Differential regulation of the expression of nucleotide pyrophosphatases/phosphodiesterases in rat liver

Stefan, C; Gijsbers, Rik; Stalmans, Willy

doi:10.1016/s0167-4889(99)00031-2

Cited by 47 publications

(32 citation statements)

References 30 publications

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“…Their cell and tissue-specific expression can vary between rodents and humans [312]. NPP1-NPP3 can be co-expressed in the same tissue and even by the same cell, as for example in cultured hepatocytes [313] or osteoblasts [314]. Similar to APs, they are often expressed on epithelial surfaces.…”

Section: General Properties and Functional Rolementioning

confidence: 99%

“…Similar to APs, they are often expressed on epithelial surfaces. This includes airway epithelia [315], the lung [313], liver epithelia, kidney epithelia [316], and intestinal epithelia [317]. Thiamine pyrophosphate, a likely substrate of E-NPPs, has been used early on as a substrate for the enzyme histochemical detection of microglia and blood vessels of the brain [318,319].…”

Section: General Properties and Functional Rolementioning

confidence: 99%

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Cellular function and molecular structure of ecto-nucleotidases

Zimmermann

Zebisch

Sträter

2012

Purinergic Signalling

878

922

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Ecto-nucleotidases play a pivotal role in purinergic signal transmission. They hydrolyze extracellular nucleotides and thus can control their availability at purinergic P2 receptors. They generate extracellular nucleosides for cellular reuptake and salvage via nucleoside transporters of the plasma membrane. The extracellular adenosine formed acts as an agonist of purinergic P1 receptors. They also can produce and hydrolyze extracellular inorganic pyrophosphate that is of major relevance in the control of bone mineralization. This review discusses and compares four major groups of ectonucleotidases: the ecto-nucleoside triphosphate diphosphohydrolases, ecto-5′-nucleotidase, ecto-nucleotide pyrophosphatase/phosphodiesterases, and alkaline phosphatases. Only recently and based on crystal structures, detailed information regarding the spatial structures and catalytic mechanisms has become available for members of these four ecto-nucleotidase families. This permits detailed predictions of their catalytic mechanisms and a comparison between the individual enzyme groups. The review focuses on the principal biochemical, cell biological, catalytic, and structural properties of the enzymes and provides brief reference to tissue distribution, and physiological and pathophysiological functions.

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Section: General Properties and Functional Rolementioning

confidence: 99%

Section: General Properties and Functional Rolementioning

confidence: 99%

Cellular function and molecular structure of ecto-nucleotidases

Zimmermann

Zebisch

Sträter

2012

Purinergic Signalling

878

922

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“…We identi®ed and cloned a potent cytokine, autotaxin (ATX), that stimulates in vitro migration of the human melanoma producer cell line, A2058, at sub-nanomolar levels (Murata et al, 1994). DNA sequence analysis determined that ATX was homologous to a family of exo/ecto nucleotide-pyrophosphatase phosphodiesterases (NPPs) that includes the B cell activation marker, PC-1, and the neural di erentiation antigen, B10 (Stefan et al, 1999). Like other members of the NPP family, ATX has multiple enzymatic activities .…”

Section: Introductionmentioning

confidence: 99%

Autotaxin (ATX), a potent tumor motogen, augments invasive and metastatic potential of ras-transformed cells

et al. 2000

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Autotaxin (ATX), an exo-nucleotide pyrophosphatase and phosphodiesterase, was originally isolated as a potent stimulator of tumor cell motility. In order to study whether ATX expression a ects motility-dependent processes such as invasion and metastasis, we stably transfected full-length ATX cDNA into two nonexpressing cell lines, parental and ras-transformed NIH3T3 (clone7) cells. The e ect of ATX secretion on in vitro cell motility was variable. The ras-transformed, ATX-secreting subclones had enhanced motility to ATX as chemoattractant, but there was little di erence in the motility responses of NIH3T3 cells transfected with atx, an inactive mutant gene, or empty vector. In Matrigel TM invasion assays, all subclones, which secreted enzymatically active ATX, demonstrated greater spontaneous and ATX-stimulated invasion than appropriate controls. This di erence in invasiveness was not caused by di erences in gelatinase production, which was constant within each group of transfectants. In vivo studies with athymic nude mice demonstrated that injection of atx-transfected NIH3T3 cells resulted in a weak tumorigenic capacity with few experimental metastases. Combination of ATX expression with ras transformation produced cells with greatly ampli®ed tumorigenesis and metastatic potential compared to ras-transformed controls. Thus, ATX appears to augment cellular characteristics necessary for tumor aggressiveness.

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“…Michaelis constant (K M ) and V max calculated from the Eadie-Hofstee plot with p-Nph-5′-TMP as substrate demonstrated values that are in accordance with previous studies related to E-NPPs 26,29,32 . E-NPP expression in cardiac tissue has already been demonstrated in some works 31,33 . However, subcellular distribution and the exact participation of this enzyme activity on nucleotide hydrolysis are poorly understood.…”

Section: Discussionmentioning

confidence: 78%