Skip to content
Licensed Unlicensed Requires Authentication Published by De Gruyter June 1, 2005

Characteristics of prolinase against various iminodipeptides in erythrocyte lysates from a normal human and a patient with prolidase deficiency

  • Weifang Wang , Gang Liu , Koichi Yamashita , Masanobu Manabe and Hiroyuki Kodama

Abstract

The effect of various amino acids and MnCl2 on prolinase activity in erythrocyte lysates from a healthy individual and a patient with prolidase deficiency was investigated. A concentration of 0.1 mM MnCl2 increased prolinase activity in normal erythrocytes against pro-gly, pro-glu, pro-leu, pro-ser and pro-phe, but inhibited that against pro-ala, pro-val, pro-met and pro-asp. However, prolinase activity against these iminodipeptides was enhanced by pre-incubation with glycine, independent of MnCl2. The same studies on erythrocytes from a prolidase-deficient patient showed almost the same results as the normal control, except that prolinase activity against pro-gly and pro-ser was slightly inhibited by adding 0.1 mM MnCl2. Some amino acids, glutamic acid and glutamine, slightly enhanced prolinase activity against progly in erythrocytes from both the normal control and the prolidase-deficient patient, but N-acetyl-L-glutamic acid, γ-aminobutyric acid (GABA) and β-alanine showed no effect. Branched amino acids, L-valine, L-leucine and L-isoleucine strongly inhibited the prolinase activity against pro-gly. However, conversely, their isomers, D-valine, D-leucine and D-isoleucine, enhanced it.

The kinetics of prolinase activity in the erythrocytes from both the normal individual and the prolidase-deficient patient were also studied. Their Km values were changed by adding glycine or 0.1 mM MnCl2, but Vmax values were almost the same.

References

1 Goodman SI, Solomons CC, Muschenheim F, McIntyre CA, Miles B, O’Brien D. A syndrome resembling lathyrism associated with iminodipeptiduria. Am J Med 1968; 45:152–9.10.1016/0002-9343(68)90016-8Search in Google Scholar

2 Powell GF, Rasco MA, Maniscalco RM. A prolidase deficiency in man with iminopeptiduria. Metabolism 1974; 23:505–13.10.1016/0026-0495(74)90078-XSearch in Google Scholar

3 Kodama H, Umemura S, Shimomura M, Mizuhara S, Arata J, Yamamoto Y, et al. Studies on a patient with iminopeptiduria. I. Identification of urinary iminopeptides. Physiol Chem Phys 1976; 8:463–73.Search in Google Scholar

4 Umemura S. Studies on a patient with iminodipeptiduria. II. Lack of prolidase activity in blood cells. Physiol Chem Phys 1978; 10:279–83.Search in Google Scholar

5 Arata J, Umemura S, Yamamoto Y, Hagiyama M, Nohara N. Prolidase deficiency: its dermatological manifestations and some additional biochemical studies. Arch Dermatol 1979; 115:62–7.10.1001/archderm.1979.04010010034010Search in Google Scholar

6 Butterworth J, Priestman DA. Substrate specificity of manganese-activated prolidase in control and prolidase-deficient cultured skin fibroblasts. J Inherit Metab Dis 1984; 7:32–4.10.1007/BF01805618Search in Google Scholar

7 Priestman DA, Butterworth J. Prolidase deficiency: characteristics of human skin fibroblast prolidase using colorimetric and fluorimetric assays. Clin Chim Acta 1984; 142:263–71.10.1016/0009-8981(84)90385-1Search in Google Scholar

8 Butterworth J, Priestman DA. Presence in human cells and tissues of two prolidases and their alteration in prolidase deficiency. J Inherit Metab Dis 1985; 8:193–7.10.1007/BF01805434Search in Google Scholar

9 Kodama H, Ohhashi T, Ohba C, Ohno T, Arata J, Kubonishi I, Miyoshi I. Characteristics and partial purification of prolidase and prolinase from leukocytes of a normal human and a patient with prolidase deficiency. Clin Chim Acta 1989; 180:65–72.10.1016/0009-8981(89)90297-0Search in Google Scholar

10 Ohhashi T, Ohno T, Arata J, Kodama H. Characteristics of partially purified prolidase from erythrocytes of normal individuals, of two patients with prolidase deficiency, and of the patient’s mother. J Clin Biochem Nutr 1988; 5:183–92.10.3164/jcbn.5.183Search in Google Scholar

11 Butterworth J, Priestman DA. Fluorimetric assay for prolinase and partial characterisation in cultured skin fibroblasts. Clin Chim Acta 1982; 122:51–60.10.1016/0009-8981(82)90094-8Search in Google Scholar

12 Chinard FP. Photometric estimation of proline and ornithine. J Biol Chem 1952; 199:91–5.10.1016/S0021-9258(18)44814-4Search in Google Scholar

13 Lineweaver H, Burk D. The determination of enzyme dissociation constants. J Am Chem Soc 1934; 56:658–66.10.1021/ja01318a036Search in Google Scholar

14 Lowry OH, Rosebrough NJ, Farr AL, Randall RJ. Protein measurement with the Folin phenol reagent. J Biol Chem 1951; 193:265–75.10.1016/S0021-9258(19)52451-6Search in Google Scholar

15 Jackson SH, Dennis AW, Greenberg M. Iminodipeptiduria: a genetic defect in recycling collagen; a method for determining prolidase in erythrocytes. Can Med Assoc J 1975; 113:759, 762–3.Search in Google Scholar

16 Pedersen PS, Christensen E, Brandt NJ. Prolidase deficiency. Acta Paediatr Scand 1983; 72:785–8.10.1111/j.1651-2227.1983.tb09815.xSearch in Google Scholar

17 Arata J, Hatakenaka K, Oono T. Effect of topical application of glycine and proline on recalcitrant leg ulcers of prolidase deficiency. Arch Dermatol 1986; 122:626–7.10.1001/archderm.1986.01660180026006Search in Google Scholar

18 Zhang J, Sugahara K, Yasuda K, Kodama H, Sagara Y, Kodama H. The effect of serum iminodipeptides and prednisolone on superoxide generation and tyrosyl phosphorylation of proteins in neutrophils from a patient with prolidase deficiency. Free Radic Biol Med 1998; 24:689–98.10.1016/S0891-5849(97)00361-4Search in Google Scholar

19 Nakayama K, Awata S, Zhang J, Kaba H, Manabe M, Kodama H. Characteristics of prolidase from the erythrocytes of normal humans and patients with prolidase deficiency and their mother. Clin Chem Lab Med 2003; 41:1323–8.10.1515/CCLM.2003.202Search in Google Scholar PubMed

Received: 2004-4-21
Accepted: 2004-8-20
Published Online: 2005-6-1
Published in Print: 2004-10-1

© Walter de Gruyter

Downloaded on 30.5.2024 from https://www.degruyter.com/document/doi/10.1515/CCLM.2004.227/html
Scroll to top button