Signal Transduction and Cell Locomotion
Signal Transduction Overview
- Definition: Signal transduction is the process by which a cell converts an external signal into a specific internal response.
- Steps Involved:
- Reception: A ligand binds to a receptor on the cell surface.
- Transduction: The signal is relayed and amplified inside the cell.
- Response: The cell executes a specific action based on the received signal.
Signal Molecule Interaction
- Non-Entering Ligand: A signal molecule (ligand) binds to a membrane receptor, causing a conformational change in the receptor, which activates intracellular signaling pathways. The ligand does not enter the cell.
Ligand Types
- Extracellular Ligand:
- Remains outside the cell and binds to integral membrane proteins (e.g., peptide hormones).
- Cytoplasmic Ligand:
- Composed of small or nonpolar molecules that diffuse across the cell membrane and bind inside the cell (e.g., steroid hormones like testosterone).
Receptor-Ligand Interactions
- Characteristics:
- Highly specific interactions, resembling enzyme-substrate interactions.
- Shape compatibility: Often described as a "lock-and-key" fit.
- Binding: Primarily non-covalent interactions including hydrogen and ionic bonds.
- Ligand binding triggers conformational changes in the receptor, similar to enzymatic reactions.
Levels of Signaling
- Local Signaling:
- Paracrine: Affects nearby cells.
- Autocrine: Affects the same cell that secreted it.
- Long Distance Signaling:
- Endocrine: Hormonal signals travel via the bloodstream to distant target cells.
Paracrine vs. Endocrine Hormones
- Paracrine Hormone: Short-distance signaling acts on nearby cells.
- Endocrine Hormone: Travels through the bloodstream and acts on distant cells.
Signal Amplification
- Definition: Enables a small number of ligands to activate a large number of intracellular molecules.
- Significance:
- Produces a strong internal response from a tiny external signal.
- Enhances the speed and magnitude of cellular responses.
G-Protein-Coupled Receptors (GPCRs)
- Structure:
- Consists of 7 transmembrane alpha-helices.
- Contains a ligand-binding domain (extracellular) and a G-protein interaction domain (intracellular).
- Function: Upon ligand binding, GPCRs activate G-proteins within the cell.
G-Proteins
- Structure:
- Composed of three subunits: alpha (α), beta (β), and gamma (γ).
- β and γ are tightly associated while α can detach when activated.
- Activation Cycle:
- GDP-bound α is inactive; GTP-bound α is active.
Mechanisms of G-Protein Signal Transduction
- Ligand binds to GPCR.
- GPCR undergoes conformational change.
- GPCR activates G-protein by exchanging GDP for GTP on the α subunit.
- The activated α subunit dissociates from the βγ complex and interacts with target proteins (e.g., adenylyl cyclase).
cAMP: A Second Messenger
- Definition: Cyclic AMP (cAMP) is a second messenger involved in various signaling pathways.
- General Pathway:
- Active Gα activates adenylyl cyclase.
- Adenylyl cyclase converts ATP to cAMP.
- cAMP activates protein kinase A (PKA).
- PKA phosphorylates target proteins leading to a cellular response.
cAMP Regulation
- Adenylyl Cyclase: Produces cAMP when activated by Gα-GTP.
- cAMP Phosphodiesterase: Degrades cAMP to AMP, terminating the signal.
Key Enzyme Definitions
- Kinase: Adds a phosphate group to a molecule using ATP.
- Phosphorylase: Adds inorganic phosphate without using ATP.
- Phosphatase: Removes a phosphate group from a molecule.
- Glycogenesis (Synthesis):
- Converts glucose to glucagon for storage.
- Glycogenolysis (Breakdown):
- Converts glycogen back to glucose for energy.
Regulation of Glycogen Phosphorylase
- Mechanism: Activated by phosphorylation via PKA.
- Forms:
- Inactive: phosphorylase b (unphosphorylated)
- Active: phosphorylase a (phosphorylated)
Fight or Flight Response via Epinephrine
- Epinephrine binds GPCR on liver/muscle cells.
- GPCR activates Gα protein.
- Gα activates adenylyl cyclase.
- Adenylyl cyclase increases cAMP production.
- cAMP activates PKA leading to phosphorylation of key enzymes.
IP3/DAG Signaling Pathway
- Activation: Phospholipase C (PLC) activated by G-protein or RTK cleaves PIP2 forming IP3 and DAG.
- Effects:
- IP3 releases Ca2+ from the ER.
- DAG activates protein kinase C (PKC).
Calcium Signaling
- Basal levels of cytoplasmic [Ca2+]: ~10^-4 mM (low).
- [Ca2+] in ER/Extracellular: Higher than cytoplasm to control signaling.
- Calmodulin: A small protein with four binding sites for Ca2+. Changes conformation when Ca2+ binds, regulating other proteins.
Blood Vessel Structure
- Inner Layer: Endothelium (composed of endothelial cells).
- Middle Layer: Smooth muscle cells.
- Outer Layer: Connective tissue (collagen and elastin fibers).
Vasodilation vs Vasoconstriction
- Vasodilation: Relaxation of smooth muscle, resulting in vessel widening.
- Vasoconstriction: Contraction of smooth muscle, leading to vessel narrowing.
- Signal molecule binds to endothelial cells.
- Production of IP3 leads to Ca2+ release from the ER.
- Ca2+ binds to calmodulin.
- Activated calmodulin stimulates nitric oxide synthase (NOS).
- NOS produces NO.
- NO diffuses to smooth muscle cells.
- NO activates guanylyl cyclase converting GTP to cGMP.
- cGMP leads to muscle relaxation and vasodilation.
Role of cGMP-Phosphodiesterase
- Breaks down cGMP to GMP, terminating vasodilation and resulting in muscle contraction.
Effects of Nitroglycerin and Viagra
- Nitroglycerin: Increases NO production, enhancing vasodilation.
- Viagra: Inhibits cGMP-phosphodiesterase, preventing cGMP breakdown and prolonging vasodilation.
Enzyme-Coupled Receptors: RTKs
- Definition: Receptors with intrinsic enzyme activity or associated with an enzyme post-ligand binding.
- Structure: Extracellular domain for binding, single transmembrane helix, and an intracellular tyrosine kinase domain.
- Function: Dimerization and autophosphorylation activate downstream pathways.
Growth Factors and Signaling Pathway
- Definition: Signaling molecules that stimulate cell growth and differentiation (e.g., EGF, PDGF).
- Pathway Steps:
- Growth factor binds RTK.
- RTKs dimerize and autophosphorylate.
- Adaptor proteins bind phosphorylated tyrosines.
- Activate downstream pathways (e.g., RAS-MAPK) leading to growth.
Insulin/Glucagon System and Blood Glucose Regulation
- High blood sugar: Insulin promotes uptake and glycogenesis.
- Low blood sugar: Glucagon promotes glycogenolysis and gluconeogenesis.
Diabetes Overview
- Definition: Chronic high blood glucose levels due to insulin deficiency or resistance.
- Types:
- Type I: Autoimmune destruction of pancreatic β-cells.
- Type II: Insulin resistance mainly tied to lifestyle.
- Gestational diabetes: Temporary insulin resistance during pregnancy (Type II).
Cytoskeleton Functions
- Provides structure, organizes components, enables transport, powers movement, and is essential for division.
Cytoskeletal Elements
- Microtubules: Organize cell interior, transport vesicles, and form mitotic spindles. Diameter ~25 nm.
- Microfilaments: Maintain shape and drive movement. Diameter ~7 nm.
- Intermediate Filaments: Provide tensile strength and support. Diameter ~7-12 nm, varies by cell type.
Motor Proteins and Functions
- Kinesin: Moves toward the plus end; transports vesicles outward.
- Dynein: Moves toward the minus end; transports vesicles inward.
Cell Movement Types
- Intracellular movement (organelle transport).
- Whole-cell movement (crawling).
- Movement across surfaces (cilia-driven).
Cilia vs Flagella
- Cilia: Short, numerous, and beat to move fluids.
- Flagella: Long, few, propel cells (e.g., sperm).
Ciliary Structure
- Both have 9+2 arrangement of microtubules.
- Dynein arms facilitate movement by creating bending through inter-microtubule interaction.
- Cancer: Uncontrolled cell growth.
- Metastasis: Spread of cancer cells to other body parts.
- Mechanisms are similar: both leukocytes and cancer cells must migrate through endothelium, utilizing adhesion molecules and cytoskeletal changes.