Correction: Fam57b (family with sequence similarity 57, member B), a novel peroxisome proliferator-activated receptor γ target gene that regulates adipogenesis through ceramide synthesis.
Yzumi Yamashita-SugaharaYoshimi TokuzawaYutaka NakachiYukiko Kanesaki-YatsukaMasahito MatsumotoYosuke MizunoYasushi Okazaki
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VOLUME 288 (2013) PAGES 4522–4537 In Fig. 6B, the wrong image was used for siFam57b-B. This error has been corrected with the correct image and does not affect any results or conclusions of this work.Keywords:
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Adipogenesis was defined as a differentiation process of preadipocytes into adipocytes. It is a key process in determining the number of mature adipocytes in the development of obesity. Thus, to regulation of adipogenesis is crucial target in obesity prevention. Mussel (Mytilus corscus ) has been reported to possess abundant dietary proteins and savory amino acids. However, antiadipogenic role and function in obesity prevention remains unknown. Here, we employed green-shelled mussel and its water extract (GME) was prepared. To elucidate the potential role of GME in 3T3-L1 adipogenesis, 3T3-L1 cells were treated with GME between day –2 to day 6. We found that GME dose-dependently suppressed adipogenesis and inhibited formation of lipid droplets accompanied by reduced level of adipogenic transcriptional factors such as C/EBPα and FAS. Our study further revealed that inhibitory function of GME wa largely limited to the adipogenesis day 0 to day 6. Taken together, our evidences provide new insights into the molecular basis underlying the antiadipogenic function of GME.
Lipid droplet
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Sestrin-3, together with the other two members Sestrin-1 and Sestrin-2, belongs to the Sestrin family. The Sestrin protein family has been demonstrated to be involved in antioxidative, metabolic homeostasis, and even the development of nonalcoholic steatohepatitis (NASH). However, the adipogenic regulatory role of SESN3 in adipogenesis still needs to be further explored. In this study, we demonstrated SESN3 inhibited porcine pre-adipocyte proliferation, thus suppressing its adipogenesis. Meanwhile, SESN3 has been demonstrated to inhibit Smad3 thus protecting against NASH. Further, for our previous study, we found mmu-miR-124 involved in 3T3-L1 cell adipogenesis regulation. In this study, we also identified that ssc-miR-124 inhibited porcine pre-adipocyte proliferation, thus suppressing its adipogenesis, and the SMAD3 was an inhibitor of ssc-miR-124 by binding to its promoter. Furthermore, the ssc-miR-124 targeted porcine C/EBPα and GR and thus inhibited pre-adipocyte adipogenesis. In conclusion, SESN3 inhibited SMAD3, thus improving ssc-miR124, and then suppressed C/EBPα and GR to regulate pre-adipocytes adipogenesis.
Nonalcoholic steatohepatitis
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Arl4D is a developmentally-regulated member of the ADP-ribosylation factor/ARF-like protein (ARF/Arl) family of Ras-related GTPases. Although Arl4 protein is reported to be expressed in adipose tissue, the function of Arl4D is unknown. To investigate the potential role of Arl4D in adipogenesis, we examined Arl4D expression during adipocyte differentiation and the effects of Arl4D overexpression on adipogenesis. Arl4D protein increased early in adipogenesis, with the highest expression at 4 h after adipogenesis initiation, followed by a decrease thereafter. Overexpression of Arl4D in 3T3-L1 cells potently inhibited their ability to differentiate and accumulate lipid, and reduced the expression of adipogenic genes. Furthermore, treatment with valproic acid, an Arl4D inducer, suppressed adipogenesis. These results suggest that rapid reduction of Arl4D is required for adipogenesis to proceed.
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Dysfunctional family
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Background During mesenchymal stem cell (MSC) conversion into adipocytes, the adipogenic cocktail consisting of insulin, dexamethasone, indomethacin and 3-isobutyl-1-methylxanthine not only induces adipogenic-specific but also genes for non-adipogenic processes. Therefore, not all significantly expressed genes represent adipogenic-specific marker genes. So, our aim was to filter only adipogenic-specific out of all expressed genes. We hypothesize that exclusively adipogenic-specific genes change their expression during adipogenesis, and reverse during dedifferentiation. Thus, MSC were adipogenic differentiated and dedifferentiated. Results Adipogenesis and reverse adipogenesis was verified by Oil Red O staining and expression of PPARG and FABP4. Based on GeneChips, 991 genes were differentially expressed during adipogenesis and grouped in 4 clusters. According to bioinformatic analysis the relevance of genes with adipogenic-linked biological annotations, expression sites, molecular functions, signaling pathways and transcription factor binding sites was high in cluster 1, including all prominent adipogenic genes like ADIPOQ, C/EBPA, LPL, PPARG and FABP4, moderate in clusters 2–3, and negligible in cluster 4. During reversed adipogenesis, only 782 expressed genes (clusters 1–3) were reverted, including 597 genes not reported for adipogenesis before. We identified APCDD1, CHI3L1, RARRES1 and SEMA3G as potential adipogenic-specific genes. Conclusion The model system of adipogenesis linked to reverse adipogenesis allowed the filtration of 782 adipogenic-specific genes out of total 991 significantly expressed genes. Database analysis of adipogenic-specific biological annotations, transcription factors and signaling pathways further validated and valued our concept, because most of the filtered 782 genes showed affiliation to adipogenesis. Based on this approach, the selected and filtered genes would be potentially important for characterization of adipogenesis and monitoring of clinical translation for soft-tissue regeneration. Moreover, we report 4 new marker genes.
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Abstract Objective Extracts of Artemisia scoparia (SCO) have antidiabetic properties in mice and enhance adipogenesis in vitro , but the underlying mechanisms are unknown. Thiazolidinediones, including rosiglitazone (ROSI), are pharmacological activators of peroxisome proliferator‐activated receptor gamma that also promote adipogenesis. The aim of this study was to examine adipogenic pathways responsible for SCO‐mediated adipogenesis and identify potential differences between SCO and ROSI in the ability to promote adipocyte development. Methods The ability of SCO or ROSI to promote adipogenesis in 3T3‐L1 cells following systematic omission of the common triad of adipogenic effectors dexamethasone, 1‐methyl‐3‐isobutylxanthine (MIX), and insulin was examined. Adipogenesis was assessed by both neutral lipid quantitation and adipocyte marker gene expression. Results The results demonstrate that SCO and ROSI promote adipogenesis and increase the expression of several peroxisome proliferator‐activated receptor gamma target genes involved in lipid accumulation in the absence of MIX. However, ROSI can enhance adipogenesis in the absence of MIX and insulin and differentially regulates adipogenic and lipid metabolism genes as compared with SCO. Conclusions These data demonstrate the adipogenic capabilities of SCO are similar but not identical to ROSI, thereby warranting further research into SCO as a promising source of therapeutic compounds in the treatment of metabolic disease states.
Rosiglitazone
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Our understanding of the processes that lead to adipocyte differentiation has been greatly enhanced in the past few years by researchers' unraveling of the key molecular events in adipogenesis. Adipocyte differentiation is controlled by a transcriptional cascade, a master regulator of which is PPARγ, a member of the nuclear hormone receptor superfamily of transcription factors. This review examines the mechanisms involved in the regulation of PPARγ's adipogenic potential, the role of key molecules involved in adipogenesis, like C/EBP's and ADD1, and their relationship with PPARγ
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Peroxisomes are dynamic organelles that often proliferate in response to compounds that they metabolize. Peroxisomes can proliferate by two apparent mechanisms, division of preexisting peroxisomes and de novo synthesis of peroxisomes. Evidence for de novo peroxisome synthesis comes from studies of cells lacking the peroxisomal integral membrane peroxin Pex3p. These cells lack peroxisomes, but peroxisomes can assemble upon reintroduction of Pex3p. The source of these peroxisomes has been the subject of debate. Here, we show that the amino-terminal 46 amino acids of Pex3p of Saccharomyces cerevisiae target to a subdomain of the endoplasmic reticulum and initiate the formation of a preperoxisomal compartment for de novo peroxisome synthesis. In vivo video microscopy showed that this preperoxisomal compartment can import both peroxisomal matrix and membrane proteins leading to the formation of bona fide peroxisomes through the continued activity of full-length Pex3p. Peroxisome formation from the preperoxisomal compartment depends on the activity of the genes PEX14 and PEX19, which are required for the targeting of peroxisomal matrix and membrane proteins, respectively. Our findings support a direct role for the endoplasmic reticulum in de novo peroxisome formation.
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Organelle biogenesis
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Abstract Adipogenesis is a complex and tightly regulated process that plays a vital role in multiple aspects of human health. The molecular mechanisms regulating adipogenesis are incompletely understood, although key facets of the signaling and regulatory pathways have been defined. ADP-ribosylation – the process whereby ADP-ribose moieties are covalently transferred from NAD+ to substrate proteins – has been shown to control multiple components of the adipogenic regulatory machinery, including the transcription factor C/EBPb. In order to explore the role of mono(ADP-ribosyl)transferases (MARTs) during adipogenesis, we used an siRNA-mediated knockdown screen in mouse 3T3-L1 preadipocytes to determine which MARTs are required for the differentiation of the preadipocytes into mature adipocytes. This screen identified PARP7 the primary candidate. Using a variety of cell-based and biochemical assays, we have identified key aspects of PARP7's involvement throughout adipogenesis. We observed dynamic localization of PARP7 during adipogenesis, moving from the nucleus in early adipogenesis to the cytosol during mid to late adipogenesis. The requirement for PARP7, as determined by knockdown, was most evident in early stages of adipogenesis. Knockdown of PARP7 was rescued by a PPAR g agonist, suggesting that PARP7 acts before the onset of the later stages of adipogenesis leading to mature adipocytes. Together, these findings led us to hypothesize that PARP7 plays a critical role in the nucleus during early adipogenesis. Preliminary data have revealed that PARP7 binds to C/EBPb, a key "first wave" transcription factor that drives adipogenesis, during a time when C/EBPb is poly(ADP-ribosyl)ated by PARP1 in the nucleus. Ongoing investigations are exploring: (1) the mechanisms by which PARP7 binds to C/EBPb; (2) the impact of PARP7 binding on C/EBPb stability; and (3) the biological outcomes of PARP7-C/EBPb interactions. Collectively, these studies provide an avenue to better understand the role of PARP7 in the regulation of adipogenesis. This work is supported by a grant from the NIH/NIDDK (R01 DK069710) and funds from the Cecil H. and Ida Green Center for Reproductive Biology Sciences Endowment to W.L.K., and a predoctoral fellowship from the American Heart Association to M.S.S. Presentation: Monday, June 13, 2022 12:15 p.m. - 12:30 p.m.
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