Prolidase deficiency with imidodipeptiduria. A familial case with and without clinical symptoms

Isemura, Mamoru; Hanyu, Takaaki; Gejyo, Fumitake; Nakazawa, R.; Igarashi, R; Matsuo, Shigetoshi; Ikeda, K; Sato, Yoshinobu

doi:10.1016/0009-8981(79)90291-2

Cited by 70 publications

(48 citation statements)

References 13 publications

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“…More than 20 cases of prolidase deficiency have been reported, and some of the patients had no clinical symptoms of the disease (2,3). The symptoms do not seem to be related to severities produced by the enzyme defect, as deduced from individual case reports.…”

Section: Introductionmentioning

confidence: 98%

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Biochemical basis of prolidase deficiency. Polypeptide and RNA phenotypes and the relation to clinical phenotypes.

Endo¹,

Tanoue²,

Kitano³

et al. 1990

J. Clin. Invest.

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Cultured skin fibroblasts or lymphoblastoid cells from eight patients with clinical symptoms of prolidase deficiency were analyzed in terms of enzyme activity, presence of material crossreacting with specific antibodies, biosynthesis of the polypeptide, and mRNA corresponding to the enzyme. There are at least two enzymes that hydrolyze imidodipeptides in these cells and these two enzymes could be separated by an immunochemical procedure. The specific assay for prolidase showed that the enzyme activity was virtually absent in six cell strains and was markedly reduced in two (< 3% of controls). The activities of the labile enzyme that did not immunoprecipitate with the anti-prolidase antibody were decreased in the cells (30-60% of controls).Cell strains with residual activities of prolidase had immunological polypeptides crossreacting with a Mr 56,000, similar to findings in the normal enzyme. The polypeptide biosynthesis in these cells and the controls was similar. Northern blot analyses revealed the presence of mRNA in the polypeptide-positive cells, yet it was absent in the polypeptide-negative cells. The substrate specificities analyzed in the partially purified enzymes from the polypeptide-positive cell strains differed, presumably due to different mutations. Thus, there seems to be a molecular heterogeneity in prolidase deficiency.There was no apparent relation between the clinical symptoms and the biochemical phenotypes, except that mental retardation was present in the polypeptide-negative patients. The activities of the labile enzyme may not be a major factor in modifying the clinical symptoms. (J. Clin. Invest. 1990.

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Section: Introductionmentioning

confidence: 98%

“…The DNA probe was radiolabeled as described (10). [a-32P]CTP (3,000 Ci/mmol) and [35S]methionine (1,100 Ci/mmol) were purchased from ICN radiochemicals (Irvine, CA). Nitrocellulose membranes were obtained from Schleicher and Schuell (Dassel, FRG).…”

Section: Introductionmentioning

confidence: 99%

Biochemical basis of prolidase deficiency. Polypeptide and RNA phenotypes and the relation to clinical phenotypes.

Endo¹,

Tanoue²,

Kitano³

et al. 1990

J. Clin. Invest.

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“…The most abundant of these urinary iminodipeptides is glycylproline (1). Some asymptomatic individuals have been detected by neonatal screening programs (2), and by investigation of sibs of clinically affected probands (3,4).…”

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confidence: 99%

“…Although failure to recover the proline from iminodipeptides may play a role in the pathogenesis of prolidase deficiency it cannot account for all the symptomology. Numerous reports (3,(6)(7)(8) document the failure of oral administration of L-proline to relieve the dermatological lesions associated with prolidase deficiency.…”

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confidence: 99%

In Situ Activation of Human Erythrocyte Prolidase: Potential for Enzyme Replacement Therapy in Prolidase Deficiency

et al. 1988

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“…However, the relationship between phenotype and genotype is not clear. Patients with mental retardation lack expression of transcripts of the PEPD gene (Endo et al 1990), but discrepancies in clinical symptoms between siblings with the same mutation have been pointed out (Isemura M. et al 1979;Tanoue et al 1991). This suggests that additional factors not related to the mutation may modify the expression of the disorder.…”

Section: Introductionmentioning

confidence: 99%

A novel nonsense mutation of the PEPD gene in a Japanese patient with prolidase deficiency

Kikuchi¹,

Tanoue²,

Endo

et al. 2000

J Hum Genet

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Prolidase deficiency with imidodipeptiduria. A familial case with and without clinical symptoms

Cited by 70 publications

References 13 publications

Biochemical basis of prolidase deficiency. Polypeptide and RNA phenotypes and the relation to clinical phenotypes.

Biochemical basis of prolidase deficiency. Polypeptide and RNA phenotypes and the relation to clinical phenotypes.

In Situ Activation of Human Erythrocyte Prolidase: Potential for Enzyme Replacement Therapy in Prolidase Deficiency

A novel nonsense mutation of the PEPD gene in a Japanese patient with prolidase deficiency

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