FKBP65-dependent peptidyl-prolyl isomerase activity potentiates the lysyl hydroxylase 2-driven collagen cross-link switch
Sign Up to like & getrecommendations! Published in 2017 at "Scientific Reports"
DOI: 10.1038/srep46021
Abstract: Bruck Syndrome is a connective tissue disease associated with inactivating mutations in lysyl hydroxylase 2 (LH2/PLOD2) or FK506 binding protein 65 (FKBP65/FKBP10). However, the functional relationship between LH2 and FKBP65 remains unclear. Here, we postulated… read more here.
Keywords: collagen; peptidyl prolyl; lysyl hydroxylase; collagen cross ... See more keywords
Collagen cross-linking mediated by lysyl hydroxylase 2: an enzymatic battlefield to combat fibrosis.
Sign Up to like & getrecommendations! Published in 2019 at "Essays in biochemistry"
DOI: 10.1042/ebc20180051
Abstract: The hallmark of fibrosis is an excessive accumulation of collagen, ultimately leading to organ failure. It has become evident that the deposited collagen also exhibits qualitative modifications. A marked modification is the increased cross-linking, leading… read more here.
Keywords: cross linking; collagen cross; fibrosis; cross ... See more keywords
A Fe2+-dependent self-inhibited state influences the druggability of human collagen lysyl hydroxylase (LH/PLOD) enzymes
Sign Up to like & getrecommendations! Published in 2022 at "Frontiers in Molecular Biosciences"
DOI: 10.3389/fmolb.2022.876352
Abstract: Multifunctional human collagen lysyl hydroxylase (LH/PLOD) enzymes catalyze post-translational hydroxylation and subsequent glycosylation of collagens, enabling their maturation and supramolecular organization in the extracellular matrix (ECM). Recently, the overexpression of LH/PLODs in the tumor microenvironment… read more here.
Keywords: human collagen; hydroxylase; plod; lysyl hydroxylase ... See more keywords