Physiology Ch. 5 exam review
Termini in questo insieme (27)
1) Signal 2) Reception 3) Transduction 4) Response 5) Termination
Whether the signaling molecule can pass through membranes on its own (small/hydrophobic = on demand) or cannot (large/hydrophilic = stored in vesicles).
Amino acid messengers, amine messengers, peptide/protein messengers, steroid messengers, eicosanoid messengers.
Hydrophilic neurotransmitters like glutamine, aspartate, glycine, and GABA, synthesized in the cytoplasm of neurons and stored in vesicles.
Dopamine, norepinephrine, and epinephrine; all derived from the amino acid tyrosine.
Translated as prepropeptides in rough ER, cleaved to propeptides, further processed in Golgi, then packaged in secretory vesicles for release.
Steroids are hydrophobic, diffuse through membranes easily, cannot be stored, and are synthesized on demand from cholesterol in smooth ER.
From membrane phospholipids or second messengers into arachidonic acid, then via COX or lipoxygenase pathways into prostaglandins, thromboxanes, leukotrienes.
Gap junctions (connexin protein channels allowing ion/metabolite passage) and juxtacrine signaling (direct cell surface protein contact).
Chemical messengers secreted and diffusing short distances to neighboring cells; examples include growth factors, clotting factors, cytokines.
A form of paracrine signaling where the source cell is also the target cell, often seen in development and cancer cells.
Hormones travel through the blood from source to distant target cells, often secreted by endocrine glands.
On the cell surface membrane or intracellularly in the cytoplasm or nucleus.
Hydrophobic signals bind cytoplasmic or nuclear receptors forming hormone-receptor complexes that regulate gene transcription via hormone response elements.
1) External docking site for ligand, 2) Transmembrane domain, 3) Cytoplasmic tail region.
Ion channel-linked receptors, G protein-linked receptors, enzyme-linked receptors.
Ligand binding changes receptor shape to open or close ion channels, converting chemical signals into electrical signals.
Ligand binding activates G-proteins that trigger intracellular signaling cascades; targeted by ~60% of prescription drugs.
They act as enzymes or associate with enzymes inside the cell, often phosphorylating proteins to trigger responses.
Signal concentration, number of receptors, and receptor affinity for the ligand.
Down-regulation: decrease in receptor number due to high signal levels; Up-regulation: increase in receptor number due to low signal levels.
Agonists bind receptors and cause a response; antagonists bind but do not cause a response, competing for receptor sites.
Small intracellular molecules triggered by receptor activation that amplify and relay the signal inside the cell.
cAMP (activates protein kinase A), cGMP (activates protein kinase G), IP3 (releases Ca2+ from ER), DAG (activates protein kinase C), Ca2+ ions.
Regulates processes like muscle contraction, synapses, blood clotting; binds calmodulin to activate enzymes; maintained at low cytosolic levels.
Change membrane potential, change metabolic rate, change gene expression.
Via negative feedback loops or enzymatic degradation of the signal, stopping receptor activation and ending the response.