The Muscular System
The Muscular System
The Muscular System
C. Muscle Proteins
Myofibrils are built from three kinds of proteins:
1. Contractile proteins
- Generates force during contraction.
2 types:
a. Myosin: Thick filaments; functions as a motor protein in all three types of muscle tissue.
b. Actin: Thin filaments; point of attachment of myosin.
2. Regulatory proteins
- Help switch the contraction process on and off.
2 types:
a. Tropomyosin: Cover the myosin-binding sites on actin in a relaxed muscle.
b. Troponin: Binds to actin to facilitate actin-myosin binding which may cause muscle contraction.
3. Structural proteins
- Keeps the thick and thin filaments in the proper alignment, give the myofibril elasticity and extensibility, and
link the myofibrils to the sarcolemma and extracellular matrix.
4 types:
a. Titin
- Third most plentiful protein in skeletal muscle (after actin and myosin).
- Thereby helping stabilize the position of the thick filament.
b. Actinin
- Bind to actin molecules of the thin filament and to titin.
c. Myomesin
- Form the M line; The M line proteins bind to titin and connect adjacent thick filaments to one
another.
d. Nebulin
- Long, nonelastic protein wrapped around the entire length of each thin filament. Helps anchor the
thin filaments to the Z discs and regulates the length of thin filaments during development.
e. Dystrophin
- A cytoskeletal protein that links thin filaments of the sarcomere to integral membrane proteins of
the sarcolemma.
B. Fascicle
- Bundle of muscle fibers wrapped in perimysium.
D. Myofibril
- Threadlike contractile elements within sarcoplasm of muscle fiber that extend entire length of fiber;
composed of filaments.
E. Filaments (myofilaments)
- Contractile proteins within myofibrils that are of two types: thick filaments composed of myosin and thin fi
laments composed of actin, tropomyosin, and troponin; sliding of thin fi laments past thick fi laments
produces muscle shortening.
Figure 1. The contraction cycle. Sarcomeres exert force and shorten through repeated cycles during which the myosin
heads attach to actin (cross-bridges), rotate, and detach. During the power stroke of contraction, cross-bridges rotate and
move the thin filaments past the thick filaments toward the center of the sarcomere.
B. Length–Tension Relationship
- The length–tension relationship for skeletal muscle, which indicates how the forcefulness of muscle
contraction depends on the length of the sarcomeres within a muscle before contraction begins.
At a sarcomere length of about 2.0–2.4 µm (which is very close to the resting length in most muscles),
the zone of overlap in each sarcomere is optimal, and the muscle fiber can develop maximum tension.
Maximum tension (100%) occurs when the zone of overlap between a thick and thin filament extends
from the edge of the H zone to one end of a thick filament.
As the sarcomeres of a muscle fiber are stretched to a longer length, the zone of overlap shortens, and
fewer myosin heads can make contact with thin filaments. Therefore, the tension the fiber can produce
decreases.
When a skeletal muscle fiber is stretched to 170% of its optimal length, there is no overlap between the
thick and thin filaments. Because none of the myosin heads can bind to thin filaments, the muscle fiber
cannot contract, and tension is zero.
As sarcomere lengths become increasingly shorter than the optimum, the tension that can develop again
decreases. This is because thick filaments crumple as they are compressed by the Z discs, resulting in
fewer myosin heads making contact with thin filaments.
Normally, resting muscle fiber length is held very close to the optimum by firm attachments of skeletal
muscle to bones (via their tendons) and to other inelastic tissues.
Figure 2. Length–tension relationship in a skeletal muscle fiber. Maximum tension during contraction occurs when
the resting sarcomere length is 2.0–2.4 µm. A muscle fiber develops its greatest tension when there is an optimal zone of
overlap between thick and thin filaments.
Figure 3. Summary of the events of contraction and relaxation in a skeletal muscle fiber.
Sources:
Derrickson, B., Tortora, G. (2014). Principles of Anatomy and Physiology. Quad Graphics/Versailles.
Seeley et al. (2017). Seeley’s Anatomy and Physiology. Georgia State University Press.