Cyclic AMP regulation of lactate dehydrogenase. Isoproterenol and N6,O2-dibutyryl cyclic amp increase the rate of transcription and change the stability of lactate dehydrogenase a subunit messenger RNA in rat C6 glioma cells.

Jungmann, Richard A.; Kelley, Daniel; Miles, Michael F.; Milkowski, Deborah M.

doi:10.1016/s0021-9258(18)32573-0

Cited by 145 publications

(2 citation statements)

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“…Maximal activation by forskolin-induced cAMP accumulation led to a rapid translocation of C to the nucleus, which was reversible upon removal of forskolin (Nigg et al, 1985b). Together with other reports on the activation of certain genes by cAMP-dependent protein kinases (Maurer, 1981;Murdoch et al, 1982;Lamers et al, 1982;Boney et al, 1983;Jungmann et al, 1983;Lewis et al, 1983), these data may suggest that protein kinase II is dissociated only after a strong stimulus as evoked by high levels of cAMP, thus allowing induction of key enzymes by specific gene activation. Special functions of protein kinase II are also indicated by the existence of tissue-specific isoforms of R II subunits (Erlichman et al, 1980;Robinson-Steiner et al, 1984;Jahnsen et al, 1985).…”

Section: Discussionsupporting

confidence: 65%

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cAMP-dependent protein kinases I and II: divergent turnover of subunits

Weber¹,

Hilz²

1986

Biochemistry

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cAMP-dependent protein kinase subunits were isolated from livers of rats that had been subjected to biosynthetic labeling with radioactive leucine. By application of ligand and antibody affinity techniques pure regulatory (R I; R II) and catalytic (C) subunits could be obtained in high yields, which allowed measurement of the apparent degradation rate constants and half-lives following a double isotope labeling protocol. In this way marked differences of apparent half-lives of regulatory subunits R I (t1/2 = 31 h) and R II (t1/2 = 125 h) were observed. To avoid the negative influence of reutilization inherent in the decay experiments, specific radioactivities were determined after a short isotope pulse. This parameter, which under steady-state conditions reflects the fractional turnover rate of the subunits, was found to be different for all three protein kinase subunits. Relative to total liver protein, the ratios R I:R II:C corresponded to 3.9:0.6:2. Our data indicate that in each type of protein kinase isoenzymes regulatory and catalytic subunits turn over with similar rates. The type I isoenzyme, however, is renewed much faster than protein kinase II. Furthermore, our findings are consistent with the thesis that free subunits as generated by activation are more susceptible to degradation than the holoenzymes, leading under steady-state conditions to compensatory resynthesis. Since renewal of R I exceeded that of R II also in two other tissues, the elevated turnover of protein kinase I as an indicator of preferential activation appears to be a general phenomenon. The different turnover of the two isoenzymes, then, may relate to different cellular functions like modulation of enzyme activity vs. modulation of gene activity.

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Section: Discussionsupporting

confidence: 65%

“…0006-2960/86/0425-566 ISO 1.50/0 ciated holoenzyme II under conditions of maximal stimulation (Nigg et al, 1985b) as well as other data on a nuclear function of C (Maurer, 1981;Murdoch et al, 1982;Lamers et al, 1982;Boney et al, 1983;Jungmann et al, 1983; Lewis et al, 1983) lend support to such an interpretation.…”

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confidence: 81%

cAMP-dependent protein kinases I and II: divergent turnover of subunits

Weber¹,

Hilz²

1986

Biochemistry

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Regulation ofLDH-A gene expression by transcriptional and posttranscriptional signal transduction mechanisms

1998

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Expression of lactate dehydrogenases A and B during chicken spermatogenesis: Characterization of testis specific transcripts

Arias

Mezquita

2000

J. Cell. Biochem.

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The substrates required for glycolysis change markedly at successive stages of spermatogenesis suggesting a considerable plasticity in the expression of glycolytic enzymes. Lactate dehydrogenase (LDH) isoenzymes, LDH-A and LDH-B, are expressed in premeiotic, meiotic cells, and early spermatids, both in avian and mammalian spermatogenesis. Highly polyadenylated forms, particularly of LDH-A, were detected in chicken testis. While mammals and columbid birds express the testis specific LDH-C gene in meiotic and postmeiotic cells, several LDH-B testis specific transcripts were detected in the corresponding cells during chicken spermatogenesis. These testis specific transcripts and the mRNA of mammalian LDH-C show several properties in common, such as temporal correlation of expression, mRNA stability, and repression of premature translation. These observations suggest that the testis specific transcripts could perform during chicken spermatogenesis the functions of the LDH-C mRNA in mammalian testis.

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Cyclic AMP regulation of lactate dehydrogenase. Isoproterenol and N6,O2-dibutyryl cyclic amp increase the rate of transcription and change the stability of lactate dehydrogenase a subunit messenger RNA in rat C6 glioma cells.

Cited by 145 publications

References 49 publications

cAMP-dependent protein kinases I and II: divergent turnover of subunits

cAMP-dependent protein kinases I and II: divergent turnover of subunits

Regulation ofLDH-A gene expression by transcriptional and posttranscriptional signal transduction mechanisms

Expression of lactate dehydrogenases A and B during chicken spermatogenesis: Characterization of testis specific transcripts

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