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1.
Cell Tissue Res ; 379(1): 45-62, 2020 Jan.
Artigo em Inglês | MEDLINE | ID: mdl-31858241

RESUMO

Lipid droplet (LD) binding proteins in mammary glands and in adipocytes were previously compared and striking similar sets of these specific proteins demonstrated. Xanthine oxidoreductase (XOR) together with perilipins and the lactating mammary gland protein butyrophilin play an important role in the secretion process of LDs into milk ducts. In contrast, in adipose tissue and in adipocytes, mainly perilipins have been described. Moreover, XOR was reported in mouse adipose tissue and adipocyte culture cells as "novel regulator of adipogenesis". This obvious coincidence of protein sets prompted us to revisit the formation of LDs in human-cultured adipocytes in more detail with special emphasis on the possibility of a LD association of XOR. We demonstrate by electron and immunoelectron microscopy new structural details on LD formation in adipocytes. Surprisingly, by immunological and proteomic analysis, we identify in contrast to previous data showing the enzyme XOR, predominantly the expression of aldehyde oxidase (AOX). AOX could be detected tightly linked to LDs when adipocytes were treated with starvation medium. In addition, the majority of cells show an enormous interconnected, tubulated mitochondria network. Here, we discuss that (1) XOR is involved-together with perilipins-in the secretion of LDs in alveolar epithelial cells of the lactating mammary gland and is important in the transcytosis pathway of capillary endothelial cells. (2) In cells, where LDs are not secreted, XOR cannot be detected at the protein level, whereas in contrast in these cases, AOX is often present. We detect AOX in adipocytes together with perilipins and find evidence that these proteins might direct LDs to mitochondria. Finally, we here report for the first time the exclusive and complementary localization of XOR and AOX in diverse cell types.


Assuntos
Adipócitos/metabolismo , Aldeído Oxidase/biossíntese , Gotículas Lipídicas/metabolismo , Adipócitos/enzimologia , Adipócitos/ultraestrutura , Animais , Células Cultivadas , Meios de Cultura , Humanos , Perilipinas/metabolismo , Xantina Desidrogenase/metabolismo
2.
Sheng Li Xue Bao ; 71(3): 379-387, 2019 Jun 25.
Artigo em Inglês | MEDLINE | ID: mdl-31218328

RESUMO

Adipose tissue is the main energy reserve of the body. When energy is required, adipocyte triglycerides stored in lipid droplets (LDs) are broken down by lipase, and free fatty acids are released to supply the physiological need. Intracellular LDs are active metabolic organelles in mammalian cells, particularly in adipocytes. The present study was aimed to investigate the morphological changes of LDs and the alternation of LD-associated perilipin family proteins during long-term lipolysis stimulated by forskolin. Primary differentiated adipocytes derived from epididymal fat pads of Sprague-Dawley (SD) rats were incubated in the presence or absence of 1 µmol/L forskolin for 24 h. Content of glycerol released to the culture medium was determined by a colorimetric assay and served as an index of lipolysis. Morphological changes of LDs were observed by Nile red staining. The mRNA level of perilipin family genes was detected by quantitative real-time PCR. The protein level and subcellular localization were examined by immunoblotting and immunofluorescence staining, respectively. The results showed that forskolin induced sustained lipolysis in differentiated adipocytes. The morphology of LDs changed in a time-dependent manner. Large clustered LDs became gradually smaller in size and eventually disappeared; in contrast, peripheral micro-LDs increased gradually in number until the cytoplasm was filled with numerous micro-LDs. The protein level of the perilipin family proteins showed obvious alternation. Mature adipocytes physiologically expressed a very low level of Plin2 protein, whereas in adipocytes stimulated with lipolytic forskolin, the protein and mRNA levels of Plin2 were significantly increased, and the increased Plin2 was specifically bound to the surface of LDs. During chronic stimulation of forskolin, the mRNA level of Plin3 was unchanged, but the mRNA levels of Plin1, Plin4 and Plin5 were significantly decreased. These results suggest that the morphology of LDs and perilipin family proteins on the surface of LDs are significantly altered during long-term lipolysis stimulated by forskolin, representing a dynamic process of the remodeling of LDs.


Assuntos
Adipócitos/efeitos dos fármacos , Colforsina/farmacologia , Gotículas Lipídicas , Lipólise , Perilipinas/metabolismo , Animais , Células Cultivadas , Perilipina-2/metabolismo , Ratos , Ratos Sprague-Dawley
3.
Mol Biol Cell ; 30(5): 703-716, 2019 03 01.
Artigo em Inglês | MEDLINE | ID: mdl-30649995

RESUMO

Lipid droplets (LDs) in all eukaryotic cells are coated with at least one of the perilipin (Plin) family of proteins. They all regulate key intracellular lipases but do so to significantly different extents. Where more than one Plin is expressed in a cell, they associate with LDs in a hierarchical manner. In vivo, this means that lipid flux control in a particular cell or tissue type is heavily influenced by the specific Plins present on its LDs. Despite their early discovery, exactly how Plins target LDs and why they displace each other in a "hierarchical" manner remains unclear. They all share an amino-terminal 11-mer repeat (11mr) amphipathic region suggested to be involved in LD targeting. Here, we show that, in vivo, this domain functions as a primary highly reversible LD targeting motif in Plin1-3, and, in vitro, we document reversible and competitive binding between a wild-type purified Plin1 11mr peptide and a mutant with reduced binding affinity to both "naked" and phospholipid-coated oil-water interfaces. We also present data suggesting that a second carboxy-terminal 4-helix bundle domain stabilizes LD binding in Plin1 more effectively than in Plin2, whereas it weakens binding in Plin3. These findings suggest that dual amphipathic helical regions mediate LD targeting and underpin the hierarchical binding of Plin1-3 to LDs.


Assuntos
Gotículas Lipídicas/metabolismo , Perilipinas/química , Perilipinas/metabolismo , Motivos de Aminoácidos , Linhagem Celular Tumoral , Humanos , Proteínas Mutantes/metabolismo , Óleos , Fosfolipídeos/metabolismo , Ligação Proteica , Domínios Proteicos , Água
4.
Br Poult Sci ; 59(5): 494-505, 2018 Oct.
Artigo em Inglês | MEDLINE | ID: mdl-30004246

RESUMO

1. Adipose differentiation related protein (ADFP), fatty acid transport protein 1 (FATP1) and apolipoprotein B (APOB) are suspected to play an important role in determining intramuscular fat and in overall meat quality. 2. Yunnan's top six famous chicken breeds (the Daweishan Mini, Yanjin Black-bone, Chahua, Wuding, Wuliangshan Black-bone and Piao chicken) are known for the high quality of their meat, but little is known about their expression of these three genes. 3. The present study aimed to examine the ADFP, FATP1 and APOB genes in different tissues of these six breeds at different development stages. The subcutaneous fat from the back midline and front, abdominal fat, liver and muscle tissue was sampled at 28, 49, 70, 91 and 112 days. The expression of ADFP, FATP1 and APOB was measured by real-time PCR. 4. The results showed that the expression of the three genes differed depending on age, tissue types and breeds. However, the expression of the three genes correlated with fat traits. In conclusion, the expression of the ADFP, FATP1 and APOB genes is associated with the fat traits of Yunnan's top six chicken breeds. These results could help with molecular marker screening and marker-assisted breeding to improve the quality of poultry for meat production.


Assuntos
Tecido Adiposo/metabolismo , Apolipoproteínas B/genética , Cruzamento , Galinhas/fisiologia , Proteínas de Transporte de Ácido Graxo/genética , Perilipinas/genética , Animais , Biomarcadores/análise , Galinhas/genética , China , Perfilação da Expressão Gênica , Músculos/metabolismo , Perilipina-2 , Fenótipo , Aves Domésticas/genética , Aves Domésticas/fisiologia , RNA Mensageiro , Reação em Cadeia da Polimerase em Tempo Real
5.
J Histochem Cytochem ; 66(6): 447-465, 2018 06.
Artigo em Inglês | MEDLINE | ID: mdl-29361239

RESUMO

Determination of lipid droplet (LD) volume has depended on direct measurement of the diameter of individual LDs, which is not possible when LDs are small or closely apposed. To overcome this problem, we describe a new method in which a volume-fluorescence relationship is determined from automated analysis of calibration samples containing well-resolved LDs. This relationship is then used to estimate total cellular droplet volume in experimental samples, where the LDs need not be individually resolved, or to determine the volumes of individual LDs. We describe quantitatively the effects of various factors, including image noise, LD crowding, and variation in LD composition on the accuracy of this method. We then demonstrate this method by utilizing it to address a scientifically interesting question, to determine the density of green fluorescent protein (GFP)-tagged Perilipin-Adipocyte-Tail (PAT) proteins on the LD surface. We find that PAT proteins cover only a minority of the LD surface, consistent with models in which they primarily serve as scaffolds for binding of regulatory proteins and enzymes, but inconsistent with models in which their major function is to sterically block access to the droplet surface.


Assuntos
Processamento de Imagem Assistida por Computador/métodos , Gotículas Lipídicas/ultraestrutura , Microscopia Confocal/métodos , Perilipinas/análise , Técnicas de Cultura de Células/métodos , Transferência Ressonante de Energia de Fluorescência/métodos , Proteínas de Fluorescência Verde/análise , Células HeLa , Células Hep G2 , Humanos , Gotículas Lipídicas/química , Software
6.
Anim Sci J ; 89(5): 743-751, 2018 May.
Artigo em Inglês | MEDLINE | ID: mdl-29380492

RESUMO

The objective of this study was to identify genomic regions associated with fat-related traits using a Japanese Black cattle population in Hyogo. From 1836 animals, those with high or low values were selected on the basis of corrected phenotype and then pooled into high and low groups (n = 100 each), respectively. DNA pool-based genome-wide association study (GWAS) was performed using Illumina BovineSNP50 BeadChip v2 with three replicate assays for each pooled sample. GWAS detected that two single nucleotide polymorphisms (SNPs) on BTA7 (ARS-BFGL-NGS-35463 and Hapmap23838-BTA-163815) and one SNP on BTA12 (ARS-BFGL-NGS-2915) significantly affected fat percentage (FAR). The significance of ARS-BFGL-NGS-35463 on BTA7 was confirmed by individual genotyping in all pooled samples. Moreover, association analysis between SNP and FAR in 803 Japanese Black cattle revealed a significant effect of SNP on FAR. Thus, further investigation of these regions is required to identify FAR-associated genes and mutations, which can lead to the development of DNA markers for marker-assisted selection for the genetic improvement of beef quality.


Assuntos
Distribuição da Gordura Corporal , Bovinos/genética , Bovinos/metabolismo , DNA/genética , Qualidade dos Alimentos , Estudo de Associação Genômica Ampla , Processamento de Imagem Assistida por Computador/métodos , Carne , Polimorfismo de Nucleotídeo Único/genética , Locos de Características Quantitativas/genética , Fatores de Troca de Nucleotídeo Guanina Rho/genética , Proteína 4 Semelhante a Angiopoietina/genética , Animais , Feminino , Frequência do Gene , Técnicas de Genotipagem , Japão , Masculino , Perilipinas/genética
7.
Acta Cir Bras ; 32(11): 891-902, 2017 Nov.
Artigo em Inglês | MEDLINE | ID: mdl-29236794

RESUMO

PURPOSE: To evaluate the feasibility of an experimental model of autologous fat graft (AFG) in different interstitial pressure (IP) environments. METHODS: Three mini-pigs(Minipig-BR) with age of 8 months (weight: 25-30 kg) were used. AFG were collected from the bucal fat pad, and grafted in the intramuscular pocket (biceps femoralis muscle). IP model was based on a fusiform ressection followed by primary closure "under tension". A blood pressure catheter located in the intramuscular region connected to a pressure module was applied to quantify IP. RESULTS: The mean operative time was 236 min (210 - 272 min). All the AFG and muscular segments were removed successfully. Average interstitial pressure CP and H were 3 and 10.6 mmHg respectively. The AFG were biopsied for histopathological analysis 30 days after graft. Hematoxylin-eosin staining and immunohistochemical analyzes (TNF-alpha, CD31 and Perilipine with monoclonal antibodies) were employed. CONCLUSION: The data show that minipigs model could be used as a recipient site for autologous fat graft techniques and allow the development of studies to explore the AFG intake and pathophysiology response.


Assuntos
Tecido Adiposo/transplante , Modelos Animais de Doenças , Procedimentos Cirúrgicos Reconstrutivos/métodos , Transplante Autólogo/métodos , Animais , Estudos de Viabilidade , Sobrevivência de Enxerto , Imuno-Histoquímica , Masculino , Perilipinas/análise , Molécula-1 de Adesão Celular Endotelial a Plaquetas/análise , Pressão , Procedimentos Cirúrgicos Reconstrutivos/normas , Suínos , Porco Miniatura , Transplante Autólogo/normas , Fator de Necrose Tumoral alfa
8.
Biochem Biophys Res Commun ; 494(1-2): 292-297, 2017 12 09.
Artigo em Inglês | MEDLINE | ID: mdl-29024632

RESUMO

Mammary gland is an important organ for milk synthesis and secretion. It undergoes dramatic physiological changes to adapt the shift from peak to late lactation stage. Protein plays a final very vital role in many life functions, and the protein changes during different lactation stages potentially reflect the biology of lactation and the functions of mammary gland in cows. In current study, we adopted tandem mass tags label-based quantitative analysis technique and to investigate proteome changes occurring in bovine mammary gland from peak to late lactation stages. A total of 3753 proteins from mammary tissues taken at two lactation points from four individual cows by biopsy were quantified, out of which 179 proteins were expressed differentially between two stages. We observed five new DEPs (AACS, DHCR7, GSTM3, SFRP1 and SFRP4) and nine functional well-studies known proteins (PLIN2, LPIN1, PLIN3, GSN, CD74, MMP2, SOD1, SOD3 and GPX3) related to milk performance and mammary morphology. Bioinformatics analyses of the DEPs showed a majority of the up-regulated proteins during late lactation stage were related to apoptosis and immune process, while the downregulated proteins were mainly involved in localization, lipid metabolic and transport process. This suggests that the mammary gland can adapt to different molecular functions according to the biological need of the animal. From the integrated analysis of the differentially expressed proteins with known quantitative trait loci and genome-wide association study data, we identified 95 proteins may potentially affect milking performance. We expect findings in this study could be a valuable resource for future studies investigating the bovine proteome and functional studies.


Assuntos
Regulação da Expressão Gênica no Desenvolvimento , Lactação/genética , Glândulas Mamárias Animais/metabolismo , Proteoma/genética , Locos de Características Quantitativas , Animais , Apoptose , Bovinos , Feminino , Ontologia Genética , Glutationa Transferase/genética , Glutationa Transferase/imunologia , Imunidade Inata , Isoenzimas/genética , Isoenzimas/imunologia , Glândulas Mamárias Animais/crescimento & desenvolvimento , Metaloproteinase 2 da Matriz/genética , Metaloproteinase 2 da Matriz/imunologia , Anotação de Sequência Molecular , Oxirredutases atuantes sobre Doadores de Grupo CH-CH/genética , Oxirredutases atuantes sobre Doadores de Grupo CH-CH/imunologia , Perilipinas/genética , Perilipinas/imunologia , Proteoma/imunologia , Proteômica , Superóxido Dismutase/genética , Superóxido Dismutase/imunologia
11.
Int J Obes (Lond) ; 41(12): 1745-1754, 2017 Dec.
Artigo em Inglês | MEDLINE | ID: mdl-28736444

RESUMO

BACKGROUND/OBJECTIVES: In obesity, improved muscle insulin sensitivity following exercise training has been linked to the lowering of diacylglycerol (DAG) and ceramide concentrations. Little is known, however, about how improved insulin action with exercise training in obese individuals relates to lipid droplet (LD) adaptations in skeletal muscle. In this study we investigated the hypothesis that short-term sprint interval training (SIT) and moderate-intensity continuous training (MICT) in obese individuals would increase perilipin (PLIN) expression, increase the proportion of LDs in contact with mitochondria and reduce muscle concentrations of DAGs and ceramides. METHODS: Sixteen sedentary obese males performed 4 weeks of either SIT (4-7 × 30 s sprints at 200% Wmax, 3 days week) or MICT (40-60 min cycling at ~65% VO2peak, 5 days per week), and muscle biopsies were obtained pre- and post-training. RESULTS: Training increased PLIN2 (SIT 90%, MICT 68%) and PLIN5 (SIT 47%, MICT 34%) expression in type I fibres only, and increased PLIN3 expression in both type I (SIT 63%, MICT 67%) and type II fibres (SIT 70%, MICT 160%) (all P<0.05). Training did not change LD content but increased the proportion of LD in contact with mitochondria (SIT 12%, MICT 21%, P<0.01). Ceramides were reduced following training (SIT -10%, MICT -7%, P<0.05), but DAG was unchanged. No training × group interactions were observed for any variables. CONCLUSIONS: These results confirm the hypothesis that SIT and MICT results in remodelling of LDs and lowers ceramide concentrations in skeletal muscle of sedentary obese males.


Assuntos
Ceramidas/metabolismo , Treinamento Intervalado de Alta Intensidade , Gotículas Lipídicas/metabolismo , Músculo Esquelético/metabolismo , Obesidade/metabolismo , Adulto , Humanos , Resistência à Insulina , Peptídeos e Proteínas de Sinalização Intracelular , Gotículas Lipídicas/ultraestrutura , Masculino , Obesidade/fisiopatologia , Obesidade/terapia , Consumo de Oxigênio , Perilipinas/fisiologia , Comportamento Sedentário
12.
J Diabetes Res ; 2017: 1789395, 2017.
Artigo em Inglês | MEDLINE | ID: mdl-28676863

RESUMO

Skeletal muscle is one of the main regulators of carbohydrate and lipid metabolism in our organism, and therefore, it is highly susceptible to changes in glucose and fatty acid (FA) availability. Skeletal muscle is an extremely complex tissue: its metabolic capacity depends on the type of fibers it is made up of and the level of stimulation it undergoes, such as acute or chronic contraction. Obesity is often associated with increased FA levels, which leads to the accumulation of toxic lipid intermediates, oxidative stress, and autophagy in skeletal fibers. This lipotoxicity is one of the most common causes of insulin resistance (IR). In this scenario, the "isolation" of certain lipids in specific cell compartments, through the action of the specific lipid droplet, perilipin (PLIN) family of proteins, is conceived as a lifeguard compensatory strategy. In this review, we summarize the cellular mechanism underlying lipid mobilization and metabolism inside skeletal muscle, focusing on the function of lipid droplets, the PLIN family of proteins, and how these entities are modified in exercise, obesity, and IR conditions.


Assuntos
Ácidos Graxos/metabolismo , Gotículas Lipídicas/metabolismo , Metabolismo dos Lipídeos/fisiologia , Músculo Esquelético/metabolismo , Perilipinas/metabolismo , Animais , Autofagia/fisiologia , Estresse Oxidativo/fisiologia
13.
J Physiol ; 595(16): 5587-5601, 2017 08 15.
Artigo em Inglês | MEDLINE | ID: mdl-28560826

RESUMO

KEY POINTS: The lipid droplet (LD)-associated perilipin (PLIN) proteins promote intramuscular triglyceride (IMTG) storage, although whether the abundance and association of the PLIN proteins with LDs is related to the diverse lipid storage in muscle between trained and sedentary individuals is unknown. We show that lipid infusion augments IMTG content in type I fibres of both trained and sedentary individuals. Most importantly, despite there being no change in PLIN protein content, lipid infusion did increase the number of LDs connected with PLIN proteins in trained individuals only. We conclude that trained individuals are able to redistribute the pre-existing pool of PLIN proteins to an expanded LD pool during lipid infusion and, via this adaptation, may support the storage of fatty acids in IMTG. ABSTRACT: Because the lipid droplet (LD)-associated perilipin (PLIN) proteins promote intramuscular triglyceride (IMTG) storage, we investigated the hypothesis that differential protein content of PLINs and their distribution with LDs may be linked to the diverse lipid storage in muscle between trained and sedentary individuals. Trained (n = 11) and sedentary (n = 10) subjects, matched for age, sex and body mass index, received either a 6 h lipid or glycerol infusion in the setting of a concurrent hyperinsulinaemic-euglycaemic clamp. Sequential muscle biopsies (0, 2 and 6 h) were analysed using confocal immunofluorescence microscopy for fibre type-specific IMTG content and PLIN associations with LDs. In both groups, lipid infusion increased IMTG content in type I fibres (trained: +62%, sedentary: +79%; P < 0.05) but did not affect PLIN protein content. At baseline, PLIN2 (+65%), PLIN3 (+105%) and PLIN5 (+53%; all P < 0.05) protein content was higher in trained compared to sedentary individuals. In trained individuals, lipid infusion increased the number of LDs associated with PLIN2 (+27%), PLIN3 (+73%) and PLIN5 (+40%; all P < 0.05) in type I fibres. By contrast, in sedentary individuals, lipid infusion only increased the number of LDs not associated with PLIN proteins. Acute free fatty acid elevation therefore induces a redistribution of PLIN proteins to an expanded LD pool in trained individuals only and this may be part of the mechanism that enables fatty acids to be stored in IMTG.


Assuntos
Exercício Físico/fisiologia , Lipídeos/farmacologia , Músculo Esquelético/fisiologia , Perilipinas/fisiologia , Adulto , Feminino , Humanos , Masculino , Adulto Jovem
15.
J Physiol Pharmacol ; 68(1): 3-11, 2017 Feb.
Artigo em Inglês | MEDLINE | ID: mdl-28456765

RESUMO

For 40 years, the enzyme hormone sensitive lipase was considered to hydrolyze the first ester bond of the triacylglycerol moiety and thus initiate hydrolysis. However, 12 years ago a new lipolytic enzyme, termed adipose triglyceride lipase was discovered. It was further shown that the process of lipolysis of triacylglycerol to diacylglycerol and fatty acid is initiated by adipose triglyceride lipase and not by hormone sensitive lipase, responsible for hydrolysis of diacylglycerol to monoacyglycerol and fatty acid. Adipose triglyceride lipase is present in all types of cells containing neutral fat. The enzyme is activated by a protein called comparative gene identification-58 and inhibited by a protein called G0/G1 switch protein 2. It has also been discovered that perilipins, the main proteins coating lipid droplets in the cells, are involved in the process of triacylglycerol lipolysis. Five perilipins (1-5) were identified, however, up to now their role has been poorly assessed. In skeletal muscles, exercise and training affect the mRNA expression and protein content of adipose triglyceride lipase, comparative gene identification-58, G0/G1 switch protein 2, perilipin 2 and 5. The effect of exercise/training depends on exercise intensity and type of muscle fiber. An interaction between comparative gene identification-58 and adipose triglyceride lipase seems to be responsible for the enzyme activation during contractile activity. Adipose triglyceride lipase is also responsible for the activation of the first step of triacylglycerol lipolysis in the heart. There is substantial evidence that cardiac triacylglycerol metabolism affects the function of the heart. ATGL gene mutations leads to the development of neutral lipid storage diseases.


Assuntos
Músculo Esquelético/metabolismo , Miocárdio/metabolismo , Triglicerídeos/metabolismo , Tecido Adiposo/metabolismo , Animais , Humanos , Hidrólise , Lipólise , Perilipinas/metabolismo
16.
FASEB J ; 31(8): 3689-3694, 2017 08.
Artigo em Inglês | MEDLINE | ID: mdl-28476896

RESUMO

Plasma endothelial cell-derived exosomes (EDEs) and platelet-derived exosomes (PDEs) were precipitated and enriched separately by immunospecific absorption procedures for analyses of cargo proteins relevant to atherosclerosis. EDEs had usual exosome size and marker protein content, and significantly higher levels than PDEs of the endothelial proteins vascular cell adhesion molecule-1 (VCAM-1) and endothelial nitric oxide synthase, whereas PDEs had significantly higher levels of platelet glycoprotein VI. EDE levels of VCAM-1, von Willebrand factor, platelet-derived growth factor (PDGF)-BB, angiopoietin-1, and lysyl oxidase-2 and the cerebrovascular-selective proteins glucose transporter 1, permeability-glycoprotein, and large neutral amino acid transporter 1 were significantly higher for 18 patients with cerebrovascular disease (CeVD) than for 18 age- and gender-matched control subjects. PDE levels of PDGF-AA, platelet glycoprotein VI, integrin-linked kinase-1, high mobility group box-1 protein, chemokine CXCL4, and thrombospondin-1 were significantly higher in patients with CeVD than in control subjects, but differences were less with greater overlaps than for EDE proteins. EDE levels of Yes-associated protein (YAP) were higher and of P(S127)-YAP lower in patients with CeVD than in control subjects, consistent with heightened activity of this mechanical force-sensitive system in atherosclerosis. Elevated EDE and PDE levels of atherosclerosis-promoting proteins in CeVD justify clinical studies of their potential value as biomarkers.-Goetzl, E. J., Schwartz, J. B., Mustapic, M., Lobach, I. V., Daneman, R., Abner, E. L., Jicha, G. A. Altered cargo proteins of human plasma endothelial cell-derived exosomes in atherosclerotic cerebrovascular disease.


Assuntos
Aterosclerose/metabolismo , Plaquetas/fisiologia , Proteínas de Transporte/metabolismo , Transtornos Cerebrovasculares/metabolismo , Células Endoteliais/fisiologia , Exossomos/fisiologia , Idoso , Feminino , Regulação da Expressão Gênica/fisiologia , Humanos , Masculino , Perilipinas/metabolismo
17.
J Am Acad Dermatol ; 77(2): 268-273.e6, 2017 Aug.
Artigo em Inglês | MEDLINE | ID: mdl-28551069

RESUMO

BACKGROUND: Hidradenitis suppurativa (HS) is a debilitating skin disease characterized by painful recurrent nodules and abscesses caused by chronic inflammation. Early events in the development of HS are believed to occur in the folliculopilosebaceous unit; however, the signaling pathways behind this mechanism are unknown. Sphingolipids, such as ceramide, are essential components of the skin and appendages and have important structural and signaling roles. OBJECTIVE: We sought to explore whether the gene expression of enzymes involved in sphingolipid metabolic pathways is altered in HS. METHODS: A microarray data set including 30 samples was used to compare the expression of sphingolipid-related enzymes in inflammatory skin lesions from HS patients (n = 17) with the expression in clinically healthy skin tissue (n = 13). Differential expression of sphingolipid metabolism-related genes was analyzed using Gene Expression Omnibus 2R. RESULTS: HS lesional skin samples have significantly decreased expression of enzymes generating ceramide and sphingomyelin, increased expression of enzymes catabolizing ceramide to sphingosine, and increased expression of enzymes converting ceramide to galactosylceramide and gangliosides. LIMITATIONS: Limitations of this study include assessing the expression of sphingolipid-related enzymes without assessing the levels of the related sphingolipids. CONCLUSION: Our study suggests that sphingolipid metabolism is altered in HS lesional skin compared with normal skin.


Assuntos
Expressão Gênica , Hidradenite Supurativa/enzimologia , Hidradenite Supurativa/genética , Perilipinas/genética , Pele/enzimologia , Esfingolipídeos/metabolismo , Ceramidase Alcalina/genética , Estudos de Casos e Controles , Ceramidas/metabolismo , Proteínas Quinases Dependentes de AMP Cíclico/genética , Glucosilceramidase/genética , Glucosiltransferases/genética , Glicoesfingolipídeos/metabolismo , Hexosaminidases/genética , Humanos , Lisofosfolipídeos/metabolismo , Proteínas de Membrana/genética , Redes e Vias Metabólicas/genética , Fosfotransferases (Aceptor do Grupo Álcool)/genética , Serina C-Palmitoiltransferase/genética , Transdução de Sinais/genética , Esfingolipídeos/biossíntese , Esfingomielina Fosfodiesterase/genética , Esfingomielinas/metabolismo , Esfingosina/análogos & derivados , Esfingosina/metabolismo , Esfingosina N-Aciltransferase/genética , Proteínas Supressoras de Tumor/genética
18.
Lipids Health Dis ; 16(1): 83, 2017 Apr 28.
Artigo em Inglês | MEDLINE | ID: mdl-28454542

RESUMO

Intracellular lipid droplets (LDs) are found in a wide variety of cell types and have been recognized as organelles with unique spherical structures. Although LDs are not stable lipid-depots, they are active sites of neutral lipid metabolism, and comprise neutral lipid or cholesterol cores surrounded by phospholipid monolayers containing specialized proteins. However, sizes and protein compositions vary between cell and tissue types. Proteins of the perilipin family have been associated with surfaces of LDs and all carry a conserved 11-mer repeat motif. Accumulating evidence indicates that all perilipins are involved in LD formation and that all play roles in LD function under differing conditions. In this brief review, we summarize current knowledge of the roles of perilipins and lipid metabolizing enzymes in a variety of mammalian cell types.


Assuntos
Adipócitos/metabolismo , Hidroxiesteroide Desidrogenases/genética , Gotículas Lipídicas/metabolismo , Metabolismo dos Lipídeos/genética , Perilipinas/genética , Animais , Colesterol/metabolismo , Retículo Endoplasmático/metabolismo , Regulação da Expressão Gênica , Humanos , Hidroxiesteroide Desidrogenases/metabolismo , Mitocôndrias/metabolismo , Perilipinas/química , Perilipinas/classificação , Perilipinas/metabolismo , Domínios Proteicos , Transdução de Sinais , Triglicerídeos/metabolismo
19.
Lipids Health Dis ; 16(1): 52, 2017 Mar 09.
Artigo em Inglês | MEDLINE | ID: mdl-28274232

RESUMO

BACKGROUND: The variations in perilipin gene (PLIN) were previously associated with obesity. We examined the association of polymorphisms at the PLIN locus in adolescents with obesity and their connection with serum adipokines. METHODS: A total of 308 children (206 obese, 66.8% and 102 healthy control, 33.2%) between the ages of 10-18 years were included into the study. PLIN gene analysis [PLIN 1, PLIN 4, PLIN 6, PLIN 5'UTR-1234 C > G and PLIN 10171 A/T] were studied by Real Time-PCR. Serum leptin, adiponectin, resistin and ghrelin levels were studied by ELISA method in both groups and their link with perilipin polymorphisms were analyzed. RESULTS: Serum leptin level was found significantly high in obese adolescents. Other adipokine levels were similar in both groups. The incidence of PLIN 1, PLIN 4, PLIN 5'UTR-1234 C > G and PLIN 10171 A/T minor and major alleles was similar in both groups. PLIN 6 T/T allele was determined significantly high in obese adolescents compared to that of control group. No correlation was detected between perilipin polymorphism and serum levels of adipokines. CONCLUSION: The PLIN 6 polymorphism of the perilipin gene may influence the risk of the obesity during adolescence. TRIAL REGISTRATION: Retrospectively registered.


Assuntos
Obesidade Pediátrica/genética , Perilipinas/genética , Adipocinas/sangue , Adolescente , Estudos de Casos e Controles , Criança , Feminino , Frequência do Gene , Estudos de Associação Genética , Predisposição Genética para Doença , Humanos , Masculino , Obesidade Pediátrica/sangue , Polimorfismo de Nucleotídeo Único , Fatores de Risco
20.
Anat Sci Int ; 92(1): 50-54, 2017 Jan.
Artigo em Inglês | MEDLINE | ID: mdl-27822589

RESUMO

Lipid droplets (LDs) are ubiquitous organelles that store and supply lipids to regulate cellular lipid homeostasis. Fatty acids are packaged as triglyceride and cholesterol ester into endoplasmic reticulum (ER) membranes to synthesize LDs. Cytosolic LDs move dynamically and interact with organelles, including other LDs. In this process, functional proteins for metabolism are also transferred to LDs. In this review, I focus on interactions between the ER and LDs related to lipid metabolism.


Assuntos
Retículo Endoplasmático/metabolismo , Gotículas Lipídicas/metabolismo , Metabolismo dos Lipídeos , Retículo Endoplasmático/fisiologia , Humanos , Gotículas Lipídicas/fisiologia , Lipólise , Membranas Mitocondriais/metabolismo , Organelas , Perilipina-1/metabolismo , Perilipina-1/fisiologia , Perilipinas/metabolismo , Perilipinas/fisiologia , Fosfatidilcolinas/biossíntese , Ligação Proteica , Proteólise
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