The dipeptidyl peptidase-IV (DPP-IV) family has outgrown its humble origins as a simple enzymatic... more The dipeptidyl peptidase-IV (DPP-IV) family has outgrown its humble origins as a simple enzymatic activity cleaving dipeptides from peptides with an accessible N-terminal penultimate proline with no clear role in metabolism. It is now understood to play a critical role in regulating signaling capacity of chemokines, neuropeptides and other extracellular messengers in addition to playing direct roles by means of non-enzymatic interactions to regulate the local extracellular proliferative environment. Consequently, examination of DPP-IV family representation and activity in immune and oncogenic processes has become a major focus. To review the evidence for DPP-IV family members as markers of malignancy. Overview of published data. The DPP-IV family, which is probably linked directly to the pathogenesis of cancer, holds significant promise for exploitation in the diagnostic arena.
Dipeptidyl peptidase-IV (DPP-IV) represents a unique proteolytic activity cleaving N-terminal X-P... more 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.
Dipeptidyl peptidase-IV (DPP-IV) and fibroblast activation protein-α (FAP) are speculated to part... more Dipeptidyl peptidase-IV (DPP-IV) and fibroblast activation protein-α (FAP) are speculated to participate in the regulation of multiple biological processes, because of their unique enzymatic activity, as well as by non-hydrolytic molecular interactions. At present, the role of DPP-IV and FAP in the development and progression of various types of tumors, including glioblastoma, is intensively studied, and their functional crosstalk is hypothesized. In this article, we describe the correlative expression of DPP-IV and FAP mRNA in primary cell cultures derived from human glioblastoma and associated expression dynamics of both molecules in astrocytoma cell lines depending on culture conditions. Although the molecular mechanisms of DPP-IV and FAP co-regulations remain unclear, uncoupled expression of transgenic DPP-IV and the endogenous FAP suggests that it occurs rather at the transcriptional than at the posttranscriptional level. Understanding of the expressional and functional coordinations of DPP-IV and FAP may help clarify the mechanisms of biological roles of both molecules in transformed astrocytic cells.
... 60 PETR BUSEK ET AL ... Chen, State University of New York, USA, for a kind gift of DPP-IV cl... more ... 60 PETR BUSEK ET AL ... Chen, State University of New York, USA, for a kind gift of DPP-IV clones, Cyril Barinka and Jan Konvalinka, Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, for the construction of the vector. REFERENCES ...
The dipeptidyl peptidase-IV (DPP-IV) family has outgrown its humble origins as a simple enzymatic... more The dipeptidyl peptidase-IV (DPP-IV) family has outgrown its humble origins as a simple enzymatic activity cleaving dipeptides from peptides with an accessible N-terminal penultimate proline with no clear role in metabolism. It is now understood to play a critical role in regulating signaling capacity of chemokines, neuropeptides and other extracellular messengers in addition to playing direct roles by means of non-enzymatic interactions to regulate the local extracellular proliferative environment. Consequently, examination of DPP-IV family representation and activity in immune and oncogenic processes has become a major focus. To review the evidence for DPP-IV family members as markers of malignancy. Overview of published data. The DPP-IV family, which is probably linked directly to the pathogenesis of cancer, holds significant promise for exploitation in the diagnostic arena.
Dipeptidyl peptidase-IV (DPP-IV) represents a unique proteolytic activity cleaving N-terminal X-P... more 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.
Dipeptidyl peptidase-IV (DPP-IV) and fibroblast activation protein-α (FAP) are speculated to part... more Dipeptidyl peptidase-IV (DPP-IV) and fibroblast activation protein-α (FAP) are speculated to participate in the regulation of multiple biological processes, because of their unique enzymatic activity, as well as by non-hydrolytic molecular interactions. At present, the role of DPP-IV and FAP in the development and progression of various types of tumors, including glioblastoma, is intensively studied, and their functional crosstalk is hypothesized. In this article, we describe the correlative expression of DPP-IV and FAP mRNA in primary cell cultures derived from human glioblastoma and associated expression dynamics of both molecules in astrocytoma cell lines depending on culture conditions. Although the molecular mechanisms of DPP-IV and FAP co-regulations remain unclear, uncoupled expression of transgenic DPP-IV and the endogenous FAP suggests that it occurs rather at the transcriptional than at the posttranscriptional level. Understanding of the expressional and functional coordinations of DPP-IV and FAP may help clarify the mechanisms of biological roles of both molecules in transformed astrocytic cells.
... 60 PETR BUSEK ET AL ... Chen, State University of New York, USA, for a kind gift of DPP-IV cl... more ... 60 PETR BUSEK ET AL ... Chen, State University of New York, USA, for a kind gift of DPP-IV clones, Cyril Barinka and Jan Konvalinka, Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, for the construction of the vector. REFERENCES ...
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