Biochemical and mass spectrometric characterization of soluble ecto-5'-nucleotidase from bull seminal plasma

Fini, Carlo; Talamo, Fabio; Cherri, Silvia; Coli, Marcello; Floridi, Ardesio; Ferrara, L.; Scaloni, Andrea

doi:10.1042/bj20021687

Cited by 31 publications

(21 citation statements)

References 32 publications

(36 reference statements)

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“…Forms of released eN may have different cellular origins. They can be derived by proteolytic cleavage devoid of the GPI anchor, as shown for the soluble eN in bull seminal plasma [263]. In this case, enzyme activity of the soluble and truncated eN was different from that of the GPI-anchored enzyme and AMP was not the preferred substrate.…”

Section: Soluble Formsmentioning

confidence: 88%

Cellular function and molecular structure of ecto-nucleotidases

Zimmermann

Zebisch

Sträter

2012

Purinergic Signalling

879

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: Soluble Formsmentioning

confidence: 88%

Cellular function and molecular structure of ecto-nucleotidases

Zimmermann

Zebisch

Sträter

2012

Purinergic Signalling

879

922

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“…From a structural point of view, CD73 is organized in three domains: (i) one N‐terminal domain containing metal binding sites; (ii) one C‐terminal domain containing the catalytic site; and (iii) one short alpha helix bridging the N‐ and C‐terminal domains. CD73 glycoforms with different molecular weights and enzymatic activities have been described . Functional CD73 consists of a non‐covalently linked homodimer stabilized by hydrophobic interactions between adjacent C‐terminal domains.…”

Section: Biochemistry Of Cd39 and Cd73mentioning

confidence: 99%

The ectonucleotidases CD39 and CD73: Novel checkpoint inhibitor targets

Allard

Longhi

Robson

et al. 2017

Immunological Reviews

702

610

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Summary Cancers are able to grow by subverting immune suppressive pathways, to prevent the malignant cells as being recognized as dangerous or foreign. This mechanism prevents the cancer from being eliminated by the immune system and allows disease to progress from a very early stage to a lethal state. Immunotherapies are newly developing interventions that modify the patient’s immune system to fight cancer, by either directly stimulating rejection-type processes or by blocking suppressive pathways. Extracellular adenosine generated by the ectonucleotidases CD39 and CD73 is a newly recognized “immune checkpoint mediator” that interferes with anti-tumor immune responses. In this review, we focus on CD39 and CD73 ectoenzymes and encompass aspects of the biochemistry of these molecules as well as detailing the distribution and function on immune cells. Effects of CD39 and CD73 inhibition in preclinical and clinical studies are discussed. Finally, we provide insights into potential clinical application of adenosinergic and other purinergic-targeting therapies and forecast how these might develop in combination with other anti-cancer modalities.

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“…254,255 Ecto-5′-NTs are typically bound to the outer surface of the plasma membrane with their C-terminus anchored via a glycosylphosphatidylinositol (GPI) group, but have also been isolated in soluble form. 267,268 The amino acid sequences of mammalian ecto-5′-NTs are highly conserved, with an identity of greater than 85%. 268 In bacteria, different forms of 5′-NT have also been identified.…”

mentioning

confidence: 99%