Guanyl cyclase. Determination of enzyme activity

Schultz, Günter; Böhme, Eycke; Munske, K.

doi:10.1016/0024-3205(69)90189-1

Cited by 110 publications

(31 citation statements)

References 7 publications

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“…Cyclic GMP is formed in mammalian cells by the enzyme, guanylate cyclase [116,268,344]. The enzyme utilizes GTP and has several properties which distinguish it from adenylate cyclase.…”

Section: Guanylate Cyclasementioning

confidence: 99%

Second Messenger System in Neoplasia

Criss¹

1974

Oncology

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Hormones have been observed to initiate tumors in animals and are thought to be involved in cellular selection and/or progression of neoplastic lesions in humans. Hormones are the ‘First messengers’ in mammalian systems as they allow cell to cell and organ to organ communication A ‘second messenger’ system is currently being elucidated. This second messenger system involves several cellular membraneous and intracellular components which act to relay extracellular messages to intracellular targets including the genomic machinery within the nucleus. The current manuscript reviews and discusses the following components of the second messenger system in normal versus neoplastic tissues: hormone binding, message transduction, adenylate cyclases, guanylate cyclases, cyclic AMP, cyclic GMP, cyclic nucleotide phosphodiesterases, cyclic nucleotide binding proteins, protein kinases (protein phosphorylation), and phosphoprotein dephosphatases (phosphoprotein de-phosphorylation).

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“…Cyclic GMP is formed in mammalian cells by the enzyme, guanylate cyclase [116,268,344]. The enzyme utilizes GTP and has several properties which distinguish it from adenylate cyclase.…”

Section: Guanylate Cyclasementioning

confidence: 99%

Second Messenger System in Neoplasia

Criss¹

1974

Oncology

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“…1. 2) (GCase), which catalyzes guanosine triphosphate (GTP) to guanosine 3', 5'-monophosphate (cGMP) and liberates pyrophosphate, is found in a variety of tissues throughout the animal kingdom (4,23,27,59,67). In earlier reported attempts to separate guanylate cyclase, activity was detected in supernatant fractions (67), while in others it was found that the larger part of the activity was in particulate fraction (22,23,27), indicating that the activity of guanylate cyclase is made to move to the sypernatant by Triton X-100 (24,27).…”

mentioning

confidence: 99%

“…The demonstration of ACase with lead citrate was also done for comparison with the pattern presented by GCase activity. Finally, the sites of the enzyme activity were compared between those found in the immersion fixed and the rapid freeze substituted rat retina (59,61). MATERIALS AND METHODS such as the liver, skeletal and cardiac muscles, and the fungus using ATP as substrate (2,11,16,26,28,30,43,58,60,64,66).…”

mentioning

confidence: 99%

Lead citrate method of guanylate cyclase and its application to tissue receiving rapid freeze substitution fixation.

Saito

Sano

Keino

et al. 1992

Acta Histochem. Cytochem

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“…uberstand [39]. Um zu prufen, ob die bei Verwendung des 1000 x g-Sediments gemessene Guo-3' : S'-P-Bildung durch eine partikuliire Guanylat-Cyclase, die wie die Adenylat-Cyclase an Plasmamembranen gebunden ist, oder durch die losliche Guanylat-Cyclase nicht aufgeschlossener Zellen bedingt ist, bestimmten wir die an plasmamembranreiche Fraktionen aus der Niere gebundene Guanylat-Cyclase-Aktivitiit.…”

unclassified

“…Es ist nicht ausgeschlossen, daB bei der Steuerung des Natriumtransports nicht Ado-3' : 5'-P, sondern ein anderes cyclisches Nucleotid eingeschaltet ist, eine Annahme, die Orloff und Handler [15] schon 1967 aussprachen. I n Untersuchungen von Bourgoignie et al an der Krotenblase steigerte au13er Ado-3': 5'-P auch Guo-3': 5'-P den Naf-Transport ; Guo-3' : 5'-P hatte im Gegensatz zu Ado-3' : 5'-P jedoch keine Wirkung auf die Wasserpermeabilitiit Die Guanylat-Cyclase, welche die Bildung von Guo-3':5'-P aus GTP katalysiert, wird in Homogenaten der Niere zum groBten Teil i m 1OOOOOxg-Oberstand gefunden [39]. Neben dieser ,,loslichen" Form konnen wir eine an die Plasmamembranen gebundene Guanylat-Cyclase-Fraktion nachweisen.…”

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Einfluß verschiedener Hormone auf die Bildung von Adenosin‐3′ : 5′‐monophosphat und Guanosin‐3′: 5′‐monophosphat durch partikuläre Präparationen aus der Rattenniere

Schultz

Jakobs²,

Böhme³

et al. 1972

European Journal of Biochemistry

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Hormonal influences on the formation of adenosine 3': 5'-monophosphate (Ado-3': 5I-P) have been studied in particulate preparations from rat kidney. Adenylate cyclase activity has been determined by measuring labeled Ado-3': 5'-P formed from labeled ATP (1 mM) in the presence of Mg++ (10 mM) and an ATP regenerating system.Hormonal effects on adenylate cyclase obtained from different parts ofthe kidney were found to correspond with the known tubular sites of action of these hormones in micropuncture studies. -Parathyroid hormone and thyrocalcitonin which are known to inhibit the reabsorption of inorganic phosphate in the proximal part of the renal tubule, increased the activity of adenylate cyclase obtained from renal cortex. The influence of these hormones on medullary adenylate cyclase activity was very small. Cortical adenylate cyclase activity was increased by parathyroid hormone in concentrations as low as 3 nM. A maximum 4.5-fold stimulation occurred with 10 pM parathyroid hormone. Over the same concentration range, thyrocalcitonin stimulated cortical adenylate cyclase. I n contrast to parathyroid hormone, maximal stimulation by thyrocalcitonin was only 2.5-fold. -The permeability for water of the distal convoluted tubules and the collecting ducts of the rat kidney is known to be increased by antidiuretic hormone. This hormone (Lysa-vasopressin) as well as oxytocin stimulated both cortical and medullary adenylate cyclase. The enzyme prepared from the medulla of rats with a hereditary hypothalamic diabetes insipidus (Bratteboro strain) was activated up to 4-fold by the addition of lysine vasopressin in concentrations between and 10-6 M. For comparable stimulation by oxytocin about 50 times higher concentrations were necessary than of lysine vasopressin. This finding corresponds to the lower antidiuretic potency of oxytocin compared to antidiuretic hormone. -By addition of neurohypophyseal hormones as well as of parathyroid hormone or thyrocalcitonin in very high concentrations, medullary and cortical adenylate cyclase activities were decreased compared to the activities measured in the presence of maximally effective hormone amounts. Trichlorisobutanol, which is used as a preservative in hormone preparations, caused no decrease in enzyme activity. -When antidiuretic hormone was added a t a maximally effective concentration to a cortical adenylate cyclase preparation in combination with parathyroid hormone or thyrocalcitonin a t nearly maximally effective concentrations, the effects of the hormones were essentially additive.Prostaglandin E, known to influence the permeability for water in the urinary bladder of the toad and in collecting ducts from mammalian kidneys, had no significant effect on medullary adenylate cyclase activity when added in concentrations between 3 -10-lo and 3 * lop6 M.Prostaglandin El was also without effect in the presence of lysine vasopressin (25 nM). Neither isoproterenol nor noradrenaline (50 pM) altered medullary adenylate cyclase activity although adrenergic stimulating agents h...

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Guanyl cyclase. Determination of enzyme activity

Cited by 110 publications

References 7 publications

Second Messenger System in Neoplasia

Second Messenger System in Neoplasia

Lead citrate method of guanylate cyclase and its application to tissue receiving rapid freeze substitution fixation.

Einfluß verschiedener Hormone auf die Bildung von Adenosin‐3′ : 5′‐monophosphat und Guanosin‐3′: 5′‐monophosphat durch partikuläre Präparationen aus der Rattenniere

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