
The prolyl isomerase Pin1 specifically isomerizes certain phosphorylated Ser/Thr-Pro bonds and thereby regulates various cellular processes. Pin1 is a target of several oncogenic pathways and is overexpressed in human breast cancer. Its overexpression can lead to upregulation of cyclin D1 and transformation of breast epithelial cells in collaboration with the oncogenic pathways. In contrast, inhibition of Pin1 can suppress the transformation of breast epithelial cells. In addition, Pin1 knockout in mice prevents massive proliferation of breast epithelial cells during pregnancy. Pin1 plays a pivotal role in breast development and may be a promising new anticancer target.
breast development, cyclin D1, 610, Breast Neoplasms, Epithelial Cells, Peptidylprolyl Isomerase, Gene Expression Regulation, Enzymologic, Gene Expression Regulation, Neoplastic, NIMA-Interacting Peptidylprolyl Isomerase, Mice, breast cancer, Pin1, Cell Transformation, Neoplastic, Mammary Glands, Animal, Animals, Humans, Female, Breast, phosphorylation signaling
breast development, cyclin D1, 610, Breast Neoplasms, Epithelial Cells, Peptidylprolyl Isomerase, Gene Expression Regulation, Enzymologic, Gene Expression Regulation, Neoplastic, NIMA-Interacting Peptidylprolyl Isomerase, Mice, breast cancer, Pin1, Cell Transformation, Neoplastic, Mammary Glands, Animal, Animals, Humans, Female, Breast, phosphorylation signaling
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