| Literature DB >> 32329225 |
Yiping Yu1,2, Jia-Huan He1,2, Lin-Li Hu1,2, Lin-Lin Jiang2, Lanlan Fang1,2, Gui-Dong Yao1,2, Si-Jia Wang1, Qingling Yang1,2, Yanjie Guo1,2, Lin Liu2, Trisha Shang2, Yorino Sato3, Kazuhiro Kawamura3, Aaron Jw Hsueh2, Ying-Pu Sun1.
Abstract
FBN1 encodes asprosin, a glucogenic hormone, following furin cleavage of the C-terminus of profibrillin 1. Based on evolutionary conservation between FBN1 and FBN2, together with conserved furin cleavage sites, we identified a peptide hormone placensin encoded by FBN2 based on its high expression in trophoblasts of human placenta. In primary and immortalized murine hepatocytes, placensin stimulates cAMP production, protein kinase A (PKA) activity, and glucose secretion, accompanied by increased expression of gluconeogenesis enzymes. In situ perfusion of liver and in vivo injection with placensin also stimulate glucose secretion. Placensin is secreted by immortalized human trophoblastic HTR-8/SVneo cells, whereas placensin treatment stimulates cAMP-PKA signaling in these cells, accompanied by increases in MMP9 transcripts and activities, thereby promoting cell invasion. In pregnant women, levels of serum placensin increase in a stage-dependent manner. During third trimester, serum placensin levels of patients with gestational diabetes mellitus are increased to a bigger extent compared to healthy pregnant women. Thus, placensin represents a placenta-derived hormone, capable of stimulating glucose secretion and trophoblast invasion.Entities:
Keywords: gluconeogenesis; hormone; invasiveness; placensin
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Year: 2020 PMID: 32329225 PMCID: PMC7271319 DOI: 10.15252/embr.201949530
Source DB: PubMed Journal: EMBO Rep ISSN: 1469-221X Impact factor: 8.807