LiSa-2, a novel human liposarcoma cell line with a high capacity for terminal adipose differentiation

Wabitsch, Martin; Brüderlein, Silke; Melzner, Ingo; Braun, Mike; Mechtersheimer, Gunhild; Möller, Peter

doi:10.1002/1097-0215(20001215)88:6<889::aid-ijc8>3.0.co;2-n

Cited by 69 publications

(56 citation statements)

References 18 publications

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“…The LS2 cell line (18) was cultured in RPMI-1640 (Gibco) with 20% FBS, 1Â minimum essential medium (MEM) vitamin mix (BioWhittaker), 1Â insulin/transferrin/ethanolamine/selenium (ITES) (BioWhittaker), 1Â penicillin (100 U/mL)/streptomycin (100 mg/mL)/L-glutamine (292 mg/mL; Invitrogen), 1 mmol/L sodium pyruvate, and 1Â nonessential amino acids (Lonza). The LiSa2 cell line (19) was cultured in DMEM high glucose (Gibco) supplemented with 1Â penicillin (100 U/mL)/streptomycin (100 mg/mL)/L-glutamine (292 mg/mL; Invitrogen), 10% FBS (Gibco), and 25 mmol/L HEPES, pH 7.9. Three cell lines derived from dedifferentiated liposarcomas, Lipo224, Lipo246, and Lipo863 (gift of D. Lev; The University of Texas MD Anderson Cancer Center, Houston, TX), were cultured in DMEM high glucose (Gibco) supplemented with 1Â penicillin (100 U/mL)/streptomycin (100 mg/mL; Invitrogen) and 10% FBS (Gibco).…”

Section: Cell Culturementioning

confidence: 99%

Telomerase Suppresses Formation of ALT-Associated Single-Stranded Telomeric C-Circles

Plantinga

Pascarelli

Merkel

et al. 2013

Molecular Cancer Research

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Telomere maintenance is an essential characteristic of cancer cells, most commonly achieved by activation of telomerase. Telomeres can also be maintained by a recombination-based mechanism, alternative lengthening of telomeres (ALT). Cells using ALT are characterized by the presence of ALT-associated promyelocytic leukemia (PML) bodies (APB), long, heterogeneously sized telomeres, extrachromosomal telomeric circular DNA, and elevated telomeric recombination. Consistent with other reports, we found that liposarcomas containing APBs, but lacking telomerase expression, always contained C-rich circles (C-circles), and these C-circles were never present in the absence of APBs, indicating a tight link between these features in ALT cells. However, a rare subgroup of tumors showing evidence of telomere maintenance by both telomerase and ALT did not contain C-circles. To test the hypothesis that telomerase expression disrupts the tight link between APBs and C-circles, we used ALT cell lines that were engineered to express telomerase. Introduction of telomerase activity in these ALT cells resulted in, on average, shorter telomeres with retention of APBs. However, at high passage, the level of C-circles was significantly reduced, which was paralleled by a switch from C-strand overhangs to G-strand overhangs. We propose that by extending critically short telomeres in these cells, telomerase is disrupting a key step in the ALT pathway necessary for production and/or maintenance of C-circles. Mol Cancer Res; 11(6); 557-67. Ó2013 AACR.

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Section: Cell Culturementioning

confidence: 99%

Telomerase Suppresses Formation of ALT-Associated Single-Stranded Telomeric C-Circles

Plantinga

Pascarelli

Merkel

et al. 2013

Molecular Cancer Research

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“…The early passages of the cells were used in this study. The human adipocyte LiSa-2 cell line was generated and characterized by Dr Peter Moller (Wabitsch et al 2000). Both 3T3-L1 cells and LiSa cells were maintained in Dulbecco's modified Eagle's medium (DMEM) supplied with 10% fetal bovine serum in incubator with 5% CO 2 at 37 8C.…”

Section: Cell Cultures and Differentiationmentioning

confidence: 99%

“…We set up an adiponectin ELISA-based screen in 96-well plates to test a compound library composed of known drugs and natural products. A human liposarcoma cell line, LiSa, capable of differentiation under chemically defined culture conditions (Wabitsch et al 2000) was used in the screening. After induction, LiSa cells express high levels of genes that are specific for differentiated adipocytes, such as PPARg.…”

Section: Isoginkgetin Enhances Adiponectin Production In Adipocytesmentioning

confidence: 99%

Isoginkgetin enhances adiponectin secretion from differentiated adiposarcoma cells via a novel pathway involving AMP-activated protein kinase

Liu¹,

Grifman²,

Macdonald³

et al. 2007

Journal of Endocrinology

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Adiponectin is an anti-diabetic hormone secreted by adipocytes. Circulating adiponectin levels are lower in obese and type II diabetic patients than in healthy people. Weight loss or thiazolidinedione treatment increases plasma adiponectin levels. Animal models and human studies suggest that elevated adiponectin levels increase insulin sensitivity. We screened a library of drug-like compounds and natural products for novel agents enhancing adiponectin production. We identified isoginkgetin, a compound derived from the leaves of Ginkgo biloba, to up-regulate adiponectin secretion with potency comparable to that of rosiglitazone, a known modulator of adiponectin production. However, unlike rosiglitazone, peroxisome proliferators-activated receptor g activity seems not required for the action of isoginkgetin, and isoginkgetin has only a slight effect on adipogenesis, which makes it an attractive candidate for anti-diabetic treatment. Further investigation revealed that both isoginkgetin and rosiglitazone activate AMPactivated protein kinase (AMPK) in adipocytes. Our findings suggest a novel mechanism for the elevation of adiponectin by isoginkgetin, which is different from that of rosiglitazone. Furthermore, this novel mechanism for adiponectin regulation involving AMPK can potentially facilitate new understanding of metabolic diseases and identification of new targets, as well as agents that increase plasma adiponectin levels.

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“…Besides the A549 cell line, an additional SSTR2‐positive human tumor cell line, LiSa‐2,60 was also evaluated as positive reference to substantiate SSTR2‐mediated uptake in receptor positive cell lines. The rapidly dividing LiSa‐2 cells are derived from a poorly differentiated, pleomorphic liposarcoma, a cancer that arises in fat cells in deep soft tissue.…”

Section: Resultsmentioning

confidence: 99%

Boosting Antitumor Drug Efficacy with Chemically Engineered Multidomain Proteins

et al. 2018

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A facile chemical approach integrating supramolecular chemistry, site‐selective protein chemistry, and molecular biology is described to engineer synthetic multidomain protein therapeutics that sensitize cancer cells selectively to significantly enhance antitumor efficacy of existing chemotherapeutics. The desired bioactive entities are assembled via supramolecular interactions at the nanoscale into structurally ordered multiprotein complexes comprising a) multiple copies of the chemically modified cyclic peptide hormone somatostatin for selective targeting and internalization into human A549 lung cancer cells expressing SST‐2 receptors and b) a new cysteine mutant of the C3bot1 (C3) enzyme from Clostridium botulinum, a Rho protein inhibitor that affects and influences intracellular Rho‐mediated processes like endothelial cell migration and blood vessel formation. The multidomain protein complex, SST3‐Avi‐C3, retargets C3 enzyme into non‐small cell lung A549 cancer cells and exhibits exceptional tumor inhibition at a concentration ≈100‐fold lower than the clinically approved antibody bevacizumab (Avastin) in vivo. Notably, SST3‐Avi‐C3 increases tumor sensitivity to a conventional chemotherapeutic (doxorubicin) in vivo. These findings show that the integrated approach holds vast promise to expand the current repertoire of multidomain protein complexes and can pave the way to important new developments in the area of targeted and combination cancer therapy.

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LiSa-2, a novel human liposarcoma cell line with a high capacity for terminal adipose differentiation

Cited by 69 publications

References 18 publications

Telomerase Suppresses Formation of ALT-Associated Single-Stranded Telomeric C-Circles

Telomerase Suppresses Formation of ALT-Associated Single-Stranded Telomeric C-Circles

Isoginkgetin enhances adiponectin secretion from differentiated adiposarcoma cells via a novel pathway involving AMP-activated protein kinase

Boosting Antitumor Drug Efficacy with Chemically Engineered Multidomain Proteins

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