A cyclic AMP-dependent protein kinase from frog bladder epithelial cells

Jard, Serge; Bastide, Françoise

doi:10.1016/0006-291x(70)90240-8

Cited by 70 publications

(16 citation statements)

References 16 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…It appears that the intracellular mechanism of the hormonal control on the membrane might provide a basis for such a modification. A consequence of hormonal action on the serosal membrane is the activation of a protein kinase present in the urinary bladder epithelial cell [10]. The target protein of this kinase is not known yet, but there is evidence that this kinase phosphorylates a membrane protein as suggested by Dousa and co-workers [6], in the case of the mammalian kidney collecting tubule; the phosphorylated protein may be finally responsible for the membrane permeability change.…”

Section: Discussionmentioning

confidence: 93%

Lanthanum inhibition of the action of oxytocin on the water permeability of the frog urinary bladder: Effect on the serosal and the apical membrane

1974

View full text Add to dashboard Cite

Summary. The effect of La 3+ ion on the hydrosmotic response of the frog urinary bladder to oxytocin has been studied. When added to the serosal medium, in the concentration range 10-4M to 10 -3 M, La 3+ inhibits the response to oxytocin, theophylline and cyclic-AMP, but not to hypertonicity. When added to the apical medium at a concentration greater than 5 x 10 -a M, La 3+ exhibits an inhibitory effect only during respective stimulation, either by hormone or by hypertonicity, but has no significant effect on the developed response. The significance of this particular mode of action is discussed in terms of possible electrical potential variations of the apical membrane during stimulation.It is well known that the action of the neurohypophysial hormones on the serosal side of the urinary bladder epithelium results in an increase in the water permeability of the apical membrane of the epithelial cells [5,9,12,13,15]. The mechanism of this action is not understood, although since the work of Handler and Orloff [8,[19][20][21] several of the intraceilular biochemical steps have been elucidated.While the mechanism by which the water permeability of the apical membrane itself is modified is unknown, hypotheses may be made concerning the possible structural transformation underlying the membrane permeability change.It is currently accepted, on the basis of evidence obtained on model systems and on biological membranes [7,23], that calcium plays an important role in maintaining the tight and ordered organization of biological membranes and therefore their low and selective permeability. It may be reasonably assumed that the apical membrane of epithelial ceils has similar

show abstract

Section: Discussionmentioning

confidence: 93%

Lanthanum inhibition of the action of oxytocin on the water permeability of the frog urinary bladder: Effect on the serosal and the apical membrane

1974

View full text Add to dashboard Cite

show abstract

“…Colchicine-binding protein in renal medullary cytosol showed some characteristic properties described for analogous protein from brain (19): the colchicine-binding activity was labile after prolonged incubation of 00C or after short incubation at 60'C, and (3) 4.98±0.33 (3) 4.86±0.12 (3) 38.4±0.56 (3) 42.434±2.26 (3) 39.1 1 ±2.35 (3) Cyclic AMP phosphodiesterase after preincubationj with colchicine or vinblastine nmol/min per mg protein* control 1.61±0.11 (6) Preincubated with colchicine 1.62±i0.11 (6) Preincubated with vinblastine 1.58±0.16 (6) * Mean±SE; number of experiments in parentheses. colchicine-binding protein was completely precipitated from the cytosol by incubation with vinblastine (Table VI).…”

Section: In Vivo Studiesmentioning

confidence: 83%

“…The mechanism by which cyclic AMP formed under the influence of vasopressin increases water permeability of collecting ducts remains unknown. Still hypothetical is the idea that cyclic AMP acts on the lumenal plasma membrane through its influence on protein phosphorylation (3)(4)(5). Taylor, Mamelak, Raven, and Maffly (6) found that some drugs known to disrupt the structure of microtubules partially inhibit the increase in water permeability in response to vasopressin and exogenous cyclic AMP in isolated toad urinary bladders.…”

Section: Introductionmentioning

confidence: 99%

Effects of Colchicine and Vinblastine on the Cellular Action of Vasopressin in Mammalian Kidney A POSSIBLE ROLE OF MICROTUBULES

Douša¹,

Barnes²

1974

J. Clin. Invest.

View full text Add to dashboard Cite

show abstract

“…The existence of protein kinases that are activated by adenosine 3': 5'-cyclic monophosphate (cAMP) has been documented extensively for various tissues from several species (1)(2)(3)(4)(5)(6)(7)(8)(9), and some regulatory functions of cAMP have been shown to be mediated by this type of enzyme (1,5,(9)(10)(11)(12). On the basis of kinetic studies, and in view of the stability properties of the heart-muscle cAMP-dependent protein kinase, it was proposed (6) that the enzyme was made up of regulatory (R) and catalytic (C) subunits, which dissociated in the presence of cAMP:…”

mentioning

confidence: 99%

Interaction of the Subunits of Adenosine 3′:5′-Cyclic Monophosphate-Dependent Protein Kinase of Muscle

Brostrom

Corbin

King

et al. 1971

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

123

View full text Add to dashboard Cite

Two cAMP-dependent protein kinases purified from rabbit skeletal muscle were shown to bind the same amount of cAMP per unit of enzyme activity at several concentrations of this nucleotide. A preparation containing both of these kinases was separated into catalytic (C) and regulatory (R) subunit fractions in the presence of cAMP, the regulatory subunit being obtained as an R cAMP complex. Addition of increasing amounts of the R cAMP complex to the holoenzyme (RC) increased the concentration of cAMP required for half-maximal activity of the enzyme. cAMP was liberated from the R cAMP complex in the presence of added catalytic subunit in a reaction that was facilitated by Mg2+, ATP, and warming. These findings are presented in support of a model for activation of the protein kinase by cAMP. The possibility that excess regulatory subunit may serve as a sink for intracellular cAMP is also discussed. It is shown that cAMP bound to the R subunit is not a-substrate for the cAMP phosphodiesterase.

show abstract

A cyclic AMP-dependent protein kinase from frog bladder epithelial cells

Cited by 70 publications

References 16 publications

Lanthanum inhibition of the action of oxytocin on the water permeability of the frog urinary bladder: Effect on the serosal and the apical membrane

Lanthanum inhibition of the action of oxytocin on the water permeability of the frog urinary bladder: Effect on the serosal and the apical membrane

Effects of Colchicine and Vinblastine on the Cellular Action of Vasopressin in Mammalian Kidney A POSSIBLE ROLE OF MICROTUBULES

Interaction of the Subunits of Adenosine 3′:5′-Cyclic Monophosphate-Dependent Protein Kinase of Muscle

Contact Info

Product

Resources

About