Effect of indole-3-acetic acid on the synthesis of cyclic 3′–5′ adenosine phosphate by bengal gram seeds

Azhar, Salman; Murti, C. R. Krishna

doi:10.1016/s0006-291x(71)80085-2

Cited by 45 publications

(10 citation statements)

References 9 publications

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“…Other reports provide circumstantial evidence for the possible occurrence of cAMP in green plants. These reports describe effects of exogenously supplied cAMP (6)(7)(8)(9)(10)(11), or chromatographic similarities between authentic cAMP and a plant metabolite derived from adenine (12)(13)(14), or the presence of enzyme activities that may function in cAMP metabolism (5,(15)(16)(17).…”

mentioning

confidence: 99%

Adenosine 3′:5′-Cyclic Monophosphate in Chlamydomonas reinhardtii: Isolation and Characterization

Amrhein

Filner

1973

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

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Chlamydomonas reinhardtii contains a factor that can replace adenosine 3':5'-cyclic monophosphate (cAMP) in the stimulation of rabbit-muscle protein kinase. The factor cochromatographs and coelectrophoreses with authentic cAMP, and is inactivated by beef heart cyclic nucleotide phosphodiesterase. When C. reinhardtii is exposed to aminophylline (theophylline2 ethylenediamine), the concentration of the factor in the cells increases within 1 hr, from about 25 pmol of cAMP equivalents per g dry weight to more than 250 pmol. Cyclic nucleotide phosphodiesterase activity is present in crude extract of C. reinhardtii and is inhibited by theophylline. We conclude that cAMP occurs in C. reinhardtii and that the endogenous concentration is governed at least in part by a theophylline-sensitive cyclic nucleotide phosphodiesterase. These findings provide a sound basis for attributing the effects of methylxanthines on flagellar function and regeneration in C. reinhardtii to the resultant elevation of endogenous cAMP.We have recently obtained evidence (1, 2) that methylxanthines can inhibit the function and regeneration of flagella of the green alga, Chlamydomonas reinhardtii. These compounds are known to increase the amount of adenosine 3': 5'-cyclic monophosphate (cAMP) in mammalian cells by inhibiting cyclic nucleotide phosphodiesterase activity (3).To our knowledge, there is no published evidence concerning the occurrence of cAMP or a methylxanthine-sensitive cyclic nucleotide phosphodiesterase in C. reinhardtii or any other alga. Furthermore, the evidence for their occurrence in higher green plants is tenuous. Lettuce is the only species that has been reported to contain cAMP, by means of an assay involving conversion of cAMP to ATP (4). Other reports provide circumstantial evidence for the possible occurrence of cAMP in green plants. These reports describe effects of exogenously supplied cAMP (6-11), or chromatographic similarities between authentic cAMP and a plant metabolite derived from adenine (12-14), or the presence of enzyme activities that may function in cAMP metabolism (5,(15)(16)(17).Theophylline-sensitive activity of cyclic nucleotide phosphodiesterase was recently detected in cultured Vinca rosea tumor cells (5). TAP medium is prepared by dissolving 2.42 g of tris(hydroxymethyl)aminomethane in a mixture of 1.0 ml of 1 M potassium phosphate buffer (pH 7.2), 50 ml of Beijerinck's solution, 1 ml of trace elements solution, and water. The pH is brought back to 7.2 by addition of about 1 ml of glacial acetic acid, and the volume is adjusted to 1 liter. Beijerinck's solution consists of 8 g of NH4C1, 1 g of CaCl2.2H20, and 2 g of MgSO4 7H20, dissolved in water to a final volume of 1 liter. To prepare the trace-elements solution, dissolve 50 g of disodium ethylenediaminetetraacetate (EDTA) in 250 ml of heated water. Then, dissolve 22.0 g of ZnSO4. 7H20, 11.4 g of H3BO3, 5.06 g of MnCl2-4H20, 4.99 g of FeSO4-7H20, 1.61 g of CoCl2 -6H20, 1.57 g of CuSO4 5H20, and 1.1 g of (NH4)&Mo7024 4H20 in 550 ml of H20 at ...

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confidence: 99%

Adenosine 3′:5′-Cyclic Monophosphate in Chlamydomonas reinhardtii: Isolation and Characterization

Amrhein

Filner

1973

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

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“…The following tests were applied to establish the identity of the labeled product with CAMP : (a) paper and thin-layer chromatography in two or three different solvent systems ; (b) degradation by Ba(OH)2 to 3' AMP and 5' AMP, or NaNO2 and acetic acid to cyclic inosine monophosphate, or hydrolysis by carrot leaf diesterase to adenosine . These tests were performed according to procedures described by Azhar and Krishna Murti (1971) . Radioactivity counts were taken in a Packard Liquid Scintillation Spectrometer essentially as described by Hadi and Krishna Murti (1967) .…”

Section: Brief Notesmentioning

confidence: 99%

TRANSFORMATION OF TROPHIC HARTMANNELLA CULBERTSONI INTO VIABLE CYSTS BY CYCLIC 3',5'-ADENOSINE MONOPHOSPHATE

Raizada

Murti

1972

The Journal of Cell Biology

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“…Although this nucleotide has not yet been identified in higher plants, the activity of cAMP-specific phosphodiesterase has been noted (Wood et al 1972). Also the conversion to cAMP of labelled adenine (Pollard 1970, Salomon and Mascarenhas 1971a, Azhar and Krishna-Murti 1971 and labelled ATP (Wood et al 1972) in various plant tissues has been re-ported. Furthermore, phytohormone-like effects of cAMP (Kessler 1969, Galsky and Lippincott 1969, Salomon and Mascarenhas 1971 and cGMP (guanosine-3',5'-cyclic monophosphate) (Kessler 1969) have been reported.…”

Section: Introductionmentioning

confidence: 99%

Cyclic Purine Mononucleotides: Induction of Gibberellin Biosynthesis in Barley Endosperm

Kessler

Kaplan

1972

Physiologia Plantarum

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The de novo synthesis of α‐amylase in barley endosperm and isolated aleurone layers is induced by 3′,5′‐cyclic purine mononucleotides and gibberellic acid. The induction of α‐amylase by cyclic purine mononucleotides is prevented by 2,4‐DNP, inhibitors of RNA and protein syntheses, CCC, AMO‐1618 and phosfon. The induction of α‐amylase formation by 3′,5′‐cyclic purine mononucleotides, but not by gibberellic acid, is also blocked by inhibitors of DNA synthesis. Extracts from cyclic AMP‐treated endosperm halves exhibit a characteristic gibberellin‐like activity which is detectable within 12 hours from the addition of the cyclic AMP. On paper chromatograms this gibberellin‐like activity is located at the Rf typical for GA3. Its formation is prevented by inhibitors of DNA synthesis, CCC and AMO‐1618. Glucose inhibits the formation of α‐amylase induced by gibberellic acid. Glucose has no effect on the cAMP‐induced gibberellin biosynthesis. The evidence shows that the cyclic purine mononucleotides induce DNA synthesis, which results in gibberellin biosynthesis, which in turn activates the synthesis of α‐amylase.

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Effect of indole-3-acetic acid on the synthesis of cyclic 3′–5′ adenosine phosphate by bengal gram seeds

Cited by 45 publications

References 9 publications

Adenosine 3′:5′-Cyclic Monophosphate in Chlamydomonas reinhardtii: Isolation and Characterization

Adenosine 3′:5′-Cyclic Monophosphate in Chlamydomonas reinhardtii: Isolation and Characterization

TRANSFORMATION OF TROPHIC HARTMANNELLA CULBERTSONI INTO VIABLE CYSTS BY CYCLIC 3',5'-ADENOSINE MONOPHOSPHATE

Cyclic Purine Mononucleotides: Induction of Gibberellin Biosynthesis in Barley Endosperm

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