New Aspects of Polyamine Biosynthesis in Eukaryotic Organisms

Williams-Ashman, H.G.; Jänne, Juhani; Coppoc, Gordon L.; Geroch, Mary E.; Schenone, Amelia

doi:10.1016/0065-2571(72)90016-7

Cited by 127 publications

(43 citation statements)

References 34 publications

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“…The inhibition brought about by a carbonyl reagent and a pyridoxal phosphate inhibitor is similar to that shown by other decarboxylases [5]. Methylglyoxal-bis(guanylhydrazone), a specific inhibitor of putrescine-dependent S-adenosylmethionine decarboxylase of mammalian tissues and yeast [22], inhibits this plant enzyme as well. The actively growing shoot had maximum amounts of the enzyme, as could be expected of the tissue which elaborates a major portion of the polyamines of the whole seedling [23].…”

Section: Discussionmentioning

confidence: 67%

Putrescine‐Sensitive (Artifactual) and Insensitive (Biosynthetic) S‐Adenosyl‐L‐Methionine Decarboxylase Activities of Lathyrus sativus Seedlings

Suresh

Adiga

1977

European Journal of Biochemistry

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The crude extracts of 3-day-old etiolated seedlings of Lathyrus sativus contained two S-adenosyl-L-methionine decarboxylase activities. The artifactual putrescine-dependent activity was due to the H202 generated by diamine oxidase (EC 1.4.3.6) of this plant system and was inhibited by catalase. This observation was confirmed by using an electrophoretically and immunologically homogeneous preparation of L. sativus diamine oxidase. In the presence of putrescine, diamine oxidase, in addition to S-adenosylmethionine, decarboxylated L-lysine, L-arginine, L-ornithine, L-methionine and L-glutamic acid to varying degrees. The decarboxylation was not metal-ion dependent.The biosynthetic S-adenosylmethionine decarboxylase (EC 4.1.1.21) was detected after removing diamine oxidase specifically from the crude extracts by employing an immunoaffinity column. This Mg2 +-dependent decarboxylase was not stimulated by putrescine or inhibited by catalase. The enzyme activity was inhibited by semicarbazide, 4-bromo-3-hydroxybenzoylamine dihydrogen phosphate and methylglyoxal-bis (guanylhydrazone). It was largely localized in the shoots of the etiolated seedlings and was purified 40-fold by employing ap-hydroxymercuribenzoate/AH-Sepharose affinity column, which also separated the decarboxylase activity from spermidine synthase.S-Adenosyl-L-methionine decarboxylase, a key enzyme of polyamine biosynthesis, catalyses the decarboxylation of S-adenosylmethionine yielding Smethyladenosylhomocysteamine, which in turn donates its propylamine moiety for the stepwise biosynthesis of polyamines, spermidine and spermine. Contrary to earlier reports, it is now well established that the decarboxylation and the propylamine transfer reactions are catalysed by different enzymes [l]. Three types of S-adenosylmethionine decarboxylase activities were described : (a) prokaryotic enzymes, which were Mg2 +-dependent but putrescine insensitive ; (b) lower eukaryotic enzymes, which were not influenced either by divalent cations or putrescine; and (c) the enzymes from animals and yeast, which were markedly stimulated by putrescine [2]. An evolutionary significance for the presence of the last-mentioned activity was attributed to the need for adequate levels of decarboxylated S-adenosylmethionine for enhanced polyamine biosynthesis [3]. Interestingly enough, in higher plants all the three types of activities were described [4]. Arginine decarboxylase and a highly active diamine oxidase, two other enzymes of polyamine metabolism, were earlier purified and characterized from Lathyrus sativus seedlings [5,6] (and unpublished observations). In this paper we report the presence of two S-adenosylmethionine decarboxylase activities from etiolated seedlings of L. sativus, which were separated by immunoaffinity chromatography. One of these, being putrescine dependent but inhibited by catalase, was apparently artifactual. This artifactual activity was catalysed by the contaminating diamine oxidase activity. The other activity, besides being unaffected by putrescine and...

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Section: Discussionmentioning

confidence: 67%

Putrescine‐Sensitive (Artifactual) and Insensitive (Biosynthetic) S‐Adenosyl‐L‐Methionine Decarboxylase Activities of Lathyrus sativus Seedlings

Suresh

Adiga

1977

European Journal of Biochemistry

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“…This response is of particular interest because the enzyme is rate-limiting in the synthesis of polyamines (10), which are implicated in the control of tissue growth (11)(12)(13). Because accumulation of cyclic AMP temporally precedes changes in ornithine decarboxylase activity and cyclic AMP analogues reproduce the hormonal effect, a cyclic AMP-dependent mechanism has been postulated for hormonal regulation of ornithine decarboxylase activity (1)(2)(3)(4)(5).…”

mentioning

confidence: 99%

Regulation of ornithine decarboxylase activity by corticotropin in adrenocortical tumor cell clones: roles of cyclic AMP and cyclic AMP-dependent protein kinase.

Kudlow¹,

Rae²,

Gutmann³

et al. 1980

Proc. Natl. Acad. Sci. U.S.A.

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In Y1 adrenocortical tumor cells, corticotropin (ACTH), cyclic AMP, and 8-bromoadenosine 3',5'-monophosphate (8BrcAMP) stimulated ornithine decarboxylase activity (L-ornithine carboxy-lyase, EC 4.1.1.17) and steroidogenesis. The concentrations required for half-maximal activation of ornithine decarboxylase were 60 pM for ACTH and 1 mM for 8BrcAMP; the concentrations required for half-maximal activation of steroidogenesis were 50 pM for ACTH and 0.2 mM for 8BrcAMP. Ornithine decarboxylase activity increased 1.5 hr after the addition of these agents, reached a maximum between 4 and 6 hr, and then declined. Mutant clones with impaired ACTH-responsive adenylate cyclase systems [ATP pyrophosphate-lyase (cyclizing), EC 4.6.1.1] did not respond to ACTH with increased ornithine decarboxylase activity, but they responded normally to added cyclic AMP. These results indicate that adenylate cyclase and cyclic AMP are necessary for the stimulation of ornithine decarboxylase activity by ACTH. In a series of Y1(Kin) mutants with altered cyclic AMP-dependent protein kinase activities (ATP:protein phosphotransferase, EC 2.7.1.37), the effects of ACTH on ornithine decarboxylase also were attenuated. These findings suggest that cyclic AMP-dependent protein kinase also plays a necessary role in the stimulation of ornithine decarboxylase activity by ACTH. The effects of ACTH on ornithine decarboxylase in the Kin mutants, however, were quantitatively different from the effects on steroidogenesis and did not closely reflect the degree of defect in cyclic AMP-dependent protein kinase activity. These differences suggest that the pathways of ACTH action leading to stimulation of steroidogenesis and ornithine decarboxylase activity diverge subsequent to activation of the protein kinase.

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“…These finding contrast with reports that cAMP induces ornithine decarboxylase in other cell types and further suggest that passage of cells through the cell cycle is required for maintaining the activities of ornithine and S-adenosylmethionine decarboxylases. Polyamines have been implicated as regulators of protein synthesis in a variety of biologic tissues (1)(2)(3)(4)(5)(6)(7)(8). In certain regenerating tissues and cultured cells, increased levels of ornithine decarboxylase (L-ornithine carboxy-lyase; EC 4.1.1.17), the rate-limiting enzyme in polyamine biosynthesis in eukaryotes, closely correlate with increased rates of cellular growth and proliferation (2,3).…”

mentioning

confidence: 99%

“…Polyamines have been implicated as regulators of protein synthesis in a variety of biologic tissues (1)(2)(3)(4)(5)(6)(7)(8). In certain regenerating tissues and cultured cells, increased levels of ornithine decarboxylase (L-ornithine carboxy-lyase; EC 4.1.1.17), the rate-limiting enzyme in polyamine biosynthesis in eukaryotes, closely correlate with increased rates of cellular growth and proliferation (2,3). In fibroblasts (4), mammary tissue (5), chinese hamster V79 cells (6), hepatoma (7), glioma, and neuroblastoma cells (8), and L cells (9), adenosine 3':5'cyclic monophosphate (cAMP) appears to induce ornithine decarboxylase; but in other model systems (10,11) changes in cAMP levels can be dissociated from increased ornithine decarboxylase activity.…”

mentioning

confidence: 99%

Cyclic AMP-dependent protein kinase mediates a cyclic AMP-stimulated decrease in ornithine and S-adenosylmethionine decarboxylase activities.

Insel¹,

Fenno²

1978

Proc. Natl. Acad. Sci. U.S.A.

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Incubation of S49 lymphoma cells with N6,02'-dibutyryl cyclic AMP (Bt2cAMP) decreases the activities of ornithine decarboxylase (L-ornithine carboxy-lyase; EC 4.1.1.17) and S-adenosylmethionine decarboxylase (S-adenosyl-L-methionine carboxy-lyase; EC 4.1.1.50), the two principal enzymes in the pathway of polyamine synthesis. This decrease is dose-dependent, commences after a 3-hr delay, virtually abolishes the assayable activities of the two enzymes, and is not associated with a soluble inhibitor of the enzyme activities. Studies in mutant S49 clones that have altered protein kinase indicate that cAMP-dependent protein kinase mediates the decreases in enzyme activities. The dose-response pattern for the cAMP-stimulated decrease in enzyme activities parallels the pattern for the cAMP-stimulated, cell cycle-specific (GI) growth arrest of S49 cells. The activity of ornithine decarboxylase decreases faster than Bt2cAMP arrests wild-type S49 cells and, similarly, release of cells from the cAMP-stimulated arrest in GI increases the activity of ornithine decarboxylase faster than cells exit from G1. These finding contrast with reports that cAMP induces ornithine decarboxylase in other cell types and further suggest that passage of cells through the cell cycle is required for maintaining the activities of ornithine and S-adenosylmethionine decarboxylases. Polyamines have been implicated as regulators of protein synthesis in a variety of biologic tissues (1-8). In certain regenerating tissues and cultured cells, increased levels of ornithine decarboxylase (L-ornithine carboxy-lyase; EC 4.1.1.17), the rate-limiting enzyme in polyamine biosynthesis in eukaryotes, closely correlate with increased rates of cellular growth and proliferation (2, 3). In fibroblasts (4), mammary tissue (5), chinese hamster V79 cells (6), hepatoma (7), glioma, and neuroblastoma cells (8), and L cells (9), adenosine 3':5'cyclic monophosphate (cAMP) appears to induce ornithine decarboxylase; but in other model systems (10, 11) changes in cAMP levels can be dissociated from increased ornithine decarboxylase activity. Russell and colleagues (12) (17). We therefore used S49 cells to test the hypothesis (12, 13) that cAMP and protein kinase induce ornithine decarboxylase, but found instead that in these cells, in contrast with all other cells reported previously, cAMP strikingly decreases the activities of ornithine decarboxylase and S-adenosylmethionine decarboxylase and that this effect is mediated by cAMP-dependent protein kinase. MATERIALS AND METHODS S49.1 mouse lymphoma cells (19) were propagated in suspension culture in Dulbecco's modified Eagle's medium that contained 10% heat-inactivated horse serum as described (14,17). Cell concentrations and viability were determined by a hemocytometer and by trypan blue exclusion, respectively. The isolation and characterization of the mutant clones have been described (17,20). Cellular lysates were obtained by suspending cell pellets in ice-cold hypotonic buffer (5 mM Tris-HCl, pH 7.5/2 mM dithio...

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New Aspects of Polyamine Biosynthesis in Eukaryotic Organisms

Cited by 127 publications

References 34 publications

Putrescine‐Sensitive (Artifactual) and Insensitive (Biosynthetic) S‐Adenosyl‐L‐Methionine Decarboxylase Activities of Lathyrus sativus Seedlings

Putrescine‐Sensitive (Artifactual) and Insensitive (Biosynthetic) S‐Adenosyl‐L‐Methionine Decarboxylase Activities of Lathyrus sativus Seedlings

Regulation of ornithine decarboxylase activity by corticotropin in adrenocortical tumor cell clones: roles of cyclic AMP and cyclic AMP-dependent protein kinase.

Cyclic AMP-dependent protein kinase mediates a cyclic AMP-stimulated decrease in ornithine and S-adenosylmethionine decarboxylase activities.

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