tropomyosin


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tropomyosin

 [tro″po-mi´o-sin]
a muscle protein of the I band that inhibits contraction by blocking the interaction of actin and myosin, except when influenced by troponin.

tro·po·my·o·sin

(trō'pō-mī'ō-sin),
A fibrous protein extractable from muscle; sometimes specified as tropomyosin B to distinguish it from tropomyosin A (paramyosin) prominent in mollusks.

tropomyosin

/tro·po·my·o·sin/ (-mi´o-sin) a muscle protein of the I band that inhibits contraction by blocking the interaction of actin and myosin, except when influenced by troponin.

tropomyosin

(trō′pə-mī′ə-sĭn, trŏp′ə-)
n.
A protein that binds to and stabilizes actin filaments in cells. In skeletal and cardiac muscle cells, tropomysin is released after interacting with troponin and calcium, facilitating the binding of actin to myosin that causes muscle contraction.

tropomyosin

[trop′əmī′əsin]
Etymology: Gk, trepein + mys, muscle
a protein component of sarcomere filaments, which, together with troponin, regulates interactions of actin and myosin in muscle contractions.

tro·po·my·o·sin

(trō'pō-mī'ŏ-sin)
A fibrous protein extractable from muscle; sometimes specified as tropomyosin B to distinguish it from tropomyosin A (paramyosin) prominent in mollusks.

tropomyosin

A regulatory protein in striated muscle concerned with the binding sites for the cross bridges on thin filaments in the SARCOMERE. Tropomyosin reversibly prevents bonding, thereby preventing muscles form being in a continuous state of contraction.

tropomyosin

a long protein molecule found in the grooves of muscle ACTIN filaments. It inhibits muscle contraction by blocking the interaction between the filaments and MYOSIN.

tropomyosin

a muscle protein of the I band that inhibits contraction by blocking the interaction of actin and myosin, except when influenced by troponin.
References in periodicals archive ?
In that case, a quicker move off the tropomyosin would result in a speedier contraction.
5] Human genes: TPM1, tropomyosin 1 (alpha); PDCD4, programmed cell death 4 (neoplastic transformation inhibitor); PTEN, phosphatase and tensin homolog.
Muscle fiber proteins consisting of actin, myosin, troponin and tropomyosin were determined to investigate alternative mechanisms for changes in contractile properties and myofibrillar ATPase activity with body size.
Calponin is a 34-kd protein that interacts with F-actin and tropomyosin in a calcium-independent manner and with calmodulin in a calcium-dependent manner.
Troponin T binds tropomyosin, forming the troponin-tropomyosin complex.
A mutation in the alpha tropomyosin gene TPM3 associated with autosomal dominant nemaline myopathy.
miR-21 expression has subsequently been shown to influence several other relevant targets, including the programmed cell death 4 (neoplastic transformation inhibitor) (PDCD4) [5] (30,31), tropomyosin 1 (alpha) (TPM1) (32), phosphatase and tensin homolog (PTEN) (33), andTIMP metallopeptidase inhibitor 3 (TIMP3) genes in breast cancer (34) (see Fig.
8,9] Recently, it was demonstrated that high-molecular-weight caldesmon, a protein that binds to actin and tropomyosin and regulates cellular contraction,[23-25] is highly specific to smooth muscle cells and is not expressed in reactive myofibroblasts and myofibroblast-related tumors.
Evidence suggests that miR-21 targets and inhibits tropomyosin 1 (alpha) (TPM1) [5] (9), programmed cell death 4 (neoplastic transformation inhibitor) (PDCD4) (10), and phosphatase and tensin homolog (PTEN) (13) and other tumor-related genes.
Peptide mass fingerprinting (23) with protein sequence database searching of the tryptic peptides from fraction I-3 that were not attributable to cTnI produced 2 human proteins that can explain the MALDI-MS results for fraction I-3: human tropomyosin 1 a-chain (calculated [M.