Characterization of prolidase activity in erythrocytes from a patient with prolidase deficiency: Comparison with prolidase I and II purified from normal human erythrocytes

Liu, Gang; Nakayama, Kazunori; Sagara, Yusuke; Awata, Shiro; Yamashita, Koichi; Manabe, Masanobu; Kodama, Hiroyuki

doi:10.1016/j.clinbiochem.2005.03.007

Cited by 11 publications

(5 citation statements)

References 22 publications

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“…contrast, PEPD is a cytosolic protein (34,35), and there is no evidence that PEPD undergoes proteolytic maturation. The exact PEPD sequence to bind and activate EGFR remains to be elucidated.…”

Section: Discussionmentioning

confidence: 99%

Prolidase Directly Binds and Activates Epidermal Growth Factor Receptor and Stimulates Downstream Signaling

Yang

Ding

et al. 2013

Journal of Biological Chemistry

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Background: All known ligands of EGF receptor (EGFR) are characterized by the EGF motif and generated from transmembrane precursors. Results: Prolidase, a cytosolic dipeptidase devoid of EGF motif, binds and activates EGFR independent of its dipeptidase activity when present outside of cell. Conclusion: Prolidase is a novel EGFR ligand.Significance: This shows a new function of prolidase and new mechanism of EGFR activation.

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Section: Discussionmentioning

confidence: 99%

Prolidase Directly Binds and Activates Epidermal Growth Factor Receptor and Stimulates Downstream Signaling

Yang

Ding

et al. 2013

Journal of Biological Chemistry

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“…The gene is located on the short arm of chromosome 19 (22,23). Prolidase activity is present in patients with prolidase deficiency and enzymatic properties of the patient's prolidase are essentially the same as those of PD II (19). Therefore, this study was undertaken to characterize and determine physiologic roles of different prolidase isoenzymes and to further investigate the molecular basis of prolidase deficiency.…”

Section: Discussionmentioning

confidence: 99%

“…We have also purified PD I and PD II from normal human erythrocytes, and found that the two isolated isoforms of prolidase differed in molecular mass (PD I, 56 kD, and PD II, 95 kD, in SDS-PAGE), response to manganese, substrate specificity, and heat stability (17,18). Moreover, prolidase activity is indeed present in patients with prolidase deficiency, and enzymatic properties of the patient's prolidase are essentially the same as those of PD II (19). Therefore, we attempted to give further insight into the understanding of the biosynthesis and physiologic roles of PD I and PD II isoenzymes.…”

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confidence: 99%

Prolidase Isoenzymes in the Rat: Their Organ Distribution, Developmental Change and Specific Inhibitors

et al. 2007

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Lack of prolidase I (PD I) leads to prolidase deficiency, a disease characterized by intractable skin lesions, recurrent respiratory infections, and mental retardation. The present study was undertaken to characterize and determine the physiologic roles of different prolidase isoenzymes. Two isoforms of prolidase were isolated from rat kidney. PD I showed higher activity against serylproline and alanyl-proline, whereas PD II was active especially against methionyl-proline. PD I was highly concentrated in the small intestine and kidney, whereas PD II was shown not to vary in the organs examined. Expression of PD I and PD II in the small intestine were maximal within 1 wk of birth, and then rapidly declined. The changes of prolidase in the kidney and heart were found to differ slightly. N-benzyloxycarbonyl-L-proline and captopril inhibited PD I dose-dependently, but showed no inhibition of PD II at low concentrations. NiCl 2 inhibited PD II much more effectively than PD I. Our findings suggest that PD I functions by way of an intestinal peptide carrier, which may also be regulated by the uptake of various iminodipeptides. Similarly, age-related alterations of prolidase isoenzymes suggest that intestinal PD II also participates in absorption of proline and other amino acids early in life.

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“…Although still in use [21], this method is time-consuming and not very specific since the presence of other aminoacids (i.e. lysine and ornithine) and of the reduced form of glutathione can interfere with the colorimetric reaction.…”

Section: Determination Of Prolidase Activitymentioning

confidence: 99%

The role of emerging techniques in the investigation of prolidase deficiency: From diagnosis to the development of a possible therapeutical approach

Viglio¹,

Annovazzi²,

Conti³

et al. 2006

Journal of Chromatography B

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Characterization of prolidase activity in erythrocytes from a patient with prolidase deficiency: Comparison with prolidase I and II purified from normal human erythrocytes

Cited by 11 publications

References 22 publications

Prolidase Directly Binds and Activates Epidermal Growth Factor Receptor and Stimulates Downstream Signaling

Prolidase Directly Binds and Activates Epidermal Growth Factor Receptor and Stimulates Downstream Signaling

Prolidase Isoenzymes in the Rat: Their Organ Distribution, Developmental Change and Specific Inhibitors

The role of emerging techniques in the investigation of prolidase deficiency: From diagnosis to the development of a possible therapeutical approach

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