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For a specific neurotransmitter to respond to a chemical or hormone, the target cell must have a specific neurotransmitter receptor protein or hormone. Cells act on a special hormone or neurotransmitter that does not have these receptor proteins. The management of molecular interactions with receptor proteins has a very specific fashion, similar to enzyme-specific proteins seen in or carrier proteins.
Receptor proteins are not enzymes, but they do not do transport regulators to break down molecules into target cells. In contrast, the receptor protein molecule has a high affinity for regulation and binds to create specific changes in the target cell. These alterations can undergo many changes in specific membrane permeability, changes in enzyme activity, or changes in gene expression.
Protein receptors lipid-soluble hormones (steroid hormones, thyroid hormones) are located in target cell grounds. Other hormone receptors and neurotransmitters, however, are located in the cell membrane of the target cell. In this case, the binding site of the receptor extracellular fluid is regulated and the receptor molecule can not enter the target cell.
This can lead to altered membrane permeability, or it may lead to the production of chemicals within the target cell, more directly regulating the effects on hormones or neurotransmitters.
Regardless of whether a particular chemical acts as a neurotransmitter or hormone, in order to achieve physiological regulation, there must be a mechanism to turn off the action regulators. Physiological control is impossible without a "off switch." This process includes rapid removal or chemical inactivation of regulated molecules.
This occurs to a large extent ** the target cells and nerve endings, but it may also contain (cases of hormones) metabolically inactivating other organs, such as the liver, releasing active hormones in the blood. As a result, a negative feedback control that continuously activates the corresponding response must maintain a given response and can be balanced.
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In response to specific neurotransmitters and hormones, target cells must have specific receptor proteins, neurotransmitters and hormones. Cells are not targeted for action, and a particular hormone or neurotransmitter does not have these receptor proteins. Receptor-protein interactions with regulatory molecules in a very specific way, similar to those seen in enzyme-specific proteins or proteins.
Receptor proteins do not have enzymes, however: do not put regulatory molecules into the target cell. In contrast, receptor proteins bind regulatory molecules with high affinity, by binding, initiating specific changes in target cells.
These changes may involve changes in membrane permeability of specific ions, changes in enzyme activity, or changes in gene expression. Receptor protein lipid-soluble hormones (steroid hormones and thyroid hormones) are located in target cells. Among other hormone receptors and neurotransmitters, however, are located in the cell membrane of the target cell.
In these cases, the extracellular fluid facing the receptor at the binding site allows the regulatory molecule to bind to the receptor into the target cell. This can lead to alterations in cell membrane permeability and may also lead to the production of hormones or neurotransmitters by target cells that are chemically more directly regulated. Whether a particular chemical is acting as a neurotransmitter or as a hormone, there must be a mechanism to enable physiological regulation to shut down the regulator of action.
Physiological control is not possible without a "off switch." This process involves the rapid removal or chemical inactivation of regulatory molecules. This occurs primarily in the field of targeted cells and nerve endings, but it can also involve metabolic inactivation (such as hormones) in other organs, such as the liver, that can remove active hormones from the bloodstream.
Therefore, the sustained activation effect, the response to negative feedback control must maintain a certain response, and the equilibrium can be maintained.
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