Muscle 1 Flashcards

Semester 1 year 1

1
Q

What is skeletal muscle responsible for?

A

-voluntary movement of bones
-control of inspiration
-skeletal muscle pump

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

Describe the appearance of skeletal muscle

A

Striated

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

Describe the structure of skeletal muscle

A

-muscle cell/fibre surrounded by endomysium
-muscle cells come together to make fascicles surrounded by perimysium
-muscle units made up of many fascicles surrounded by the epimysium
-myofibrils run through muscle cells + are made up of sarcomeres

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

What are sarcomeres made up of?

A

-thick filaments (myosin)
-thin filaments (actin)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

How do the I and A bands appear and why?

A

-I band appears light - predominantly actin
-A band appears dark - overlap of actin and myosin

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

Where is the Z line/disc in the sarcomere?

A

At the ends

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

What are the 2 other proteins in the sarcomere and what do they do?

A

-nebulin protein is linked around actin
-titin protein anchors myosin to z disc

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

When the muscle contracts, what changes in the sarcomere?

A

Actin is pulled inward, so the I band becomes smaller and the A band stays the same

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

How is muscle contraction initiated?

A

-ACh released at neuromuscular junction causing action potential in plasma membrane of muscle fibre
-depolarisation passes along sarcolemma + through T-tubule network to cell interior
-T tubule runs near 2 areas of sarcoplasmic reticulum, forming a triad
-depolarisation causes increases in intracellular calcium

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

How many actin filaments are around myosin?

A

6

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

How are cross-bridges formed?

A

-myosin head is tightly bound with actin
-ATP binds to myosin head, weakening its binding to actin, so it dissociates
-ATP is hydrolysed, causing myosin head to return to resting configuration
-myosin head binds loosely to new actin molecule, forming a cross-bridge

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

How does the sarcomere contract?

A

-after cross-bridge is formed, phosphate is released, causing a strong association between actin + myosin
-myosin head changes from open to closed position, pulling actin towards middle of sarcomere
-ADP released, returning head to original position

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

How can the myosin head attach to a new actin molecule further down the filament?

A

When the myosin head returns to resting configuration, it’s in an open position, lengthening it

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

What happens to calcium ions after contraction?

A

Taken out of cytoplasm, so muscle goes into relaxation period

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

What happens to skeletal muscle at an increased frequency (10 Hz)?

A

-muscle doesn’t fully relax before net contraction
-stronger contraction
-temporal summation

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

What happens to skeletal muscle at 25 Hz?

A

-unfused tetanus
-contraction force plateaus

17
Q

What happens to skeletal muscle at 50 Hz?

A

-fused tetanus
-not time for calcium to be taken out of cytoplasm
-constant generation of force

18
Q

What are the 3 classes of muscle fibres?

A

-type I - slow oxidative
-type IIa - fast oxidative
-type IIb - fast glycolytic

19
Q

Are the classes of muscle fibres fast or slow?

A

-type I - slow
-type II - fast

20
Q

Are slow fibres larger or smaller, and do they take longer to contract?

A

-slow fibres are half the diameter of fast fibres
-take longer to contract

21
Q

Describe the speed and force of the 3 classes of muscle fibre

A

-type I - react slowly + generate a low level of force
-type IIb - react quickly + high level of force
-type IIa - in between type I and IIb

22
Q

Describe the unfused tetanus force + fatigability of the 3 muscle fibre classes

A

-type I - muscle doesn’t tire, continually generates the same force
-type IIa - generates a large force, sustains for a while but drops off quickly
-type IIb - generates a large force, drops off quickly

23
Q

What is the difference between isometric and isotonic muscle contraction

A

-isometric - muscle remains at fixed length
-isotonic - muscle stimulation causes a change in length

24
Q

Describe how transmission occurs at the neuromuscular junction

A

-action potential enters the neuron
-sodium channels open + sodium moves in, causing depolarisation
-activates calcium channels + calcium moves in
-causes fusion of vesicles containing ACh with membrane
-ACh released unto synaptic cleft + stimulates AChR receptors
-depolarisation in muscle, so muscle sodium channels open + wave of depolarisation can continue

25
Q

What does acetylcholinesterase do?

A

Breaks down ACh to prevent overstimulation of muscle

26
Q

Why do potassium ion channels open in the neuron at the neuromuscular junction?

A

Potassium ions move out, repolarising neuron, so new wave of depolarisation can occur

27
Q

What are the V snares and T snares and where are they?

A

-V snare in vesicle - synaptobrevin
-T snares in membrane - SNAP-25 + syntaxin

28
Q

What is the function of T snares and v snares?

A

Complex forms between them, causing the vesicle containing ACh to fuse with the membrane and release ACh into cleft

29
Q

How do botulinum toxins act as inhibitors?

A

Botulinum toxins cleave V and T snares, so vesicle doesn’t fuse with the membrane, so ACh not released

30
Q

Which types of botulinum toxin cleave which snares?

A

-A,C,E - SNAP-25
-B,D,F,G - synaptobrevin
-C - syntaxin