98%
921
2 minutes
20
Large numbers of melanoma lesions develop resistance to targeted inhibition of mutant BRAF or fail to respond to checkpoint blockade. We explored whether modulation of intratumoral antigen-presenting cells (APCs) could increase responses to these therapies. Using mouse melanoma models, we found that CD103(+) dendritic cells (DCs) were the only APCs transporting intact antigens to the lymph nodes and priming tumor-specific CD8(+) T cells. CD103(+) DCs were required to promote anti-tumoral effects upon blockade of the checkpoint ligand PD-L1; however, PD-L1 inhibition only led to partial responses. Systemic administration of the growth factor FLT3L followed by intratumoral poly I:C injections expanded and activated CD103(+) DC progenitors in the tumor, enhancing responses to BRAF and PD-L1 blockade and protecting mice from tumor rechallenge. Thus, the paucity of activated CD103(+) DCs in tumors limits checkpoint-blockade efficacy and combined FLT3L and poly I:C therapy can enhance tumor responses to checkpoint and BRAF blockade.
Download full-text PDF |
Source |
---|---|
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4980762 | PMC |
http://dx.doi.org/10.1016/j.immuni.2016.03.012 | DOI Listing |
FEBS J
September 2025
Department of Biological Science and Technology, Faculty of Advanced Engineering, Tokyo University of Science, 6-3-1 Niijuku, Katsushika-ku, Tokyo, 125-8585, Japan.
Mucosal mast cells (MMCs) are distinguished from connective tissue mast cells (MCs) by the specific cell-surface expression of integrin CD103 (also known as integrin αE/β7; αE is encoded by Itgae) and mast cell protease 1 and 2 (Mcpt1 and Mcpt2, respectively). Although the expression of the Mcpt1 and Mcpt2 genes is cooperatively regulated by the transcription factor GATA-binding protein 2 (GATA2) and transforming growth factor beta (TGF-β) signaling in MMCs, the transcriptional mechanism of the cell-surface expression of CD103 remains unknown. We herein found that surface CD103 and Itgae mRNA levels were significantly increased by the knockdown (KD) of Gata2 in mouse bone marrow-derived MCs (BMMCs), which was accelerated by TGF-β stimulation.
View Article and Find Full Text PDFJCI Insight
August 2025
Department of Chemistry, School of Engineering, Stanford, United States of America.
In celiac disease (CeD), a gluten-dependent autoimmune disorder, transglutaminase 2 (TG2) deamidates selected glutamine residues in gluten peptides, while HLA-DQ2 presents deamidated antigens to inflammatory T cells. The cellular sources of pathogenic TG2 and DQ2 are unclear. Using chemical biology tools, we show that intestinal CD103+ dendritic cells (DCs) couple cell-surface TG2 to the endocytic LRP1 receptor to simultaneously deamidate gluten antigens and concentrate them in lysosomes.
View Article and Find Full Text PDFCell Rep Med
August 2025
Department of Radiation Oncology, Nanfang Hospital, Southern Medical University, Guangzhou 510515, China. Electronic address:
Liver kinase B1 (LKB1)-deficient non-small cell lung cancers (NSCLCs) exhibit primary resistance to immune checkpoint inhibitors (ICIs). The redox imbalance inherent in these tumors may represent a potential therapeutic vulnerability. High-dose ascorbic acid (AA) could induce cell redox imbalance.
View Article and Find Full Text PDFJ Agric Food Chem
August 2025
School of Food Science and Biotechnology, Zhejiang Gongshang University, Hangzhou 310018, P.R. China.
This study examines how α-dicarbonyl compounds─methylglyoxal (MGO) and glyoxal (GO)─affect the structure and allergenicity of β-lactoglobulin (β-LG) and α-casein (α-CN) during thermal processing. Glycation-induced changes were analyzed using SDS-PAGE, circular dichroism, and HPLC-MS/MS, while advanced glycation end-products (AGEs) were quantified via UHPLC-QqQ-MS/MS. Results showed that GO was more reactive than MGO, modifying Lys/Arg residues and increasing AGEs in a temperature- and concentration-dependent manner.
View Article and Find Full Text PDFACS Chem Biol
August 2025
Bristol-Myers Squibb Research & Development, 700 Bay Road, Redwood City, California 94063, USA.
C-type lectin receptor, Clec9a, is a highly specific receptor expressed on cross-presenting conventional dendritic cells (cDC1). This receptor specificity for this rare population of dendritic cells (DCs), combined with their inherent ability to internalize and localize to the endocytic compartment, presents a unique opportunity for targeted delivery of innate immune agonists. By leveraging an anti-Clec9a antibody, we can specifically deliver these agonists to cross-presenting cDCs, thereby enhancing the cross-priming and expansion of tumor-specific cytotoxic T lymphocytes (CTLs).
View Article and Find Full Text PDF