Membrane Transport Flashcards
- characteristics that affect permeability of molecules - membrane proteins & topology - examples of common membrane proteins - important differences btwn ion channels and transport proteins (carriers) - channels? how are they activated? - facilitated diffusion across plasma membrane - primary, secondary, tertiary active transport
membrane permeability and transport
- interior of lipid bilayer is hydrophobic -> passage of most polar molecules is restricted
- 15-30% of all membrane proteins are transport proteins
transport proteins
- transfer specific water/soluble molecules across plasma membrane
- the smaller the molecule and the less strongly associated with water, the more rapidly it diffuses across the membrane:
(most easily diffused to most difficult)
hydrophobic molecules: O2, CO2, N2, steroid hormones
small uncharged polar molecules: H2O, urea, glycerol
large uncharged polar molecules: glucose, sucrose
ions: H+, Na+, HCO-3, K+, Ca2+, Cl-, Mg2+
membrane potential
- resting membrane potential: membrane potential of unstimulated cell
- difference in electrical charge on the 2 sides of the membrane is due to a slight excess of positive ions over negative ones on one side and slight deficit on other
resting membrane potential of cells
- result of an active transport (electrogenic) and a passive diffusion:
- Na,K ATPase pumps Na+ out of cell and draws K+ ions into cell
- K+ tends to diffuse out of cell through potassium channels to reach an equilibrium whereas negative charged ions (phosphates and proteins) stay inside the cell
- interior of cell will turn more negative (-70 to -90 mV)
electrochemical gradient
- combination of membrane potential and concentration gradient of solute
- electrochemical gradient of a charged solute affects its transport
proteins can associate with plasma membrane by different ways:
- single alpha helix
- multiple alpha helices
- rolled-up beta sheet (beta barrel)
- attached only to one layer (with one hydrophobic face)
- attached to membrane by a covalently bound lipid chain
- via an oligosaccharide
- /8. attached to other proteins
transporters share common structural features:
- typically built from 10 or more alpha helices that span the membrane (transmembrane domains)
- substrate binding sites are located midway through the membrane
- show 2 different states: 1) inward-open, and 2) outward-open conformation
- binding sites are accessible by passageways from only one side of membrane at one time
- they would be able to work in the reverse direction if ion and solute gradients are adjusted
most membrane proteins cross lipid bilayer in an alpha-helical conformation:
- Na/glucose contransporter SGLT
- glucose transporter GLUT
- Na/Ca exchanger (NCX)
2 main classes of membrane transport proteins are:
- channels
2. transporters (carriers)
channels
- form pores for specific solutes (ions, water, ammonia)
- they interact with solute much more weakly compared to transporters
transporters
- bind specific substrate (solute) to be transported and undergo a series of conformational changes that alternately expose solute-binding sites on one side of membrane and then to other to transfer solute across it
ion channels
- have a region that forms a gate and a region that forms a pore for one specific solute
- pore narrows to atomic dimensions in one region -> selectivity filter
vestibule and selectivity filter in K+ channel
- in vestibule: ions are hydrated
- in selectivity filter: ions have lost their water and oxygens of the carbonyl groups of the channel to accommodate dehydrated solutes
- since Na+ is smaller than potassium, it can not be successfully accommodated and will not be recognized in the filter
Ion channel types
- voltage-gated
- ligand-gated (extracellular ligand)
- ligand-gated (intracellular ligand)
- mechanically gated
aquaporins
- specific WATER channels
- cells that secrete or absorb high amounts of water express aquaporins on their plasma membrane making water movement more efficient
- ex: cells lining ducts of exocrine glands and cells in the kidney
- some aquaporins are hormone-responsive and play an important role in formation of a concentrated urine