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

• Published in: International journal of molecular sciences Vol. 24; no. 7; p. 6096
• Main Authors: Wojciechowicz, Tatiana, Kolodziejski, Paweł A, Billert, Maria, Strowski, Mathias Z, Nowak, Krzysztof W, Skrzypski, Marek
• Format: Journal Article
• Language: English
• Published: Switzerland MDPI AG 23.03.2023; MDPI
• 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; neuropeptide B; Neuropeptides; Peroxisome proliferator-activated receptors; Phosphorylation; Physiological aspects; PPAR gamma - metabolism; Preadipocytes; proliferation; Proteins; Rats; RNA; RNA, Messenger - genetics; Signal transduction; Swine; Transcription factors; Poland; Germany; neuropeptide B; adipogenesis; differentiation; p38; proliferation; porcine; preadipocytes; adipocytes
• ISSN: 1422-0067; 1661-6596; 1422-0067
• DOI: 10.3390/ijms24076096

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.