Association of the HNK-1 epitope with 5′-nucleotidase from <i>Torpedo marmorata</i> (electric ray) electric organ

Vogel, Manfred; Kowalewski, H; Zimmermann, Herbert; Janetzko, Alfred; Margolis, Richard U.; Wollny, H E

doi:10.1042/bj2780199

Cited by 51 publications

(20 citation statements)

References 35 publications

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“…in [201,246]). In addition, in Torpedo electric organ [246] and in developing kitten visual cortex [247], the HNK-1 epitope, a sulfated, glucuronic acid-containing carbohydrate epitope, that has been found in a variety of cell adhesion molecules, has been identified. The glycosylation pattern presumably varies not only between species but also between tissues.…”

Section: Glycosylationmentioning

confidence: 99%

Cellular function and molecular structure of ecto-nucleotidases

Zimmermann

Zebisch

Sträter

2012

Purinergic Signalling

890

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: Glycosylationmentioning

confidence: 99%

Cellular function and molecular structure of ecto-nucleotidases

Zimmermann

Zebisch

Sträter

2012

Purinergic Signalling

890

922

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“…The isolation of 5'-nucleotidase from bovine adrenal medulla, rat brain and porcine brain capillaries (Weber et al, 1987) was carried out essentially by the same method, except that the detergent sulfobetain-14 (1 YO), instead of Triton X-300 ( 5 % ) and deoxycholate (2'/0), was used to solubilize the membranes. N-terminal amino acid residues from the Torpedo enzyme were determined by direct protein sequencing using automated Edman degradation (Vogel et al, 1991). Polyclonal antibodies were obtained by immunization of rabbits with the purified protein.…”

Section: Purification Of 5'-nucleotidase and Production Of Antibodiesmentioning

confidence: 99%

“…The function of ecto-5'-nucleotidase has generally been allocated to the dephosphorylation of extracellular mononucleotides. Interestingly, 5'-nucleotidase isolated from the electric ray electric organ contains the HNK-1 epitope (Vogel et al, 1991), which has been identified as glucuronyl3-sulfate. This epitope is associated with a number of surface-located membrane proteins which are involved in cell adhesion or cell recognition.…”

mentioning

confidence: 99%

“…At least two cytosolic forms have been characterized which may be differentiated on the basis of their relative preferences for AMP and IMP, their pH dependence, or by the effect of ATP on enzyme activity (Orford et al, 3 991 ;Skladanowski and Newby, 1990). The plasma-membranebound form of the enzyme is surface-located, anchored by glycosylphosphatidylinositol and can be released by treatment with phosphatidylinositol-specific phospholipase C (Misumi et al, 1990a;Vogel et al, 1991). This form is characterized by a low-K, (micromolar range) and may, on solubilization, give rise to cytosolic low-K, 5'-nucleotidase (Piec and Le Hir, 1991 (EC 3.1.3.5); phosphodiesterase (EC 3.1.4.1 j ; NAD+-glycohydrolase (EC 3.2.2.5).…”

mentioning

confidence: 99%

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5′‐Nucleotidase from the electric ray electric lobe

Volknandt

Vogel

Pevsner

et al. 1991

European Journal of Biochemistry

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A cDNA encoding a 5'-nucleotidase was identified by screening a lgtlO cDNA library from the electric lobe of Discopyge ommata using a cDNA probe containing the complete open reading frame coding for the rat liver enzyme. Nucleotide sequence analysis defines an open reading frame of 577 amino acids, corresponding to a calculated molecular mass of 63833 Da. The N-terminus of the mature protein, as determined by direct protein sequencing, is preceded by 29 amino acid residues comprising a signal peptide. The C-terminus contains a stretch of hydrophobic amino acids, considered to be cleaved on post-translational modification and exchanged for glycosylphosphatidylinositol as a membrane anchor. The predicted protein contains four potential N-linked glycosylation sites. Electric ray 5'-nucleotidase shares 61 % amino acid identity with the enzymes from rat liver and human placenta, and about 23 YO with bacterial proteins possessing 5'-nucleotidase activity and also additional enzyme activities like UDP-glucose hydrolase. Polyclonal antibodies raised against 5'-nucleotidase from mammalian sources or the electric ray electric organ reveal mutual crossreactivity. Interestingly, there are 5 -7 domains highly conserved in procaryotes and vertebrates in enzymes exhibiting 5'-nucleotidase, 3'-nucleotidase or phosphodiesterase activity. 5'-nucleotidase isolated from Torpedo electric organ hydrolyzes UDP-glucose at 8 % of the rate of AMP hydrolysis. The possible phylogenetic origin of vertebrate 5'-nucleotidase from multifunctional nucleotide hydrolases is discussed.

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“…15 CD57 1 T cells fail to proliferate after antigen-specific stimulation in vitro and are highly vulnerable to activation-induced apoptosis. 16,17 Furthermore, it was demonstrated that replicative senescence of T cells is better defined by the expression of CD57 than by a lack of CD28 expression, as determined by measurement of the T-cell receptor excision circle content and of the proliferative ability of T cells. 17 Notably, while CD57 1 T cells have been shown to be associated with various inflammatory diseases, [18][19][20][21][22] the pathogenic roles of CD57 1 T cells have yet to be elucidated in coronary artery disease.…”

Section: Introductionmentioning

confidence: 99%

Characterization of CD8+CD57+ T cells in patients with acute myocardial infarction

Youn

Lee

et al. 2014

Cell Mol Immunol

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Although T cells are known to be involved in the pathogenesis of coronary artery disease, it is unclear which subpopulation of T cells contributes to pathogenesis in acute myocardial infarction (MI). We studied the immunological characteristics and clinical impact of CD8 1 CD57 1 T cells in acute MI patients. The frequency of CD57 1 cells among CD8 1 T cells was examined in peripheral blood sampled the morning after acute MI events. Interestingly, the frequency of CD57 1 cells in the CD8 1 T-cell population correlated with cardiovascular mortality 6 months after acute MI. The immunological characteristics of CD8 1 CD57 1 T cells were elucidated by surface immunophenotyping, intracellular cytokine staining and flow cytometry. Immunophenotyping revealed that the CD8 1 CD57 1 T cells were activated, senescent T cells with pro-inflammatory and tissue homing properties. Because a high frequency of CD8 1 CD57 1 T cells is associated with short-term cardiovascular mortality in acute MI patients, this specific subset of CD8 1 T cells might contribute to acute coronary events via their pro-inflammatory and high cytotoxic capacities. Identification of a pathogenic CD8 1 T-cell subset expressing CD57 may offer opportunities for the evaluation and management of acute MI.

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Association of the HNK-1 epitope with 5′-nucleotidase from Torpedo marmorata (electric ray) electric organ

Cited by 51 publications

References 35 publications

Cellular function and molecular structure of ecto-nucleotidases

Cellular function and molecular structure of ecto-nucleotidases

5′‐Nucleotidase from the electric ray electric lobe

Characterization of CD8+CD57+ T cells in patients with acute myocardial infarction

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