China

    Cheng Li, Lili Yang, Zhongyun Zhang, Ying Liu, Xu Li, Kai Yang & Ming Chen

Authors
  1. Cheng Li
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Lili Yang
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Zhongyun Zhang
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. Ying Liu
    View author publications

    You can also search for this author in PubMed Google Scholar

  5. Xu Li
    View author publications

    You can also search for this author in PubMed Google Scholar

  6. Kai Yang
    View author publications

    You can also search for this author in PubMed Google Scholar

  7. Ming Chen
    View author publications

    You can also search for this author in PubMed Google Scholar

Contributions

CL and MC wrote the main manuscript text. LY prepared Figs. 1–7, ZZ prepared Fig. 5, YL prepared Fig. 6, XL prepared Fig. 7, KY prepared Fig. 8. All authors reviewed the manuscript.

Corresponding authors

Correspondence to Cheng Li or Ming Chen.

Ethics declarations

Conflict of interest

The authors declare no competing financial interest.

Additional information

Publisher's Note

Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional affiliations.

Rights and permissions

Springer Nature or its licensor (e.g. a society or other partner) holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law.

Reprints and permissions

About this article

Check for updates. Verify currency and authenticity via CrossMark

Cite this article

Li, C., Yang, L., Zhang, Z. et al. Molecular Cloning and Functional Analysis of Secretory Phospholipase A2 from Apostichopus japonicus. Biochem Genet (2024). https://doi.org/10.1007/s10528-024-10738-0

Download citation

  • Received:

  • Accepted:

  • Published:

  • DOI: https://doi.org/10.1007/s10528-024-10738-0

Keywords

Search

Navigation