Oil red-O stains non-adipogenic cells: a precautionary note

Kinkel, Adrienne D.; Fernyhough, Melinda E.; Helterline, Deri; Vierck, Janet L.; Oberg, Karen S.; Vance, Tyler J.; Hausman, Gary; Hill, Rodney A.; Dodson, Michael V.

doi:10.1007/s10616-004-3903-4

Cited by 79 publications

(64 citation statements)

References 7 publications

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“…Oil Red O Staining and Quantification-Differentiated 3T3-L1 transformants (day 8) were fixed and stained with Oil Red O to visualize lipid accumulation (91). Cells were then counterstained with hematoxylin.…”

Section: Methodsmentioning

confidence: 99%

Alternative mRNA Splicing of Corepressors Generates Variants That Play Opposing Roles in Adipocyte Differentiation

Goodson

Mengeling

Jonas

et al. 2011

Journal of Biological Chemistry

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Background:The SMRT and NCoR corepressors play key biological roles in transcriptional repression. Results: Alternative mRNA splicing produces corepressor variants that can exert opposite effects on adipocyte differentiation. Conclusion: Corepressors are diversified by alternative mRNA splicing, allowing one locus to encode multiple proteins with distinct functions. Significance: Changes in alternative splicing may help drive the differentiation and customize the physiology of specific cell types.

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Section: Methodsmentioning

confidence: 99%

Alternative mRNA Splicing of Corepressors Generates Variants That Play Opposing Roles in Adipocyte Differentiation

Goodson

Mengeling

Jonas

et al. 2011

Journal of Biological Chemistry

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“…HSCs were stained with oil red O to visualize lipid droplets, essentially as described previously (Kinkel et al, 2004), except that oil red O was diluted in triethyl phosphate instead of isopropanol.…”

Section: Oil Red O Stainingmentioning

confidence: 99%

Retinol Binding Protein-Albumin Domain III Fusion Protein Deactivates Hepatic Stellate Cells

Park

Choi

Lee

et al. 2012

Molecules and Cells

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Liver fibrosis is characterized by accumulation of extracellular matrix, and activated hepatic stellate cells (HSCs) are the primary source of the fibrotic neomatrix and considered as therapeutic target cells. We previously showed that albumin in pancreatic stellate cells (PSCs), the key cell type for pancreatic fibrogenesis, is directly involved in the formation of vitamin A-containing lipid droplets, inhibiting PSC activation. In this study, we evaluated the anti-fibrotic activity of both albumin and retinol binding protein-albumin domain III fusion protein (R-III), designed for stellate cell-targeted delivery of albumin III, in rat primary HSCs and investigated the underlying mechanism. Forced expression of albumin or R-III in HSCs after passage 2 (activated HSCs) induced lipid droplet formation and deactivated HSCs, whereas point mutations in high-affinity fatty acid binding sites of albumin domain III abolished their activities. Exogenous R-III, but not albumin, was successfully internalized into and deactivated HSC-P2. When HSCs at day 3 after plating (pre-activated HSCs) were cultured in the presence of purified R-III, spontaneous activation of HSCs was inhibited even after passage 2, suggestive of a potential for preventive effect. Furthermore, treatment of HSCs-P2 with R-III led to a significant reduction in both cytoplasmic levels of all-trans retinoic acid and the subsequent retinoic acid signaling. Therefore, our data suggest that albumin deactivates HSCs with reduced retinoic acid levels and that R-III may have therapeutic and preventive potentials on liver fibrosis.

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“…It was suggested previously that cytosolic lipid droplets are derived from Sig-1R-circumscribed LRs of the MAM by the budding of the cytoplasmic leaflet (30,32,84). To test if pUL37x1/vMIA, like the HCV core protein, buds into cytoplasmic lipid droplets, we examined the colocalization of wt pUL37x1/vMIA tagged with yellow fluorescent protein (pUL37x1 wt 1-163 -YFP) with a cytosolic lipid droplet marker, Oil Red O dye (7,38). pUL37x1 wt 1-163 -YFP did not detectably colocalize with the cytosolic lipid droplet marker (Fig.…”

Section: Pul37x1/vmia Intercalates Into Lipid-rich Er/mam Domainsmentioning

confidence: 99%

The Human Cytomegalovirus Protein UL37 Exon 1 Associates with Internal Lipid Rafts

Williamson

Zhang

Colberg-Poley

2011

J Virol

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The human cytomegalovirus (HCMV) protein UL37 exon 1 (pUL37x1), also known as viral mitochondrionlocalized inhibitor of apoptosis (vMIA), sequentially traffics from the endoplasmic reticulum (ER) through mitochondrion-associated membranes (MAMs) to the outer mitochondrial membrane (OMM), where it robustly inhibits apoptosis. Here, we report the association of pUL37x1/vMIA with internal lipid rafts (LRs) in the ER/MAM. The MAM, which serves as a site for lipid transfer and calcium signaling to mitochondria, is enriched in detergent-resistant membrane (DRM)-forming lipids, including cholesterol and ceramide, which are found in lower concentrations in the bulk ER. Sigma 1 receptor (Sig-1R), a MAM chaperone affecting calcium signaling to mitochondria, is anchored in the MAM by its LR association. Because of its trafficking through the MAM and partial colocalization with Sig-1R, we tested whether pUL37x1/vMIA associates with MAM LRs. Extraction with methyl-␤-cyclodextrin (M␤CD) removed pUL37x1/vMIA from lysed but not intact cells, indicating its association with internal LRs. Furthermore, the isolation of DRMs from purified intracellular organelles independently verified the localization of pUL37x1/vMIA within ER/MAM LRs. However, pUL37x1/vMIA was not detected in DRMs from mitochondria. pUL37x1/vMIA associated with LRs during all temporal phases of HCMV infection, indicating the likely importance of this location for HCMV growth. Although detected during its sequential trafficking to the OMM, the pUL37x1/vMIA LR association was independent of its mitochondrial targeting signals. Rather, it was dependent upon cholesterol binding. These studies suggest a conserved ability of UL37 proteins to interact with cholesterol and LRs, which is functionally distinguishable from their sequential trafficking to mitochondria.Human cytomegalovirus (CMV) (HCMV) is a medically important herpesvirus which causes serious diseases in congenitally infected infants and in immunocompromised individuals (54). To extend cell survival during its protracted lytic replication, HCMV encodes several antiapoptotic products, including the UL37, UL36, UL38, and major immediate-early 1/2 (IE1/2) gene products (24,25,49,77,85,93) as well as the ␤2.7 RNA, which inhibits proapoptotic signals from the mitochondrial GRIM complex (66).The HCMV UL37 IE product, the UL37 exon 1 (UL37x1) protein (pUL37x1), also known as viral mitochondrion-localized inhibitor of apoptosis (vMIA), sequesters proapoptotic Bax at the outer mitochondrial membrane (OMM) and prevents cytochrome c release and the subsequent initiation of the proapoptotic cascade (3, 58, 60, 62). pUL37x1/vMIA also causes calcium (Ca 2ϩ ) efflux from endoplasmic reticulum (ER) stores and F-actin cytoskeleton disruption, which results in early and late cytopathologies (63,72). pUL37x1/vMIA also transactivates the expression of HCMV early genes whose products are required for its genome replication (5,14,67,90). At late times of infection, pUL37x1/vMIA further extends cell viability by inhibiting a mitoc...

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Oil red-O stains non-adipogenic cells: a precautionary note

Cited by 79 publications

References 7 publications

Alternative mRNA Splicing of Corepressors Generates Variants That Play Opposing Roles in Adipocyte Differentiation

Alternative mRNA Splicing of Corepressors Generates Variants That Play Opposing Roles in Adipocyte Differentiation

Retinol Binding Protein-Albumin Domain III Fusion Protein Deactivates Hepatic Stellate Cells

The Human Cytomegalovirus Protein UL37 Exon 1 Associates with Internal Lipid Rafts

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