5′-Nucleotide phosphodiesterase isozyme-V in health, in cancer, and in viral hepatitis

Lei-Injo, L. E.; Tsou, K. C.; Lo, K. W.; Lopez, C G; Balasegaram, Manica; Ganesan, Srinivasan

doi:10.1002/1097-0142(19800215)45:4<795::aid-cncr2820450431>3.0.co;2-l

Cited by 8 publications

(6 citation statements)

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“…Normal human serum showed four isoenzymes on a native polyacrylamide gel. Sera from patients with liver metastases and viral hepatitis yielded an additional fifth activity band on the zymograms [36]. It seems possible that one of these isoenzymes is related to or identical with the hydrolase described here.…”

Section: Discussionmentioning

confidence: 61%

Catabolism of Ap3A and Ap4A in human plasma. Purification and characterization of a glycoprotein complex with 5'-nucleotide phosphodiesterase activity

Lüthje

Ogilvie

1985

Eur J Biochem

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A hydrolase splitting adenosine(S)triphospho(S')adenosine (Ap3A) to AMP and ADP has recently been detected in human plasma [Liithje, J. and Ogilvie, A. (1984) Biochem. Biophys. Res. Commun. 118,. The enzyme has been purified to apparent homogeneity, as stained in a native polyacrylamide gel. From gel filtration data a Stokes radius of 5.9 nm was calculated, suggesting a molecular mass of about 230 kDa. The presence of the non-ionic detergent Triton X-100 did not change the molecular mass. The hydrolase dissociated to three major protein components (66 kDa; 45 kDa; 16 kDa) during polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate and mercaptoethanol. Binding of the native enzyme to concanavalin-ASepharose and specific inhibition of binding by methyl mannoside indicated that the hydrolase is a glycoprotein. Two of the subunits (66 kDa; 45 kDa) could be affinity-labeled with radioiodinated concanavalin A.Active hydrolase could be prepared in buffers without added metal ions. Treatment with EDTA, however, completely abolished the hydrolytic activity. The enzyme could be reactivated by incubation with Ca2 + , Co2 + and, at best, with Zn2+, whereas Mg2+ was ineffective. The affinity of the enzyme for Ap3A was high (K, = 1 pM), with normal Michaelis-Menten kinetics. The homolog dinucleotide Ap4A was also substrate (K, =0.6 pM) yielding AMP and ATP as products after the asymmetric split. Other dinucleotides, such as NAD, and also mononucleotides (ATP, UTP) were degraded to nucleoside monophosphates indicating a broad specificity of the enzyme. The synthetic compound thymidine 5'-monophosphate p-nitrophenyl ester was substrate with low affinity whereas its 3'-homolog was not hydrolyzed. Optimal activity of the hydrolase was found at pH 8.5. Adenosine(5')triphospho(5')adenosine (Ap3A) has recently been identified in eukaryotic cells [l, 21. It has been suggested that Ap3A might play an antagonistic role toward the homolog dinucleotide Ap4A, which is a potential signal molecule for the initiation of DNA replication [3-51 and might pleiotropically act as an intracellular 'alarmone' [6, 71. Human platelets store Ap3A as well as Ap4A in a metabolically inactive state [2, 81. Both dinucleotides are released on exposure to thrombin, which induces platelet activation. When added to platelet-rich plasma, Ap3A gradually induces aggregation of the platelets [9]. The addition of Ap4A antagonizes this effect by rapidly disaggregating the platelets. These studies suggested that both dinucleotides also have an extracellular function in modulating platelet aggregation and, therefore, in regulating the initiation of hemostasis.The molecular mechanism of aggregation induced by Ap,A has been clarified [9] by showing a slow degradation of Abbreviations. Ap3A, adenosine(5')triphospho(5')adenosine; Ap,A, adenosine(5')tetraphospho(5')adenosine; SDS, sodium dodecyl sulfate.

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Section: Discussionmentioning

confidence: 61%

Catabolism of Ap3A and Ap4A in human plasma. Purification and characterization of a glycoprotein complex with 5'-nucleotide phosphodiesterase activity

Lüthje

Ogilvie

1985

Eur J Biochem

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“…The enzyme has been widely utilized as a tool for structural and sequential studies of nucleic acids. The 5′-nucleotide phosphodiesterase isozyme-V test is useful in detecting liver metastatis in breast, gastrointestinal, lung, and various other forms of cancers (Lei-Injo et al, 1980). Prolyl endopeptidase catalyzes the hydrolysis of peptide bonds at the l -proline carboxy terminal and, thus, plays an important role in the biological regulation of proline-containing neuropeptides and peptide hormones, which are recognized to be involved in learning and memory (Szeltner et al, 2000).…”

Section: Investigation Of the Pharmacological Potential Of Medicinal mentioning

confidence: 99%

Cameroonian Medicinal Plants: Pharmacology and Derived Natural Products

Kuete¹,

Efferth²

2010

Front. Pharm.

228

153

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Many developing countries including Cameroon have mortality patterns that reflect high levels of infectious diseases and the risk of death during pregnancy and childbirth, in addition to cancers, cardiovascular diseases and chronic respiratory diseases that account for most deaths in the developed world. Several medicinal plants are used traditionally for their treatment. In this review, plants used in Cameroonian traditional medicine with evidence for the activities of their crude extracts and/or derived products have been discussed. A considerable number of plant extracts and isolated compounds possess significant antimicrobial, anti-parasitic including antimalarial, anti-proliferative, anti-inflammatory, anti-diabetes, and antioxidant effects. Most of the biologically active compounds belong to terpenoids, phenolics, and alkaloids. Terpenoids from Cameroonian plants showed best activities as anti-parasitic, but rather poor antimicrobial effects. The best antimicrobial, anti-proliferative, and antioxidant compounds were phenolics. In conclusion, many medicinal plants traditionally used in Cameroon to treat various ailments displayed good activities in vitro. This explains the endeavor of Cameroonian research institutes in drug discovery from indigenous medicinal plants. However, much work is still to be done to standardize methodologies and to study the mechanisms of action of isolated natural products.

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“…The enzyme has been widely utilized as a tool for structural and sequential studies of nucleic acids. The 5‘-nucleotide phosphodiesterase isozyme-V test is useful in detecting liver metastatis in breast, gastrointestinal, lung, and various other forms of cancers …”

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confidence: 99%

“…Phytochemical investigation of the stem bark extract of Boswellia papyrifera afforded two new stilbene glycosides, trans-4′,5-dihydroxy-3-methoxystilbene-5-O-{R-L-rhamnopyranosyl-(1f2)-[R-L-rhamnopyranosyl-(1f6)]-β-D-glucopyranoside (1), trans-4′,5-dihydroxy-3-methoxystilbene-5-O-[R-L-rhamnopyranosyl-(1f6)]-β-D-glucopyranoside (2), and a new triterpene, 3R-acetoxy-27-hydroxylup-20(29)-en-24-oic acid (3), along with five known compounds, 11-keto-β-boswellic acid (4), β-elemonic acid (7), 3R-acetoxy-11-ketoβ-boswellic acid (8), β-boswellic acid (9), and β-sitosterol (10). The stilbene glycosides exhibited significant inhibition of phosphodiesterase I and xanthine oxidase.…”

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confidence: 99%

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Bioactive Constituents fromBoswelliapapyrifera

et al. 2005

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Phytochemical investigation of the stem bark extract of Boswellia papyrifera afforded two new stilbene glycosides, trans-4',5-dihydroxy-3-methoxystilbene-5-O-{alpha-L-rhamnopyranosyl-(1-->2)-[alpha-L-rhamnopyranosyl-(1-->6)]-beta-D-glucopyranoside (1), trans-4',5-dihydroxy-3-methoxystilbene-5-O-[alpha-L-rhamnopyranosyl-(1-->6)]-beta-D-glucopyranoside (2), and a new triterpene, 3alpha-acetoxy-27-hydroxylup-20(29)-en-24-oic acid (3), along with five known compounds, 11-keto-beta-boswellic acid (4), beta-elemonic acid (7), 3alpha-acetoxy-11-keto-beta-boswellic acid (8), beta-boswellic acid (9), and beta-sitosterol (10). The stilbene glycosides exhibited significant inhibition of phosphodiesterase I and xanthine oxidase. The triterpenes (3-9) exhibited prolyl endopeptidase inhibitory activities.

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5′-Nucleotide phosphodiesterase isozyme-V in health, in cancer, and in viral hepatitis

Cited by 8 publications

References 1 publication

Catabolism of Ap3A and Ap4A in human plasma. Purification and characterization of a glycoprotein complex with 5'-nucleotide phosphodiesterase activity

Catabolism of Ap3A and Ap4A in human plasma. Purification and characterization of a glycoprotein complex with 5'-nucleotide phosphodiesterase activity

Cameroonian Medicinal Plants: Pharmacology and Derived Natural Products

Bioactive Constituents fromBoswelliapapyrifera

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