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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

Collagen biosynthesis anomalies in prolidase deficiency: effect of glycyl-L-proline on the degradation of newly synthesized collagen.

Prolidase deficiency is a rare hereditary disease characterized by an iminodipeptiduria especially composed by glycyl-L-proline which is not further degraded. The study of collagen metabolism in fibroblast cultures from three prolidase-deficient patients showed an increase in the rapidly degraded collagen and a decrease in the proline pool. In order to elucidate the mechanism of this metabolic disturbance, glycyl-L-proline was added to the cell cultures. In the control cultures, the addition of this dipeptide caused an increase in the rapidly degraded collagen and a decrease in the proline pool. The effects on the patient fibroblasts depended on the severity of the deficiency. The metabolic function of the dipeptide glycyl-L-proline was discussed in the light of these results.[1]

References

  1. Collagen biosynthesis anomalies in prolidase deficiency: effect of glycyl-L-proline on the degradation of newly synthesized collagen. Chamson, A., Voigtländer, V., Myara, I., Frey, J. Clinical physiology and biochemistry. (1989) [Pubmed]
 
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