Publications by authors named "Catherine A Ibarra"
Article Synopsis
- Interactions between normal mammary epithelial cells and extracellular matrix (ECM) are crucial for maintaining the health of the mammary gland, and disruptions in these interactions could trigger early stages of breast cancer.
- Suppressing the CREB-binding protein (CBP) in specific mammary epithelial cells leads to a loss of growth control and apoptosis, likely due to decreased expression of laminin-5 alpha3-chain and its regulatory gene LAMA3A.
- Reintroducing CBP in these cells restores ECM-mediated growth regulation and apoptosis by enhancing LAMA3A activity and laminin-5 alpha3-chain expression, indicating CBP's critical role in preventing early carcinogenic events in breast tissue.
The binding of plasminogen activator inhibitor-1 (PAI-1) to serine proteinases, such as tissue-type plasminogen activator (tPA) and urokinase-type plasminogen activator (uPA), is mediated by the exosite interactions between the surface-exposed variable region-1, or 37-loop, of the proteinase and the distal reactive center loop (RCL) of PAI-1. Although the contribution of such interactions to the inhibitory activity of PAI-1 has been established, the specific mechanistic steps affected by interactions at the distal RCL remain unknown. We have used protein engineering, stopped-flow fluorimetry, and rapid acid quenching techniques to elucidate the role of exosite interactions in the neutralization of tPA, uPA, and beta-trypsin by PAI-1.
View Article and Find Full Text PDFThe pKa of the catalytic Tyr-9 in glutathione S-transferase (GST) A1-1 is lowered from 10.3 to approximately 8.1 in the apoenzyme and approximately 9.
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