Search

Your search keyword '"Buzza, Marguerite S."' showing total 40 results
Start Over Author "Buzza, Marguerite S."
40 results on '"Buzza, Marguerite S."'

9. Selective targeting of metastatic ovarian cancer using an engineered anthrax prodrug activated by membrane-anchored serine proteases

Author

Duru, Nadire, primary, Pawar, Nisha R., additional, Martin, Erik W., additional, Buzza, Marguerite S., additional, Conway, Gregory D., additional, Lapidus, Rena G., additional, Liu, Shihui, additional, Reader, Jocelyn, additional, Rao, Gautam G., additional, Roque, Dana M., additional, Leppla, Stephen H., additional, and Antalis, Toni M., additional

Published
2022
Full Text
View/download PDF

15. Membrane-anchored Serine Proteases and Protease-activated Receptor-2 (PAR-2)-mediated Signaling: Co-conspirators in Cancer Progression

Author

Pawar, Nisha R., Buzza, Marguerite S., and Antalis, Toni M.

Subjects
Glycosylphosphatidylinositols, Neoplasms, Cell Membrane, Disease Progression, Animals, Humans, Receptor, PAR-2, Serine Proteases, Article, Signal Transduction
Abstract

Pericellular proteolysis provides a significant advantage to developing tumors through the ability to remodel the extracellular matrix, promote cell invasion and migration, and facilitate angiogenesis. Recent advances demonstrate that pericellular proteases can also communicate directly to cells by activation of a unique group of transmembrane G protein-coupled receptors (GPCRs) known as protease activated receptors (PARs). In this review we discuss the specific roles of one of four mammalian PARs, namely PAR-2, which is over-expressed in advanced stage tumors and is activated by trypsin-like serine proteases that are highly expressed or otherwise dysregulated in many cancers. We highlight recent insights into the ability of different protease agonists to bias PAR-2 signaling and the newly emerging evidence for an interplay between PAR-2 and membrane-anchored serine proteases, which may co-conspire to promote tumor progression and metastasis. Interfering with these pathways might provide unique opportunities for the development of new mechanism-based strategies for the treatment of advanced and metastatic cancers.

Published
2019

24. Candidate genes for limiting cholestatic intestinal injury identified by gene expression profiling

Author

Alaish, Samuel M., primary, Timmons, Jennifer, additional, Smith, Alexis, additional, Buzza, Marguerite S., additional, Murphy, Ebony, additional, Zhao, Aiping, additional, Sun, Yezhou, additional, Turner, Douglas J., additional, Shea-Donahue, Terez, additional, Antalis, Toni M., additional, Cross, Alan, additional, and Dorsey, Susan G., additional

Published
2013
Full Text
View/download PDF

40. Matriptase drives dissemination of ovarian cancer spheroids by a PAR-2/PI3K/Akt/MMP9 signaling axis.

Author

Pawar NR, Buzza MS, Duru N, Strong AA, and Antalis TM

Subjects
Female, Humans, Matrix Metalloproteinase 9 genetics, Phosphatidylinositol 3-Kinases genetics, Proto-Oncogene Proteins c-akt genetics, Spheroids, Cellular, Ovarian Neoplasms genetics, Signal Transduction, Serine Endopeptidases metabolism
Abstract

The transmembrane serine protease matriptase is a key regulator of both barrier-disruptive and protective epithelial cell-cell interactions. Elevated matriptase is a consistent feature of epithelial ovarian cancers (OvCa), where multicellular spheroids shed from the primary tumor into the peritoneal cavity are critical drivers of metastasis. Dynamic cell-to-cell adhesive contacts are required for spheroid formation and maintenance. Here, we show that overactive matriptase, reflected in an increased ratio of matriptase to its inhibitor hepatocyte growth factor activator inhibitor 1 (HAI-1), disrupts cell-cell contacts to produce loose prometastatic spheroids that display increased mesothelial cell adhesion and submesothelial invasion. We show that these activities are dependent on the matriptase activation of a protease-activated receptor-2 (PAR-2) signaling pathway involving PI3K/Akt and MMP9-induced disruption of cell-cell adhesion by the release of the soluble E-cadherin ectodomain. These data reveal a novel pathological connection between matriptase activation of PAR-2 and disruption of cell-cell adhesion, and support the clinical investigation of this signaling axis as a therapeutic strategy for aggressive metastatic OvCa., (© 2023 Pawar et al.)

Published
2023
Full Text
View/download PDF

Catalog

Books, media, physical & digital resources
See catalog results