Soluble dipeptidyl peptidase IV from terminal differentiated rat epidermal cells: Purification and its activity on synthetic and natural peptides

Kikuchi, Mamoru; Fukuyama, Kimie; Epstein, William L.

doi:10.1016/0003-9861(88)90268-8

Cited by 30 publications

(9 citation statements)

References 31 publications

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“…Thus, barley DPP IV may be involved in this later step of storage protein mobilization, releasing dipeptides, tripeptides, and amino acids in the scutellum and/or embryo. Although the K m values for the substrates described here are in the micromolar range, short oligopeptides may have much higher K m values, as found for rat DPP IV (Kikuchi et al, 1988). The di-and tri-peptides released could then be degraded to free amino acids by aminopeptidases (Sopanen and Mikola, 1975), dipeptidases (Sopanen, 1976), and carboxypeptidases (Breddam and Sørensen, 1987), which are also present in the barley embryo (Dal Degan et al, 1994).…”

Section: Discussionmentioning

confidence: 69%

Purification and Characterization of Barley Dipeptidyl Peptidase IV

et al. 2000

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Barley (Hordeum vulgare L.) storage proteins, which have a high content of proline (Pro) and glutamine, are cleaved by cysteine endoproteases to yield peptides with a Pro next to the N-terminal and/or C-terminal amino acid residues. A peptidase cleaving after Xaa-Pro-at the N terminus of peptides was purified from green barley malt. It was identified as a serine-type dipeptidyl peptidase (DPP), based on inhibitor studies, and the nature of the cleavage product. It is a monomeric glycoprotein with an apparent molecular mass of 105 kD (85 kD after deglycosylation), with a pI of 3.55 and a pH optimum at 7.2. Substrate specificity was determined with a series of fluorogenic peptide substrates with the general formula Xaa-Pro-AMC, where Xaa is an unspecified amino acid and AMC is 7-amino-4-methylcoumarin. The best substrates were Xaa ‫؍‬ lysine and arginine, while the poorest were Xaa ‫؍‬ aspartic acid, phenylalanine, and glutamic acid. The K m values ranged from 0.071 to 8.9 M, compared with values of 9 to 130 M reported for mammalian DPP IVs. We discuss the possible role of DPP IV in the degradation of small Pro-containing peptides transported from the endosperm to the embryo of the germinating barley grain.

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Section: Discussionmentioning

confidence: 69%

Purification and Characterization of Barley Dipeptidyl Peptidase IV

et al. 2000

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“…The cutaneous recruitment of eosinophils in rats is supposed to be modulated by DPPIV, as it has been shown that DPPIV is present in rat epidermis (35). Furthermore, the capacity of human CCL11 to attract eosinophils to rat skin has been shown previously (33).…”

Section: Discussionmentioning

confidence: 97%

Inhibition of CD26/Dipeptidyl Peptidase IV Enhances CCL11/Eotaxin-Mediated Recruitment of Eosinophils In Vivo

Forssmann

Stoetzer

Stephan

et al. 2008

The Journal of Immunology

103

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Chemokines mediate the recruitment of leukocytes to the sites of inflammation. N-terminal truncation of chemokines by the protease dipeptidyl peptidase IV (DPPIV) potentially restricts their activity during inflammatory processes such as allergic reactions, but direct evidence in vivo is very rare. After demonstrating that N-terminal truncation of the chemokine CCL11/eotaxin by DPPIV results in a loss of CCR3-mediated intracellular calcium mobilization and CCR3 internalization in human eosinophils, we focused on the in vivo role of CCL11 and provide direct evidence for specific kinetic and rate-determining effects by DPPIV-like enzymatic activity on CCL11-mediated responses of eosinophils. Namely, it is demonstrated that i.v. administration of CCL11 in wild-type F344 rats leads to mobilization of eosinophils into the blood, peaking at 30 min. This mobilization is significantly increased in DPPIV-deficient F344 rats. Intradermal administration of CCL11 is followed by a dose-dependent recruitment of eosinophils into the skin and is significantly more effective in DPPIV-deficient F344 mutants as well as after pharmacological inhibition of DPPIV. Interestingly, CCL11 application leads to an up-regulation of DPPIV, which is not associated with negative feedback inhibition via DPPIV-cleaved CCL11(3–74). These findings demonstrate regulatory effects of DPPIV for the recruitment of eosinophils. Furthermore, they illustrate that inhibitors of DPPIV have the potential to interfere with chemokine-mediated effects in vivo including but not limited to allergy.

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“…Gliadin from gluten and casein from dairy products show surprisingly high substrate specificity for DPP IV when compared with other endogenous DPP IV substrates. For example, DPP IV shows higher affinity for gliadin and casein than for substance P (SP) [ 41 ] and glucagon-like peptide (GLP) [ 42 ]. Gliadin is highly specific for DPP IV [ 36 ], which is further evidenced by its binding affinity with human DPP IV.…”

Section: Gliadin Is Degraded To a Collection Of Polypeptides Called Ementioning

confidence: 99%

The opioid effects of gluten exorphins: asymptomatic celiac disease

Pruimboom

Punder

2015

J Health Popul Nutr

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Gluten-containing cereals are a main food staple present in the daily human diet, including wheat, barley, and rye. Gluten intake is associated with the development of celiac disease (CD) and related disorders such as diabetes mellitus type I, depression, and schizophrenia. However, until now, there is no consent about the possible deleterious effects of gluten intake because of often failing symptoms even in persons with proven CD. Asymptomatic CD (ACD) is present in the majority of affected patients and is characterized by the absence of classical gluten-intolerance signs, such as diarrhea, bloating, and abdominal pain. Nevertheless, these individuals very often develop diseases that can be related with gluten intake. Gluten can be degraded into several morphine-like substances, named gluten exorphins. These compounds have proven opioid effects and could mask the deleterious effects of gluten protein on gastrointestinal lining and function. Here we describe a putative mechanism, explaining how gluten could “mask” its own toxicity by exorphins that are produced through gluten protein digestion.

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Soluble dipeptidyl peptidase IV from terminal differentiated rat epidermal cells: Purification and its activity on synthetic and natural peptides

Cited by 30 publications

References 31 publications

Purification and Characterization of Barley Dipeptidyl Peptidase IV

Purification and Characterization of Barley Dipeptidyl Peptidase IV

Inhibition of CD26/Dipeptidyl Peptidase IV Enhances CCL11/Eotaxin-Mediated Recruitment of Eosinophils In Vivo

The opioid effects of gluten exorphins: asymptomatic celiac disease

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