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Fusions, Cell

Fusions, Cell refers to the process by which two or more cells merge their cellular membranes and cytoplasmic contents to form a single, new cell.
This fundamental biological event occurs during critical developmental and physiological processes, such as fertilization, skeletal muscle formation, and immune cell activation.
Fusions, Cell allows the combination of genetic material and the sharing of organelles and other cellular components, enabling the creation of new cell types with unique properties.
Understanding the mechanisms and regulation of Fusions, Cell is crucial for advancing research in fields like stem cell biology, tissue engineering, and immunology.
Explore the latest discoveries and potential applications of this dynamic cellular phenomenon.

Most cited protocols related to «Fusions, Cell»

Virus-Cell Fusion Kinetics Quantification

Cited 34 times

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Publication 2009

Cells Cold Temperature Fluorescence Fusions, Cell HIV-1 inhibitors Peptides Place Cells Pronase Virus

Evaluation of Gene Fusion Detection Tool

Cited 19 times

In addition to our internally generated data, we tested deFuse using published paired end RNA-Seq data sets known to contain gene fusions. These datasets were used as positive controls in the evaluation of deFuse. We used the NCI-H660 prostate cell line from the FusionSeq website http://info.gersteinlab.org/FusionSeq_Test_Datasets) known to harbour a TMPRSS2-ERG fusion. In addition, we downloaded the datasets derived from 13 melanoma samples and cell lines and one chronic myelogenous leukemia (CML) cell line K-562 described in Berger et al. [16] (link). Datasets were obtained from the Short Read Archive (http://www.ncbi.nlm.nih.gov/sra) under submission number SRA009053. As described in Berger et al. [16] (link), the CML cell line harbours three previously described gene fusions including BCR-ABL1, and the melanoma data harbours 11 gene fusions.

McPherson A., Hormozdiari F., Zayed A., Giuliany R., Ha G., Sun M.G., Griffith M., Heravi Moussavi A., Senz J., Melnyk N., Pacheco M., Marra M.A., Hirst M., Nielsen T.O., Sahinalp S.C., Huntsman D, & Shah S.P. (2011). deFuse: An Algorithm for Gene Fusion Discovery in Tumor RNA-Seq Data. PLoS Computational Biology, 7(5), e1001138.

Publication 2011

Cell Lines Cells Fusions, Cell Gene Fusion Genes Leukemias, Chronic Granulocytic Melanoma Prostate RNA-Seq TMPRSS2 protein, human

Cell-Cell Fusion Assays for Coronaviruses

Cited 14 times

The establishment and detection of several cell–cell fusion assays are as previously described.^{14 (link),16 (link)} In brief, Huh-7 cells (for testing all coronaviruses) or 293T/ACE2 cells (for testing SARS-CoV-2) were used as target cells. For preparing effector cells expressing S protein a coronavirus, 293T cells were transfected with one of the S protein expression vectors, including 293T/SARS-CoV-2/GFP, 293T/MERS-CoV/GFP, 293T/HCoV-229E/GFP, 293T/SARS-CoV/GFP, or 293T/SL-CoV/GFP, 293T/HCoV-OC43/GFP, 293T/HCoV-NL63/GFP or empty plasmid pAAV-IRES-EGFP. For SARS-CoV S-, SL-CoV S-, OC43 S- or NL63 S-mediated cell–cell fusion assays, effector cells and target cells were cocultured in DMEM containing trypsin (80 ng/mL) for 4 h, while for SARS-CoV-2 and MERS-CoV S-mediated cell–cell fusion assays, effector cells and target cells were cocultured in DMEM without trypsin but 10% FBS for 2 h. After incubation, five fields were randomly selected in each well to count the number of fused and unfused cells under an inverted fluorescence microscope (Nikon Eclipse Ti-S).

Xia S., Liu M., Wang C., Xu W., Lan Q., Feng S., Qi F., Bao L., Du L., Liu S., Qin C., Sun F., Shi Z., Zhu Y., Jiang S, & Lu L. (2020). Inhibition of SARS-CoV-2 (previously 2019-nCoV) infection by a highly potent pan-coronavirus fusion inhibitor targeting its spike protein that harbors a high capacity to mediate membrane fusion. Cell Research, 30(4), 343-355.

Publication 2020

ACE2 protein, human Biological Assay Cells Cloning Vectors Coronavirus Coronavirus 229E, Human Coronavirus OC43, Human Fusions, Cell HEK293 Cells Internal Ribosome Entry Sites Microscopy, Fluorescence Middle East Respiratory Syndrome Coronavirus NL63, Human Coronavirus Plasmids SARS-CoV-2 Severe acute respiratory syndrome-related coronavirus spike protein, SARS-CoV-2 Trypsin

MERS-CoV Spike Protein Cell-Cell Fusion Assay

Cited 11 times

MERS-CoV S protein-mediated cell–cell fusion was assessed using a method similar to that for determining HIV-1 Env-mediated cell–cell fusion^{59 (link)}. Briefly, 293T cells were transfected with the plasmid pAAV-IRES-EGFP encoding the EGFP (293T/EGFP) or pAAV-IRES-MERS-EGFP encoding the MERS-CoV S protein and EGFP (293T/MERS/EGFP) and cultured in DMEM containing 10% FBS at 37 °C for 48 h. Huh-7 cells (5 × 10⁴) expressing the MERS-CoV receptor DPP4 were incubated in 96-well plates at 37 °C for 5 h, followed by the addition of 1 × 10⁴ 293T/EGFP or 293T/MERS/EGFP cells, respectively, in the absence or presence of the test peptides at graded indicated concentrations. After co-culture at 37 °C for 4 h, the 293T/MERS/EGFP cells (293T/EGFP cells were used as the negative control) fused or unfused with Huh-7 cells were counted under an inverted fluorescence microscope (Nikon Eclipse Ti-S). The fused cell was much larger by at least twofold than the unfused cell, and the intensity of fluorescence in the fused cell was weaker than that of the unfused cell as a result of the diffusion of EGFP from one cell to two or more cells (see Fig. 5a). The percent inhibition of cell–cell fusion was calculated using the following formula: (1−(E−N)/(P−N)) × 100. ‘E’ represents the % cell–cell fusion in the experimental group. ‘P’ represents the % cell–cell fusion in the positive control group, to which no inhibitor was added. ‘N’ is the % cell–cell fusion in negative control group, in which 293T/MERS/EGFP cells were replaced by 293T/EGFP cells. The concentration for 50% inhibition (IC₅₀) was calculated using the CalcuSyn software kindly provided by Dr T.C. Chou^{60 (link)}.
After further co-culture at 37 °C for 48 h, syncytium formation between 293T/MERS/EGFP and Huh-7 could be observed under an inverted microscope with or without fluorescence (Fig. 5b), and the syncytia were photographed for the record.

Lu L., Liu Q., Zhu Y., Chan K.H., Qin L., Li Y., Wang Q., Chan J.F., Du L., Yu F., Ma C., Ye S., Yuen K.Y., Zhang R, & Jiang S. (2014). Structure-based discovery of Middle East respiratory syndrome coronavirus fusion inhibitor. Nature Communications, 5, 3067.

Publication 2014

Coculture Techniques Diffusion DPP4 protein, human Fluorescence Fusions, Cell Giant Cells GPER protein, human HEK293 Cells HIV-1 Internal Ribosome Entry Sites Microscopy Microscopy, Fluorescence Middle East Respiratory Syndrome Coronavirus Peptides Plasmids Psychological Inhibition spike protein, SARS-CoV-2

Trypsin-Mediated Hemagglutinin Fusion Assay

Cited 11 times

HAb2 cells were treated by 5 μg/ml trypsin (Fluka, Buchs, Switzerland) for 10 min at room temperature to cleave HA0 into its fusion-competent HA1-S-S-HA2 form. For HA300a and BHA-PI cells, trypsin (5 μg/ml) was supplemented with neuraminidase (0.2 mg/ml; Sigma Chemical Co.) to improve binding of RBC. The enzymes were applied together for 10 min at room temperature. To terminate the reaction, HA-expressing cells were washed twice with complete medium containing 10% fetal serum. After two washings with PBS, cells were incubated for 10 min with a 1 ml suspension of RBC (0.05% hematocrit). HA-expressing cells with zero to two bound RBC per cell were washed three times with PBS to remove unbound RBC and then used. When measuring RBC binding to cells, several areas of the dish were selected. We screened at least 200 cells to find the average number of RBC bound to each HA-expressing cell.
Fusion was triggered by incubation of cells with PBS titrated by citrate to acidic pH. After low-pH treatment, acidic solution was replaced by PBS. Fusion extent was assayed by fluorescence microscopy more than 20 min after low-pH application as the ratio of dye-redistributed bound RBC to the total number of the bound RBC. Longer incubations (up to 2 h) did not increase the extent of fusion. We performed the fluorescence microscopy for lipid and content mixing either in a cold room at 4°C or at room temperature, as required.
For spectrofluorometric measurements (SLM-Aminco, Urbana, IL), excitation and emission wavelengths were 550 and 590 nm for R18, and 473 and 515 nm for NBD-taurine. The standard fusion assay was performed as in Chernomordik et al. (1997) (link). Suspensions of HA-expressing cells with bound RBC in PBS were placed into a thermostated fluorescence cuvette and stirred with a Teflon-coated flea. Citric acid was injected into the cuvette to lower pH to 4.9. The increase in fluorescence was normalized to that at infinite dilution of the probe by lysing cells with 0.06% SDS. Spectrofluorometry was also used to evaluate LPC incorporation into RBC membranes at different temperature from the decrease in R18 quenching caused by adding exogenous lipid to HAb2 cells with bound R18-labeled RBC (Chernomordik et al., 1997 (link)). To induce swelling of cells by applying hypotonic medium (osmotic shock), HA-expressing cells with bound RBC were placed into PBS diluted by H₂O (1:3) as in Melikyan et al. (1995b) (link).
Each set of experiments for each graph presented here was repeated on at least three occasions with similar results. Presented data were averaged from the same set of experiments.

Chernomordik L.V., Frolov V.A., Leikina E., Bronk P, & Zimmerberg J. (1998). The Pathway of Membrane Fusion Catalyzed by Influenza Hemagglutinin: Restriction of Lipids, Hemifusion, and Lipidic Fusion Pore Formation. The Journal of Cell Biology, 140(6), 1369-1382.

Publication 1998

Acids Biological Assay Cells Citrates Citric Acid Cold Temperature Enzymes Fetus Fleas Fluorescence Fusions, Cell Hyperostosis, Diffuse Idiopathic Skeletal Lipids Microscopy, Fluorescence NBD-taurine Neuraminidase Osmotic Shock Serum Spectrometry, Fluorescence Technique, Dilution Teflon Tissue, Membrane Trypsin Volumes, Packed Erythrocyte

Most recents protocols related to «Fusions, Cell»

Enhancing EBOV GP Trimer Stability

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Example 3

We hypothesized that HR1_Cis essential to EBOV GP metastability. Since HR1_Cin wildtype EBOV GP is equivalent in length (8 aa) to a truncated HR1_Nin the prefusion-optimized HIV-1 Env, metastability in EBOV GP may not be sensitive to the HR1_Clength and likely requires a different solution. We thus hypothesized that a proline mutation in HR1_C, termed P^1-8, may rigidify the HR1_Cbend and improve the EBOV GP trimer stability.

To examine this possibility, eight GPΔmuc-W615L variants, each bearing a proline mutation in HR1_Cbut without the L extension and foldon at the C terminus, were validated experimentally. All constructs were transiently expressed in 250-ml 293 F cells and purified using an mAb114 column, which captures all GP species. The proline mutation at most positions in HR1_Cshowed little effect on the composition of GP species except for T577P (P²) and L579P (P⁴), which displayed notable trimer peaks at ˜11 ml in the SEC profiles. In a separate experiment, all eight constructs were transiently expressed in 250-ml 293 F cells and purified using an mAb100 column. Only P²and P⁴showed any measurable trimer yield, with a notably high SEC peak observed for P⁴that corresponds to well-formed trimers. The mAb100-purified GP was also analyzed by BN-PAGE, which showed a trimer band for P²and P⁴. Overall, the T577P mutation, P², can substantially increase trimer yield, while the L579P mutation, P⁴, exhibited a less pronounced effect.

Next, the T577P mutation (P²) was incorporated into the GPΔmuc-WL²-foldon construct, resulting in a construct named GPΔmuc-WL²P²-foldon. This construct was expressed transiently in 1-liter 293 F cells and purified using an mAb100 column for SEC characterization on a HiLoad Superdex 200 16/600 GL column. In three production runs, GPΔmuc-WL²P²-foldon generated a trimer peak that was two- and four-fold higher than GPΔmuc-WL²-foldon and wildtype GPΔmuc-foldon, respectively, with an average yield of 2.6 mg after SEC. Protein collected in the SEC range of 55.5-62.0 ml was analyzed by BN-PAGE, which displayed a trimer band across all fractions without any hint of impurity. The thermostability of GPΔmuc-WL²P²-foldon was determined by DSC after mAb100 and SEC purification.

Unexpectedly, two transition peaks were observed in the thermogram, one registered at a lower Tm of 61.6° C. and the other at a higher Tm of 68.2° C. To this end, a second construct bearing the L579P mutation (P⁴), termed GPΔmuc-WL²P⁴-foldon, was also assessed by DSC. Although only one peak was observed in the thermogram with a Tm of 67.0° C., a slight widening at the onset of the peak suggested a similar unfolding behavior upon heating. DSC thus revealed the complexity associated with a proline-rigidified HR1_Cbend, which may increase the trimer yield at the cost of reducing GP thermostability. The antigenicity of GPΔmuc-WL²P²-foldon was assessed using the same panel of 10 antibodies by ELISA (FIG. 3F-G) and bio-layer interferometry (BLI). The T577P mutation (P²) appeared to improve GP binding to most antibodies with respect to GPΔmuc-WL²-foldon (FIG. 3G), with a 40% reduction in EC₅₀observed for bNAb BDBV223, which targets HR2-MPER. Although BLI profiles were almost indistinguishable between wildtype and redesigned GPΔmuc-foldon trimers—all with fast on-rates and flattened dissociation curves, a two-fold higher signal at the lowest concentration (12.5 nM) was observed for GPΔmuc-WL²P²-foldon binding to bNAb BDBV223, consistent with the ELISA data.

Our results thus demonstrated the importance of HR1_Cto EBOV GP metastability and an unexpected sensitivity of HR1_Cto proline mutation. Recently, Rutten et al. tested proline mutations in HR1_Calong with a K588F mutation to stabilize filovirus GP trimers (Cell Rep. 30, 4540-50, 2020). While a similar pattern of increased trimer yield was observed for the T577P mutant, the reported thermostability data appeared to be inconsistent with our DSC measurement. Further investigation is warranted to fully understand the role of HR1_Cin filovirus-cell fusion and its impact on GP stability.

US11872277B2. Compositions and methods related to ebolavirus vaccines (2024-01-16). THE SCRIPPS RESEARCH INSTITUTE [US]. Inventors: Linling He [US], Jiang Zhu [US], Anshul Chaudhary [US], Ian Wilson [US].

Patent 2024

Antibodies Antigens Broadly Neutralizing Antibodies Cells Decompression Sickness Enzyme-Linked Immunosorbent Assay Filoviridae Fusions, Cell HIV-1 Hypersensitivity Interferometry mAb114 Mutation Proline Proteins Thermography

Recombinant Protein Production in CHOZN Cells

CHOZN GS−/− cells (Merck) were maintained in suspension cultures in serum-free media (EX-CELL CHO CD Fusion, Merck) supplemented with 4 mM L-glutamine, as previously described (Tian et al., 2019 (link)). An expression construct containing the entire coding sequence of human AGA was synthesized by Genewiz, United States. Full-length cDNA of human GUSB, TPP1, and GAA were purchased from Horizon Discovery, United Kingdom, while human IDS cDNA was purchased from Sino Biological. C-terminal His-tagged CTSD was produced as previously reported (Marques et al., 2020 (link)). All reporter constructs were cloned into pCGS3 (Merck). Cells were seeded at a density of 0.5 × 10⁶ cells/mL in T25 flasks (NUNC) 24 h prior to transfection. Approximately 2 × 10⁶ cells were transfected with 8 μg endotoxin-free plasmids using Amaxa kit V and program U24 with Amaxa Nucleofector 2B (Lonza). 72 h post-transfection, cells were plated at 500–1,000 cells/well in 96-wells in 200 μL Minipool Plating Medium containing 80% EX-CELL^® CHO Cloning Medium (Merck) and 20% EX-CELL CD CHO Fusion media without glutamine for selection. Screening of high expression minipools were performed by determining enzyme activity in spent media for AGA, GUSB, GAA and IDS, by SDS-PAGE for TPP1 and CTSD. Selected minipools were further single cell sorted by fluorescence-activated cell sorting (FACS) (Sony) and expanded in 50 mL TPP TubeSpin^® shaking Bioreactors (180 rpm, 37°C and 5% CO₂).

Chen Y.H., Tian W., Yasuda M., Ye Z., Song M., Mandel U., Kristensen C., Povolo L., Marques A.R., Čaval T., Heck A.J., Sampaio J.L., Johannes L., Tsukimura T., Desnick R., Vakhrushev S.Y., Yang Z, & Clausen H. (2023). A universal GlycoDesign for lysosomal replacement enzymes to improve circulation time and biodistribution. Frontiers in Bioengineering and Biotechnology, 11, 1128371.

Publication 2023

Biopharmaceuticals Bioreactors Cells CHO Cells CTSD protein, human Culture Media, Serum-Free DNA, Complementary Endotoxins enzyme activity Fusions, Cell Glutamine Homo sapiens isononanoyl oxybenzene sulfonate Open Reading Frames Plasmids SDS-PAGE Transfection

Inducing Oxidative Stress in HLE-B3 Cells

The human lens epithelial cell line of HLE-B3 cells was purchased from BFB BLUEFBIO (BFN60805970; Bluebio (Yantai) Bio-Pharmaceutical Co., Ltd., Yantai, China) and cultured in high glucose DMEM (10-013-CVRC; Corning, Shanghai, China) supplemented with 10% FBS (10099, GIBCO) and 1% PS (E607011, Sangon). HLE-B3 cells were maintained in an incubator with a 5% CO₂ atmosphere at 37 °C. To construct ARC cell model, HLE-B3 cells were exposed to UVB light (from top to bottom) for 10 min, according to a previous study, with slight modifications in exposure time (Xiang et al., 2019 (link)).
For the knockdown of has_circ_0007905 and METLL3, siRNAs were designed and synthesized by GenePharma. The has-miR-6749-3p mimic and has-miR-6749-3p inhibitor were also synthesized by GenePharma to overexpress and knockdown the has-miR-6749-3p, respectively. For overexpression of EIF4EBP1, the full length of EIF4EBP1 was cloned into pCDNA3.1 vectors (OE-EIF4EBP1), and the blank vector served as NC.
Transfection was conducted using Lipofectamine 2000 reagent (Invitrogen) according to the manufacturer’s instructions. Briefly, when the fusion rate of the cells reached 80–90%, the fresh medium was replaced. All siRNA, vectors, and Lipofectamine 2000 reagents were diluted with OPTI-MEM (5 µL:45 µL). Next, diluted Lipofectamine and RNA sequences were mixed for 20 min and added to the cell sample.

Li R., Zhu H., Li Q., Tang J., Jin Y, & Cui H. (2023). METTL3-mediated m6A modification of has_circ_0007905 promotes age-related cataract progression through miR-6749-3p/EIF4EBP1. PeerJ, 11, e14863.

Publication 2023

Atmosphere Cell Lines Cells Cloning Vectors Epithelial Cells Fusions, Cell Glucose Homo sapiens Lens, Crystalline Light Lipofectamine lipofectamine 2000 Pharmaceutical Preparations RNA, Small Interfering RNA Sequence Transfection

Establishing Stable Lentiviral Cell Lines

For adherent Bel7402 cells, the cell number was diluted to 1.2×10⁵ cells/mL, and the cells were seeded into a 24-well plate at 500 μL/well. The culture was continued, and viral infection was performed when the degree of cell fusion reached 40%. For suspended THP-1 cells, The number of cells was diluted to 1×10⁵/mL, and 500 μL/well was seeded into a 24-well plate for direct viral infection. Then, 250 μL of fresh medium containing 1×Hitans GP or 1×Hitans GA was added, and the corresponding virus volume was converted according to the selected multiplicity of infection(MOI) gradient (10 (link), 24 (link)–26 (link)) and added to fresh medium containing the viral infection booster solution. Cell culture plates were shaken using the crossing method. After 4 h, 250 μL of fresh medium containing the infection booster solution was added again for 15 h. The cells were washed twice with sterile PBS, and fresh virus-free medium was added. The efficiency of the viral infection was observed after 48 and 72 h. After the puromycin concentration was screened, cells in the blank group were seeded in a 24-well plate, and the culture medium was replaced with fresh medium containing puromycin after 24 h. The puromycin screening gradients was 0.6, 1.2, 1.8, 2.4, and 3.0 μg/mL. The fresh medium was replaced according to the cell state, and the minimum puromycin concentration that killed all cells in the blank group for 3-4 days was selected as the experimental concentration of infected lentiviral cell lines. To screen stable virus-infected cell lines, 72 h after lentiviral infection, the concentration of puromycin found in the pre-experiment was used to simultaneously screen the lentivirus-infected and blank groups. After the cells in the blank group died completely, the concentration of puromycin in the lentivirus-infected cells was reduced to 50% of the original concentration and the culture was maintained. After 3 days, the medium was replaced with fresh medium without puromycin, and the obtained cells were considered THP-1 stable cells.

Zhang M., Liu K., Zhang Q., Xu J., Liu J., Lin H., Lin B., Zhu M, & Li M. (2023). Alpha fetoprotein promotes polarization of macrophages towards M2-like phenotype and inhibits macrophages to phagocytize hepatoma cells. Frontiers in Immunology, 14, 1081572.

Publication 2023

Cell Culture Techniques Cell Lines Cells Fusions, Cell Infection Lentivirus Puromycin Secondary Immunization Sterility, Reproductive THP-1 Cells Virus Virus Diseases

Somatic Cell Nuclear Transfer Protocol

Dermal fibroblasts from a proband female donor were cultured in 4-well dishes under standard conditions until they reach confluency. Confluent cells were synchronized in the G0/G1 phase of the cell cycle by culture in medium with low serum (DMEM/F12 medium with 0.5% FBS) for 2–4 days before SCNT. Enucleations, cell fusion, and artificial activations were performed. Briefly, meiotic metaphase II (MII) spindles were visualized under polarized microscopy and removed. Next, a disaggregated fibroblast was aspirated into a micropipette, exposed briefly to HVJ-E extract (Cosmo Bio LTD #ISK-CF-001-EX) and placed into the enucleated oocyte perivitelline space. After cell fusion, the SCNT oocytes were subjected to artificial activation.

Liang D., Mikhalchenko A., Ma H., Marti Gutierrez N., Chen T., Lee Y., Park S.W., Tippner-Hedges R., Koski A., Darby H., Li Y., Van Dyken C., Zhao H., Wu K., Zhang J., Hou Z., So S., Han J., Park J., Kim C.J., Zong K., Gong J., Yuan Y., Gu Y., Shen Y., Olson S.B., Yang H., Battaglia D., O’Leary T., Krieg S.A., Lee D.M., Wu D.H., Duell P.B., Kaul S., Kim J.S., Heitner S.B., Kang E., Chen Z.J., Amato P, & Mitalipov S. (2023). Limitations of gene editing assessments in human preimplantation embryos. Nature Communications, 14, 1219.

Publication 2023

Cell Cycle Cells Females Fibroblasts Fusions, Cell G1 Phase Meiotic Spindle Apparatus Metaphase Microscopy Oocytes Serum Tissue Donors Training Programs

Top products related to «Fusions, Cell»

Facsaria fusion cell sorter by BD

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The BD FACSAria Fusion cell sorter is a high-performance flow cytometry instrument designed for multicolor analysis and sorting of complex biological samples. It features advanced optics and electronics to provide precise and reproducible data.

Fetal bovine serum (fbs) by Thermo Fisher Scientific

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Fetal Bovine Serum (FBS) is a cell culture supplement derived from the blood of bovine fetuses. FBS provides a source of proteins, growth factors, and other components that support the growth and maintenance of various cell types in in vitro cell culture applications.

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Lipofectamine 2000 is a cationic lipid-based transfection reagent designed for efficient and reliable delivery of nucleic acids, such as plasmid DNA and small interfering RNA (siRNA), into a wide range of eukaryotic cell types. It facilitates the formation of complexes between the nucleic acid and the lipid components, which can then be introduced into cells to enable gene expression or gene silencing studies.

Dulbecco modified eagle medium (dmem) by Thermo Fisher Scientific

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DMEM (Dulbecco's Modified Eagle's Medium) is a cell culture medium formulated to support the growth and maintenance of a variety of cell types, including mammalian cells. It provides essential nutrients, amino acids, vitamins, and other components necessary for cell proliferation and survival in an in vitro environment.

Lipofectamine 3000 by Thermo Fisher Scientific

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Lipofectamine 3000 is a transfection reagent used for the efficient delivery of nucleic acids, such as plasmid DNA, siRNA, and mRNA, into a variety of mammalian cell types. It facilitates the entry of these molecules into the cells, enabling their expression or silencing.

Penicillin streptomycin by Thermo Fisher Scientific

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Penicillin/streptomycin is a commonly used antibiotic solution for cell culture applications. It contains a combination of penicillin and streptomycin, which are broad-spectrum antibiotics that inhibit the growth of both Gram-positive and Gram-negative bacteria.

Rpmi 1640 medium by Thermo Fisher Scientific

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RPMI 1640 medium is a commonly used cell culture medium developed at Roswell Park Memorial Institute. It is a balanced salt solution that provides essential nutrients, vitamins, and amino acids to support the growth and maintenance of a variety of cell types in vitro.

Peg1500 by Roche

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PEG1500 is a polyethylene glycol compound with a molecular weight of 1,500 Daltons. It is a commonly used reagent in various laboratory applications, including protein purification, drug delivery, and enzyme conjugation.

Opti mem by Thermo Fisher Scientific

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Opti-MEM is a cell culture medium designed to support the growth and maintenance of a variety of cell lines. It is a serum-reduced formulation that helps to reduce the amount of serum required for cell culture, while still providing the necessary nutrients and growth factors for cell proliferation.

Penicillin by Thermo Fisher Scientific

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Penicillin is a type of antibiotic used in laboratory settings. It is a broad-spectrum antimicrobial agent effective against a variety of bacteria. Penicillin functions by disrupting the bacterial cell wall, leading to cell death.

What are the different types of cell fusions and their biological significance?

Cell fusions can occur through various mechanisms, including viral-induced fusion, cell-cell fusion, and induced cell fusion. Viral-induced fusions happen during viral infections when the virus triggers the merger of host cells. Cell-cell fusions are crucial for processes like fertilization, muscle development, and immune cell activation. Induced cell fusions can be engineered in the lab to create hybridoma cells for antibody production or to generate stem cell-derived cell types for regenerative medicine. Understanding these different fusion mechanisms is key to leveraging this fundamental biological process for therapeutic and research applications.

How can PubCompare.ai help optimize research on cell fusions?

PubCompare.ai allows researchers to more efficiently screen the literature on cell fusion protocols and leverage AI to pinpoit critical insights. The platform's AI-driven analysis can help identify the most effective protocols related to cell fusions for your specific research goals. By highlighting key differences in protocol effectiveness, PubCompare.ai enables you to choose the best option to ensure reproducibility and accuracy in your cell fusion experiments.

What are some common challenges in studying cell fusions?

Some key challenges in studying cell fusions include achieving efficient and controlled cell-cell fusion, monitoring the fusion process in real-time, and characterizing the properties of the resulting fused cells. Techniques like polyethylene glycol (PEG)-induced fusion or electrofusion can be temperamental, requiring careful optimization. Fluorescent labeling and live-cell imaging are helpful for visualizing fusion events, but interpreting the data can be complex. Additionally, maintaining the stability and functionality of fused cells, especially in the context of regenerative medicine applications, presents hurdles that ongoing research continues to address.

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PubCompare.ai can help overcome cell fusion research challenegs by providing a centralized platform to efficiently explore the latest protocols and technlologies from the literature, preprints, and patents. The AI-powered comparisons on the platform can highlight the critical differences between fusion protocols, allowing researchers to idenfity the most effective methods for their specific application. This can save time and improve the odds of success in optimizing cell fusion experiments and downstream analyses. The platform's ability to pinpoit key insights can be invaluable in navigating the complexities of this dynamic biological process.

What are some of the emerging applications of cell fusions in biomedicine?

Cell fusions have exciting potential applications in biomedicine, such as the generation of hybridoma cells for monoclonal antibody production, the creation of stem cell-derived cell types for regenerative therapies, and the study of cell reprogramming for disease modeling. Futher, the fusion of immune cells like T cells and natural killer cells is being explored to enhance cancer immunotherapies. Additionally, understanding the role of cell fusions in processes like muscle regeneration and tissue repair could lead to new therapeutic strategies for degenerative diseases. The versatility of cell fusions continues to inspire innovative research across meedical disciplines.

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Cellular Fusion, Membrane Fusion, Cell Hybridization, Cell Fusion Techniques, Cell Fusion Assays, Cell Fusion Mechanisms, Cell-Cell Fusion, Cytoplasmic Fusion, Syncytium Formation, Heterokaryon Formation, Myoblast Fusion, Fertilization, Immune Cell Activation, Stem Cell Differentiation, Tissue Engineering, Regenerative Medicine, BD FACSAria Fusion, Fluorescence-Activated Cell Sorting (FACS), Fetal Bovine Serum (FBS), Lipid Transfection Reagents (e.g., Lipofectamine 2000, Lipofectamine 3000), Cell Culture Media (e.g., DMEM, RPMI 1640), Antibiotics (e.g., Penicillin, Streptomycin), Polyethylene Glycol (PEG1500), Serum-Free Media (e.g., Opti-MEM) Cellular fusion, also known as cell fusion or membrane fusion, is a fundamental biological process in which two or more cells merge their cellular membranes and cytoplasmic contents to form a single, new cell.
This dynamic event occurs during critical developmental and physiological processes, such as fertilization, skeletal muscle formation, and immune cell activation.
By allowing the combination of genetic material and the sharing of organelles and other cellular components, cellular fusion enables the creation of new cell types with unique properties.
Understanding the mechanisms and regulation of cellular fusion is crucial for advancing research in fields like stem cell biology, tissue engineering, and immunology.
Researchers utilize various cell fusion techniques and assays, such as fluorescence-activated cell sorting (FACS) with the BD FACSAria Fusion cell sorter, to study and manipulate this phenomenon.
Cell culture media like DMEM and RPMI 1640, supplemented with fetal bovine serum (FBS) and antibiotics (e.g., penicillin/streptomycin), provide the optimal environment for cell fusion experiments.
Lipid transfection reagents, such as Lipofectamine 2000 and Lipofectamine 3000, can facilitate the fusion process, while serum-free media like Opti-MEM and polyethylene glycol (PEG1500) are also employed in cell fusion studies.
Exploring the latest discoveries and potential applications of cellular fusion is essential for driving scientific progress and unlocking new possibilities in fields ranging from regenerative medicine to immunotherapy.
By leveraging the power of this dynamic cellular process, researchers can push the boundaries of their work and uncover groundbreaking insights that can transform our understanding of biology and lead to innovative solutions for human health and disease.