Which group of hormones interact with membrane bound receptors and use second messengers?

Understanding:

•  Steroid hormones bind to receptor proteins in cytoplasm of target cells to form a receptor-hormone complex

•  The receptor-hormone complex promotes the transcription of specific genes

    
Steroid Hormones

• Steroid hormones are lipophilic (fat-loving) – meaning they can freely diffuse across the plasma membrane of a cell
• They bind to receptors in either the cytoplasm or nucleus of the target cell, to form an active receptor-hormone complex
• This activated complex will move into the nucleus and bind directly to DNA, acting as a transcription factor for gene expression
• Examples of steroid hormones include those produced by the gonads (i.e. estrogen, progesterone and testosterone)

Understanding:

•  Peptide hormones bind to receptors in the plasma membrane of the target cell

•  Binding to membrane receptors activates a cascade mediated by a second messenger inside the cell

    
Peptide Hormones

• Peptide hormones are hydrophylic and lipophobic (fat-hating) – meaning they cannot freely cross the plasma membrane
• They bind to receptors on the surface of the cell, which are typically coupled to internally anchored proteins (e.g. G proteins)
• The receptor complex activates a series of intracellular molecules called second messengers, which initiate cell activity
• This process is called signal transduction, because the external signal (hormone) is transduced via internal intermediaries
• Examples of second messengers include cyclic AMP (cAMP), calcium ions (Ca2+), nitric oxide (NO) and protein kinases
• The use of second messengers enables the amplification of the initial signal (as more molecules are activated)

  Vagalnociceptors express severaltransient receptor potential (TRP) channels. Capsaicin and temperature-sensitivetransient receptor potential vanilloid-1 (TRPV1) receptors are directly activated by capsaicin, used commonly as a tussive agent in clinical studies of cough; these receptors are additionally sensitized or indirectly activated by heat, protons, bradykinin, arachidonic acid derivatives,adenosine triphosphate (ATP), and phosphokinase C. TRPV4 is osmotically sensitive and mostly found on epithelial cells but also on a subset of vagal sensory nerve fibers, whereas TRP ankyrin 1 is often coexpressed with TRPV1 on many vagal nociceptors in the airways and is activated by allyl isothiocyanate (mustard oil), cinnamaldehyde (from cinnamon), and acrolein (from cigarette smoke). C fibers also express tetrodotoxin-insensitive voltage-gated sodium channels, many G protein–coupled receptors for inflammatory mediators, and receptors for neurotrophins, such as nerve growth factor.

  Vagalmechanosensors are thought to express mechanically gated membrane ion channels that are unique to this class of airway sensory fibers but have yet to be identified. In addition, they have other channels that can be activated by acids and belong to theacid-sensing ion channel (ASIC) family. They possess different types of voltage-sensitive ion channels needed for action potential formation and conduction, including the NaV1.7 subtype of voltage-gated sodium channels, characterized by sensitivity to the neurotoxin tetrodotoxin. However, the vagal mechanosensors lack several TRP channels found in vagal nociceptors, although these TRP channels may be induced during inflammation.

  Both nociceptors and mechanosensors often also express receptors for ATP and other purines. Of note, P2X2 and P2X3 purinergic receptors can be expressed alone or in combination, and it is thought that local release of ATP from the injured or inflamed airways is a major contributor to cough hypersensitivity syndrome acting via these receptors.3

  Membrane Receptors

  Philip L. Yeagle, in The Membranes of Cells (Third Edition), 2016

  15.10 Highlights

  Cell plasma membranes (and a few intracellular membranes as well) contain membrane receptors. These receptors mediate signal transduction for cellular responses to extracellular stimuli. Membrane receptors are usually transmembrane proteins. Transmembrane proteins with part of their mass on both sides of the membrane are poised structurally to transmit information from one side of the membrane to the other.

  The domain of the receptor exposed to the external medium often has a binding site for a ligand. Ligands can be hormones, neurotransmitters, lipoproteins, transferrins, extracellular matrix, and a wide variety of other molecules. The domain of the receptor exposed to the cytoplasm has functionality to activate intracellular proteins such as kinases, G proteins, guanylate cyclase, ion transporters, among a myriad of other functionalities. In general ligand binding to the extracellular domain causes conformational changes that are transmitted to the intracellular domain and initiate intracellular changes as a result.

  The LDL receptor and transferrin receptors are examples of receptors that function by receptor-mediated endocytosis. The LDL receptor is a transmembrane protein of the plasma membrane. Occupancy of the ligand binding site of the LDL receptor in the extracellular domain of the receptor by LDL initiates endocytosis. Clathrin-coated vesicles transport the receptor–LDL complex to endosomes within the cell. The receptor and LDL are separated and the LDL is ultimately catabolized, which can lead to regulation of cholesterol biosynthesis while the receptor can be recycled to the cell surface.

  The insulin receptor is a transmembrane protein in the plasma membrane functioning as a dimer. The insulin receptor modulates the cellular response to insulin, through insulin binding to the extracellular domain of the receptor. Insulin binding stimulates kinase activity that leads, among other results, to the autophosphorylation of the receptor. One of the responses of cells to activation of the insulin receptor is the recruitment of glucose transporters to the plasma membrane leading to increased glucose transport into the cell.

  The nicotinic acetylcholine receptor is a transmembrane protein consisting of five subunits. The receptor is a ligand-gated cation channel that responds to the neurotransmitter, acetylcholine, at the synapse between nerve and muscle. Occupancy of the ligand binding site by acetylcholine leads to an opening of the sodium channel (that is part of the receptor) and a depolarization of the plasma membrane.

  Integrins are receptors in the plasma membranes of cells. They are multisubunit transmembrane proteins. They have large extracellular domains, consisting of individually structured subdomains covalently linked by flexible linkers. The transmembrane domain is a single α-helix and the intracellular domain is small. Integrins play a major role in cellular attachment to extracellular matrix proteins. Intracellular responses include tyrosine kinase activation and modulation of intracellular calcium.

  G-protein coupled receptors are a large class of important cell surface receptors. They have become major drug targets. These receptor systems consist of three major components: the ligand, the transmembrane receptor, and the G protein. G-protein coupled receptors are usually found in the plasma membrane. The receptor binds a ligand from outside the cell. This binding causes a conformational change in the receptor such that the conformation of the cytoplasmic face of the receptor is altered. The receptor can then bind the G protein, a heterotrimer from the inside of the cell. These G proteins become activated after binding to an activated receptor. The subunits of the G proteins disassociate, and the Gα subunit and separately the Gβγ subunit activate target proteins to alter behavior of the cell. Target enzymes include phospholipases, adenylate cyclase, and phosphodiesterases, among others.

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  Signal Transduction, Membrane Receptors, Second Messengers, and Regulation of Gene Expression

  Bruce M. Koeppen MD, PhD, in Berne and Levy Physiology, 2018

  Receptors

  All signaling molecules bind to specific receptors that act as signal transducers, thereby converting a ligand-receptor binding event into intracellular signals that affect cellular function. Receptors can be divided into four basic classes on the basis of their structure and mechanism of action: (1)ligand-gated ion channels, (2)G protein–coupled receptors (GPCRs), (3)enzyme-linked receptors, and (4)nuclear receptors (Table 3.1;Figs. 3.4 and3.5).

  Ligand-gated ion channels mediate direct and rapid synaptic signaling between electrically excitable cells (seeFig. 3.4A). Neurotransmitters bind to receptors and either open or close ion channels, thereby changing the ionic permeability of the plasma membrane and altering the membrane potential. For examples and more details, seeChapter 6.

  GPCRs regulate the activity of other proteins, such as enzymes and ion channels (seeFig. 3.4B). In the example inFig. 3.4B, the interaction between the receptor and the target protein is mediated by heterotrimeric G proteins, which are composed of α, β, and γ subunits. Stimulation of G proteins by ligand-bound receptors activates or inhibits downstream target proteins that regulate signaling pathways if the target protein is an enzyme or changes membrane ion permeability if the target protein is an ion channel.

  Enzyme-linked receptors either function as enzymes or are associated with and regulate enzymes (seeFig. 3.4C). Most enzyme-linked receptors are protein kinases or are associated with protein kinases, and ligand binding causes the kinases to phosphorylate a specific subset of proteins on specific amino acids, which in turn activates or inhibits protein activity.

  Nuclear receptors are small hydrophobic molecules, including steroid hormones, thyroid hormones, retinoids, and vitamin D, that have a long biological half-life (hours to days), diffuse across the plasma membrane, and bind to nuclear receptors or to cytoplasmic receptors that, once bound to their ligand, translocate to the nucleus (seeFig. 3.5). Some nuclear receptors, such as those that bind cortisol and aldosterone, are located in the cytosol and enter the nucleus after binding to hormone, whereas other receptors, including the thyroid hormone receptor, are located in the nucleus. In both cases, inactive receptors are bound to inhibitory proteins, and binding of hormone results in dissociation of the inhibitory complex. Hormone binding causes the receptor to bind coactivator proteins that activate gene transcription. Once activated, the hormone-receptor complex regulates the transcription of specific genes. Activation of specific genes usually occurs in two steps: an early primary response (≈30 minutes), which activates genes that stimulate other genes to produce a delayed (hours to days) secondary response (seeFig. 3.5). Each hormone elicits a specific response that is based on cellular expression of the cognate receptor, as well as on cell type–specific expression of gene regulatory proteins that interact with the activated receptor to regulate the transcription of a specific set of genes (seeChapter 38 for more details). In addition to steroid receptors that regulate gene expression, evidence also suggests the existence of membrane and juxtamembrane steroid receptors that mediate the rapid, nongenomic effects of steroid hormones.

  Allosteric Regulation

  Barry S. Cooperman, in Encyclopedia of Biological Chemistry, 2004

  Cell-Surface Receptors Involved in Signal Transduction

  Membrane receptors for transmitters, peptides, and pharmacological agents are central to signal transduction. They selectively recognize chemical effectors (neuronal or hormonal) and allosterically transduce binding recognition into biological action though the activation of ligand-gated ion channels (LGICs) and/or G-protein-coupled receptors (GPCRs). Various features of membrane receptors for neurotransmitters are well accommodated by the MWC model. These receptor proteins are typically heterooligomers and exhibit transmembrane polarity. In general, the regulatory site to which the neurotransmitter binds is exposed to the synaptic side of the membrane while the biologically active site is either a transmembrane ion channel, a G protein-binding site, or a kinase-catalytic site facing the cytoplasm. Interactions between the two classes of sites are mediated by a transmembrane allosteric transition. Signal transduction or activation is mediated by a concerted cooperative transition between a silent resting state and an active state. Agonists stabilize the active state and competitive antagonists the silent state, and partial agonists may bind nonexclusively to both. These receptors can also undergo a cascade of slower, discrete allosteric transitions, which include refractory regulatory states that result in the desensitization or potentiation of the physiological response.

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  Membrane Receptors and Signal Transduction

  John W. Baynes PhD, in Medical Biochemistry, 2019

  Membrane receptors couple to signaling pathways utilizing diverse mechanisms

  Some membrane receptors - for example, the β-adrenergic receptors or the antigen receptors on lymphocytes - have no intrinsic catalytic activity and serve simply as specific recognition units. These receptors use a variety of mechanisms, including adaptor molecules or catalytically active regulatory molecules such asG-proteins (guanosine triphosphatases [GTPases], which hydrolyze GTP) to couple them to their effector signaling elements, which are generally enzymes (often called signaling enzymes or signal transducers), or ion channels (Fig. 25.2). In contrast, other receptors (e.g., the intrinsic tyrosine kinase receptors for insulin and many growth factors; the intrinsic serine kinase receptors for molecules such as transforming growth factor-β) have extracellular ligand-binding domains and cytoplasmic catalytic domains. After receptor ligation, these receptors can directly initiate their signaling cascades by phosphorylating and modulating the activities of target signal-transducing molecules (downstream signaling enzymes). These in turn propagate the growth factor signal by modulating the activity of further specific signal transducers or transcription factors, leading to gene induction (Chapter 23). Furthermore, sensory systems such as vision (Chapter 39), taste, and smell use similar mechanisms of cell-surface membrane receptor–coupled signal transduction (Table 25.1).

  Allosteric Regulation

  B.S. Cooperman, in Encyclopedia of Biological Chemistry (Second Edition), 2013

  Cell-Surface Receptors Involved in Signal Transduction

  Membrane receptors for transmitters, peptides, and pharmacological agents are central to signal transduction. They selectively recognize chemical effectors (neuronal or hormonal) and allosterically transduce binding recognition into biological action though the activation of ligand-gated ion channels (LGICs) and/or G-protein-coupled receptors (GPCRs). Various features of membrane receptors for neurotransmitters are well accommodated by the MWC model. These receptor proteins are typically heterooligomers and exhibit transmembrane polarity. In general, the regulatory site to which the neurotransmitter binds is exposed to the synaptic side of the membrane while the biologically active site is either a transmembrane ion channel, a G-protein-binding site, or a kinase-catalytic site facing the cytoplasm. Interactions between the two classes of sites are mediated by a transmembrane allosteric transition. Signal transduction or activation is mediated by a concerted cooperative transition between a silent resting state and an active state. Agonists stabilize the active state and competitive antagonists the silent state, and partial agonists may bind nonexclusively to both. These receptors can also undergo a cascade of slower, discrete allosteric transitions, which include refractory regulatory states that result in the desensitization or potentiation of the physiological response.

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  Aldosterone

  Anastasia S. Mihailidou, ... Anthony W. Ashton, in Vitamins and Hormones, 2019

  4.1 Mineralocorticoid Receptor

  Membrane receptors have been identified for several of the steroid hormones. For many years there has been healthy debate on whether the non-genomic actions of aldosterone were mediated by an MR at the plasma rather than the intracellular receptor since these actions were not prevented by MR antagonists spironolactone or canrenone and not mimicked by cortisol (Gekle, Silbernagl, & Wunsch, 1998; Grossmann et al., 2010; Le Moellic et al., 2004; Wehling et al., 1991; Wildling, Hinterdorfer, Kusche-Vihrog, Treffner, & Oberleithner, 2009). While there have been intense attempts to isolate and characterize the membrane receptor for aldosterone, the identity eluded characterization until recently. This was possibly due to early studies using bovine serum albumin (BSA)-coupled aldosterone (Gekle et al., 1998; Le Moellic et al., 2004) which did not consider that BSA can dissociate from aldosterone. In separate studies, atomic force microscopy technology (Wildling et al., 2009) or fluorescence resonance energy transfer (Grossmann et al., 2010) was used; however, the specific location in the plasma membrane could not be identified. We and others have shown that for heart (Mihailidou et al., 1998) and vascular smooth muscle cells (Alzamora, Michea, & Marusic, 2000), the rapid actions of aldosterone were prevented by the MR antagonists suggesting involvement of the intracellular MR.

  In further studies (Ashton et al., 2015) we succeeded in separating the non-genomic from genomic signaling by using an aldosterone analog, aldosterone-3-carboxymethoxylamine-TFP ester conjugated to methoxypegylated amine (Aldo-PEG) (Fig. 4). While having similar structure to aldosterone, Aldo-PEG has a larger molecular size and the hydrophilic nature of pegylated amine results in preventing membrane permeability which we confirmed in fractionated H9c2 cells (Fig. 5). In the absence of aldosterone, MR is localized predominantly in the cytoplasm rather than nucleus. While addition of aldosterone changed this distribution from cytoplasm to nuclear MR, whereas the Aldo-PEG did not change subcellular localization, confirming that it cannot enter the cell.

  

  Fig. 4. Structure of aldosterone analog. Aldosterone-3-carboxymethoxylamine-TFP ester conjugated to methoxypegylated amine (Aldo-PEG, MW 40,000) compared to aldosterone (MW 360.44), similar in structure to aldosterone but membrane impermeable.

  Adapted from Ashton, A. W., Le, T. Y., Gomez-Sanchez, C. E., Morel-Kopp, M. C., McWhinney, B., Hudson, A., et al. (2015). Role of nongenomic signaling pathways activated by aldosterone during cardiac reperfusion injury. Molecular Endocrinology, 29(8), 1144–1155. doi:10.1210/ME.2014-1410.

  

  Fig. 5. Subcellular distribution of MR and GPER. Representative immunoblots for distribution of MR and GPER in H9c2 cells during exposure to Aldo (10 nM) or Aldo-PEG (10 nM) for 4 h. Total protein, membrane, cytosolic, and nuclear protein fractions were extracted and subjected to immunoblot analysis. As markers of membrane, cytosol and nuclear extracts we used aquaporin-1, α-tubulin, and histone H1.

  Reproduced with permission Ashton, A. W., Le, T. Y., Gomez-Sanchez, C. E., Morel-Kopp, M. C., McWhinney, B., Hudson, A., et al. (2015). Role of nongenomic signaling pathways activated by aldosterone during cardiac reperfusion injury. Molecular Endocrinology, 29(8), 1144–1155. doi:10.1210/ME.2014-1410.

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  Regulation of Hemostasis and Thrombosis

  Maureane Hoffman, in Cardiac Intensive Care (Second Edition), 2010

  Platelets

  Membrane receptors for collagen and other subendothelial and extravascular matrix proteins are present on the platelet membrane and mediate binding of unactivated platelets at sites of injury.3-5 Platelet binding is also mediated by von Willebrand factor (vWF) bridging between collagen and the platelet receptor glycoprotein (GP) Ib. These receptor binding events also transmit an activation signal to the platelets. Full platelet activation also requires stimulation by thrombin, however, which is produced as the coagulation reactions are initiated. The platelet surface receptor for fibrinogen, GPIIb/IIIa, rapidly changes conformation from an inactive to an active form on platelet activation.6 This change in conformation allows platelet aggregates to be stabilized by binding to fibrinogen even before conversion to fibrin begins. Platelet activation also initiates the synthesis of prostaglandins and thromboxanes—compounds that modulate platelet activation and promote vasoconstriction.7

  Platelet adhesion and activation at a site of injury, in concert with local vasoconstriction, provides initial hemostasis for small caliber vessels. When hemostasis is achieved by these mechanisms, the subsequent stabilization of the platelet plug in a fibrin meshwork can proceed more effectively than if bleeding continues. Initial hemostasis may be established even if a deficiency of plasma coagulation proteins is present. The platelet plug is insufficient, however, to provide long-term hemostasis, and delayed rebleeding occurs if it is not reinforced by a stable fibrin clot during secondary hemostasis.

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  Regulation of Hemostasis and Thrombosis

  Maureane Hoffman, in Cardiac Intensive Care (Third Edition), 2019

  Platelets.

  Membrane receptors for collagen (glycoprotein [GP] VI) and other subendothelial and extravascular matrix proteins are present on the platelet membrane and mediate binding of unactivated platelets at sites of injury.3–5 Platelet binding is also mediated by von Willebrand factor (vWF) bridging between collagen and the platelet receptor GP Ib. These receptor-binding events also transmit an activation signal to the platelets. Full platelet activation also requires stimulation by thrombin that is produced as the coagulation reactions are initiated. The platelet surface receptor for fibrinogen, GPIIb/IIIa, rapidly changes conformation from an inactive to an active form on platelet activation.6 This conformational change allows platelet aggregates to be stabilized by binding to fibrinogen even before conversion to fibrin begins.

  Platelet activation also initiates the synthesis of prostaglandins and thromboxanes—compounds that modulate platelet activation and promote vasoconstriction.7 Platelet adhesion and activation at a site of injury, in concert with local vasoconstriction, provides initial hemostasis for small-caliber vessels. Once hemostasis is achieved by these mechanisms, the subsequent stabilization of the platelet plug in a fibrin meshwork can proceed more effectively than if bleeding continues. Initial hemostasis may be established even if a deficiency of plasma coagulation proteins is present. The platelet plug is insufficient, however, to provide long-term hemostasis and delayed rebleeding occurs if it is not reinforced by a stable fibrin clot during secondary hemostasis. Even after overt bleeding (loss of red blood cells) is stopped by the stable fibrin clot, leakage of plasma proteins from the microvasculature continues. A hemostatic clot structure with a densely packed core of platelets is required to form a tight vascular seal that minimizes the leakage of plasma proteins at a site of injury.8

  It is becoming clear that, in addition to providing primary hemostasis following an overt injury, platelets also play more complex and subtle roles in maintaining vascular integrity. It has long been known that platelets maintain endothelial integrity in the microvasculature.9 A failure of this function is responsible for petechiae resulting from thrombocytopenia. However, platelets also directly prevent microvascular bleeding at sites of inflammation10 and angiogenesis11 by mechanisms that are independent of fibrin generation.12

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  Volume I

  J. Larry Jameson, in Endocrinology: Adult and Pediatric (Seventh Edition), 2016

  Membrane Receptors

  Membrane receptors can be divided into several major groups (Fig. 1-7): (1) seven transmembrane domain G protein–coupled receptors (GPCRs), (2) tyrosine kinase receptors, (3) cytokine receptors, and (4) transforming growth factor-beta (TGF-β) family serine kinase receptors. There are several hundred GPCRs.25 They bind a broad array of hormones, including large proteins (e.g., TSH, PTH), small peptides (e.g., TRH, somatostatin), catecholamines (epinephrine, dopamine), and even minerals (e.g., calcium). These receptors possess seven transmembrane-spanning regions composed of hydrophobic α-helical domains that are connected by extracellular and intracellular loops. After the receptor binds a hormone, these transmembrane domains undergo conformational changes that alter interactions with intracellular G proteins. The G proteins provide a link to intracellular signaling pathways such as adenyl cyclase, phospholipase C, mitogen-activated protein kinases (MAPK), and others. G proteins form a heterotrimeric complex that is composed of various Gα and Gβ-γ subunits. The α subunit contains the guanine nucleotide–binding site and hydrolyzes GTP to GDP. Gα is active when GTP is bound and inactive after hydrolysis to GDP. The β-γ subunits modulate activity of the α subunit and mediate their own effector-signaling pathways. A variety of endocrinopathies result from G protein mutations or from mutations in receptors that modify their interactions with G proteins. For example, McCune-Albright syndrome is caused by somatic mutations in Gα that prevent GTP hydrolysis, thereby causing constitutive activation of the Gα-signaling pathway. Selected mutations in the transmembrane domains of GPCRs can mimic hormone-induced conformational changes, leading to activation of G proteins independent of hormone binding. This type of mutation in the TSH receptor accounts for a significant fraction of solitary autonomously functioning thyroid nodules. Activating mutations in the LH receptor cause LH-independent precocious puberty in boys.

  Tyrosine kinase receptors transmit signals for insulin and a variety of growth factors, such as IGF-1, epidermal growth factor, platelet-derived growth factor, and fibroblast growth factors. Ligand binding induces autophosphorylation, leading to interactions with intracellular adaptor proteins such as Shc and insulin receptor substrates (IRS). Depending on the receptor and adaptor complexes, one or more kinases, including the Raf-Ras-MAPK and the Akt/protein kinase B pathways, are activated. The tyrosine kinase receptors play a prominent role in cell growth and differentiation, as well as in intermediary metabolism.

  The GH and PRL receptors belong to the cytokine receptor family. Ligand binding induces receptor interactions with intracellular kinases such as the Janus kinases (JAKs), which phosphorylate members of the signal transduction and activators of transcription (STAT) family, and other signaling pathways (Ras, PI3-K, MAPK). The activated STAT proteins translocate to the nucleus and stimulate expression of target genes.

  The TGF-β receptor family mediates the actions of TGF-βs, activins, Müllerian inhibiting substance (MIS; also known as anti-Müllerian hormone), and bone morphogenic proteins. This receptor family consists of type I and II subunits, which undergo autophosphorylation after ligand binding. The phosphorylated receptors bind intracellular Smads (named for a fusion of terms for Caenorhabditis elegans sma + mammalian mad). Like the STAT proteins, the Smads serve a dual role of transducing the receptor signal and acting as transcription factors.

  Which hormone interact with membrane bound receptors and generate second messenger?

  Reason: Insulin is a peptide hormone which can easily pass cell membrane to interact with hormone-receptor complex. Q. Assertion :Hormones interacting with cell surface receptors do not enter the target but they generate secondary messengers.

  What type of hormones use 2nd messengers?

  Some of the hormones that achieve their effects through cAMP as a second messenger:.

  adrenaline..

  glucagon..

  luteinizing hormone (LH).

  Which hormone binds with membrane bound receptors?

  1: Second messenger systems: The amino acid-derived hormones epinephrine and norepinephrine bind to beta-adrenergic receptors on the plasma membrane of cells.