Cyclic adenosine monophosphate, See

Corey lactol, 4 Cormethasone acetate, 194 Cormethasone acetate, 196 Cortisone, 176, 179 Cortivazol, 191 Cotinine, 235 Curare, 162 Cgclacillin, 439 Cgclazocine, 327 Cyclic adenosine monophosphate, see CAMP Cgclobendazole, 353 Cyclopropanation, 32, 166, 168, 174. 223, 297 Cgheptamide, 222 Cypenamine, 7 Cyprazepam, 402 Cyprolidol, 31 Cyproquinate, 368 Cyproterone acetate, 166 Cyproximide, 293... 

If MLCK activates contraction by increasing myosin phosphorylation, then an increase in the activity of myosin light chain phosphatase, MLCP, by decreasing the fraction of myosin which is phosphorylated, should lead to relaxation from the active (contractile) state. Cyclic adenosine monophosphate (AMP) is a strong inhibitor of smooth muscle contraction and it has been suggested that activation of MLCP could result from its phosphorylation via cAMP activated protein kinase (see Figure 5). 

To date, five subtypes of these receptors have been cloned. However, initial studies relied on the pharmacological effects of the muscarinic antagonist pirenzepine which was shown to block the effect of several muscarinic agonists. These receptors were termed Mi receptors to distinguish them from those receptors for which pirenzepine had only a low affinity and therefore failed to block the pharmacological response. These were termed M2 receptors. More recently, M3, M4 and M5 receptors have been identified which, like the Mi and M2 receptors occur in the brain. Recent studies have shown that Mi and M3 are located posts)maptically in the brain whereas the M2 and M4 receptors occur pres)maptically where they act as inhibitory autoreceptors that inhibit the release of acetylcholine. The M2 and M4 receptors are coupled to the inhibitory Gi protein which reduces the formation of cyclic adenosine monophosphate (cyclic AMP) within the neuron. By contrast, the Mi, M3 and M5 receptors are coupled to the stimulatory Gs protein which stimulates the intracellular hydrolysis of the phosphoinositide messenger within the neuron (see Figure 2.8). 

The activation of adenylyl cyclase enables it to catalyze the conversion of adenosine triphosphate (ATP) to 3 5 -cyclic adenosine monophosphate (cAMP), which in turn can activate a number of enzymes known as kinases. Each kinase phosphorylates a specific protein or proteins. Such phosphorylation reactions are known to be involved in the opening of some calcium channels as well as in the activation of other enzymes. In this system, the receptor is in the membrane with its binding site on the outer surface. The G protein is totally within the membrane while the adenylyl cyclase is within the membrane but projects into the interior of the cell. The cAMP is generated within the cell (see Rgure 10.4). 

Glucagon appears to exert its effects on liver cells by a classic adenyl cyclase-cyclic adenosine monophosphate (cAMP) second messenger system (see Chapter 4).93 Glucagon binds to a specific receptor located on the hepatic cell membrane. This stimulates the activity of the adenyl cyclase enzyme that transforms adeno-... 

Draw the structure of cyclic adenosine monophosphate icAMP). a mcssengCT involved in the regulation of glucose production in the body. Cyclic AMP has a phosphate ring connectii the 3 - and 5 -hydroxyl groups on adenosine. (See S [Pg.1212]

Phosphoenolpyruvate carboxykinase is induced. Oxaloacetate produces PEP in a reaction catalyzed by PEPCK. Cytosolic PEPCK is an inducible enzyme, which means that the quantity of the enzyme in the cell increases because of increased transcription of its gene and increased translation of its mRNA. The major inducer is cyclic adenosine monophosphate (cAMP), which is increased by hormones that activate adenylate cyclase. Adenylate cyclase produces cAMP from ATP. Glucagon is the hormone that causes cAMP to rise during fasting, whereas epinephrine acts during exercise or stress. cAMP activates protein kinase A, which phosphorylates a set of specific transcription factors (CREB) that stimulate transcription of the PEPCK gene (see Chapter 16 and Pig. 16.18). Increased synthesis of mRNA for PEPCK results in increased synthesis of the enzyme. Cortisol, the major human glucocorticoid, also induces PEPCK. 

A few observations establish the influence of bacterial components on animals, mainly protozoans. The ingestion of bacteria by protozoans may be controlled by secretions or constituent compounds of their preys. Unicellular organisms may even be able to choose the bacteria they feed on, avoiding such species as Chromobacterium or Serratia, which contain toxic or repulsive products (see Paoletti, 1964). Cyclic AMP (cyclic adenosine monophosphate), a well-known intra-cellular mediator, may play a role outside the cell, monitoring certain chemical communication systems. Chassy et al. (1969) observed that the slime mould Dictyostelum discoideum was attracted, in oligotrophic conditions, by C—AMP released by the bacteria on which it feeds. 

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