Muscle Concept Map

Muscle

Skeletal Muscles

Epimysium

Muscle fiber

Allow a person to move, speak, and chew. They control heartbeat, breathing, and digestion. Other seemingly unrelated functions, including temperature regulation and vision, also rely on the muscular system

Type of muscle:

Sacromere

Myosin

Myosin and Actin create the structure for the sacromere:

Each sarcomere is composed of two main protein filaments—actin and myosin—which are the active structures responsible for muscular contraction

Myofibril

A protein that converts chemical energy in the form of ATP to mechanical energy, thus generating force and movement

Myofilaments

I band

M line

H zone

A Band

Actin

The function of the myofibril is to perform muscle contraction via the sliding-filament model.

Allows a muscle to contract and move powerfully while maintaining its structural integrity

Surrounded by:

Myofilaments are key molecular regulators of the contraction. Indeed, thick-thin filament interactions (via the formation of myosin cross-bridges) lead to force production and motion

Muscle contraction, cell motility, cell division and cytokinesis, vesicle and organelle movement, cell signaling, and the establishment and maintenance of cell junctions and cell shape

Made up of:

They help to control the physical forces within the body. When grouped together, they can facilitate organized movement of your limbs and tissues

The component of the sarcomere that appears lighter because it contains only thin filaments. Allow more light to pass through them

Titin

Giving elastic stabilization of relative positions of myosin and actin filaments

Sacroplasm

have special features unlike general cells:

Sacrolemma

Muscle Fascicle

Bundles are called:

Dark region of striation, which contains thick filaments. Includes the H zone which is slightly darker than the rest of the A band

Determine what type of movement a muscle can make

the cytoplasm of a muscle fibre. It is a water solution containing ATP and phosphagens, as well as the enzymes and intermediate and product molecules involved in many metabolic reactions.

It acts as a barrier between the extracellular and intracellular compartments, defining the individual muscle fiber from its surroundings

in the H zone, the filaments consist only of the thick filament. The H zone becomes smaller as the muscle contracts and the sarcomere shortens.


These proteins are thought to be involved in anchoring the thick filaments of the sarcomere (myosin) to other filaments, namely titin, stabilizing and aligning the structure.

T-Tubules

Forms:

Their role is to maintain the SR calcium store under the tight control of membrane depolarization via the voltage sensor channel DHPR

Stabilized by:

Sacromere:

the basic contractile unit of muscle fiber. Each sarcomere is composed of two main protein filaments—actin and myosin—which are the active structures responsible for muscular contraction.

Permysium

surrounded by:

Sarcoplasmic Reticulum

Found within muscle cells are:

a regulator of Ca2+ storage and release homeostasis during and after muscle contraction

Perimysium is a sheath of connective tissue that groups muscle fibers into bundles (anywhere between 10 and 100 or more) or fascicles.

endomysium

the key element that separates single muscle fibres from one another. It allows their autonomous gliding during muscle contraction.

surrounded by:

Nebulin

Protein in actin is:

An actin-binding protein which can bind up to 200 actin molecules.

Muscle contraction:

Tropomyosin

Troponin

dystrophine

a protein involved in skeletal muscle contraction and that wraps around actin and prevents myosin from grabbing it.

a calcium-regulatory protein for the calcium regulation of contractile function in skeletal and cardiac muscles

Proteins involved:

dystrophin is part of a group of proteins (a protein complex) that work together to strengthen muscle fibers and protect them from injury as muscles contract and relax.

ATP

the source of energy for use and
storage at the cellular level.

functions as

the N-terminal extremity of the catalytic domain, where there is a glycine-rich stretch of residues in the vicinity of a lysine residue. It is this lysine residue that has been shown to be involved in ATP binding.

located in