Biological activities of a recombinant fortilin from Fenneropenaeus merguiensis

PLoS One. 2020 Oct 1;15(10):e0239672. doi: 10.1371/journal.pone.0239672. eCollection 2020.

Abstract

Human Fortilin, an antiapoptotic protein, has also been implicated in several diseases; however, several potential uses of fortilin have also been proposed. Bearing the implications of fortilin in mind, fortilin analog, which has no complication with diseases, is required. Since a recombinant full-length fortilin from Fenneropenaeus merguiensis (rFm-Fortilin (FL)) reported only 44% (3e-27) homologous to human fortilin, therefore the biological activities of the Fm-Fortilin (FL) and its fragments (F2, F12, and F23) were investigated for potential use against HEMA toxicity from filling cement to pulp cell. The rFm-Fortilin FL, F2, 12, and F23 were expressed and assayed for proliferation activity. The rFm-Fortilin (FL) showed proliferation activity on human dental pulp cells (HDPCs) and protected the cells from 2-hydroxy-ethyl methacrylate (HEMA) at 1-20 ng/ml. In contrast, none of the rFm-Fortilin fragments promoted HDPC growth that may be due to a lack of three conserved amino acid residues together for binding with the surface of Rab GTPase for proliferative activity. In addition, rFm-Fortilin (FL) activated mineralization and trend to suppressed production of proinflammatory cytokines, including histamine (at 10 ng/ml) and TNF-α (at 100 ng/ml). Besides, the rFm-Fortilin (FL) did not mutate the Chinese hamster ovary (CHO) cell. Therefore, the rFm-Fortilin (FL) has the potential use as a supplementary medical material to promote cell proliferation in patients suffering severe tooth decay and other conditions.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Arthropod Proteins / genetics
  • Arthropod Proteins / isolation & purification
  • Arthropod Proteins / pharmacology*
  • Cells, Cultured
  • Dental Pulp / cytology
  • Dental Pulp / drug effects
  • Histamine / metabolism
  • Methacrylates / toxicity
  • Penaeidae / chemistry*
  • Recombinant Proteins
  • Sequence Alignment
  • Tumor Necrosis Factor-alpha / metabolism

Substances

  • Arthropod Proteins
  • Methacrylates
  • Recombinant Proteins
  • Tumor Necrosis Factor-alpha
  • hydroxyethyl methacrylate
  • Histamine

Grants and funding

This research was supported by the Center of Excellence on Medical Biotechnology (CEMB), the S&T Postgraduate Education and Research Development Office (PERDO), the Commission on Higher Education (CHE), Thailand. This work was also supported by Government fund DEN610034S. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.