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.
Chamson
A
A
Biochemistry Department, Medical School, Saint-Etienne, France.
Voigtländer
V
V
Myara
I
I
Frey
J
J
D000328:Adult; D002478:Cells, Cultured; D003094:Collagen / Q000096:biosynthesis*; D004150:Dipeptidases; D004151:Dipeptides / Q000494:pharmacology*; D005260:Female; D005347:Fibroblasts / Q000201:enzymology / Q000378:metabolism*; D006801:Humans; D006900:Hydroxylation; D006899:Mixed Function Oxygenases / Q000378:metabolism*; D011489:Protein Denaturation
D004151:Dipeptides; C015248:glycylproline; D003094:Collagen; D006899:Mixed Function Oxygenases; D004150:Dipeptidases; C022449:proline dipeptidase