Article
Lack of prolidase causes a bone phenotype both in human and in mouse.
Bone - 1 Mar 2015
Besio Roberta, Maruelli Silvia, Gioia Roberta, Villa Isabella, Grabowski Peter, Gallagher Orla, Bishop Nicholas J, Foster Sarah, De Lorenzi Ersilia, Colombo Raffaella, Diaz Josè Luis Dapena, Moore-Barton Haether, Deshpande Charu, Aydin Halil Ibrahim, Tokatli Aysegul, Kwiek Bartlomiej, Kasapkara Cigdem Seher, Adisen Esra Ozsoy, Gurer Mehmet Ali, Di Rocco Maja, Phang James M, Gunn Teresa M, Tenni Ruggero, Rossi Antonio, Forlino Antonella
Abstract excerpt
The degradation of the main fibrillar collagens, collagens I and II, is a crucial process for skeletal development. The most abundant dipeptides generated from the catabolism of collagens contain proline and hydroxyproline. In humans, prolidase is the only enzyme able to hydrolyze dipeptides containing these amino acids at their C-terminal end, thus being a key player in collagen synthesis and turnover. Mutations...
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