The Effects of Neuropeptide B on Proliferation and Differentiation of Porcine White Preadipocytes into Mature Adipocytes

Neuropeptide B (NPB) affects energy homeostasis and metabolism by binding and activating NPBWR1 and NPBWR2 in humans and pigs. Recently, we reported that NPB promotes the adipogenesis of rat white and brown preadipocytes as well as 3T3-L1 cells. In the present study, we evaluated the effects of NPB...

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Published in:International journal of molecular sciences 2023-03, Vol.24 (7), p.6096
Main Authors: Wojciechowicz, Tatiana, Kolodziejski, Paweł A, Billert, Maria, Strowski, Mathias Z, Nowak, Krzysztof W, Skrzypski, Marek
Format: Article
Language:English
Subjects:
3T3-L1 Cells
Adipocytes
Adipocytes - metabolism
Adipogenesis
Adipogenesis - genetics
Animals
Cell Differentiation
Cell Proliferation
Cyclin-dependent kinases
Differentiation
Energy balance
Energy metabolism
Extracellular signal-regulated kinase
Fatty acids
Gene expression
Genes
Homeostasis
Humans
Insulin
Kinases
Lipids
Mice
Nervous system
Neuropeptides
Peroxisome proliferator-activated receptors
Phosphorylation
Physiological aspects
PPAR gamma - metabolism
Preadipocytes
Proteins
Rats
RNA
RNA, Messenger - genetics
Signal transduction
Swine
Transcription factors
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Summary:Neuropeptide B (NPB) affects energy homeostasis and metabolism by binding and activating NPBWR1 and NPBWR2 in humans and pigs. Recently, we reported that NPB promotes the adipogenesis of rat white and brown preadipocytes as well as 3T3-L1 cells. In the present study, we evaluated the effects of NPB on the proliferation and differentiation of white porcine preadipocytes into mature adipocytes. We identified the presence of NPB, NPBWR1, and NPBWR2 on the mRNA and protein levels in porcine white preadipocytes. During the differentiation process, NPB increased the mRNA expression of PPARγ, C/EBPβ, C/EBPα, PPARγ, and C/EBPβ protein production in porcine preadipocytes. Furthermore, NPB stimulated lipid accumulation in porcine preadipocytes. Moreover, NPB promoted the phosphorylation of the p38 kinase in porcine preadipocytes, but failed to induce ERK1/2 phosphorylation. NPB failed to stimulate the expression of C/EBPβ in the presence of the p38 inhibitor. Taken together, we report that NPB promotes the differentiation of porcine preadipocytes via a p38-dependent mechanism.
ISSN:1422-0067
1661-6596
1422-0067
DOI:10.3390/ijms24076096