Nonenzymic ADP-ribosylation of poly(adenosine diphosphate ribose)

Ikejima, Miyoko; Dm, Gill

doi:10.1021/bi00340a013

Cited by 11 publications

(4 citation statements)

References 27 publications

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“…Nonenzymatic ADP-ribosylation of poly(ADP-ribose) (Ikejima & Gill, 1985) can occur at high salt concentration or at alkaline pH by the hydrolysis of NAD through a glycosidic bond. However, the velocity of this reaction is very slow as compared to that of the ADP-ribosylation reaction.…”

Section: Resultsmentioning

confidence: 99%

ADP-ribosyl transferase and NAD glycohydrolase activities in rat liver mitochondria

Masmoudi¹,

Mandel²

1987

Biochemistry

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Section: Resultsmentioning

confidence: 99%

ADP-ribosyl transferase and NAD glycohydrolase activities in rat liver mitochondria

Masmoudi¹,

Mandel²

1987

Biochemistry

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“…thiol and carboxylate groups) can link ADPR [2]. Indeed, non-enzymic ADP-ribosylation has been described in several biological systems [2][3][4][5][6][7][8].…”

Section: Introductionmentioning

confidence: 99%

Free ADP-ribose in human erythrocytes: pathways of intra-erythrocytic conversion and non-enzymic binding to membrane proteins

Zocchi

Guida

Franco

et al. 1993

Biochemical Journal

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We have previously identified free ADP-ribose (ADPR) as a normal metabolite in mature human erythrocytes. In this study the metabolic transformations of ADPR were investigated in both supernatants from erythrocyte lysates and intact erythrocytes, loaded with ADPR by means of a procedure involving hypotonic haemolysis and isotonic resealing. In both experimental systems, the main pathway was a dinucleotide pyrophosphatase-catalysed hydrolysis to yield AMP, which was readily converted into the adenylic and inosinic nucleotide pools. To a lesser extent, ADPR underwent conversion into a compound that was identified as ADP-ribulose (ADPRu), on the basis of m.s., n.m.r. spectroscopy and enzymic analysis. ADPRu was also susceptible to degradation by the dinucleotide pyrophosphatase, which was partially purified from erythrocyte lysates and characterized with respect to its substrate specificity. Isomerization of ADPR to ADPRu was markedly enhanced by ATP. Incubation of unsealed haemoglobin-free erythrocyte membranes with labelled ADPR did not cause any transformation of this nucleotide and resulted in its trichloroacetic acid- and formic acid-resistant binding to a number of membrane cytoskeletal proteins. These proteins include spectrin, glyceraldehyde 3-phosphate dehydrogenase (Ga3PDH), three proteins of molecular masses 98, 79 and 72 kDa, which apparently comigrate with bands 3, 4.1 and 4.2 respectively, and two additional proteins of molecular masses 58 and 41 kDa. Acid-resistant binding of ADPR, as well as of NAD+, to Ga3PDH was confirmed for the enzyme purified from human erythrocytes.

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“…Previous studies have shown that, under high-salt and alkaline conditions, NAD can be a highly reactive molecule that reacts non-enzymatically with ADP-ribose polymers and covalently attaches ADP-ribose (35). To exclude the unlikely possibility of non-enzymatic ADP-ribosylation in our system, mono-ADP-ribosylated agmatine, ADP-ribose polymer, and auto-ADP-ribosylated cholera toxin, which is known to be mono-ADP-ribosylated at multiple sites (25), were analyzed using the same conditions (Fig.…”

Section: Conservation Of Structural Elements and Catalyticmentioning

confidence: 99%

“…Digestion of PARPgenerated ADP-ribose polymers with SVP generates two major products, 2Ј-O-␣-D-ribosyladenosine 5Ј,5Љ-bisphosphate (PR-AMP) and AMP (1,36). In contrast, digestion of non-enzymatically generated polymers does not generate PR-AMP (35). The observation of PR-AMP provides strong evidence that a polymer had been digested.…”

Section: Conservation Of Structural Elements and Catalyticmentioning

confidence: 99%

ART2, a T Cell Surface Mono-ADP-ribosyltransferase, Generates Extracellular Poly(ADP-ribose)

Morrison

Moss

Stevens

et al. 2006

Journal of Biological Chemistry

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NAD functions in multiple aspects of cellular metabolism and signaling through enzymes that covalently transfer ADP-ribose from NAD to acceptor proteins, thereby altering their function. NAD is a substrate for two enzyme families, mono-ADP-ribosyltransferases (mARTs) and poly(ADP-ribose) polymerases (PARPs), that covalently transfer an ADP-ribose monomer or polymer, respectively, to acceptor proteins. ART2, a mART, is a phenotypic marker of immunoregulatory cells found on the surface of T lymphocytes, including intestinal intraepithelial lymphocytes (IELs). We have shown that the auto-ADP-ribosylation of the ART2.2 allelic protein is multimeric. Our backbone structural alignment of ART2 (two alleles of the rat art2 gene have been reported, for simplicity, the ART2.2 protein investigated in this study will be referred to as ART2) and PARP suggested that multimeric auto-ADP-ribosylation of ART2 may represent an ADP-ribose polymer, rather than multiple sites of mono-ADPribosylation. To investigate this, we used highly purified recombinant ART2 and demonstrated that ART2 catalyzes the formation of an ADP-ribose polymer by sequencing gel and by HPLC and MS/MS mass spectrometry identification of PR-AMP, a breakdown product specific to poly(ADP-ribose). Furthermore, we identified the site of ADP-ribose polymer attachment on ART2 as Arg-185, an arginine in a crucial loop of its catalytic core. We found that endogenous ART2 on IELs undergoes multimeric auto-ADP-ribosylation more efficiently than ART2 on peripheral T cells, suggesting that these distinct lymphocyte populations differ in their ART2 surface topology. Furthermore, ART2.2 IELs are more resistant to NAD-induced cell death than ART2.1 IELs that do not have multimeric auto-ADP-ribosylation activity. The data suggest that capability of polymerizing ADP-ribose may not be unique to PARPs and that poly(ADP-ribosylation), an established nuclear activity, may occur extracellularly and modulate cell function.

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Nonenzymic ADP-ribosylation of poly(adenosine diphosphate ribose)

Cited by 11 publications

References 27 publications

ADP-ribosyl transferase and NAD glycohydrolase activities in rat liver mitochondria

ADP-ribosyl transferase and NAD glycohydrolase activities in rat liver mitochondria

Free ADP-ribose in human erythrocytes: pathways of intra-erythrocytic conversion and non-enzymic binding to membrane proteins

ART2, a T Cell Surface Mono-ADP-ribosyltransferase, Generates Extracellular Poly(ADP-ribose)

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