Presentation Type

Oral/Paper Presentation

Abstract

Triple-negative breast cancer (TNBC) is a highly invasive and difficult-to-target form of cancer. It is characterized by a lack of estrogen receptors, progesterone receptors, and human epidermal growth factor 2 receptors, making current targeted therapies ineffective and leaving chemotherapy as the primary treatment option. Previous studies in this lab have linked reduced expression of neprilysin (NEP), a membrane-bound protease that cleaves and inactivates mitogenic peptides, to a highly invasive phenotype in TNBC. Our data indicates that while NEP promotes phosphoinositol 3-kinase (PI3K) signaling, it simultaneously inhibits cellular invasion. Here, we begin to explain a possible mechanism behind the anti-invasive role of NEP in TNBC cells. We have found that NEP interacts with AKT—a mediator of the PI3K pathway—to negatively regulate TNBC invasion, possibly through AKT-1 isoform specificity. The invasive phenotype of TNBC cells might be attributed to NEP involvement in actin remodeling. Preliminary data also suggests the involvement of casein kinase 2 (CKII), an intracellular kinase that phosphorylates both NEP and AKT1. The results of this research can help better understand the mechanisms by which NEP regulates PI3K signaling and TNBC cell invasion and metastasis. We hypothesize that CKII and NEP work together to promote AKT-1 regulation of TNBC cell invasion. Clinically, this research may help better predict which TNBC patients respond to PI3K-targeted therapies and provide insight into potential drug resistance mechanisms.

Faculty Mentor

Beth Conway, Ph.D.

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Elucidating the Mechanism of Neprilysin-Regulated Triple-Negative Breast Cancer Invasion

Triple-negative breast cancer (TNBC) is a highly invasive and difficult-to-target form of cancer. It is characterized by a lack of estrogen receptors, progesterone receptors, and human epidermal growth factor 2 receptors, making current targeted therapies ineffective and leaving chemotherapy as the primary treatment option. Previous studies in this lab have linked reduced expression of neprilysin (NEP), a membrane-bound protease that cleaves and inactivates mitogenic peptides, to a highly invasive phenotype in TNBC. Our data indicates that while NEP promotes phosphoinositol 3-kinase (PI3K) signaling, it simultaneously inhibits cellular invasion. Here, we begin to explain a possible mechanism behind the anti-invasive role of NEP in TNBC cells. We have found that NEP interacts with AKT—a mediator of the PI3K pathway—to negatively regulate TNBC invasion, possibly through AKT-1 isoform specificity. The invasive phenotype of TNBC cells might be attributed to NEP involvement in actin remodeling. Preliminary data also suggests the involvement of casein kinase 2 (CKII), an intracellular kinase that phosphorylates both NEP and AKT1. The results of this research can help better understand the mechanisms by which NEP regulates PI3K signaling and TNBC cell invasion and metastasis. We hypothesize that CKII and NEP work together to promote AKT-1 regulation of TNBC cell invasion. Clinically, this research may help better predict which TNBC patients respond to PI3K-targeted therapies and provide insight into potential drug resistance mechanisms.

 

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