Tropomyosin

From Wikipedia, the free encyclopedia

Troponin
Troponin

Tropomyosin is an alpha helical coiled coil protein dimer.

It binds end to end along F actin filaments in striated muscle.

Tropomyosin blocks myosin binding and hence crossbridge cycling in the absence of Ca2+ and the muscle Ca2+ regulatory element troponin.

Ca2+ influx from the sarcoplasmic reticulum of striated muscle myocytes binds to troponin and subsequently moves tropomyosin on the F-actin filament exposing the myosin binding sites.

Whilst recent structural visualisation and kinetic modeling has suggested that myosin binding further moves tropomyosin on actin to a fully open state allowing for uninhibited crossbridge cycling as the muscle contracts.

This three state model of thin filament regulation involving tropomyosin and troponin is still debated by experts who believe that two state regulation of muscle contraction (involving a blocked and open state) is sufficient to explain current experimental data and models.

Contents

Tropomyosin has a lot to do with the sliding filament theory which relates to the contraction of the muscular system.

Troponin and tropomyosin together form the tropomyosin protein complex.

This protein complex is very closely related and near the actin filaments that help create sarcomeres, which are part of the muscule structure in whole.

The important attribute of this is that it prevents the muscles from contracting constantly which over time would lead to intense pain.

They disable myosin from constantly connecting with actin unless a chemical reaction with Acetylcholine, which is the neurotransmiter which releases Ca2+, a calcium ion; after electrical stimulus has been applied to the neuron, which releases the Acetylcholine to the nerve synapse.

After the contraction is finished the Ca+ is removed using active transport.

Without the calcium ion attached to the troponin the tropomyosin relaxes and covers the actin binding site.

This keeps the myosin crossbridge from binding with the actin, and therefore the muscle relaxes.

Certain tropomyosins are known to cause allergies in certain people, and those who have cross-reactive allergies can get symptons from a range of sources due to a common allergen found in all these sources.

Common allergies include shrimp, dust mites and mollusks.

Tropomyosin is a pan-allergen (an allergen wide-distributed in the nature) because is a conserved protein among species. That is the reason why some people sensitized with mites tropomyosin could have an allergic reaction after eating seafood.

Advanced Search
Included Web Search Engines


Safe Search

close

Top Matching Results

Occasionally Search.com will highlight specialized results that are based on the context of your query. Examples of specialized results include specific links to news, images, or video.

Top Matching Results may highlight information from other Search.com pages, content from the CNET Network of sites, or third party content. The listings are based purely on relevance. Search.com does not receive payment for listings in this section but our partners that provide this data may get paid for listing these products.

Sponsored Links

This section contains paid listings which have been purchased by companies that want to have their sites appear for specific search terms and related content. These listings are administered, sorted and maintained by a third party and are not endorsed by Search.com.

Search Results

Search.com sends your search query to several search engines at one time and integrates the results into one list which has been sorted by relevance using Search.com's proprietary algorithm. You can customize the list of search engines included in your metasearch from the preferences.

The search engines that are used in your metasearch may allow companies to pay to have their Web sites included within the results. To view the Paid Inclusion policy for a specific search engine, please visit their Web site. Search.com does not accept payment or share revenue with any search engine partner for listings in this section.