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Your search keyword '"Yuspa, Stuart H."' showing total 46 results
Start Over Author "Yuspa, Stuart H." Publisher wiley-blackwell
46 results on '"Yuspa, Stuart H."'

1. Crosstalk between tumour and stroma modifies CLIC4 cargo in extracellular vesicles.

Author

Sanchez, Vanesa C., Craig‐Lucas, Alayna, Cataisson, Christophe, Carofino, Brandi L., and Yuspa, Stuart H.

Subjects
EXTRACELLULAR vesicles, TUMORS, BREAST cancer, CANCER cells, CANCER patients
Abstract

Mouse models of breast cancer have revealed that tumour‐bearing hosts must express the oxidoreductase CLIC4 to develop lung metastases. In the absence of host CLIC4, primary tumours grow but the lung premetastatic niche is defective for metastatic seeding. Primary breast cancer cells release EVs that incorporate CLIC4 as cargo and circulate in plasma of wildtype tumour‐bearing hosts. CLIC4‐deficient breast cancer cells also form tumours in wildtype hosts and release EVs in plasma, but these EVs lack CLIC4, suggesting that the tumour is the source of the plasma‐derived EVs that carry CLIC4 as cargo. Paradoxically, circulating EVs are also devoid of CLIC4 when CLIC4‐expressing primary tumours are grown in CLIC4 knockout hosts. Thus, the incorporation of CLIC4 (and perhaps other factors) as EV cargo released from tumours involve specific signals from the surrounding stroma determined by its genetic composition. Since CLIC4 is also detected in circulating EVs from human breast cancer patients, future studies will address its association with disease. [ABSTRACT FROM AUTHOR]

Published
2023
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3. Cell autonomous or systemic EGFR blockade alters the immune-environment in squamous cell carcinomas.

Author

Mascia, Francesca, Schloemann, Derek T., Cataisson, Christophe, McKinnon, Katherine M., Krymskaya, Ludmila, Wolcott, Karen M., and Yuspa, Stuart H.

Abstract

Targeting mutations and amplifications in the EGFR has been successful precision therapy for cancers of the lung, oral cavity and gastrointestinal track. However, a systemic immune reaction manifested by dose-limiting inflammation in the skin and gut has been a consistent adverse effect. To address the possibility that intra-tumoral immune changes contribute to the anti-cancer activity of EGFR inhibition, squamous cancers were produced by syngeneic orthografts of either EGFR null or wildtype mouse primary keratinocytes transduced with an oncogenic H-ras retrovirus. Flow cytometric, RNA and Bioplex immunoassay analyses of the tumor immune milieu were performed. Cancers forming from keratinocytes genetically depleted of EGFR were smaller than wildtype cancers and had fewer infiltrating FoxP3 Treg cells, lower Foxp3 RNA and a lower percentage of CD4 PD1 positive cells indicating a tumor cell autonomous regulation of its microenvironment. Hosts bearing wildtype cancers treated with gefitinib for 1 week showed a trend for smaller tumors. In this short term pharmacological model, there was also a trend to reduced FoxP3 cells and FoxP3 RNA in the tumors of treated mice as well as a substantial increase in the ratio of IL-1A/IL-1RA transcripts. These results suggest that relatively brief systemic inhibition of EGFR signaling alters the immune environment of the targeted cancer. Together these data imply that an EGFR dependent Treg function supports the growth of squamous cancers and is a target for the therapeutic activity of EGFR inhibition. [ABSTRACT FROM AUTHOR]

Published
2016
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9. Purification, crystallization and preliminary X-ray diffraction of human S100A15.

Author

Boeshans, Karen M., Wolf, Ronald, Voscopoulos, Christopher, Gillette, William, Esposito, Dominic, Mueser, Timothy C., Yuspa, Stuart H., and Ahvazi, Bijan

Subjects
PSORIASIS, CALCIUM-binding proteins, X-ray diffraction, CRYSTALLIZATION, GENES, SKIN diseases
Abstract

Human S100A15 is a novel member of the S100 family of EF-hand calcium-binding proteins and was recently identified in psoriasis, where it is significantly upregulated in lesional skin. The protein is implicated as an effector in calcium-mediated signal transduction pathways. Although its biological function is unclear, the association of the 11.2 kDa S100A15 with psoriasis suggests that it contributes to the pathogenesis of the disease and could provide a molecular target for therapy. To provide insight into the function of S100A15, the protein was crystallized to visualize its structure and to further the understanding of how the many similar calcium-binding mediator proteins in the cell distinguish their cognate target molecules. The S100A15 protein has been cloned, expressed and purified to homogeneity and produced two crystal forms. Crystals of form I are triclinic, with unit-cell parameters a = 33.5, b = 44.3, c = 44.8 Å, α = 71.2, β = 68.1, γ = 67.8° and an estimated two molecules in the asymmetric unit, and diffract to 1.7 Å resolution. Crystals of form II are monoclinic, with unit-cell parameters a = 82.1, b = 33.6, c = 52.2 Å, β = 128.2° and an estimated one molecule in the asymmetric unit, and diffract to 2.0 Å resolution. This structural analysis of the human S100A15 will further aid in the phylogenic comparison between the other members of the S100 protein family, especially the highly homologous paralog S100A7. [ABSTRACT FROM AUTHOR]

Published
2006
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11. Cover Image, Volume 60, Issue 12.

Author

Lee, Alex J., Fraser, Elise, Flowers, Brittany, Kim, Jee, Wong, Kenneth, Cataisson, Christophe, Liu, Huaitian, Yang, Howard, Lee, Maxwell P., Yuspa, Stuart H., and Li, Luowei

Published
2021
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