Characteristics of Partially Purified Prolidase from Erythrocytes of Normal Individuals, of Two Patients with Prolidase Deficiency, and of the Patients' Mother

Ohhashi, Toshitaka; Ohno, Takashi; Arata, Jirô; Kodama, Hiroyuki

doi:10.3164/jcbn.5.183

Cited by 10 publications

(8 citation statements)

References 11 publications

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“…However, both enzymes, prolidases I and II, showed their activity when met-pro was used as the substrate. Some researchers have reported a similar result from human cells (8,14,15).…”

Section: Resultssupporting

confidence: 66%

“…It has been reported that two forms of prolidase, prolidases I and II, were separated from leukocytes (14), erythrocytes (15) and fibroblasts (19) from normal humans. Some researchers reported that in two unrelated cases of prolidase deficiency, the activity of peak II against gly-pro in fibroblasts was remarkably reduced, but its activity against all other substrates either remained the same or was enhanced.…”

Section: Resultsmentioning

confidence: 99%

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Characteristics of Prolidase from the Erythrocytes of Normal Humans and Patients with Prolidase Deficiency and Their Mother

Nakayama¹,

Awata²,

Zhang³

et al. 2003

Clinical Chemistry and Laboratory Medicine

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Prolidases I and II were highly purified from human erythrocytes. The effects of various amino acids, MnCl2 and mercaptoethanol, on these two enzymes were investigated. Normal prolidase II was very labile in the absence of MnCl2 or mercaptoethanol. The activity of prolidase II was maintained at about 76% by pre-incubation with MnCl2; it was then activated up to 140% by treatment with mercaptoethanol for 60 minutes at 37 degrees C. Normal prolidases I and II showed the highest activity against glycylproline or methionylproline in the presence of MnCl2. The activity of prolidase I against glycylproline was enhanced strongly by glycine and MnCl2, but not activated in the absence of MnCl2. The activity of prolidase II against methionylproline was enhanced three-fold in the presence of glycine and MnCl2, but its activity against glycylproline was very low even in the presence of MnCl2. A stronger enhancement of this activity was found in normal erythrocytes, and a lower level of this activity was found in erythrocytes of patients treated with glycine, MnCl2 and mercaptoethanol compared to those treated with glycine and MnCl2. The activity of prolidase II against methionylproline in all erythrocytes, of normal humans and of patients, was strongly activated by the addition of glycine with MnCl2 but suppressed by the addition of mercaptoethanol.

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“…However, both enzymes, prolidases I and II, showed their activity when met-pro was used as the substrate. Some researchers have reported a similar result from human cells (8,14,15).…”

Section: Resultssupporting

confidence: 66%

Section: Resultsmentioning

confidence: 99%

Characteristics of Prolidase from the Erythrocytes of Normal Humans and Patients with Prolidase Deficiency and Their Mother

Nakayama¹,

Awata²,

Zhang³

et al. 2003

Clinical Chemistry and Laboratory Medicine

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“…This result coincides with those of our previous studies [15,16]. The changes of K m and V max values of PD I, PD II and the patient's prolidase by the amino acids in the presence of 1 mM MnCl 2 may be due to an allosteric effect.…”

Section: Resultssupporting

confidence: 92%

“…On the other hand, the molecular mass of the PD II subunit was 95 kDa. This value is also consistent with our previous result that the molecular mass of native PD II was estimated to be 185 kDa by gel-filtration analysis [16], thus indicating that human PD II is a homodimer enzyme with a subunit of 95 kDa.…”

Section: Resultssupporting

confidence: 91%

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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

Liu

Nakayama

Sagara

et al. 2005

Clinical Biochemistry

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Prolidase is a critical enzyme for complete gliadin digestion in Tenebrio molitor larvae

Tereshchenkova

Goptar

Zhuzhikov

et al. 2017

Arch Insect Biochem Physiol

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Prolidase is a proline-specific metallopeptidase that cleaves imidodipeptides with C-terminal Pro residue. Prolidase was purified and characterized from the Tenebrio molitor larval midgut. The enzyme was localized in the soluble fraction of posterior midgut tissues, corresponding to a predicted cytoplasmic localization of prolidase according to the structure of the mRNA transcript. Expression of genes encoding prolidase and the major digestive proline-specific peptidase (PSP)-dipeptidyl peptidase 4-were similar. The pH optimum of T. molitor prolidase was 7.5, and the enzyme was inhibited by Z-Pro, indicating that it belongs to type I prolidases. In mammals, prolidase is particularly important in the catabolism of a proline-rich protein-collagen. We propose that T. molitor larval prolidase is a critical enzyme for the final stages of digestion of dietary proline-rich gliadins, providing hydrolysis of imidodipeptides in the cytoplasm of midgut epithelial cells. We propose that the products of hydrolysis are absorbed from the luminal contents by peptide transporters, which we have annotated in the T. molitor larval gut transcriptome. The origin of prolidase substrates in the insect midgut is discussed in the context of overall success of grain feeding insects.

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Characteristics of Partially Purified Prolidase from Erythrocytes of Normal Individuals, of Two Patients with Prolidase Deficiency, and of the Patients' Mother

Cited by 10 publications

References 11 publications

Characteristics of Prolidase from the Erythrocytes of Normal Humans and Patients with Prolidase Deficiency and Their Mother

Characteristics of Prolidase from the Erythrocytes of Normal Humans and Patients with Prolidase Deficiency and Their Mother

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

Prolidase is a critical enzyme for complete gliadin digestion in Tenebrio molitor larvae

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