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By: X. Sibur-Narad, M.A., M.D.

Clinical Director, Touro College of Osteopathic Medicine


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The pressor response to pain treatment center of america order aspirin with visa stimulation of somatic afferent nerves is called the somatosympathetic reflex pain management for dogs otc purchase aspirin now. Receptors are also located in the walls of the right and left atria at the entrance of the superior and inferior venae cavae and the pulmonary veins pain treatment center seattle wa 100 pills aspirin with mastercard, as well as in the pulmonary circulation. These receptors in the low-pressure part of the circulation are referred to collectively as the cardiopulmonary receptors. The carotid sinus is a small dilation of the internal carotid artery just above the bifurcation of the common carotid into external and internal carotid branches (Figure 33­4). Some are also located in the dorsal motor nucleus of the vagus; however, this nucleus primarily contains vagal motor neurons that project to the gastrointestinal tract. Increased activity of arterial baroreceptors Expiration Fear Grief Stimulation of pain fibers in trigeminal nerve wall of the arch of the aorta. The afferent nerve fibers from the carotid sinus form a distinct branch of the glossopharyngeal nerve, the carotid sinus nerve. The fibers from the aortic arch form a branch of the vagus nerve, the aortic depressor nerve. The baroreceptors are stimulated by distention of the structures in which they are located, and so they discharge at an increased rate when the pressure in these structures rises. Their afferent fibers pass via the glossopharyngeal and vagus nerves to the medulla. Thus, increased baroreceptor discharge inhibits the tonic discharge of sympathetic nerves and excites the vagal innervation of the heart. These neural changes produce vasodilation, venodilation, a drop in blood pressure, bradycardia, and a decrease in cardiac output. A decline in pulse pressure without any change in mean pressure decreases the rate of baroreceptor discharge and provokes a rise in systemic blood pressure and tachycardia. At normal blood pressure levels (about 100 mm Hg mean pressure), a burst of action potentials appears in a single baroreceptor fiber during systole, but there are few action potentials in early diastole (Figure 33­5). At lower mean pressures, this phasic change in firing is even more dramatic with activity only occurring during systole. The threshold for eliciting activity in the carotid sinus nerve is about 50 mm Hg; maximal activity occurs at about 200 mm Hg. At carotid sinus perfusion pressures of 70­110 mm Hg, there is a near linear relationship between perfusion pressure and the fall in systemic blood pressure and heart rate. At perfusion pressures above 150 mm Hg there is no further increase in response, presumably because the rate of baroreceptor discharge and the degree of inhibition of sympathetic nerve activity are maximal. Dashed line: Response in a hypertensive monkey, demonstrating baroreceptor resetting (arrow). Any drop in systemic arterial pressure decreases the inhibitory discharge in the buffer nerves, and there is a compensatory rise in blood pressure and cardiac output. Any rise in pressure produces dilation of the arterioles and decreases cardiac output until the blood pressure returns to its previous normal level. In perfusion studies on hypertensive experimental animals, raising the pressure in the isolated carotid sinus lowers the elevated systemic pressure, and decreasing the perfusion pressure raises the elevated pressure (Figure 33­6). Little is known about how and why this occurs, but resetting occurs rapidly in experimental animals. It is also rapidly reversible, both in experimental animals and in clinical situations. The function of the receptors can be tested by monitoring changes in heart rate as a function of increasing arterial pressure during infusion of the -adrenergic agonist phenylephrine. Baroreceptors are very sensitive to changes in pulse pressure as shown by the record of phasic aortic pressure. This response pattern is called the Bezold­Jarisch reflex and was named after the individuals who first reported these findings. This reflex can be elicited by a variety of substances including capsaicin, serotonin, phenylbiguanide, and veratridine in cats, rabbits, and rodents.

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In addition pain management with shingles buy cheap aspirin 100pills line, however pain after lithotripsy treatment order aspirin us, a phospholipid has a polar phosphate group (a phosphorus atom bonded to pain treatment center llc buy aspirin 100pills otc three oxygen atoms) attached to one end of the molecule. Thus, phospholipids are said to have a polar "head" (containing phosphate) that is hydrophilic, and a nonpolar "tail" (containing hydrocarbon) that is hydrophobic. This stable arrangement is called a phospholipid bilayer, and it effectively isolates the cytosol of the neuron from the extracellular fluid. Protein the type and distribution of protein molecules distinguish neurons from other types of cells. The enzymes that catalyze chemical reactions in the neuron, the cytoskeleton that gives a neuron its special shape, and the receptors that are sensitive to neurotransmitters are all made up of protein molecules. The resting potential and action potential depend on special proteins that span the phospholipid bilayer. In order to perform their many functions in the neuron, different proteins have widely different shapes, sizes, and chemical characteristics. The phospholipid bilayer is the core of the neuronal membrane and forms a barrier to water-soluble ions. As mentioned in Chapter 2, proteins are molecules assembled from various combinations of 20 different amino acids. The differences among amino acids result from differences in the size and nature of these R groups (Figure 3. The properties of the R group determine the chemical relationships in which each amino acid can participate. In this process, amino acids assemble into a chain connected by peptide bonds, which join the amino group of one amino acid to the carboxyl group of the next (Figure 3. Proteins made of a single chain of amino acids are also called polypeptides (Figure 3. The primary structure is like a chain in which the amino acids are linked together by peptide bonds. As a protein molecule is being synthesized, however, the polypeptide chain can coil into a spiral-like configuration called an alpha helix. The alpha helix is an example of what is called the secondary structure of a protein molecule. Noted in parentheses are the common abbreviations used for the various amino acids. In this way, proteins can bend, fold, and assume a complex three-dimensional shape. Finally, different polypeptide chains can bond together to form a larger molecule; such a protein is said to have quaternary structure. The bond forms between the carboxyl group of one amino acid and the amino group of another. Regions where nonpolar R groups are exposed are hydrophobic and tend to associate readily with lipid. Regions with exposed polar R groups are hydrophilic and tend to avoid a lipid environment. Therefore, it is not difficult to imagine classes of rod-shaped proteins with polar groups exposed at either end but with only hydrophobic groups showing on their middle surfaces. This type of protein can be suspended in a phospholipid bilayer, with its hydrophobic portion inside the membrane and its hydrophilic ends exposed to the watery environments on either side. Each subunit has a hydrophobic surface region (shaded) that readily associates with the phospholipid bilayer. Ion channels are made from just these sorts of membrane-spanning protein molecules. Typically, a functional channel across the membrane requires that four to six similar protein molecules assemble to form a pore between them (Figure 3. The subunit composition varies from one type of channel to the next, and this is what determines their different properties. One important property of most ion channels, specified by the diameter of the pore and the nature of the R groups lining it, is ion selectivity. Likewise, sodium channels are permeable almost exclusively to Na, calcium channels to Ca2, and so on. Channels with this property can be opened and closed-gated-by changes in the local microenvironment of the membrane.


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