Chapter 20. Cell - Cell Signaling: Hormones and Receptors. Three general types of extracellular signaling. endocrine signaling. paracrine signaling
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1 Chapter 20 Cell - Cell Signaling: Hormones and Receptors Three general types of extracellular signaling endocrine signaling paracrine signaling autocrine signaling
2 Endocrine Signaling - signaling molecules (hormones) act on target cells distant from their site of synthesis Are affected if they express the appropriate hormone receptor Fig 20-1a Paracrine Signaling - signaling molecules released by a cell only affect target cells in close proximity. Fig 20-1b
3 Conduction of signals from one nerve cell to another across a synapse is a special example of paracrine signaling. Fig. 21-4a Autocrine Signaling - cells respond to substances that they themselves release. Fig 20-1c
4 Proteins attached to the plasma membrane of one cell can interact directly with receptors on an adjacent cell. Fig 20-1d Receptors Exhibit Two Types of Specificity (1) Ligand Specificity-which ligand(s) are bound. This is similar to the specificity of an enzyme for its substrate. (2) Effector Specificity-the response to ligand binding Same ligand binding to a receptor can have different effects in different cell types same ligand specificty, different effector specificity Different ligands binding to different receptors on the same cell can have the same effect different ligand specificity, same effector specificity
5 Hormones May Be Classified by Receptor Location Intracellular Receptors lipophilic molecules (hydrophobic) Steroids Thyroxine Retinoids Cell Surface Receptors -...may be hydrophilic Peptide Hormones - insulin, glucagon, growth factors Small Charged Molecules: e.g. epinephrine, histamine or lipophilic Prostaglandins Intracellular Receptors located in the cytosol -signaling molecules must be membrane permeable (lipophilic) -they are carried in the blood bound to carrier proteins Fig 20-2a
6 CH 3 CH 3 C O CH 3 O Progesterone, see page 851 Other examples include Thyroxine and Retinoic Acid Cell Surface Receptors-receptor must have mechanism to transmit signal across membrane -involves Second Messengers Fig 20-2b
7 Examples of second messengers Fig 20-4 TABLE 20-1 Characteristic Properties of Principal Types of Mammalian Hormones Property Steroids Thyroxine Peptides and Catecholamines Proteins Feedback regulation Yes Yes Yes Yes of synthesis Storage of preformed Very little Several weeks One day Several days, in Hormone adrenal medulla Mechanism of Diffusion through Proteolysis of Exocytosis of Exocytosis of Secretion plasma membrae thyroglobulin storage vesicles storage vesicles Binding to plasma Yes Yes Rarely No Proteins For transport in blood Lifetimein blood Hours Days Minutes Seconds Plasma Time course of action Hours to days Days Minutes to hours Seconds or less Receptors Cytosolic or nuclear Nuclear Plasma membrane Plasma membrane Mechanism of action Receptor-hormone complex controls Hormone binding Hormone binding transcription and stability of mrna s triggers synthesis causes change in of cytosolic second membrane potential messengers of triggers synthesis protein kinase of cytosolic second activity messengers Source: Adapted from E.L. Smith et al., 1983, Principles of Biochemistry: Mammalian Biochemistry, 6th ed., McGraw-Hill, p 358
8 Cell-surface receptors can be categorized into four major classes G protein-linked receptors Ion-channel receptors Receptors lacking intrinsic catalytic activity tyrosine kinase linked receptor Receptors with intrinsic enzymatic activity receptor serine/threonine kinases receptor tyrosine kinases (RTKs) G protein-linked receptors: ligand binding activates a G protein that in turn activates or inhibits an enzyme that generates a specific second messenger. Fig 20-3a
9 Ion-channel receptors: ligand binding changes the conformation of the receptor so that specific ions flow through it. Ligand-Gated Channel Fig 20-3b Tyrosine kinase-linked receptors (Receptors lacking intrinisic catalytic activity): ligand binding causes receptor monomers to dimerize; the dimeric receptor then activates a cytosolic protein tyrosine kinase. Fig 20-3c
10 Receptors with intrinsic catalytic activity -binding of ligand activates Catalysis; Receptor is also an enzyme Fig 20-3d Receptor Tyrosine Kinase Second messenger How are signals involving protein phosphorylation turned off? Basics of binding interactions R + H RH K D = [R][H] [RH] Text Page
11 Total Concentration of Receptors: [R T ] = [R] + [RH] Text Page K D = [R][H] [RH] Fraction of receptors with bound hormone: [RH] [R T ] = 1 1+ K D [H] In general, the K D value of a cell-surface hormone receptor approximates the blood level of its ligand. This equation is analogous to the Michaelis-Menton Equation that describes enzyme activity. K D is similar to a Michaelis Constant, K M H* H* H* H* H* [0.1] [1] [10] [100] [1000] Hormone radioactively labeled Cells with surface receptor Isolate cells and remove excess unbound hormone Fig 20-7 Measure radioactivity (amount of H* bound)
12 Total Concentration of Receptors RH K D R + H 1/2 of total Receptors Amount of H* Bound to cell Receptor K D = [R] [H] [RH] Amount of H* added K D affinity - how tightly does the receptor bind hormone (K D ) specificity - ability to distinquish a specific interaction from a nonspecific interaction. The K D values for two different receptor / hormone systems are indicated in the table below. Which exhibits the greatest binding Affinity? greatest binding Specificity? Epinephrine Histamine Greatest Affinity Epinephrine Receptor 1 nm 200 nm Greatest Specificity Histamine Receptor 5,000 nm 20 nm 5,000 nm/20 nm > 200 nm/1 nm
13 Required for Activity Table 20-2 Structure Structure of Typical Agonists and Antagonists of the B-Adrenergic Receptor K D for Binding to the Receptor Compound On Frog Erythrocytes Epinephrine 5 x 10-6 M Hormone Required for binding Agonist Isoproterenol 0.4 x 10-6 M Antagonists Alprenolol x 10-6 M Highest Affinity Propranolol x 10-6 M Practolol 21 x 10-6 M Maximum physiological response can be achieved before the receptor is saturated with Ligand. Fig 20-8
14 IP EP NEP IP EP NEP Fig : Comparison of the abilities of 3 catecholamines to activate adenylyl cyclase and to bind to cell-surface β-adrenergic receptors G protein - heterotrimeric guanine nucleotide-binding proteins that usually are linked to a seven-membrane spanning receptor on the cell surface. Fig 20-3a
15 General structure of a G protein-linked Receptor: Fig20-10 G-Proteins are Heterotrimers consisting of α, β, and γ subunits: β and γ subunits act as one unit and bind to α-subunits α subunits act on the effector molecule and are of two types G sα stimulates the effector when GTP is bound G iα inhibits the effector when GTP is bound γ β G sα or G iα GDP GTP
16 β-adrenergic Receptors Liver & Adipose Cells==> liberation of Glucose & FA s Heart Cells ==> Increased rate of contraction Intestinal Smooth Muscle ==> Relax α-adrenergic Receptors Blood vessels of intestinal tract, skin, kidneys ==> Arteries constrict limiting blood flow The net effect is: Increased blood flow to skeletal muscle and More fuel for the muscles, Glucose and FA s (Fatty Acids) Helix number α Agonists Inhibits (binds G i ) α 2 Adrenergic receptor β Agonists Activates (binds G s ) β 2 Adrenergic receptor β Agonists Activates (binds G s ) Chimeric receptor 1 α Agonists Activates (binds G s ) Chimeric receptor 2 β Agonists Inhibits (binds G i ) Chimeric receptor 3 Fig Region binding to G protein (compare chimeras 1 and 3) Conclusion Region binding to agonists (compare chimeras 1 and 2) Fig
17 β 1 & β 2 Adrenergic Receptors are Coupled to G s ==> Activates Adenylyl Cyclase α 2 Adrenergic Receptor are Coupled to G i ==> Inhibits Adenylyl Cyclase G sα γ β α Binding of hormone Produces conformational change in receptor G sα GDP Receptor binds to G sα protein G sα Binding to receptor induces a conformational change in G sα GDP bound to G sα is replaced by GTP and the subunit dissociates from G βγ Fig 20-16
18 G sα Binding to receptor induces a conformational change in G sα GDP bound to G sα is replaced by GTP and the subunit dissociates from G βγ γ β α α G sα GDP GTP G sα binds to adenylyl cyclase, activating synthesis of camp; hormone dissociates G sα β 1 & β 2 Adrenergic Receptors are Coupled to G s ==> Activates Adenylyl Cyclase Hydrolysis of GTP to GDP causes G sα to dissociate from adenylyl cyclase and bind to G βγ Fig G sα β 1 /β 2 α 2 Fig 20-18
19 Fig : Molecular Biology of the Cell 3 rd Ed Alberts et al. Garland Pub. Fig : Voet, Voet, & Pratt Regulation of Glycogen Phosphorylase by camp-dependent Protein Kinase
20 Glycogen phosphorylase Fig b: Degradation of glycogen. Fig 20-17: Effect of cholera toxin on cycling of G sα between the active and inactive forms
21 α 1 Adrenergic Receptor are Coupled to G q ==> Stimulates Phospholipase C (PLC) producing Diacylglycerol (DAG) and Inositol Trisphosphate IP3 Cytosol Inositol Phosphatidylinositol (PI) PI 4-phosphate (PIP) PI 4,5-bisphosphate (PIP 2 ) Fig a: Several second messengers are derived from phosphatidylinositol (PI) Inositol 1,4,5- trisphosphate (IP 3 ) Stimulated by Gq Figure 20-39: Elevation of cytosolic Ca++ via the inositol-lipid signaling pathway.
22 Fig 20-37: Intracellular transduction of an extracellular signal via a cascade of sequential reactions produces a large amplification of the signal. Changes in Enzyme activities Gene expresssion Cytoskeletal structures Fig 20-6
23 Receptor Tyrosine Kinases: ligand binding causes receptor monomers to dimerize; the dimeric receptor autophosphorylates. Fig Autophosphorylation Ras is a monomeric guanine nucleotide binding protein that interacts with RTK s. Like G α, Ras alternates between an active state with bound GTP and an inactive state with bound GDP. Both are molecular switches. Unlike G α, cycling of Ras requires two proteins: GEF and GAP Guanine Exchange Factor GTPase Activating Protein Fig 20-22
24 GEF - guanine nucleotide-exchange factor - binds to Ras-GDP complex, causing dissociation of the bound GDP. GTP binds spontaneously to empty Ras. GEF is usually delivered to Ras by an activated receptor. Lifetime of Ras-GTP ~ 1 min. Fig GAP- GTPase activating protein - activates GTPase activity of Ras; functions as an inhibitor by promoting formation of the inactive Ras-GDP complex Fig 20-22
25 Receptor monomer EGF GDP Inactive Ras Binding of hormone causes dimerization and autophosphorylation of tyrosine residues Dimeric receptor Fig Dimeric receptor Binding of GRB2 and Sos couples receptor to inactive Ras Sos SH3 GRB2 GDP GTP Sos promotes dissociation of GDP from Ras; GTP binds and Sos dissociates from active Ras Sos is a GEF Active Ras Signaling Sos SH3 GRB2 Fig 20-23
26 Receptor Tyrosine Kinases (RTK s) and Ras Ligands - soluble or membrane bound peptide/protein hormones NGF - Nerve Growth Factor PDGF - Platelet Derived Growth Factor FGF - Fibroblast Growth Factor EGF - Epidermal Growth Factor Insulin Ligand Binding stimulates Tyrosine Protein Kinase Activity Effects include... Regulation of Cell Proliferation and Differentiation Promotion of Cell Survival Modulation of Cellular Metabolism Mutant RTK s stimulate cell growth in absence of hormone => Cancer
27 GTPase superfamily Group of Guanine Nucleotide-Binding Proteins that cycle between... Inactive State with bound GDP Active state with bound GTP Examples: G α proteins Ras proteins Rab proteins -regulation vesicle fusion Rho proteins - regulate actin cytoskeleton
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