Introduction

The MC38 cell line — also known as MCA-38, MCA 38, MCA38, MC-38, MC-38 B/6, Mouse Colon 38, Colon 38, Colon-38, Colon38, Murine Carcinoma-38, and C38 (Cellosaurus accession CVCL_B288) — is one of the most widely employed murine models in colorectal cancer and immuno-oncology research. The parental tumour was induced with the carcinogen 1,2-dimethylhydrazine (DMH) in C57BL/6 mice and reported by Corbett and colleagues in 1975 [1]; the cell line was subsequently established in culture by Tan, Holyoke, and Goldrosen in 1976 [2]. Its syngeneic compatibility with C57BL/6 mice, high mutational burden, and responsiveness to immune checkpoint inhibitors have made MC38 cells an indispensable tool for studying colonic neoplasms, cancer vaccines, CD8-positive T-lymphocyte responses, tumour-associated macrophages, and programmed cell death 1 receptor (PD-1) pathway biology. The model continues to underpin advances in cancer immunotherapy, gene therapy, and neoantigen discovery.

Key Takeaways

• MC38 is a murine colon adenocarcinoma cell line syngeneic with the C57BL/6 mouse strain, derived from a DMH-induced tumour.
• The cell line carries a high mutational burden and expresses neoantigens recognised by CD8-positive T-lymphocytes — but which neoantigens are present depends on the subline (see below).
• MC38 is sensitive to immune checkpoint inhibitors, making it a widely used model for PD-1/PD-L1 pathway research.
• The model has been extensively used in cancer vaccine development, cytokine gene therapy, and tumour immunology studies.
• Substantial genomic and transcriptomic differences exist between MC38 sublines from different repositories. The well-known neoepitopes Rpl18 and Adpgk are present in the Leiden subline (MC38-L) but absent from the Kerafast/NCI subline (MC38-K), which is therefore not recognised by the corresponding T cells. Careful sourcing and documentation of provenance are essential. [3]
• Numerous engineered derivative lines (knockout, reporter, overexpression) are available, extending the model's experimental versatility.

What Is MC38?

MC38 is a transplantable colon adenocarcinoma cell line of mouse origin, classified as a cancer cell line in the Cellosaurus database (CVCL_B288). The line was derived from a female C57BL/6 mouse of unspecified age bearing a colon adenocarcinoma (Mouse colon adenocarcinoma, NCIt C120044). Corbett and colleagues induced 82 colon tumours across four inbred mouse strains as part of a systematic effort to establish transplantable colon tumour models for chemotherapy assays; four tumours survived the first transplant and entered serial passage [1]. Tan, Holyoke, and Goldrosen subsequently described methods for the selective culture of the MCA-38 line in vitro, noting that fibroblastoid elements could be removed by trypsin treatment to yield a stable epithelial population [2]. Cellosaurus lists a doubling time of 24.3 hours for MC38 [4], and the line is maintained as an adherent culture. Omics characterisation has included whole exome sequencing, transcriptomics by microarray and RNA-seq, MHC class I peptidome proteomics, SNP array analysis, and mitochondrial genome sequencing. (Cellosaurus records the peptidome entry under its generic label "HLA class I peptidome"; murine cells present peptides on H-2, not HLA, molecules.)

MC38 Cell Culture Information

Note on subline-specific conditions: the medium above corresponds to the culture conditions reported for the Kerafast/NCI-derived subline (MC38-K). The Leiden subline (MC38-L) is maintained in IMDM with 8% FBS, 2 mM L-glutamine, and 50 µM 2-mercaptoethanol [3]. Users should follow the conditions specified by their supplier.

Advantages of MC38 Cells

One of the principal strengths of MC38 cells is their syngeneic compatibility with the widely available C57BL/6 mouse strain. This compatibility allows researchers to study tumour–immune interactions in a fully immunocompetent host, avoiding the confounds of immunodeficiency that limit the translational value of xenograft models. The intact immune system enables rigorous evaluation of CD8-positive T-lymphocyte responses, tumour-associated macrophage biology, natural killer cell activity, and the full spectrum of adaptive and innate anti-tumour immunity.

Because the parental tumour was chemically induced with DMH, MC38 carries a high tumour mutational burden and expresses immunogenic neoantigens, characterised through whole exome sequencing and MHC class I peptidome analysis [5]. This neoantigen-rich background makes the model responsive to immune checkpoint inhibitors targeting the programmed cell death 1 receptor pathway [3], which is one reason it is often used as an analogue for the hypermutated subset of human colorectal cancers that respond to such therapies. The cell line's responsiveness to immunotherapy has made it one of the standard preclinical tools for evaluating novel immune checkpoint inhibitor combinations and cancer vaccines. Note that the specific neoantigens present depend on the subline used [3].

An extensive ecosystem of engineered MC38 derivative lines further extends the model's utility. Knockout lines targeting immune regulators such as PD-L1 (Cd274), B2m, and CD47, as well as reporter lines expressing luciferase or fluorescent proteins, are catalogued in Cellosaurus as derivatives of CVCL_B288 and provide ready-made tools for mechanistic and in vivo imaging studies. A doubling time of roughly 24 hours [4] supports efficient experimental throughput, and the cell line's tractability to genetic manipulation — by lentivirus [12], retrovirus [10], and electroporation [3] — has been demonstrated across many published studies.

Limitations of MC38 Cells

A critical limitation of the MC38 model is the documented heterogeneity between sublines sourced from different origins. A 2023 study by Schrörs and colleagues performed comparative exome and transcriptome sequencing of MC38 cells from Kerafast (NCI/NIH origin, MC38-K) and from the Leiden University Medical Center collection (MC38-L), and found substantial differences in mutational profiles, ploidy, and neoantigen expression [3]. MC38-L harboured approximately 1.3-fold more single nucleotide variants and small insertions and deletions than MC38-K, only 35.3% of non-synonymous variants and 5.4% of fusion gene events were shared, and the inferred ploidy was two for MC38-K versus five for MC38-L. Critically, the well-characterised neoepitopes Rpl18 and Adpgk were absent from MC38-K, so T cells raised against them recognised and killed MC38-L but not MC38-K. Results obtained with one MC38 subline may therefore not be reproducible with cells from a different source.

More broadly, SNP array profiling has highlighted the problem of aneuploidy and cross-contamination among commonly used mouse cell lines; MC38 was one of 99 lines included in that panel, of which 15 diverged substantially from their reported genetic background [6]. The study reports no specific authentication failure for MC38, but it does show that STR profiling alone may fail to distinguish sublines derived from the same inbred strain and does not reveal karyotypic change. Researchers working with MC38 should apply rigorous authentication methods and document the precise provenance of the cells used in each study.

Terminology around MC38's immunogenicity requires care. Papers from the 1990s and early 2000s routinely describe MC38 as a "poorly" or "weakly" immunogenic tumour, because unmodified cells grow progressively in immunocompetent C57BL/6 mice [10] [11] [19]. Contemporary immuno-oncology literature emphasises instead its high mutational burden and checkpoint-inhibitor sensitivity [3]. Both descriptions are accurate in their own context, and readers should not treat them as contradictory.

As a chemically induced murine tumour, MC38 does not replicate the driver-mutation sequence typical of human colorectal cancer. Cellosaurus carries no curated sequence-variation entry for the line, but the absence of an annotation is not evidence that driver alterations are absent: Schrörs and colleagues, for instance, detected a Smad4 mutation in MC38-L that was not present in MC38-K [3]. Because the two sublines differ so extensively, blanket statements about "the" mutational landscape of MC38 should be avoided, and researchers should verify the genotype of their own stock. Finally, the Cellosaurus entry carries a caution note concerning a published MCA38 mitochondrial genome: the deposited sequence (KM820832.1) is a rat sequence labelled as originating from "rat isolate 406", despite MC38 being of murine origin [7], which illustrates the importance of verifying published sequence data associated with this line.

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Applications of MC38 Cells

Cancer Immunotherapy and Immune Checkpoint Research

The MC38 model has become a cornerstone of immune checkpoint inhibitor research owing to its high mutational burden and sensitivity to PD-1/PD-L1 blockade. Yadav and colleagues used MC38 together with a second murine model to develop and validate a mass spectrometry–exome sequencing pipeline for predicting immunogenic tumour mutations. Of more than 1,300 amino acid changes identified, roughly 13% were predicted to bind MHC class I, a small fraction of which were confirmed by mass spectrometry; structural modelling indicated that solvent-exposed mutations were the immunogenic ones, and vaccination of mice confirmed that each predicted peptide elicited therapeutically active T-cell responses [5]. This landmark study established MC38 as a benchmark system for neoantigen discovery and helped define principles now applied in personalised cancer vaccine development.

Research into glycan-mediated immune regulation has also relied on MC38. Cornelissen and colleagues used CRISPR/Cas9 to knock out CMAS, which encodes a key enzyme of the sialylation pathway, and completely abrogated cell-surface sialic acid expression [8]. Contrary to expectation, these fully desialylated MC38 cells grew significantly faster in vivo than controls, showed reduced intratumoural CD8-positive T-cell frequencies, and induced CD8-positive T-cell apoptosis in an antigen-independent manner. Low CMAS expression also correlated with shorter recurrence-free survival in a human colorectal cancer cohort. The work therefore serves as a caution for therapeutic strategies aimed at stripping tumour sialylation, and positions MC38 as a valuable system for dissecting glycan–immune interactions.

PD-L1 imaging with novel PET tracers represents another active application. Two linear peptide-based radiotracers, [⁶⁴Cu]/[⁶⁸Ga]HKP2201 and its dimer HKP2202, were validated in mouse models bearing MC38 colon cancer and B16F10 melanoma allografts, with PD-L1 expression confirmed by immunofluorescence and immunohistochemistry in both cell lines and their tumours [9]. Competitive binding and blocking studies confirmed target specificity, and PET imaging plus ex vivo biodistribution showed notable tumour uptake with rapid clearance from blood and major organs. The MC38 allograft thus provided one of the reference platforms for assessing tracer specificity in the translational development of non-invasive immune checkpoint imaging.

Cytokine Gene Therapy and Engineered Extracellular Vesicles

MC38 cells have been widely used as a poorly immunogenic model to test cytokine-based gene therapy strategies. Hiroishi and colleagues showed that transduction of MC38 cells with an interferon-alpha (IFN-α) gene caused rejection of the modified cells in 13 of 15 immunocompetent mice, and that admixing IFN-α- and CD80-transduced cells produced synergistic anti-tumour effects, with rejection in 14 of 15 animals [10]. Eguchi and colleagues extended this work by directly comparing IFN-α and interleukin-12 (IL-12) gene therapy in MC38, finding that IFN-α induced tumour-specific cytotoxic T lymphocyte responses and long-lasting immunity while IL-12 primarily stimulated non-specific killing involving both CD8-positive T cells and natural killer cells [11].

Rossowska and colleagues made a pivotal contribution to this field by engineering MC38 cells to release extracellular vesicles (EVs) loaded with immunostimulatory cargo [12]. Using lentiviral vectors, the authors generated MC38 sublines overexpressing murine IL-12, expressing shRNA targeting TGF-β1, or both, and showed that genetic modification of the parental cells is an effective way to load the molecules of interest into both tumour-derived exosomes and microvesicles. Modified exosomes inhibited tumour growth in mice bearing subcutaneous MC38 tumours, whereas exosomes from unmodified cells did not. The most durable effect required combination with dendritic cell-based vaccines, which restored anti-tumour immunity and induced a systemic Th1 response [12]. The study established modified MC38-derived exosomes as an adjuvant that can support a specific anti-tumour response rather than as a stand-alone vaccine.

Mesenchymal stromal cell-derived exosomes have also been studied in the MC38 context. Xing and colleagues knocked down GARP in mesenchymal stromal cells and showed that exosomes from these cells (siGARP-MSC) inhibited MC38 proliferation, migration, and invasion in vitro, reduced IL-6 secretion, and partly inactivated the JAK1/STAT3 pathway [13]. This identifies a paracrine axis between stromal and tumour cells that could be targeted therapeutically, although the findings are so far limited to cell culture. Together, these studies illustrate the MC38 model's versatility for evaluating cell-free and vesicle-based immunotherapeutic strategies.

Tumour Immunology, Adhesion, and Immune Evasion

The interaction between T lymphocytes and MC38 tumour cells has been the subject of detailed mechanistic investigation. MacKenzie, Hoskin, and Blay first reported that the adhesion of anti-CD3-activated T cells to MCA-38 cells was mediated principally through the integrin VLA-4 (α4β1), and that it was promoted by protein tyrosine kinase and protein kinase C signalling while being suppressed by cAMP-dependent pathways, with the regulatory machinery located predominantly in the effector cell [14]. A later study by the same group refined the picture: antibodies against α4 or β7, or against VCAM-1 on the tumour cells, suppressed adhesion, whereas anti-β1 antibodies did not, identifying α4β7–VCAM-1 as the dominant axis. That work also showed that adenosine, a nucleoside enriched in hypoxic tumour microenvironments, suppresses T cell adhesion specifically by blocking α4β7 function [15]. Readers should note that the two papers assign different β subunits to the same interaction.

The role of natural killer cells in controlling MC38 liver metastasis has been examined in both immunocompetent and immunodeficient hosts. Cohen and colleagues injected liver-derived MCA-38 (LD-MCA-38) cells into the ileocolic vein and found that conventional C57BL/6 mice retained the tumour cells in the liver and developed hepatic foci, whereas athymic nude mice cleared about 60% of labelled cells within 24 hours and developed no hepatic lesions [16]. Non-parenchymal liver cells from nude or poly(I:C)-treated mice — but not from untreated conventional mice — were cytotoxic to LD-MCA-38, and the responsible population was non-adherent and asialo-GM1 (AsGM1) positive; anti-AsGM1 treatment abolished this protection. Volpe and colleagues extended these findings, showing that depletion with either anti-AsGM1 or anti-NK1.1 markedly increased hepatic foci and shortened survival, whereas anti-Thy1.2 depletion of T cells significantly reduced foci, indicating that NK cells rather than T cells are the primary effectors preventing hepatic metastasis of LD-MCA-38 [17]. Johnkoski and colleagues further demonstrated that a single hepatic focus of LD-MCA-38, established by injection beneath the liver capsule, augmented the cytotoxic and proliferative function of liver non-parenchymal cells, increased the proportion of CD8-positive and γδ T cells, and elevated interleukin-6 and tumour necrosis factor levels [18].

Cancer Vaccines and Antigen Identification

MC38 cells have served as a reliable platform for developing and benchmarking whole tumour-cell vaccine strategies. Hodge and Schlom compared retroviral and poxvirus (vaccinia) vectors for delivering the co-stimulatory molecule B7-1 to MC38 cells [19]. Both vectors induced equivalent B7-1 surface expression and equal protection against challenge with native MC38 cells 14 days later. On rechallenge at 40 days, however, the retroviral vaccine was less effective, and against established pulmonary metastases the vaccinia-vectored vaccine was significantly superior (P = 0.0351; P = 0.024 in vaccinia-immune mice; P = 0.0014 on combined analysis). The study concluded that a poxvirus-vectored whole tumour-cell vaccine is at least as effective as, and sometimes more effective than, its retroviral counterpart — a finding that informed the subsequent clinical translation of poxvirus-vectored cancer vaccines. Lorenz and colleagues used MC38 cells infected with a recombinant vaccinia virus encoding murine LFA-3 (CD48) to show that enforced LFA-3 expression enhanced T cell proliferation, adhesion, and cytotoxicity in vitro and completely prevented tumour growth in syngeneic C57BL/6 mice, with partial protection against later challenge with uninfected parental cells [20].

Tumour antigen identification using the SEREX approach was applied to MC38 by Hampton and colleagues, who immunised C57BL/6 mice with MC38 cells and screened an MC38-derived expression library with immune sera [21]. This approach identified the endogenous ecotropic leukemia virus envelope (env) protein and the murine ATRX protein as candidate tumour antigens, expanding the repertoire of known murine tumour-associated antigens and providing tools for mechanistic vaccine studies. Takeda and colleagues generated fusion cells from MC38 tumour cells and dendritic cells, including dendritic cells isolated from tumour-bearing hosts, and showed that vaccination with either preparation induced equally high splenocyte cytolytic activity against MC38 and significantly suppressed established MC38 pulmonary metastases [22].

A distinct gene-therapy approach exploited immunity to the α(1,3)galactosyl (αGal) epitope. Unfer and colleagues challenged α(1,3)galactosyltransferase (αGT) knockout mice, which like humans lack the epitope and can raise anti-Gal antibodies, with αGal-expressing MC38 colon cancer cells [23]. Mice immunised with rabbit erythrocytes developed anti-αGal titres approaching those seen in human serum, predominantly IgG1 and IgG3, and showed improved survival and slower tumour development compared with non-immunised knockout and wild-type controls. The study provides in vivo proof of concept for αGT as a suicide gene in colorectal cancer gene therapy; complement-mediated lysis of αGal-transduced cells had been shown earlier in vitro using human serum.

Novel Therapeutic Strategies and Drug Testing

MC38 cells have been employed to evaluate a range of pharmacological and physical treatment modalities against colorectal cancer. Kuriyama and colleagues showed that electropermeabilization profoundly increased the sensitivity of murine colorectal cancer cells, including MC38, to bleomycin in vitro, although not to 5-fluorouracil or cisplatin [24]. In the accompanying in vivo experiments, electrochemotherapy with bleomycin or cisplatin produced complete regression of subcutaneous colorectal tumours in five and four of eight animals respectively, an effect attributable to increased intratumoural drug accumulation; the published report does not specify which of the two cell lines was used for these transplants. Manome and colleagues used MC38 cells to show that ultrasound-mediated gene delivery could transfect naked plasmid DNA into colon carcinoma cells both in vitro and in MC38 tumours growing in syngeneic mice, demonstrating the feasibility of mechanical insonation as a non-viral gene transfer technique [25].

Carborane-substituted diclofenac prodrugs have been re-evaluated using the MC38 model. Among a redesigned series, a zwitterionic amidine bearing a nido-cluster abolished MC38 viability in the low micromolar range, acting mainly through strong inhibition of cell division and moderate apoptosis accompanied by depletion of reactive oxygen and nitrogen species, whereas diclofenac itself and the carborane-substituted oxindoles were not cytotoxic [26]. Optogenetic approaches have also employed MC38 cells: MC38 and B16F10 cells expressing the light-driven outward proton pump archaerhodopsin-3 (AR3) underwent apoptotic cell death upon green light irradiation, and AR3-expressing tumours transplanted into C57BL/6 mice showed marked shrinkage or suppressed growth after irradiation [27]. Park and colleagues used MC38 cells as colon carcinoma controls in a melanoma-targeting gene therapy study, exploiting melanocyte-specific promoter/enhancer constructs linked to the Escherichia coli purine nucleoside phosphorylase gene; 96% of MC38 cells remained viable after prodrug treatment, confirming tissue-restricted expression [28].

Conclusion

MC38 cells occupy a central position in colorectal cancer and immuno-oncology research. Their syngeneic compatibility with C57BL/6 mice, high mutational burden, rich neoantigen landscape, and sensitivity to immune checkpoint inhibitors collectively make them one of the most informative preclinical models for studying colonic neoplasms, CD8-positive T-lymphocyte responses, tumour-associated macrophages, cancer vaccines, and programmed cell death 1 receptor pathway biology. Decades of published work have validated the model across gene therapy, adhesion biology, liver metastasis, and novel drug evaluation, while more recent studies leveraging extracellular vesicles, PET imaging, and optogenetics continue to expand its translational relevance. Given the documented divergence between sublines, provenance should be recorded and the genotype verified for every study. Researchers who require a reliable, well-characterised murine colorectal carcinoma model can order or enquire about MC38 cells directly at cytion.com.

Key Publications

1. Corbett TH, Griswold DP Jr, Roberts BJ, et al. (1975) Tumor induction relationships in development of transplantable cancers of the colon in mice for chemotherapy assays, with a note on carcinogen structure. Cancer Research 35:2434–2439. PMID: 1149045
2. Tan MH, Holyoke ED, Goldrosen MH (1976) Murine colon adenocarcinomas: methods for selective culture in vitro. Journal of the National Cancer Institute 56:871–873. PMID: 1255804 · DOI: 10.1093/jnci/56.4.871
3. Schrörs B, Hos BJ, Yildiz IG, et al. (2023) MC38 colorectal tumor cell lines from two different sources display substantial differences in transcriptome, mutanome and neoantigen expression. Frontiers in Immunology 14:1102282. PMID: 36969213 · DOI: 10.3389/fimmu.2023.1102282
4. Morimoto-Tomita M, Ohashi Y, Matsubara A, et al. (2005) Mouse colon carcinoma cells established for high incidence of experimental hepatic metastasis exhibit accelerated and anchorage-independent growth. Clinical & Experimental Metastasis 22:513–521. PMID: 16320114 · DOI: 10.1007/s10585-005-3585-0
5. Yadav M, Jhunjhunwala S, Phung QT, et al. (2014) Predicting immunogenic tumour mutations by combining mass spectrometry and exome sequencing. Nature 515:572–576. PMID: 25428506 · DOI: 10.1038/nature14001
6. Didion JP, Buus RJ, Naghashfar Z, et al. (2014) SNP array profiling of mouse cell lines identifies their strains of origin and reveals cross-contamination and widespread aneuploidy. BMC Genomics 15:847. PMID: 25277546 · DOI: 10.1186/1471-2164-15-847
7. Zhang CF, Yu XJ, Wang BY, et al. (2016) Whole mitochondrial genome sequence of a rat colorectal cancer MCA38 cell line. Mitochondrial DNA Part A 27:2034–2035. PMID: 25434994 · DOI: 10.3109/19401736.2014.974176 — see the caution note in Cellosaurus entry CVCL_B288.
8. Cornelissen LAM, Blanas A, van der Horst JC, et al. (2019) Disruption of sialic acid metabolism drives tumor growth by augmenting CD8+ T cell apoptosis. International Journal of Cancer 144:2290–2302. PMID: 30578646 · DOI: 10.1002/ijc.32084
9. Zhang L, Zhang S, Wu J, et al. (2023) Linear peptide-based PET tracers for imaging PD-L1 in tumors. Molecular Pharmaceutics 20:4256–4267. PMID: 37368947 · DOI: 10.1021/acs.molpharmaceut.3c00382
10. Hiroishi K, Tüting T, Tahara H, Lotze MT (1999) Interferon-alpha gene therapy in combination with CD80 transduction reduces tumorigenicity and growth of established tumor in poorly immunogenic tumor models. Gene Therapy 6:1988–1994. PMID: 10637450 · DOI: 10.1038/sj.gt.3301034
11. Eguchi J, Hiroishi K, Ishii S, Mitamura K (2003) Interferon-alpha and interleukin-12 gene therapy of cancer: interferon-alpha induces tumor-specific immune responses while interleukin-12 stimulates non-specific killing. Cancer Immunology, Immunotherapy 52:378–386. PMID: 12739068 · DOI: 10.1007/s00262-002-0367-2
12. Rossowska J, Anger N, Wegierek K, et al. (2019) Antitumor potential of extracellular vesicles released by genetically modified murine colon carcinoma cells with overexpression of interleukin-12 and shRNA for TGF-β1. Frontiers in Immunology 10:211. PMID: 30814999 · DOI: 10.3389/fimmu.2019.00211
13. Xing H, Liang C, Xu X, et al. (2020) Mesenchymal stroma/stem-like cells of GARP knockdown inhibits cell proliferation and invasion of mouse colon cancer cells (MC38) through exosomes. Journal of Cellular and Molecular Medicine 24:13984–13990. PMID: 33155413 · DOI: 10.1111/jcmm.16008
14. MacKenzie WM, Hoskin DW, Blay J (1999) The adhesion of anti-CD3-activated mouse T cells to syngeneic colon adenocarcinoma cells is differentially regulated by protein tyrosine kinase-, protein kinase C-, and cAMP-dependent pathways in the effector cell. Biochemical and Biophysical Research Communications 255:460–465. PMID: 10049731 · DOI: 10.1006/bbrc.1999.0232
15. MacKenzie WM, Hoskin DW, Blay J (2002) Adenosine suppresses alpha(4)beta(7) integrin-mediated adhesion of T lymphocytes to colon adenocarcinoma cells. Experimental Cell Research 276:90–100. PMID: 11978011 · DOI: 10.1006/excr.2002.5514
16. Cohen SA, Tzung SP, Doerr RJ, Goldrosen MH (1990) Role of asialo-GM1 positive liver cells from athymic nude or polyinosinic-polycytidylic acid-treated mice in suppressing colon-derived experimental hepatic metastasis. Cancer Research 50:1834–1840. PMID: 2306736
17. Volpe CM, Mehta N, Kim U, et al. (1999) AsGM1+ NK cells prevent metastasis of invading LD-MCA-38 tumor cells in the nude mouse. The Journal of Surgical Research 84:157–161. PMID: 10357913 · DOI: 10.1006/jsre.1999.5631
18. Johnkoski JA, Tzung SP, Doerr RJ, Cohen SA (1992) Hepatic metastasis alters the immune function of murine liver nonparenchymal cells. Archives of Surgery 127:1325–1329. PMID: 1444795 · DOI: 10.1001/archsurg.1992.01420110073015
19. Hodge JW, Schlom J (1999) Comparative studies of a retrovirus versus a poxvirus vector in whole tumor-cell vaccines. Cancer Research 59:5106–5111. PMID: 10537283
20. Lorenz MG, Kantor JA, Schlom J, Hodge JW (1999) Induction of anti-tumor immunity elicited by tumor cells expressing a murine LFA-3 analog via a recombinant vaccinia virus. Human Gene Therapy 10:623–631. PMID: 10094205 · DOI: 10.1089/10430349950018698
21. Hampton TA, Conry RM, Khazaeli MB, et al. (2000) SEREX analysis for tumor antigen identification in a mouse model of adenocarcinoma. Cancer Gene Therapy 7:446–455. PMID: 10766351 · DOI: 10.1038/sj.cgt.7700124
22. Takeda A, Homma S, Okamoto T, et al. (2003) Immature dendritic cell/tumor cell fusions induce potent antitumour immunity. European Journal of Clinical Investigation 33:897–904. PMID: 14511362 · DOI: 10.1046/j.1365-2362.2003.01194.x
23. Unfer RC, Hellrung D, Link CJ Jr (2003) Immunity to the alpha(1,3)galactosyl epitope provides protection in mice challenged with colon cancer cells expressing alpha(1,3)galactosyl-transferase: a novel suicide gene for cancer gene therapy. Cancer Research 63:987–993. PMID: 12615713
24. Kuriyama S, Matsumoto M, Mitoro A, et al. (2000) Electrochemotherapy for colorectal cancer with commonly used chemotherapeutic agents in a mouse model. Digestive Diseases and Sciences 45:1568–1577. PMID: 11007108 · DOI: 10.1023/a:1005565027969
25. Manome Y, Nakamura M, Ohno T, Furuhata H (2000) Ultrasound facilitates transduction of naked plasmid DNA into colon carcinoma cells in vitro and in vivo. Human Gene Therapy 11:1521–1528. PMID: 10945766 · DOI: 10.1089/10430340050083252
26. Selg C, Gordić V, Krajnović T, et al. (2024) Re-design and evaluation of diclofenac-based carborane-substituted prodrugs and their anti-cancer potential. Scientific Reports 14:30488. PMID: 39681576 · DOI: 10.1038/s41598-024-81414-x
27. Nakao S, Kojima K, Sato K, et al. (2025) Optogenetic cancer therapy using the light-driven outward proton pump rhodopsin archaerhodopsin-3 (AR3). Journal of the American Chemical Society 147:44131–44140. PMID: 41186408 · DOI: 10.1021/jacs.5c13053
28. Park BJ, Brown CK, Hu Y, et al. (1999) Augmentation of melanoma-specific gene expression using a tandem melanocyte-specific enhancer results in increased cytotoxicity of the purine nucleoside phosphorylase gene in melanoma. Human Gene Therapy 10:889–898. PMID: 10223723 · DOI: 10.1089/10430349950018292

Bibliographic data and abstracts retrieved from PubMed. Cell line metadata from the Cellosaurus entry for MC-38 (RRID:CVCL_B288).