Reviewing the Regulators of COL1A1.
Hanne DevosJerome ZoidakisMaria G RoubelakisAgnieszka LatosinskaAntonia VlahouPublished in: International journal of molecular sciences (2023)
The collagen family contains 28 proteins, predominantly expressed in the extracellular matrix (ECM) and characterized by a triple-helix structure. Collagens undergo several maturation steps, including post-translational modifications (PTMs) and cross-linking. These proteins are associated with multiple diseases, the most pronounced of which are fibrosis and bone diseases. This review focuses on the most abundant ECM protein highly implicated in disease, type I collagen (collagen I), in particular on its predominant chain collagen type I alpha 1 (COLα1 (I)). An overview of the regulators of COLα1 (I) and COLα1 (I) interactors is presented. Manuscripts were retrieved searching PubMed, using specific keywords related to COLα1 (I). COL1A1 regulators at the epigenetic, transcriptional, post-transcriptional and post-translational levels include DNA Methyl Transferases (DNMTs), Tumour Growth Factor β (TGFβ), Terminal Nucleotidyltransferase 5A (TENT5A) and Bone Morphogenic Protein 1 (BMP1), respectively. COLα1 (I) interacts with a variety of cell receptors including integrinβ, Endo180 and Discoidin Domain Receptors (DDRs). Collectively, even though multiple factors have been identified in association to COLα1 (I) function, the implicated pathways frequently remain unclear, underscoring the need for a more spherical analysis considering all molecular levels simultaneously.
Keyphrases
- extracellular matrix
- growth factor
- transcription factor
- gene expression
- wound healing
- binding protein
- tissue engineering
- single molecule
- stem cells
- dna methylation
- protein protein
- small molecule
- bone regeneration
- heat shock
- amino acid
- cell therapy
- oxidative stress
- circulating tumor
- postmenopausal women
- signaling pathway
- circulating tumor cells