scholarly journals Perilipin-related protein regulates lipid metabolism in C. elegans

2015 ◽  
Author(s):  
Ahmed A. Chughtai ◽  
Filip Kaššák ◽  
Markéta Kostrouchová ◽  
Jan Philipp Novotný ◽  
Michael W. Krause ◽  
...  
Keyword(s):  
Lipid Metabolism ◽  
Lipid Droplets ◽  
Fat Metabolism ◽  
Droplet Surface ◽  
Surface Proteins ◽  
Related Protein ◽  
Additional Mechanism ◽  
C Elegans ◽  
Functional Studies ◽  
Gene Inhibition

The perilipins are lipid droplet surface proteins that contribute to fat metabolism by controlling the access of lipids to lipolytic enzymes. Perilipins have been identified in organisms as diverse as metazoa, fungi, and amoebas but strikingly not in nematodes. Here we identify the protein encoded by the W01A8.1 gene in Caenorhabditis elegans as the closest homologue of metazoan perilipin. We demonstrate that nematode W01A8.1 is a cytoplasmic protein residing on lipid droplets. Human perilipins 1 and 2 localize in transgenic C. elegans on the same structures as proteins expressed from W01A8.1 gene. Inhibition and elimination of W01A8.1 affects the appearance of lipid droplets especially visible as the formation of large lipid droplets localized around the dividing nucleus during the early zygotic divisions. This phenomenon disappears in later stages of embryogenesis indicating the existence of an additional mechanism of lipid regulation in C. elegans. Our results demonstrate that perilipin-related regulation of fat metabolism is conserved in nematodes and provide new possibilities for functional studies of lipid metabolism.

scholarly journals Perilipin-related protein regulates lipid metabolism in C. elegans

2015 ◽  
Author(s):  
Ahmed A. Chughtai ◽  
Filip Kaššák ◽  
Markéta Kostrouchová ◽  
Jan Philipp Novotný ◽  
Michael W. Krause ◽  
...  
Keyword(s):  
Lipid Metabolism ◽  
Lipid Droplets ◽  
Fat Metabolism ◽  
Droplet Surface ◽  
Surface Proteins ◽  
Related Protein ◽  
Additional Mechanism ◽  
C Elegans ◽  
Functional Studies ◽  
Gene Inhibition

The perilipins are lipid droplet surface proteins that contribute to fat metabolism by controlling the access of lipids to lipolytic enzymes. Perilipins have been identified in organisms as diverse as metazoa, fungi, and amoebas but strikingly not in nematodes. Here we identify the protein encoded by the W01A8.1 gene in Caenorhabditis elegans as the closest homologue of metazoan perilipin. We demonstrate that nematode W01A8.1 is a cytoplasmic protein residing on lipid droplets. Human perilipins 1 and 2 localize in transgenic C. elegans on the same structures as proteins expressed from W01A8.1 gene. Inhibition and elimination of W01A8.1 affects the appearance of lipid droplets especially visible as the formation of large lipid droplets localized around the dividing nucleus during the early zygotic divisions. This phenomenon disappears in later stages of embryogenesis indicating the existence of an additional mechanism of lipid regulation in C. elegans. Our results demonstrate that perilipin-related regulation of fat metabolism is conserved in nematodes and provide new possibilities for functional studies of lipid metabolism.

scholarly journals Perilipin-related protein regulates lipid metabolism in C. elegans

2015 ◽  
Author(s):  
Ahmed A. Chughtai ◽  
Filip Kaššák ◽  
Markéta Kostrouchová ◽  
Jan Philipp Novotný ◽  
Michael W. Krause ◽  
...  
Keyword(s):  
Lipid Metabolism ◽  
Lipid Droplets ◽  
Fat Metabolism ◽  
Droplet Surface ◽  
Surface Proteins ◽  
Related Protein ◽  
Additional Mechanism ◽  
C Elegans ◽  
Functional Studies ◽  
Gene Inhibition

The perilipins are lipid droplet surface proteins that contribute to fat metabolism by controlling the access of lipids to lipolytic enzymes. Perilipins have been identified in organisms as diverse as metazoa, fungi, and amoebas but strikingly not in nematodes. Here we identify the protein encoded by the W01A8.1 gene in Caenorhabditis elegans as the closest homologue of metazoan perilipin. We demonstrate that nematode W01A8.1 is a cytoplasmic protein residing on lipid droplets. Human perilipins 1 and 2 localize in transgenic C. elegans on the same structures as proteins expressed from W01A8.1 gene. Inhibition and elimination of W01A8.1 affects the appearance of lipid droplets especially visible as the formation of large lipid droplets localized around the dividing nucleus during the early zygotic divisions. This phenomenon disappears in later stages of embryogenesis indicating the existence of an additional mechanism of lipid regulation in C. elegans. Our results demonstrate that perilipin-related regulation of fat metabolism is conserved in nematodes and provide new possibilities for functional studies of lipid metabolism.

scholarly journals Multifunctional pyrazoline based AIEgens: real-time tracking and specific protein “fishing” of lipid droplets

2019 ◽  
Vol 10 (39) ◽  
pp. 9009-9016 ◽  
Author(s):  
Na Zhao ◽  
Yan Li ◽  
Weiyao Yang ◽  
Jiabao Zhuang ◽  
Yue Li ◽  
...  
Keyword(s):  
Lipid Metabolism ◽  
Real Time ◽  
Intracellular Ph ◽  
Lipid Droplet ◽  
Lipid Droplets ◽  
Specific Protein ◽  
Related Protein ◽  
Dual Color ◽  
Real Time Tracking

A series of multifunctional pyrazoline based AIEgens were developed for real-time tracking of lipid metabolism, reversibly monitoring intracellular pH in dual-color mode and specific labeling of lipid droplet related protein.

scholarly journals HCV Pit Stop at the Lipid Droplet: Refuel Lipids and Put on a Lipoprotein Coat before Exit

Cells ◽  
2019 ◽  
Vol 8 (3) ◽  
pp. 233 ◽  
Author(s):  
Gabrielle Vieyres ◽  
Thomas Pietschmann
Keyword(s):  
Lipid Metabolism ◽  
Lipid Droplet ◽  
Cell Biology ◽  
Lipid Droplets ◽  
Protein Translocation ◽  
Droplet Surface ◽  
Replication Cycle ◽  
Virion Assembly ◽  
Host Interactions ◽  
Virus Replication Cycle

The replication cycle of the liver-tropic hepatitis C virus (HCV) is tightly connected to the host lipid metabolism, during the virus entry, replication, assembly and egress stages, but also while the virus circulates in the bloodstream. This interplay coins viral particle properties, governs viral cell tropism, and facilitates immune evasion. This review summarizes our knowledge of these interactions focusing on the late steps of the virus replication cycle. It builds on our understanding of the cell biology of lipid droplets and the biosynthesis of liver lipoproteins and attempts to explain how HCV hijacks these organelles and pathways to assemble its lipo-viro-particles. In particular, this review describes (i) the mechanisms of viral protein translocation to and from the lipid droplet surface and the orchestration of an interface between replication and assembly complexes, (ii) the importance of the triglyceride mobilization from the lipid droplets for HCV assembly, (iii) the interplay between HCV and the lipoprotein synthesis pathway including the role played by apolipoproteins in virion assembly, and finally (iv) the consequences of these complex virus–host interactions on the virion composition and its biophysical properties. The wealth of data accumulated in the past years on the role of the lipid metabolism in HCV assembly and its imprint on the virion properties will guide vaccine design efforts and reinforce our understanding of the hepatic lipid metabolism in health and disease.

scholarly journals Overexpression of PLIN1 Promotes Lipid Metabolism in Bovine Adipocytes

Animals ◽  
2020 ◽  
Vol 10 (11) ◽  
pp. 1944
Author(s):  
Shijun Li ◽  
Sayed Haidar Abbas Raza ◽  
Chunping Zhao ◽  
Gong Cheng ◽  
Linsen Zan
Keyword(s):  
Lipid Metabolism ◽  
Differentially Expressed Genes ◽  
Fat Metabolism ◽  
Vital Role ◽  
Surface Proteins ◽  
Differentially Expressed ◽  
Transcriptional Level ◽  
Proliferation And Differentiation ◽  
Ppar Signaling ◽  
Bovine Adipocytes

Perilipin 1 (PLIN1) is a protein encoded by the PLIN1 gene in eukaryotes. PLIN1 is a member of the PAT protein family, a family of proteins related to lipid droplet (LD) surface proteins. PLIN1 phosphorylation plays a vital role during fat metabolism of adipose tissue lipolysis and fat storage in adipocytes. However, to further explore the regulation of the PLIN1 gene on the proliferation, differentiation and lipid metabolism of bovine adipocytes. In this study, the mRNA expression of PLIN1, at day six, was the highest during bovine adipocyte differentiation. Moreover, PLIN1 can promote the proliferation and differentiation of preadipocytes in cattle. On the sixth day, after transfection with, and overexpression of, the PLIN1 gene in bovine preadipocytes via adenovirus, cell samples were collected, and transcriptome sequencing was performed. A total of 1923 differentially expressed genes were detected. Through GO and KEGG pathway analysis, the differentially expressed genes were established to be mainly enriched in the AMPK, Wnt, and PPAR signaling pathways related to fat proliferation and differentiation. In conclusion, at the transcriptional level, PLIN1 plays an important role in regulating fat proliferation and metabolism. Additionally, the sequencing results screened new differentially expressed genes related to fat metabolism, providing theoretical support for molecular breeding of Qinchuan beef cattle.

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