Lipin-1 expression is critical for keratinocyte differentiation

Chae, Minjung; Jung, Ji-Yong; Bae, Il-Hong; Kim, Hyoung-June; Lee, Tae Ryong; Shin, Dong Wook

doi:10.1194/jlr.m062588

Cited by 13 publications

(11 citation statements)

References 55 publications

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“…There are, however, limitations to the research presented by Chae et al ( 8 ). For example, although many of the effects observed upon lipin-1 knockdown are statistically signifi cant, the differences observed are often relatively minor.…”

mentioning

confidence: 69%

“…This reaction is important both because it converts one second messenger with particular responding enzymes into another lipid signal with different effectors and also because it is the fi rst step in the synthesis of triacylglycerol (TAG) and the phospholipids, phosphatidylcholine (PC) and phosphatidylethanolamine (PE). In their article in this issue of the Journal of Lipid Research , Chae et al ( 8 ) investigated the role of lipin-1 in keratinocytes and the skin, where the enzyme is found predominantly in basal keratinocytes (with reduced levels in suprabasal layers). Consistent with this in situ protein expression, in cultured keratinocytes, lipin-1 levels are reduced upon confl uence-or elevated extracellular calcium-induced differentiation.…”

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confidence: 99%

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Lipid signaling in keratinocytes: Lipin-1 plays a PArt

Bollag

2016

Journal of Lipid Research

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confidence: 69%

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confidence: 99%

Lipid signaling in keratinocytes: Lipin-1 plays a PArt

Bollag

2016

Journal of Lipid Research

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“…When the level of fatty acids is increased, lipin proteins translocate from the cytosol toward the endoplasmic reticulum membrane and catalyze the conversion of phosphatidic acid (PA) to DAG (Brohée et al, 2015; Reue & Dwyer, 2009; Seo & Shin, 2017). Both PA and DAG are signaling molecules (Chae et al, 2016; Grkovich, Johnson, Buczynski, & Dennis, 2006). Lipin‐1 is encoded by the LPIN1 gene and is one of the three members of the lipins family (Brohée et al, 2015).…”

Section: Introductionmentioning

confidence: 99%

“…In addition, it can upregulate fatty acids uptake, mitochondrial metabolism, and tricarboxylic acid cycle genes (Brohée et al, 2015). Generally, lipin‐1 can be localized in the cytoplasm, endoplasmic reticulum, and the nucleus and is involved in various cellular events, such as proliferation, gene expression, adipogenesis, lipid metabolism, mitochondrial morphology, vacuole fusion, autophagy, and migration (Brohée et al, 2018; Chae et al, 2016). Cell migration can be induced in response to signaling lipids, such as DAG, LPA, and prostaglandins (Baenke, Peck, Miess, & Schulze, 2013).…”

Section: Introductionmentioning

confidence: 99%

Expression and clinicopathological significance of lipin‐1 in human breast cancer and its association with p53 tumor suppressor gene

Dinarvand

Khanahmad

Hakimian

et al. 2020

Journal Cellular Physiology

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Breast cancer (BC) is an important cause of female cancer‐related death. It has recently been demonstrated that metabolic disorders including lipid metabolism are a hallmark of cancer cells. Lipin‐1 is an enzyme that displays phosphatidate phosphatase activity and regulates the rate‐limiting step in the pathway of triglycerides and phospholipids synthesis. The objective of this study was to evaluate lipin‐1 expression, its prognostic significance, and its correlation with p53 tumor suppressor in patients with BC. In this study, 55 pairs of fresh samples of BC and adjacent noncancerous tissue were used to analyze lipin‐1, using quantitative real‐time polymerase chain reaction and immunohistochemistry (IHC) staining. The expression of other clinicopathological variables and p53 was also examined using IHC technique. The cell migration was studied in MCF‐7 and MDA‐MB231 cells following the inhibition of lipin‐1 by propranolol. Our results show that the relative expression of lipin‐1 messenger RNA was significantly higher in BC tissues compared with the adjacent normal tissue and its inhibition reduced cell migration in cancer cells. This upregulation was negatively correlated with histological grade of tumor and p53 status (p = .001 and p = .034) respectively and positively correlated with the tumor size (p = .006). Our results also seem to indicate that the high lipin‐1 expression is related to a good prognosis in patients with BC. The expression of lipin‐1 may be considered as a novel independent prognostic factor. The inhibition of lipin‐1 may also have therapeutic significance for patients with BC. The correlation between lipin‐1 and p53 confirms the role of p53 in the regulation of lipid metabolism in cancer cells.

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“…We previously demonstrated that lipin-1 expression is critical for keratinocyte differentiation, as it controls the DAG level, activating protein kinase C (PKC) activity, particularly the alpha isoform 16 . However, little is known about the role of lipin-1 in inflammatory responses in skin cells, even though lipin-1 has been implicated in inflammation in various other cell types.…”

Section: Introductionmentioning

confidence: 99%

UVB-dependent inhibition of lipin-1 protects against proinflammatory responses in human keratinocytes

et al. 2020

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Lipin-1 is an Mg 2+-dependent phosphatidate phosphatase (PAP1) that catalyzes a critical step in the synthesis of glycerophospholipids and is also a cotranscriptional regulator. The role of lipin-1 in the regulation of inflammatory responses has been extensively studied in various cell types but not in skin cells. In the present study, the function of lipin-1 in UVB-induced proinflammatory responses was assessed in normal human epidermal keratinocytes (NHEKs). UVB radiation downregulated lipin-1 expression. Lipin-1 inhibition was mediated by UVB-dependent sterol-response element binding protein-1 (SREBP-1) inhibition. The UVB-dependent inhibition of lipin-1 and SREBP-1 was mediated by AMPK activation. UVB-induced activation of JNK was dependent on AMPK activation and mediated lipin-1 inhibition. Prevention of UVB-mediated lipin-1 repression by introducing a lipin-1 expression vector stimulated IL-6 and IL-8 production, suggesting that lipin-1 inhibition attenuates UVB-induced IL-6 and IL-8 production. The downregulation of lipin-1 ameliorated UVB-induced NF-ĸB phosphorylation, which might be attributed to the suppression of UVB-induced accumulation of free fatty acids (FFAs). Pharmacological inhibition of PAP1 with propranolol suppressed UVB-induced production of IL-6 and IL-8 in NHEKs and reconstituted human skin models. Taken together, lipin-1 is downregulated by exposure to UVB radiation, which confers protection against UVB-induced proinflammatory responses; therefore, the inhibition of lipin-1 is a potential strategy for photoaging.

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Lipin-1 expression is critical for keratinocyte differentiation

Cited by 13 publications

References 55 publications

Lipid signaling in keratinocytes: Lipin-1 plays a PArt

Lipid signaling in keratinocytes: Lipin-1 plays a PArt

Expression and clinicopathological significance of lipin‐1 in human breast cancer and its association with p53 tumor suppressor gene

UVB-dependent inhibition of lipin-1 protects against proinflammatory responses in human keratinocytes

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