Crossbridge
Crossbridge
A crossbridge is a fundamental concept in muscle physiology, particularly in the context of muscle contraction. It refers to the connection formed between the actin and myosin filaments within the sarcomere, the basic contractile unit of muscle tissue. Understanding the crossbridge cycle is crucial for comprehending how muscles generate force and movement.
Structure and Function[edit | edit source]
The crossbridge is formed by the interaction between the myosin heads, which are part of the thick filament, and the actin molecules, which are part of the thin filament. Each myosin molecule has a head that protrudes outward and is capable of binding to an actin filament. This binding is essential for the contraction process.
Myosin[edit | edit source]
Myosin is a motor protein that plays a critical role in muscle contraction. It consists of a tail, a hinge region, and a head. The head contains an ATPase enzyme that hydrolyzes ATP to provide the energy necessary for muscle contraction. The myosin head binds to actin to form a crossbridge, and through a series of conformational changes, it pulls the actin filament, resulting in muscle contraction.
Actin[edit | edit source]
Actin is a globular protein that polymerizes to form long chains or filaments. These filaments are arranged in a double helix structure and are anchored at the Z-line of the sarcomere. Actin provides the track along which myosin heads move during muscle contraction.
The Crossbridge Cycle[edit | edit source]
The crossbridge cycle is a series of events that lead to muscle contraction. It involves several key steps:
1. Crossbridge Formation: The myosin head, in its high-energy configuration, binds to an exposed active site on the actin filament, forming a crossbridge.
2. Power Stroke: The myosin head pivots, pulling the actin filament toward the center of the sarcomere. This movement is known as the power stroke and results in the shortening of the muscle fiber.
3. Crossbridge Detachment: ATP binds to the myosin head, causing it to detach from the actin filament.
4. Reactivation of Myosin Head: The hydrolysis of ATP to ADP and inorganic phosphate (Pi) re-energizes the myosin head, returning it to its high-energy state, ready to form another crossbridge.
This cycle repeats as long as calcium ions and ATP are present, allowing for sustained muscle contraction.
Regulation of Crossbridge Formation[edit | edit source]
The formation of crossbridges is regulated by the availability of calcium ions and the presence of regulatory proteins such as troponin and tropomyosin. In a relaxed muscle, tropomyosin blocks the active sites on actin, preventing crossbridge formation. When calcium ions are released from the sarcoplasmic reticulum, they bind to troponin, causing a conformational change that moves tropomyosin away from the active sites, allowing crossbridge formation.
Clinical Relevance[edit | edit source]
Understanding the crossbridge cycle is important in the context of various muscle disorders and conditions. For example, in conditions such as rigor mortis, the lack of ATP prevents the detachment of myosin heads from actin, resulting in muscle stiffness. Additionally, certain drugs and toxins can affect the crossbridge cycle, leading to muscle weakness or paralysis.
Also see[edit | edit source]
Search WikiMD
Ad.Tired of being Overweight? Try W8MD's physician weight loss program.
Semaglutide (Ozempic / Wegovy and Tirzepatide (Mounjaro / Zepbound) available.
Advertise on WikiMD
WikiMD's Wellness Encyclopedia |
Let Food Be Thy Medicine Medicine Thy Food - Hippocrates |
Translate this page: - East Asian
中文,
日本,
한국어,
South Asian
हिन्दी,
தமிழ்,
తెలుగు,
Urdu,
ಕನ್ನಡ,
Southeast Asian
Indonesian,
Vietnamese,
Thai,
မြန်မာဘာသာ,
বাংলা
European
español,
Deutsch,
français,
Greek,
português do Brasil,
polski,
română,
русский,
Nederlands,
norsk,
svenska,
suomi,
Italian
Middle Eastern & African
عربى,
Turkish,
Persian,
Hebrew,
Afrikaans,
isiZulu,
Kiswahili,
Other
Bulgarian,
Hungarian,
Czech,
Swedish,
മലയാളം,
मराठी,
ਪੰਜਾਬੀ,
ગુજરાતી,
Portuguese,
Ukrainian
Medical Disclaimer: WikiMD is not a substitute for professional medical advice. The information on WikiMD is provided as an information resource only, may be incorrect, outdated or misleading, and is not to be used or relied on for any diagnostic or treatment purposes. Please consult your health care provider before making any healthcare decisions or for guidance about a specific medical condition. WikiMD expressly disclaims responsibility, and shall have no liability, for any damages, loss, injury, or liability whatsoever suffered as a result of your reliance on the information contained in this site. By visiting this site you agree to the foregoing terms and conditions, which may from time to time be changed or supplemented by WikiMD. If you do not agree to the foregoing terms and conditions, you should not enter or use this site. See full disclaimer.
Credits:Most images are courtesy of Wikimedia commons, and templates Wikipedia, licensed under CC BY SA or similar.
Contributors: Prab R. Tumpati, MD