Role of ID Proteins in BMP4 Inhibition of Profibrotic Effects of TGF-β2 in Human TM Cells | Zendy

Avani A. Mody | Zendy; Robert J. Wordinger | Zendy; Abbot F. Clark | Zendy

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Role of ID Proteins in BMP4 Inhibition of Profibrotic Effects of TGF-β2 in Human TM Cells

Author(s) -

Avani A. Mody,

Robert J. Wordinger,

Abbot F. Clark

Publication year - 2017

Publication title -

investigative ophthalmology and visual science

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.935

H-Index - 218

eISSN - 1552-5783

pISSN - 0146-0404

DOI - 10.1167/iovs.16-20472

Subject(s) - fibronectin , bone morphogenetic protein 4 , microbiology and biotechnology , extracellular matrix , bone morphogenetic protein , transforming growth factor , biology , trabecular meshwork , tgfbi , immunocytochemistry , transfection , chemistry , cell culture , endocrinology , gene , biochemistry , glaucoma , genetics , neuroscience

Increased expression of TGF-β2 in primary open-angle glaucoma (POAG) aqueous humor (AH) and trabecular meshwork (TM) causes deposition of extracellular matrix (ECM) in the TM and elevated IOP. Bone morphogenetic proteins (BMPs) regulate TGF-β2-induced ECM production. The underlying mechanism for BMP4 inhibition of TGF-β2-induced fibrosis remains undetermined. Bone morphogenic protein 4 induces inhibitor of DNA binding proteins (ID1, ID3), which suppress transcription factor activities to regulate gene expression. Our study will determine whether ID1and ID3 proteins are downstream targets of BMP4, which attenuates TGF-β2 induction of ECM proteins in TM cells.

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