Asset Details
Do you wish to reserve the book?
Proteomic landscape of TGF-β1-induced fibrogenesis in renal fibroblasts
Hey, we have placed the reservation for you!
By the way, why not check out events that you can attend while you pick your title.
Oops! Something went wrong.
Looks like we were not able to place the reservation. Kindly try again later.
Are you sure you want to remove the book from the shelf?
Proteomic landscape of TGF-β1-induced fibrogenesis in renal fibroblasts
Do you wish to request the book?
Proteomic landscape of TGF-β1-induced fibrogenesis in renal fibroblasts
Please be aware that the book you have requested cannot be checked out. If you would like to checkout this book, you can reserve another copy
We have requested the book for you!
Your request is successful and it will be processed during the Library working hours. Please check the status of your request in My Requests.
Oops! Something went wrong.
Looks like we were not able to place your request. Kindly try again later.
Journal Article
Proteomic landscape of TGF-β1-induced fibrogenesis in renal fibroblasts
2020
Overview
Transforming growth factor-β1 (TGF-β1) plays a premier role in fibrosis. To understand the molecular events underpinning TGF-β1-induced fibrogenesis, we examined the proteomic profiling of a TGF-β1-induced in vitro model of fibrosis in NRK-49F normal rat kidney fibroblasts. Mass spectrometric analysis indicated that 628 cell-lysate proteins enriched in 44 cellular component clusters, 24 biological processes and 27 molecular functions were regulated by TGF-β1. Cell-lysate proteins regulated by TGF-β1 were characterised by increased ribosomal proteins and dysregulated proteins involved in multiple metabolic pathways, including reduced Aldh3a1 and induced Enpp1 and Impdh2, which were validated by enzyme-linked immunosorbent assays (ELISA). In conditioned media, 62 proteins enriched in 20 cellular component clusters, 40 biological processes and 7 molecular functions were regulated by TGF-β1. Secretomic analysis and ELISA uncovered dysregulated collagen degradation regulators (induced PAI-1 and reduced Mmp3), collagen crosslinker (induced Plod2), signalling molecules (induced Ccn1, Ccn2 and Tsku, and reduced Ccn3) and chemokines (induced Ccl2 and Ccl7) in the TGF-β1 group. We conclude that TGF-β1-induced fibrogenesis in renal fibroblasts is an intracellular metabolic disorder and is inherently coupled with inflammation mediated by chemokines. Proteomic profiling established in this project may guide development of novel anti-fibrotic therapies in a network pharmacology approach.
Publisher
Nature Publishing Group UK,Nature Publishing Group
Subject
/ 631/154
/ 631/337
/ 631/45
/ 631/553
/ 631/80
/ Collagen
/ Computational Biology - methods
/ Connective tissue growth factor
/ Culture Media, Conditioned - metabolism
/ Enzyme-Linked Immunosorbent Assay
/ Fibrosis
/ Humanities and Social Sciences
/ Kidney Diseases - metabolism
/ Kidneys
/ Monocyte chemoattractant protein 1
/ Proteins
/ Proteome
/ Science
