Disease relevance of DPP3

• The increase of the DPP III activity was observed in the endometrial carcinomas of various histological types, grade or the depth of myometrial invasion [1].
• A statistically significant higher DPP III activity was observed in endometrial (n = 40, P = 4.6 x 10(-7)) and ovarian (n = 11, P = 8.1 x 10(-4)) malignant tumours, whereas no significant difference was detected for leiomyomas (n = 8), if compared to the activity in normal tissue [1].
• RESULTS: Median DPP III activity expressed as milliunits per milligram protein was 6 in normal ovarian tissues (n = 29), 6.5 in benign ovarian tumors (n = 19), 19.5 in primary ovarian carcinomas (n = 41), 12.5 in nonepithelial primary ovarian tumors (n = 7), and 22.1 in metastatic ovarian malignancies (n = 12) [2].
• Tumor cytosol dipeptidyl peptidase III activity is increased with histological aggressiveness of ovarian primary carcinomas [2].
• Fluostatins A and B, new inhibitors of dipeptidyl peptidase III, produced by Streptomyces sp. TA-3391. I. Taxonomy of producing strain, production, isolation, physico-chemical properties and biological properties [3].

High impact information on DPP3

• A subset of cDNAs, encoding sequestosome 1 (SQSTM1) and dipeptidylpeptidase 3 (DPP3), activated the ARE in primary mouse-derived cortical neurons [4].
• A significantly lower DPP III level, determined by activity measurement and Western blotting, was found in the cytosols of highly oxygenated rat tissues.These results provide kinetic evidence that cysteine residues are involved in substrate binding of mammalian DPPs III [5].
• Physiological concentrations of biological thiols and H(2)O(2) inactivated the rat DPP III [5].
• Rat DPP III was hyperreactive to pHMB and showed biphasic kinetics indicating two classes of reactive SH-groups [5].
• Western blot analysis revealed a significantly (P = 0.014) increased level of DPP III in endometrial cancer [1].

Biological context of DPP3

• However, significant differences in the binding constants for several peptides indicated non-identity in the active site topography of human and rat erythrocyte DPP III [6].
• Assignment of the dipeptidyl peptidase III gene (DPP3) to human chromosome 11 band q12-->q13.1 by in situ hybridization [7].
• Human placental dipeptidyl aminopeptidase III: hydrolysis of enkephalins and its stimulation by cobaltous ion [8].

Anatomical context of DPP3

• A rapid assay for dipeptidyl aminopeptidase III in human erythrocytes [9].
• Identification of dipeptidyl peptidase III in human neutrophils [10].
• Thus, ArgArgNA in the human seminal plasma is hydrolysed by dipeptidyl peptidase III, which may originate from different reproductive organs, while the prostate is responsible for the secretion of an aminopeptidase with a wide substrate spectrum including dipeptidyl derivatives [11].
• To find a more effective inhibitor than spinorphin (LVVYPWT), an endogenous factor derived from bovine spinal cord, we synthesized spinorphin analogues and assayed their inhibitory activity toward DPPIII among enkephalin-degrading enzymes [12].

Associations of DPP3 with chemical compounds

• Zn2+ ions, sulfhydryl reagents, and aminopeptidase inhibitors, especially probestin, inhibited the rat DPP III more potently [6].
• Lens DPP III was inhibited by EDTA, p-chloromercuriphenyl sulfonate, puromycin and DFP [13].
• DPP III from human erythrocytes hydrolysed also tri- to decapeptides of different composition, provided they did not have proline at P1 or P'1 position [14].
• 3. Chloride activated arginine aminopeptidase, broad specificity aminopeptidase and dipeptidyl peptidase III were found in cytosols of all examined cells [15].
• Purification procedure for dipeptidyl peptidase III (DPP III) from human erythrocytes cytosol, entailing separations on DEAE-cellulose, hydroxylapatite and Sephacryl S-200 column, which gave homogeneous preparation in 35% yield, is described [14].

Other interactions of DPP3

• Dipeptidyl peptidase III and alanyl aminopeptidase in the human seminal plasma: origin and biochemical properties [11].
• Isolation, purification and characterization of a DPP-III homologue from goat brain [16].
• (b) All cytosolic proteinase and peptidase activities described previously (Pontremoli, S., Melloni, E., Salamino, F., Sapartore, B., Michetti, M., Benatti, U., Morelli, A. and De Flora, A. (1980) Eur. J. Biochem. 110, 421-430) decline exponentially throughout the erythrocyte life-span, with the exception of dipeptidyl aminopeptidase III [17].

Analytical, diagnostic and therapeutic context of DPP3

• Dipeptidyl peptidase III is a zinc metallo-exopeptidase. Molecular cloning and expression [18].

References