Proline at the second position of the N-terminus of biologically active peptides involved in cell growth regulation is an evolutionarily conserved motif protecting them against cleavage by non-specific proteases. Just a small number of proline-specific hydrolases including dipeptidyl peptidase IV (DPP-IV) and related molecules is capable of cleaving such post-prolyl bond. DPP-IV, originally described on the basis of its enzymatic activity, is a ubiquitous, multifunctional homodimeric plasma membrane glycoprotein of type II. Subsequently, several other molecules related to DPP-IV by their enzymatic activity and/or sequence were discovered and classified as "dipeptidyl peptidase IV activity and/or structure homologues" (DASH). Along with canonical DPP-IV this group comprises DPP-IVbeta, DPP-II, DPP6, DPP8, DPP9, DPP10 and fibroblast activation protein alpha (FAP-alpha). Recent observations of deregulated expression of several DASH molecules in multiple human cancers led to the assumptions of their pathogenetic relevance in cancerogenesis. Here we review recent information about selected DASH molecules in human malignancies.

• MeSH
• dipeptidylpeptidasa 4 chemie   metabolismus   MeSH
• dipeptidylpeptidasy a tripeptidylpeptidasy metabolismus   MeSH
• endopeptidasy MeSH
• lidé MeSH
• membránové proteiny metabolismus   MeSH
• nádory enzymologie   metabolismus   MeSH
• regulace genové exprese u nádorů * MeSH
• serinové endopeptidasy metabolismus   MeSH
• želatinasy metabolismus   MeSH
• Check Tag
• lidé MeSH
• Publikační typ
• časopisecké články MeSH
• práce podpořená grantem MeSH
• přehledy MeSH
• Názvy látek
• dipeptidylpeptidasa 4 MeSH
• dipeptidylpeptidasy a tripeptidylpeptidasy MeSH
• endopeptidasy MeSH
• fibroblast activation protein alpha MeSH Prohlížeč
• membránové proteiny MeSH
• serinové endopeptidasy MeSH
• želatinasy MeSH

In human lymphocytes three dipeptidyl peptidases were discovered in our laboratory. For a correct demonstration of activities of these enzymes discriminating substrates must be used. Dipeptidyl peptidase IV (DPP IV) is revealed with Gly-Pro-4-methoxy-2-naphthylamide (Gly-Pro-MNA) and Fast Blue B (FBB). It is present in the surface membrane of about 40% lymphocytes of the peripheral blood. Only T-lymphocytes bear the reaction. Reacting lymphocytes belong predominantly to OKT4+ subset. Some OKT8+ lymphocytes also react. With more sensitive substrates (Lys-Pro-MNA, Phe-Pro-MNA and Ala-Pro-MNA) a co-reaction of DPP II was demonstrated "in situ" and in zymograms. In haemoblastoses a positive reaction in cells indicates their derivation from the T-lineage of lymphocytes. A negative reaction does not exclude a T-cell malignancy, however. A decreased number of DPP IV positive lymphocytes in the peripheral blood indicates a diminished immunocompetent potential of T-cells, e.g. immunodeficiency in patients with malignant lymphoma, gastric and colocrectal carcinoma, AIDS, etc. DPP II demonstrated with Lys-Ala-MNA occurs in about 60% of lymphocytes belonging to T and B subsets. It is localized in lysosomes. Although Lys-Pro-MNA is a more sensitive substrate a co-reaction of DPP IV must always be considered. Patients with chronic B-lymphocytic leukaemia displaying a high number of DPP II+ cells usually have a worse prognosis. DPP I assessed with Gly-Pro-MNA and nitrosalicylaldehyde occurs in about 20% of T and B lymphocytes. The number of positively reacting cells increases after corticosteroid therapy. The influence of the treatment on the activity can be shown very well in histograms of DPP I activity measured by computer-assisted microfluorometry.

• MeSH
• dipeptidylpeptidasa 4 MeSH
• dipeptidylpeptidasy a tripeptidylpeptidasy analýza   MeSH
• fluorescenční protilátková technika MeSH
• histocytochemie MeSH
• isoelektrická fokusace MeSH
• kathepsin C MeSH
• klinické enzymatické testy MeSH
• lidé MeSH
• lymfocyty enzymologie   ultrastruktura   MeSH
• Check Tag
• lidé MeSH
• Publikační typ
• časopisecké články MeSH
• Názvy látek
• dipeptidyl peptidase II MeSH Prohlížeč
• dipeptidylpeptidasa 4 MeSH
• dipeptidylpeptidasy a tripeptidylpeptidasy MeSH
• kathepsin C MeSH

In the present work we studied the levels of activities of dipeptidyl-peptidase I (or cathepsin C, DPP-I) and dipeptidyl-peptidase II (DPP-II) and examined their isoelectric focusing profiles in matched pairs of human squamous cell lung carcinoma (SQCLC) and the lung from surgically treated patients (n = 33). The mean specific activities of DPP-I and DPP-II were higher in SQCLC (Stages I and II) than in the lung, but only the activity of DPP-II in Stage I SQCLC was significantly higher compared to the lung. The activities of both enzymes were higher in the tumor than in the lung in 10 of 20 Stage I SQCLC patients, but only in 3 of 13 Stage II SQCLC patients. The specific activities of DPP-I and DPP-II in the lungs showed a good correlation while the correlation of both enzyme activities in SQCLCs was poor. We observed only a small and mutually comparable activation of DPP-I in extracts from SQCLCs and from the lungs by dithiothreitol. The isoelectric focusing profile of several DPP-II forms in SQCLCs and the lungs was similar and the single major DPP-II isoform revealed in the tumors and lungs showed a pIapp of 5.3-5.2. The isoelectric focusing profile of DPP-I showed multiple enzyme forms in SQCLCs (pIapp 6.3-4.5) as well as in the lungs (pIapp 6.4-4.8). In SQCLCs, as well as in the lungs, the activities of the DPP-I forms with pIapp values < or = 5.6 were shifted by neuraminidase treatment to the site of the major DPP-I isoform with pIapp of about 6.0 and the zymograms then showed an another DPP-I with pIapp of 5.7, which was less discernible in the lung. In some patients, the DPP-I forms with pIapp values < or = 5.6 from SQCLC retained a greater percentage of activity distribution than did the DPP-I pIapp-counterparts from the lung.

• MeSH
• dipeptidylpeptidasy a tripeptidylpeptidasy metabolismus   MeSH
• dospělí MeSH
• isoelektrická fokusace MeSH
• kathepsin C MeSH
• lidé středního věku MeSH
• lidé MeSH
• nádory plic enzymologie   patologie   chirurgie   MeSH
• plíce enzymologie   MeSH
• senioři MeSH
• spinocelulární karcinom enzymologie   patologie   chirurgie   MeSH
• staging nádorů MeSH
• Check Tag
• dospělí MeSH
• lidé středního věku MeSH
• lidé MeSH
• senioři MeSH
• Publikační typ
• časopisecké články MeSH
• práce podpořená grantem MeSH
• Názvy látek
• dipeptidyl peptidase II MeSH Prohlížeč
• dipeptidylpeptidasy a tripeptidylpeptidasy MeSH
• kathepsin C MeSH

Post-translational modification of proteins is an important regulatory event. Numerous biologically active peptides that play an essential role in cancerogenesis contain an evolutionary conserved proline residue as a proteolytic-processing regulatory element. Proline-specific proteases could therefore be viewed as important "check-points". Limited proteolysis of such peptides may lead to quantitative but, importantly, due to the change of receptor preference, also qualitative changes of their signaling potential. Dipeptidyl peptidase-IV (DPP-IV, EC 3.4.14.5, identical with CD26) was for many years believed to be a unique cell membrane protease cleaving X-Pro dipeptides from the N-terminal end of peptides and proteins. Subsequently, a number of other molecules were discovered, exhibiting various degree of structural homology and DPP-IV-like enzyme activity, capable of cleaving similar set of substrates. These comprise for example, seprase, fibroblast activation protein alpha, DPP6, DPP8, DPP9, attractin, N-acetylated-alpha-linked-acidic dipeptidases I, II and L, quiescent cell proline dipeptidase, thymus-specific serine protease and DPP IV-beta. It is tempting to speculate their potential participation on DPP-IV biological function(s). Disrupted expression and enzymatic activity of "DPP-IV activity and/or structure homologues" (DASH) might corrupt the message carried by their substrates, promoting abnormal cell behavior. Consequently, modulation of particular enzyme activity using e.g. DASH inhibitors, specific antibodies or DASH expression modification may be an attractive therapeutic concept in cancer treatment. This review summarizes recent information on the interactions between DASH members and their substrates with respect to their possible role in cancer biology.

• MeSH
• dipeptidylpeptidasa 4 chemie   imunologie   metabolismus   MeSH
• lidé MeSH
• nádory metabolismus   MeSH
• peptidy metabolismus   MeSH
• strukturní homologie proteinů MeSH
• substrátová specifita MeSH
• zvířata MeSH
• Check Tag
• lidé MeSH
• zvířata MeSH
• Publikační typ
• časopisecké články MeSH
• práce podpořená grantem MeSH
• přehledy MeSH
• Názvy látek
• dipeptidylpeptidasa 4 MeSH
• peptidy MeSH

Meningiomas are tumors derived from arachnoid cap cells that represent approximately 30% of all intracranial tumors. In this study, we investigated 22 human meningiomas for the expression of dipeptidyl peptidase (DPP)-IV activity and/or structure homologs (DASH), including canonical DPP-IV/CD26, fibroblast activation protein-alpha (FAPalpha), DPP8 and DPP9. DPP-IV-like enzymatic activity, including all enzymatically-active DASH molecules, was found in all 18 benign meningiomas WHO grade I and IV atypical meningiomas WHO grade II by continuous rate fluorimetric assay in tissue homogenates and catalytic enzyme histochemistry in situ. In atypical meningiomas, this activity was significantly higher and was associated with higher cell proliferation as detected by Ki67 antigen immunohistochemistry. The expression of DPP-IV/CD26 and FAPalpha demonstrated by real-time RT-PCR and immunohistochemistry was low. As shown histochemically, it occurred most often on the surface of fibrous bundles and whorls rich in extracellular matrix. Compared to DPP-IV/CD26 and FAPalpha, the expression of DPP8 and DPP9 was higher and, in addition, it was present also in the cells inside these structures. Expression of CXCR4, the receptor of pro-proliferative chemokine stromal cell-derived factor-1alpha (SDF-1alpha), DPP-IV substrate, was found in all tumors, suggesting higher values in atypical grade II samples. This is the first report on the expression status of dipeptidyl peptidase-IV and related molecules in meningiomas. It shows that DPP8 and DPP9 prevail over canonical DPP-IV/CD26 and FAPalpha in all examined patients. In addition, the study suggests an increase of DPP-IV-like enzymatic activity in these tumors of WHO grade II.

• MeSH
• dipeptidasy genetika   metabolismus   MeSH
• dipeptidylpeptidasa 4 genetika   metabolismus   MeSH
• dipeptidylpeptidasy a tripeptidylpeptidasy genetika   metabolismus   MeSH
• dospělí MeSH
• endopeptidasy MeSH
• exprese genu MeSH
• imunohistochemie MeSH
• izoenzymy genetika   metabolismus   MeSH
• lidé středního věku MeSH
• lidé MeSH
• membránové proteiny genetika   metabolismus   MeSH
• meningeální nádory enzymologie   genetika   patologie   MeSH
• meningeom enzymologie   genetika   patologie   MeSH
• messenger RNA analýza   MeSH
• nádorové biomarkery analýza   MeSH
• polymerázová řetězová reakce s reverzní transkripcí MeSH
• senioři MeSH
• serinové endopeptidasy genetika   metabolismus   MeSH
• stanovení celkové genové exprese MeSH
• želatinasy genetika   metabolismus   MeSH
• Check Tag
• dospělí MeSH
• lidé středního věku MeSH
• lidé MeSH
• mužské pohlaví MeSH
• senioři MeSH
• ženské pohlaví MeSH
• Publikační typ
• časopisecké články MeSH
• práce podpořená grantem MeSH
• Názvy látek
• dipeptidasy MeSH
• dipeptidylpeptidasa 4 MeSH
• dipeptidylpeptidasy a tripeptidylpeptidasy MeSH
• DPP8 protein, human MeSH Prohlížeč
• DPP9 protein, human MeSH Prohlížeč
• endopeptidasy MeSH
• fibroblast activation protein alpha MeSH Prohlížeč
• izoenzymy MeSH
• membránové proteiny MeSH
• messenger RNA MeSH
• nádorové biomarkery MeSH
• serinové endopeptidasy MeSH
• želatinasy MeSH

Dipeptidyl peptidase-IV (DPP-IV) represents a unique proteolytic activity cleaving N-terminal X-Pro dipeptides. In addition to canonical DPP-IV/CD26, a number of other molecules have been discovered which exhibit DPP-IV-like enzymatic activity and various degree of structural similarity. These comprise enzymatically active fibroblast activation protein-alpha, DPP-II, DPP8, DPP9 and enzymatically inactive DPP6 and DPP10 that have been grouped as "DPP-IV activity and/or structure homologues" (DASH). Because the enzymatically active DASH can share similar sets of biologically active substrates and are frequently coexpressed within single cell or on tissue level, it is tempting to consider their participation on biological function(s) previously attributed to DPP-IV/CD26. It is speculated that disrupted expression and enzymatic activity of some DASH might corrupt the message carried by their substrates, with consequent promotion of abnormal cell behavior. Thus, modulation of activity of a particular enzyme using e.g. inhibitors, specific antibodies or modifying its expression may be an attractive therapeutic concept in cancer treatment. This review summarizes current knowledge of the expression and possible function of DPP-IV enzymatic activity bearing molecules in human brain tumors.

• MeSH
• biologické modely MeSH
• buněčná diferenciace MeSH
• chemokin CXCL12 metabolismus   MeSH
• chemokiny metabolismus   MeSH
• dipeptidylpeptidasa 4 metabolismus   MeSH
• glioblastom metabolismus   MeSH
• gliom enzymologie   metabolismus   MeSH
• lidé MeSH
• mozek metabolismus   MeSH
• nádory mozku enzymologie   metabolismus   MeSH
• proteasy metabolismus   MeSH
• receptory CXCR4 metabolismus   MeSH
• regulace genové exprese enzymů MeSH
• regulace genové exprese u nádorů MeSH
• Check Tag
• lidé MeSH
• Publikační typ
• časopisecké články MeSH
• práce podpořená grantem MeSH
• přehledy MeSH
• Názvy látek
• chemokin CXCL12 MeSH
• chemokiny MeSH
• dipeptidylpeptidasa 4 MeSH
• proteasy MeSH
• receptory CXCR4 MeSH

AIM: To assess intraindividually the effects of DPP-IV inhibition on the subpopulations of immune cells in type 2 diabetes mellitus (DM2) patients during the course of treatment with sitagliptin. METHODS: In this open label non-randomized observational study with a control group DM2 patients were examined before the initiation of the DPP-IV inhibitor administration (sitagliptin 100mg once daily) and then after 4weeks and 12months. Inhibition of the blood plasma DPP-IV enzymatic activity was determined by a chromogenic assay, the immunophenotyping of the blood cell subpopulations was performed using flow cytometry and blood plasma cytokine concentrations were quantified using an array-based multiplex ELISA. All parameters were evaluated in relation to the entry values in individual patients. RESULTS: The blood plasma DPP-IV enzymatic activity was effectively inhibited during the sitagliptin treatment. A significant decrease of the proportion of Treg cells (to 86±31% (median±SD) of entry values, p=0.001) and an increase of Th1 cells (to 120±103% (median±SD) of entry values, p=0.004) were observed after 4weeks but not after one year of the sitagliptin treatment. No changes were observed in the ratio of CD4(+)/CD8(+) cells, in the quantity of NK and Th2 cells and blood plasma cytokine levels. CONCLUSIONS: Sitagliptin treatment may cause temporary changes of the proportion of lymphocyte subpopulations in patients with DM2. The consequent deregulation of the immune system should be considered as a possible cause of the eventual side effects of long term DPP-IV inhibition.

• Klíčová slova
• Diabetes mellitus type 2, Dipeptidyl peptidase 4 inhibition, Gliptins, Immune cells,
• MeSH
• diabetes mellitus 2. typu krev   farmakoterapie   imunologie   MeSH
• dospělí MeSH
• inhibitory dipeptidylpeptidasy 4 aplikace a dávkování   MeSH
• lidé MeSH
• počet lymfocytů MeSH
• regulační T-lymfocyty účinky léků   imunologie   MeSH
• sitagliptin fosfát aplikace a dávkování   MeSH
• Th1 buňky účinky léků   imunologie   MeSH
• výsledek terapie MeSH
• Check Tag
• dospělí MeSH
• lidé MeSH
• mužské pohlaví MeSH
• ženské pohlaví MeSH
• Publikační typ
• časopisecké články MeSH
• pozorovací studie MeSH
• Názvy látek
• inhibitory dipeptidylpeptidasy 4 MeSH
• sitagliptin fosfát MeSH

BACKGROUND/OBJECTIVES: Pancreatic ductal adenocarcinoma (PDAC) is frequently heralded by an impairment of glucose homeostasis. Dipeptidyl peptidase-IV (DPP-IV) and fibroblast activation protein alpha (FAP) are aminopeptidases that regulate several bioactive peptides involved in glucoregulation, and are frequently dysregulated in cancer. The present study analyzes blood plasma levels and the quantity and localization of DPP-IV and FAP in PDAC tissues. METHODS: DPP-IV and FAP concentration and enzymatic activity were evaluated in the plasma from 93 PDAC, 39 type 2 diabetes mellitus (T2DM) and 29 control subjects, and in matched paired non-tumorous and tumor tissues from 48 PDAC patients. The localization of DPP-IV and FAP was determined using immunohistochemistry and catalytic histochemistry. RESULTS: The enzymatic activity and concentration of DPP-IV was higher in PDAC tumor tissues compared to non-tumorous pancreas. DPP-IV was expressed in cancer cells and in the fibrotic stroma by activated (myo)fibroblasts including DPP-IV(+)FAP(+) cells. FAP was expressed in stromal cells and in some cancer cells and its expression was increased in the tumors. Plasmatic DPP-IV enzymatic activity, and in particular the ratio between DPP-IV enzymatic activity and concentration in PDAC with recent onset DM was higher compared to T2DM. In contrast, the plasmatic FAP enzymatic activity was lower in PDAC compared to T2DM and controls and rose after tumor removal. CONCLUSIONS: DPP-IV-like enzymatic activity is upregulated in PDAC tissues. PDAC patients with recent onset diabetes or prediabetes have increased plasmatic DPP-IV enzymatic activity. These changes may contribute to the frequently observed association of PDAC and recent onset impairment of glucoregulation.

• Klíčová slova
• Diabetes mellitus, Fibroblast activation protein alpha, Peptide hydrolases, Plasma, Stromal cells,
• MeSH
• adenokarcinom enzymologie   MeSH
• buňky stromatu enzymologie   MeSH
• diabetes mellitus 2. typu enzymologie   MeSH
• dipeptidylpeptidasa 4 krev   metabolismus   MeSH
• dospělí MeSH
• duktální karcinom pankreatu enzymologie   MeSH
• endopeptidasy MeSH
• fibróza MeSH
• lidé středního věku MeSH
• lidé MeSH
• membránové proteiny metabolismus   MeSH
• mladý dospělý MeSH
• myofibroblasty enzymologie   MeSH
• nádory slinivky břišní enzymologie   MeSH
• pankreas enzymologie   MeSH
• senioři nad 80 let MeSH
• senioři MeSH
• serinové endopeptidasy metabolismus   MeSH
• želatinasy metabolismus   MeSH
• Check Tag
• dospělí MeSH
• lidé středního věku MeSH
• lidé MeSH
• mladý dospělý MeSH
• mužské pohlaví MeSH
• senioři nad 80 let MeSH
• senioři MeSH
• ženské pohlaví MeSH
• Publikační typ
• časopisecké články MeSH
• Názvy látek
• dipeptidylpeptidasa 4 MeSH
• DPP4 protein, human MeSH Prohlížeč
• endopeptidasy MeSH
• fibroblast activation protein alpha MeSH Prohlížeč
• membránové proteiny MeSH
• serinové endopeptidasy MeSH
• želatinasy MeSH

Alterations in dipeptidyl peptidase-IV (DPP-IV) enzymatic activity are characteristic of malignant transformation. Through its well-characterized functionality in regulating the activity of bioactive peptides by removal of the N-terminal dipeptide, DPP-IV activity may have profound effects upon metastatic potential and cell growth. Although DPP-IV/CD26 (EC 3.4.14.5) is the canonical representative of the group, a number of other proteins including DPP-7, 8, 9, and seprase/fibroblast activation protein-alpha (FAP-alpha) have been shown to have similar enzymatic activity. This study was set up to address the relative representation and enzymatic activity of plasma membrane localized DPP-IV/CD26 and FAP-alpha in human brain and astrocytic tumours. In parallel, expression of CXCR4, receptor for glioma cell growth stimulator chemokine SDF-1alpha known to be a DPP-IV substrate, was investigated. This is the first report showing that non-malignant brain tissue contains a DPP-IV-like enzymatic activity attributable mostly to DPP-8/9, while the substantial part of the activity in glioma is due to increased DPP-IV/CD26, localized in both the vascular and parenchymal compartments. DPP-IV enzymatic activity increased dramatically with tumour grade severity. A grade-related increase in CXCR4 receptor paralleled the rise in DPP-IV expression and activity. These data might support a role for DPP-IV regulation of the CXCR4-SDF-1alpha axis in glioma development.

• MeSH
• antigeny nádorové genetika   metabolismus   MeSH
• astrocytom enzymologie   genetika   patologie   MeSH
• buněčná membrána metabolismus   MeSH
• dipeptidylpeptidasa 4 genetika   metabolismus   MeSH
• dospělí MeSH
• endopeptidasy MeSH
• imunoenzymatické techniky MeSH
• lidé středního věku MeSH
• lidé MeSH
• membránové proteiny MeSH
• messenger RNA genetika   metabolismus   MeSH
• nádorové biomarkery genetika   metabolismus   MeSH
• nádorové buňky kultivované MeSH
• nádory mozku enzymologie   genetika   patologie   MeSH
• polymerázová řetězová reakce s reverzní transkripcí MeSH
• receptory CXCR4 genetika   metabolismus   MeSH
• regulace genové exprese enzymů fyziologie   MeSH
• RNA nádorová genetika   metabolismus   MeSH
• senioři MeSH
• serinové endopeptidasy genetika   metabolismus   MeSH
• želatinasy MeSH
• Check Tag
• dospělí MeSH
• lidé středního věku MeSH
• lidé MeSH
• mužské pohlaví MeSH
• senioři MeSH
• ženské pohlaví MeSH
• Publikační typ
• časopisecké články MeSH
• práce podpořená grantem MeSH
• srovnávací studie MeSH
• Názvy látek
• antigeny nádorové MeSH
• dipeptidylpeptidasa 4 MeSH
• endopeptidasy MeSH
• fibroblast activation protein alpha MeSH Prohlížeč
• membránové proteiny MeSH
• messenger RNA MeSH
• nádorové biomarkery MeSH
• receptory CXCR4 MeSH
• RNA nádorová MeSH
• serinové endopeptidasy MeSH
• želatinasy MeSH

Glutamate carboxypeptidase II (GCPII, EC 3.4.17.21) is a membrane peptidase expressed in a number of tissues such as kidney, prostate and brain. The brain form of GCPII (also known as NAALADase) cleaves N-acetyl-aspartyl glutamate to yield free glutamate. Animal model experiments show that inhibition of GCPII prevents neuronal cell death during experimental ischaemia. GCPII thus represents an important target for the treatment of neuronal damage caused by excess glutamate. In this paper we report expression of an extracellular portion of human glutamate carboxypeptidase II (amino acids 44-750) in Drosophila Schneider's cells and its purification to homogeneity. A novel assay for hydrolytic activity of recombinant human GCPII (rhGCPII), based on fluorimetric detection of released alpha-amino groups was established, and used for its enzymological characterization. rhGCPII does not show dipeptidylpeptidase IV-like activity assigned to the native form of the enzyme previously. Using a complete set of protected dipeptides, substrate specificity of rhGCPII was elucidated. In addition to the previously described substrates, four novel compounds, Ac-Glu-Met, Ac-Asp-Met and, surprisingly, Ac-Ala-Glu and Ac-Ala-Met were identified as substrates for GCPII, and their respective kinetic constants determined. The glycosylation of rhGCPII was found indispensable for the enzymatic activity.

• MeSH
• aktivace enzymů fyziologie   MeSH
• antigeny povrchové * MeSH
• dipeptidylpeptidasa 4 metabolismus   MeSH
• Drosophila MeSH
• glutamátkarboxypeptidasa II MeSH
• glykosylace MeSH
• hydrolýza MeSH
• karboxypeptidasy genetika   izolace a purifikace   metabolismus   MeSH
• koncentrace vodíkových iontů MeSH
• lidé MeSH
• mozek enzymologie   MeSH
• nádorové buňky kultivované MeSH
• peptidové fragmenty genetika   metabolismus   MeSH
• regulace genové exprese enzymů MeSH
• rekombinantní proteiny antagonisté a inhibitory   metabolismus   MeSH
• substrátová specifita MeSH
• zvířata MeSH
• Check Tag
• lidé MeSH
• zvířata MeSH
• Publikační typ
• časopisecké články MeSH
• práce podpořená grantem MeSH
• srovnávací studie MeSH
• Názvy látek
• antigeny povrchové * MeSH
• dipeptidylpeptidasa 4 MeSH
• FOLH1 protein, human MeSH Prohlížeč
• glutamátkarboxypeptidasa II MeSH
• karboxypeptidasy MeSH
• peptidové fragmenty MeSH
• rekombinantní proteiny MeSH