Distribution of adenosine deaminase-complexing protein in murine tissues

Dinjens, Winand N.M.; Kate, Joop ten; Wijnen, Juul T.; Linden, Edith P.M. van der; Beek, C.; Lenders, Marie-Hélène; Khan, P. Meera; Bosman, F. T.

doi:10.1016/s0021-9258(19)47289-x

Cited by 43 publications

(6 citation statements)

References 29 publications

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“…The expression of adenosine deaminase in both small and large intestine of rat and mouse has been demonstrated by immunohistochemistry, which revealed a predominant localization in the mucosal layer (Dinjens et al, 1989). The enzyme CD73 has been found in the small intestine of rat and guinea-pig as well as in rat and mouse colon (Nitahara et al, 1995;Karhausen et al, 2004;Giron et al, 2008).…”

Section: Intestinal Localization Of Adenosine Receptors Enzymes and T...mentioning

confidence: 98%

Regulation of enteric functions by adenosine: Pathophysiological and pharmacological implications

Antonioli

Fornai

Colucci

et al. 2008

Pharmacology & Therapeutics

104

121

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Section: Intestinal Localization Of Adenosine Receptors Enzymes and T...mentioning

confidence: 98%

Regulation of enteric functions by adenosine: Pathophysiological and pharmacological implications

Antonioli

Fornai

Colucci

et al. 2008

Pharmacology & Therapeutics

104

121

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“…Other means of localization could involve interactions with specific binding proteins such as the ADA complexing protein (Schrader and West, 1990) . In fact, Dinjens et al (1989) have shown that immuno-cross-reactive ADA complexing protein is precisely localized to the apical enterocyte brush border membrane in mice and humans. Interestingly, the complexing protein is also expressed in other cell types such as the proximal tubular epithelium of kidney, but the form isolated from kidney does not bind ADA, nor is ADA expressed at high level in these cells.…”

Section: Subcellular Localization Ofpurine Catabolic Enzymes In the Duodenummentioning

confidence: 99%

Coordinate developmental regulation of purine catabolic enzyme expression in gastrointestinal and postimplantation reproductive tracts.

Witte

Wiginton

Hutton

et al. 1991

The Journal of Cell Biology

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Abstract. Using histochemical detection, we have visualized in situ the complete metabolic pathway for the degradation of purine nucleotides. From the tongue to the ileum, diverse epithelial cell types lining the lumen of the mouse gastrointestinal (GI) tract strongly coexpress each of the five key purine catabolic enzymes. Dramatic increases in the expression of each enzyme occurred during postnatal maturation of the GI tract. Using in situ hybridization, an intense accumulation of adenosine deaminase (ADA) mRNA was detected only within GI epithelial cells undergoing postmitotic differentiation . In a similar manner, at the developing maternal-fetal interface, high level expression of the purine catabolic pathway also occurred in a unique subset of maternal decidual cells previously known to express high levels of alkaline phosphatase P URINE nucleotide synthesis and degradation are essential for life. Genetic defects in the purine metabolic pathway can cause devastating human disease, such as Lesch-Nyhan syndrome or severe immunodeficiency (Giblett, 1972; Camera and Carson, 1987 ;Kredich and Hershfield, 1989) . The importance of the purine pathway is also illustrated by the wide variety of potent and clinically beneficial drugs such as allopurinol, 6-mercaptopurine, methotrexate, and trimethoprim that have resulted from pharmacological targeting of purine pathway enzymes (for review, see Elion, 1989). The purine ring, large quantities of which are required for cell growth and proliferation, requires for its synthesis more than a dozen enzyme activities, a spectrum of metabolic substrates, and a substantial amount of chemical energy.Given the metabolic expense of purine biosynthesis, it might be considered surprising that mice and other mammals do not reuse dietary purine nucleotides for DNA and RNA synthesis (Sonoda and Tatibana, 1978 ;Ho et al., 1979;Savaiano et al., 1980 ;Uauy, 1989). Consistent with this, rat duodenal mucosa has long been shown to produce the nonreusable purines, uric acid and allantoin, from AMP (Getler

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“…For example, only dimeric CD26 interacts with CARMA-1 [ 5 ]. CD26/DPP4 is rather ubiquitously expressed on blood cells, fibroblasts, mesothelial, epithelial, and endothelial cells and is detected in several organs including placenta, kidney, intestine, prostate, gall bladder, pancreas, and liver [ 6 , 7 , 8 ]. In the immune system, CD26/DPP4 is expressed on dendritic cells, activated B cells, natural killer (NK) cells, T cells, and CD34 + progenitor cells (reviewed in [ 1 ]).…”

Section: Basic Features Of Cd26/dpp4mentioning

confidence: 99%

The Serine Protease CD26/DPP4 in Non-Transformed and Malignant T Cells

Chitadze

Wehkamp

Janßen

et al. 2021

Cancers

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CD26/Dipeptidylpeptidase 4 is a transmembrane serine protease that cleaves off N-terminal dipeptides. CD26/DPP4 is expressed on several immune cell types including T and NK cells, dendritic cells, and activated B cells. A catalytically active soluble form of CD26/DPP4 can be released from the plasma membrane. Given its wide array of substrates and interaction partners CD26/DPP4 has been implicated in numerous biological processes and effects can be dependent or independent of its enzymatic activity and are exerted by the transmembrane protein and/or the soluble form. CD26/DPP4 has been implicated in the modulation of T-cell activation and proliferation and CD26/DPP4-positive T cells are characterized by remarkable anti-tumor properties rendering them interesting candidates for T cell-based immunotherapies. Moreover, especially in cutaneous T-cell lymphoma CD26/DPP4 expression patterns emerged as an established marker for diagnosis and treatment monitoring. Surprisingly, besides a profound knowledge on substrates, interaction partners, and associated signal transduction pathways, the precise role of CD26/DPP4 for T cell-based immune responses is only partially understood.

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Distribution of adenosine deaminase-complexing protein in murine tissues

Cited by 43 publications

References 29 publications

Regulation of enteric functions by adenosine: Pathophysiological and pharmacological implications

Regulation of enteric functions by adenosine: Pathophysiological and pharmacological implications

Coordinate developmental regulation of purine catabolic enzyme expression in gastrointestinal and postimplantation reproductive tracts.

The Serine Protease CD26/DPP4 in Non-Transformed and Malignant T Cells

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