Bpifcl modulates kiss2 expression under the influence of 11-ketotestosterone in female zebrafish

Shogo Moriya,Nabila Tahsin,Ishwar S Parhar

doi:10.1038/s41598-017-08248-8

Shogo Moriya, Nabila Tahsin + Show 1 more

Open Access

https://doi.org/10.1038/s41598-017-08248-8

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Journal: Scientific Reports	Publication Date: Aug 11, 2017
Citations: 6	License type: open-access

Affiliation: Monash University Malaysia

Abstract

The bactericidal/permeability-increasing (BPI) fold-containing (BPIF) superfamily of genes expressed in the brain are purportedly involved in modulating brain function in response to stress, such as inflammation. Kisspeptin, encoded by kiss, is affected by inflammation in the brain; therefore, BPIF family genes might be involved in the modulation of kisspeptin in the brain. In this study, we investigated the expression of BPIF family C, like (bpifcl) in zebrafish brain and its involvement in kiss2 regulation. The identified, full-length sequence of a bpifcl isoform expressed in the zebrafish brain contained the BPI fold shared by BPIF family members. bpifcl mRNA expression in female zebrafish brains was significantly higher than that in males. Exposure of female zebrafish to 11-ketotestosterone decreased bpifcl and kiss2 mRNA expression. bpifcl knockdown by bpifcl-specific small interfering RNA administration to female zebrafish brain decreased kiss2 mRNA expression. bpifcl expression was widely distributed in the brain, including in the dorsal zone of the periventricular hypothalamus (Hd). Furthermore, bpifcl was also expressed in KISS2 neurons in the Hd. These results suggest that the Bpifcl modulates kiss2 mRNA expression under the influence of testosterone in the Hd of female zebrafish.

Highlights

The bactericidal/permeability-increasing (BPI) fold-containing (BPIF) superfamily of genes is functionally classified into five groups: palate, lung and nasal epithelium clone (PLUNC); lipopolysaccharide-binding protein (LBP); BPI protein; phospholipid transfer protein (PLTP); cholesterol ester transfer protein (CETP)[1, 2]
Simple Modular Architecture Research Tool (SMART) prediction indicated that the N- and C-terminal domains of BPIF family proteins consisted of amino acids 24-243 and 258-461, respectively (Supplementary Fig. 1A)
Functional domain analysis using SMART showed the presence of N- and C-terminal domain of the BPIF family

Summary

Introduction

The bactericidal/permeability-increasing (BPI) fold-containing (BPIF) superfamily of genes is functionally classified into five groups: palate, lung and nasal epithelium clone (PLUNC); lipopolysaccharide-binding protein (LBP); BPI protein; phospholipid transfer protein (PLTP); cholesterol ester transfer protein (CETP)[1, 2]. All BPIF family members share the BPI fold, which has an elongated, boomerang shape consisting of two distinct N- and C-terminal domain barrels with a highly similar secondary structure[3]. We have reported the expression of BPIF family of genes, such as bpifa[1], gm1006 and rya[3] in the mouse brain, in the preoptic area[12]. The expression of these genes decreases with age. Because ageing causes oxidative stress and inflammation in the brain[13], the identified BPIF family of genes might respond to oxidative stress and inflammation similar to the PLUNC protein group in the brain. Because the regulatory mechanisms of kisspeptin have not been fully identified, the BPIF family-kisspeptin interaction could be a novel kisspeptin regulatory mechanism in the brain

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Results

Conclusion