1.6 - structure + function of membranes Flashcards

1
Q

tonicity

A

is the osmotic force exerted by a solution

term used to describe the osmolarity of a solution compared with the osmolarity of a blood (isotonic, hypertonic e.g. severe dehydration, hypotonic)

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2
Q

what does the direction of diffusion depend on for ions

A

determined by electrical gradient AND chemical gradient (opposing)

The balance is determined by the Nernst potential

e.g K+ tend to diffuse out of cells via chemical gradient but are drawn back in due to electrical gradient (negative membrane potential left behind)

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3
Q

What is ficks law

A
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4
Q

Why can gases like O₂ and CO₂ freely pass through the lipid bilayer?

A

Gases are uncharged and lipid-soluble, enabling them to freely pass through the lipid bilayer.

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5
Q

Why is water theoretically unable to easily pass through the lipid bilayer?

A

Water is polar and has low lipid solubility, which should prevent it from passing easily through the membrane.

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6
Q

How does water actually move across the lipid bilayer?

A

Despite low lipid solubility, water moves rapidly and in an organized manner across the membrane, indicating specialized transport mechanisms beyond simple leakage. = aquaporins

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7
Q

What is an artificial lipid membrane?

A

An artificial lipid membrane is a model membrane composed purely of a lipid bilayer, used to study permeability.

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8
Q

Why is the permeability of ions and molecules compared between artificial and real membranes?

A

This comparison helps identify additional components, like proteins, in real membranes that affect permeability.

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9
Q

What does the comparison between artificial lipid bilayers and real membranes reveal?

A

shows that real membranes have other components enabling functions that wouldn’t be possible with just a lipid bilayer.

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10
Q

types of membrane transport

A

porins
channels
carriers

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11
Q

types of channels

A

voltage gated
ligand gated
stretch activated

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12
Q

types of carriers

A

primary active transport
secondary active transport
facilitated diffusion

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13
Q

What role do aquaporins play in the membrane?

A

Aquaporins are water channels that facilitate the rapid and organized transport of water across the membrane.

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14
Q

How does perforin function in cytotoxic T-lymphocytes?

A

Cytotoxic T-lymphocytes release perforin monomers, which form large channels to kill target cells.

Perforin monomers polymerize and assemble like staves in a barrel, forming doughnut-like channels that disrupt the target cell membrane.

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15
Q

what are porins

A

Transmembrane pores that are ALWAYS open

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16
Q

What are channels in the context of cell membranes?

A

Channels are aqueous-filled gated pores that can switch between open and closed states to regulate ion flow across the membrane.

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17
Q

what do channels allow the passage of

A

ions and some organic osmolytes e.g. taurine via passive diffusion

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18
Q

What are leak channels, and how do they function?

A

Leak channels are constitutively open channels that flicker rapidly between open and closed states without biological regulation, such as K⁺ leak channels that help control membrane potential.

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19
Q

What types of gating mechanisms can control channel opening?

A

Voltage-gated: changes in membrane potential

Ligand-gated: extracellular binding of a ligand to the channel or to an associated receptor e.g. G-protein coupled receptor (e.g., nAChR or GPCR)

Secondary messenger-gated: intracellular binding of a secondary messenger (e.g., cGMP)

Stretch-activated: membrane deformation

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20
Q

What are gap junctions, and what is their function?

A

Gap junctions are channels connecting the cytoplasm of adjacent cells, allowing diffusion of small molecules and ions to mediate cell-cell communication.

non-selective channel for electrical and chemical communication = e.g in heart. cardiac myocytes

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21
Q

How are gap junctions structured?

A

Each gap junction is formed by two connexon pores, each made of six connexin proteins, which align to create a non-selective channel for electrical and chemical communication.

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22
Q

Why can K⁺ ions pass through K⁺ channels, but Na⁺ ions cannot?

A

K⁺ channels have pore linings that efficiently replace the water molecules that shield K⁺ ions. Na⁺ ions are too small to interact effectively with these pore linings, preventing their passage.

23
Q

Describe the signaling cascade of a G protein-coupled receptor (GPCR) from activation to signal termination.

A

An external ligand (e.g., hormone, neurotransmitter) binds to the GPCR’s extracellular domain, causing a conformational change.

The GPCR activates an associated G protein by promoting the exchange of GDP for GTP on the Gα subunit, causing the Gα and Gβγ subunits to dissociate.

The activated Gα and Gβγ subunits interact with target proteins, initiating different signaling pathways:

Gαs stimulates adenylyl cyclase, increasing cAMP and activating protein kinase A (PKA).

Gαi inhibits adenylyl cyclase, reducing cAMP levels.
Gαq activates phospholipase C (PLC), generating IP₃ and DAG, which release Ca²⁺ and activate protein kinase C (PKC).

The Gβγ subunits can also activate ion channels, influence other signaling molecules, and add diversity to the cellular response.

The Gα subunit hydrolyzes GTP to GDP, allowing Gα and Gβγ to reassociate, resetting the G protein. GPCR phosphorylation by GRKs and binding of arrestins can desensitize the receptor, stopping further activation.

24
Q

How do carrier proteins facilitate transport across the membrane

A

Carrier proteins binds tosolute + traps it. Its undergoes a reversible conformational change that alternates exposure of the solute-binding site from one side of the membrane to the other. Then releases it.

while channels are often open to both sides.

25
Q

Why is carrier-mediated transport slower than channel-mediated transport?

A

The binding and conformational change required for each solute molecule make carrier-mediated transport slower than the rapid passage allowed by channels.

26
Q

What does it mean for carrier-mediated transport to be “temperature sensitive”?

A

Carrier-mediated transport depends on protein conformational changes, which are affected by temperature

27
Q

What is meant by the term “saturable” in carrier-mediated transport?

A

Carrier proteins have a limited number of binding sites and can reach a maximum transport rate (Vmax) at high solute concentrations, after which transport cannot increase.

28
Q

Define Vmax in the context of carrier proteins.

A

Vmax is the maximal rate of transport by a carrier protein when all binding sites are occupied, indicating full saturation.

29
Q

What is Km in carrier-mediated transport?

A

Km is the solute concentration at which the transport rate is half of Vmax, reflecting the affinity of the carrier for its solute.

30
Q

How do passive carriers work, and give an example?

A

Passive carriers facilitate diffusion without energy input, moving solutes down their concentration gradient. An example is the GLUT transporter, which moves glucose into cells.

31
Q

When does solute movement stop in facilitated diffusion?

A

Movement stops when equilibrium is reached—either the chemical gradient (for uncharged solutes) or the electrochemical gradient (for charged solutes) is balanced.

32
Q

Describe the equilibrium condition for uncharged solutes in facilitated diffusion.

A

For uncharged solutes, transport stops when the concentration is equal on both sides, eliminating the chemical gradient.

33
Q

What is the “occluded state” in carrier-mediated transport?

A

The occluded state is an intermediate stage where the solute is temporarily enclosed within the carrier protein, shielded from either side of the membrane.

34
Q

Explain the role of glucose-6-phosphate in glucose transport.

A

Inside cells, glucose is quickly converted to glucose-6-phosphate, maintaining a low intracellular glucose concentration and driving the continuous facilitated diffusion of glucose into the cell.

35
Q

are carriers active or passive

A

can be both

36
Q

carriers vs channels

A

-carriers…

  • slower
  • more sensitive to temp
  • saturable
37
Q

what do high and low Km suggest

A

A low Km suggests a high affinity for the solute, meaning the carrier can achieve half of its maximum transport rate (Vmax) at a low solute concentration = indicates the carrier is efficient at binding and transporting the solute even when its concentration is low

A high Km suggests a low affinity for the solute, meaning the carrier requires a higher solute concentration to reach half of its maximum transport rate (Vmax) = implies that the carrier is less efficient at binding and transporting the solute at lower concentrations.

38
Q

define active transport

A

the accumulation of a substance above the level that would be predicted at electrochemical equilibrium - evidence of active transport

39
Q

examples of passive carriers

A

GLUT
AE1 (Cl- shift)

40
Q

What is the role of ATP hydrolysis in carrier proteins?

A

The hydrolysis of ATP by the carrier protein initiates a conformational change that translocates bound ions across the membrane, enabling active transport.

41
Q

Describe the function of Na+/K+ ATPase.

A

The Na+/K+ ATPase maintains low intracellular sodium ([Na+]) levels by actively transporting 3 Na+ ions out of the cell and 2 K+ ions into the cell, using ATP for energy.

42
Q

What is the function of Ca2+ ATPase?

A

Ca2+ ATPase extrudes Ca2+ ions from cells, helping to regulate intracellular calcium levels and maintain cellular signaling.

43
Q

What is the role of H+/K+ ATPase in the stomach?

A

H+/K+ ATPase secretes gastric acid (H+) in the stomach, contributing to the acidic environment necessary for digestion.

44
Q

What are the structural components of the Na+/K+ ATPase?

A

The Na+/K+ ATPase consists of alpha and beta subunits, where the alpha subunit has 10 transmembrane segments and mediates the active transport.

45
Q

Describe the mechanism of action of the Na+/K+ ATPase.

A

E1 Conformation: ATP binds to the pump after it releases K+ into the intracellular fluid.

3 intracellular Na+ ions bind to high-affinity sites on the pump.

ATP is hydrolyzed, phosphorylating the alpha subunit at an aspartate residue, occluding Na+ ions.

The pump transitions from E1 to E2, exposing Na+ to the extracellular fluid and decreasing its binding affinity.

The 3 Na+ ions dissociate, and the pump’s conformation changes, increasing its affinity for extracellular K+.

Extracellular K+ binds to the pump.

The acyl-phosphate bond is hydrolyzed, releasing inorganic phosphate (Pi) and occluding K+.

ATP binds again, shifting the pump back to E1 conformation, de-occluding / releasing K+ and decreasing its affinity for K+.

The cycle repeats as ATP hydrolysis continues.

46
Q

What is secondary active transport?

A

Secondary active transport uses the gradients established by primary active transport (e.g., Na+/K+ ATPase) to provide energy for the transport of other solutes against their concentration gradients.

47
Q

How do symporters and antiporters differ in secondary active transport?

A

Symporters: Co-transport two solutes in the same direction across the membrane (e.g., Na+/glucose symporter).

Antiporters: Transport one solute into the cell while transporting another solute out of the cell in the opposite direction (e.g., Na+/Ca2+ exchanger).

48
Q

Describe the function of the Na+/glucose symporter.

A

he Na+/glucose symporter is found in the cell membranes lining the gut and proximal convoluted tubule, using the steep Na+ gradient created by Na+/K+ ATPase to import glucose against its concentration gradient while Na+ moves down its gradient.

49
Q

How does the Na+/glucose symporter utilize the Na+ gradient?

A

The downhill movement of Na+ into the cell provides the energy needed for the uphill transport of glucose into the cell, allowing glucose to bind more effectively upon Na+ binding, which causes a conformational change in the protein.

50
Q

What is the stoichiometry of the Na+/glucose symporter?

A

The Na+/glucose symporter typically transports 2 Na+ ions for every 1 glucose molecule.

51
Q

Describe the Na+/Ca2+ exchanger (NCX).

A

The Na+/Ca2+ exchanger is a 3 Na+/1 Ca2+ antiporter that uses the energy from the downhill transport of Na+ into the cell to drive the uphill extrusion of Ca2+ out of the cell, particularly following cardiac myocyte contraction.

52
Q

What is the significance of the Na+/Ca2+ exchanger having a low affinity for Ca2+?

A

The low affinity allows for a fast rate of Ca2+ expulsion, making it ideal for quickly reducing intracellular Ca2+ levels when concentrations are high, which is crucial for proper muscle function and relaxation.

53
Q
A