Collagen metabolism disturbances are accompanied by an increase in prolidase activity in lung carcinoma planoepitheliale.
ABSTRACT One of the consequences of neoplastic transformation is deregulation of tissue collagen metabolism. Although metalloproteinases initiate the breakdown of collagen in lung carcinoma, the final step of collagen degradation is mediated by prolidase (E.C.126.96.36.199). We investigated whether prolidase activity could reflect disturbances of collagen metabolism in human lung carcinoma planoepitheliale (Ca pl.). Ten human lung Ca pl. and 10 samples of normal lung parenchyma were compared with respect to prolidase activity and expression (western immunoblot), the content of collagen and collagen degradation products (free and bound hydroxyproline determination), beta1 integrin subunit expression (western immunoblot) and collagenolytic activity (zymography). An increase in collagen content (66%, P < 0.05), free proline pool (50%, P < 0.05) and collagenolytic activity was accompanied by a significant increase in the prolidase activity (106%, P < 0.05) and its expression in Ca pl. No differences were found between Ca pl. and the control lung tissue with respect to beta1 integrin expression. Prolidase activity may reflect disturbances in tissue collagen metabolism in lung Ca pl. and it may, therefore, serve as a sensitive marker of the disease.
Article: Collagen biosynthesis anomalies in prolidase deficiency: effect of glycyl-L-proline on the degradation of newly synthesized collagen.[show abstract] [hide abstract]
ABSTRACT: 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.Clinical physiology and biochemistry 02/1989; 7(3-4):128-36.
Analytical Biochemistry 12/1960; 1:228-39. · 3.00 Impact Factor
Article: Optimal conditions for prolidase assay by proline colorimetric determination: application to iminodipeptiduria.[show abstract] [hide abstract]
ABSTRACT: Prolidase assay was reinvestigated by determining proline, using Chinard's method. Although several authors had previously tested this colorimetric reaction, accurate details regarding enzyme activity were not available. The need for greater sensitivity led to the introduction of several modifications: dialysis was eliminated and the substrate concentration and incubation time were changed. In addition, the reaction mixture was preincubated with Mn2+ for 24 h in order to triple prolidase activity. Color development followed at 90 degrees C, because of partial glycylproline hydrolysis at higher temperatures. The effect of several divalent cations on prolidase activity were tested with and without Mn2+. This modified assay was applied to erythrocytes, plasma and skin fibroblasts from a female patient with iminodipeptiduria.Clinica Chimica Acta 11/1982; 125(2):193-205. · 2.54 Impact Factor