Sarah C Proudfoot

Department of Biochemistry, Medical College of Wisconsin, Milwaukee, WI, U.S.A.

4 publications 2016 – 2019

What does Sarah C Proudfoot research?

Sarah C Proudfoot studies the mechanisms by which protein interactions influence both pancreatic cell survival and cholesterol metabolism. Specifically, she examines how nitric oxide helps pancreatic beta cells avoid self-destruction when faced with DNA damage caused by inflammatory signals. This research is crucial for understanding diabetes, as the death of these insulin-producing cells is a key factor in the disease. Additionally, she investigates the structure and function of the SR-BI protein, which plays a significant role in removing cholesterol from the bloodstream, thereby reducing the risk of heart disease.

Key findings

  • Nitric oxide protects pancreatic beta cells from self-destruction during DNA damage by blocking their alarm system, without involving the typical pathway related to protein phosphatase 1.
  • The study on SR-BI revealed that this receptor functions by forming pairs (dimers) and relies on a specific zipper-like structure to do so; disruptions in this structure inhibit its ability to remove cholesterol, which is critical for heart disease prevention.
  • Mapping the 3D structure of SR-BI has implications for developing better therapies for high cholesterol, enhancing our understanding of cardiovascular health.

Frequently asked questions

Does Dr. Proudfoot study diabetes?
Yes, she investigates how pancreatic cells survive DNA damage, which is relevant to pancreatic beta cell death in diabetes.
What treatments has Dr. Proudfoot researched?
She focuses on the mechanisms behind protein interactions that could lead to new treatments for diabetes and cardiovascular diseases.
Is Dr. Proudfoot's work relevant to heart disease?
Absolutely, her research on the SR-BI protein is directly linked to cholesterol metabolism, which is vital for preventing heart disease.

Publications in plain English

Proline residues in scavenger receptor-BI's C-terminal region support efficient cholesterol transport.

2019

The Biochemical journal

Proudfoot SC, Sahoo D

Plain English
This study looked at how specific parts of a protein called scavenger receptor-BI (SR-BI) help it transport cholesterol in the body. Researchers found that certain proline residues are critical for this process: when they mutated these residues, they found that the receptor could not efficiently take up cholesterol or transport it correctly—specifically, mutations at Pro-412 and Pro-438 severely impacted cholesterol uptake. Understanding how SR-BI works may help develop treatments for conditions related to cholesterol, like heart disease. Who this helps: Patients at risk for heart disease and healthcare providers treating them.

PubMed

Role of Protein Phosphatase 1 and Inhibitor of Protein Phosphatase 1 in Nitric Oxide-Dependent Inhibition of the DNA Damage Response in Pancreatic β-Cells.

2018

Diabetes

Oleson BJ, Naatz A, Proudfoot SC, Yeo CT, Corbett JA

Plain English
Researchers studied how nitric oxide—a molecule produced by insulin-producing cells in the pancreas—protects these cells from dying when their DNA is damaged by inflammatory signals. They found that nitric oxide blocks the cell's normal alarm system that detects DNA damage, preventing the cell from self-destructing in response to that damage. This protection works through a mechanism independent of the protein phosphatase 1 pathway that typically controls this alarm system.

PubMed

NMR Structure of the C-Terminal Transmembrane Domain of the HDL Receptor, SR-BI, and a Functionally Relevant Leucine Zipper Motif.

2017

Structure (London, England : 1993)

Chadwick AC, Jensen DR, Hanson PJ, Lange PT, Proudfoot SC +3 more

Plain English
Researchers mapped the exact 3D shape of a protein called SR-BI that sits on cell surfaces and grabs cholesterol-carrying particles from the blood—a critical step in preventing heart disease. They discovered that SR-BI works by pairing up with itself (forming dimers), and found a specific zipper-like pattern of amino acids that enables this pairing; when this pattern is damaged, the protein can't pair up and stops working. Understanding how this protein's structure lets it function properly could lead to better treatments for high cholesterol and cardiovascular disease.

PubMed

Epac Signaling Is Required for Cocaine-Induced Change in AMPA Receptor Subunit Composition in the Ventral Tegmental Area.

2016

The Journal of neuroscience : the official journal of the Society for Neuroscience

Liu X, Chen Y, Tong J, Reynolds AM, Proudfoot SC +4 more

Plain English
This study examined how a protein called Epac affects changes in brain receptors related to cocaine addiction. Researchers found that when mice were given cocaine, those with a normal amount of Epac showed an increase in a specific type of brain receptor, while those lacking Epac did not, indicating that Epac is necessary for these changes. These findings are important because they suggest that targeting Epac could help in understanding and potentially treating cocaine addiction. Who this helps: This helps patients struggling with cocaine addiction and researchers looking for new treatment approaches.

PubMed

Publication data sourced from PubMed . Plain-English summaries generated by AI. Not medical advice.