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  2. Calcium-binding protein - Wikipedia

    en.wikipedia.org/wiki/Calcium-binding_protein

    Calcium-binding proteins can be either intracellular and extracellular. Those that are intracellular can contain or lack a structural EF-hand domain. Extracellular calcium-binding proteins are classified into six groups. [2] Since Ca (2+) is an important second messenger, it can act as an activator or inhibitor in gene transcription.

  3. Troponin C type 1 - Wikipedia

    en.wikipedia.org/wiki/Troponin_C_type_1

    As the cytoplasmic Ca 2+ concentration rises to ~1 μM during systole, [26] Ca 2+ binding to the regulatory domain of cardiac troponin C (cNTnC) is the key event that leads to muscle contraction. Hydrophobic binding of cNTnC to the "switch" region of troponin I, cTnI 148-159 , stabilizes the Ca 2+ -bound open conformation of cNTnC [ 29 ...

  4. Calcium signaling - Wikipedia

    en.wikipedia.org/wiki/Calcium_signaling

    The Ca 2+ in the myoplasm will diffuse to Ca 2+ regulator sites on the thin filaments. This leads to the actual contraction of the muscle. [16] Contractions of smooth muscle fiber are dependent on how a Ca 2+ influx occurs. When a Ca 2+ influx occurs, cross bridges form between myosin and actin leading to the

  5. Calmodulin - Wikipedia

    en.wikipedia.org/wiki/Calmodulin

    Calmodulin is a small, highly conserved protein that is 148 amino acids long (16.7 kDa). The protein has two approximately symmetrical globular domains (the N- and C- domains) each containing a pair of EF hand motifs [5] separated by a flexible linker region for a total of four Ca 2+ binding sites, two in each globular domain. [6]

  6. Calcium in biology - Wikipedia

    en.wikipedia.org/wiki/Calcium_in_biology

    The Ca 2+ concentration of the vacuole may reach millimolar levels. The most striking use of Ca 2+ ions as a structural element in algae occurs in the marine coccolithophores, which use Ca 2+ to form the calcium carbonate plates, with which they are covered. Calcium is needed to form the pectin in the middle lamella of newly formed cells.

  7. Calcium-sensing receptor - Wikipedia

    en.wikipedia.org/wiki/Calcium-sensing_receptor

    846 12374 Ensembl ENSG00000036828 ENSMUSG00000051980 UniProt P41180 Q9QY96 RefSeq (mRNA) NM_000388 NM_001178065 NM_013803 RefSeq (protein) NP_000379 NP_001171536 NP_038831 Location (UCSC) Chr 3: 122.18 – 122.29 Mb Chr 16: 36.31 – 36.38 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse The calcium-sensing receptor (CaSR) is a Class C G-protein coupled receptor which senses ...

  8. Calcium ATPase - Wikipedia

    en.wikipedia.org/wiki/Calcium_ATPase

    In myocytes (muscle cells) Ca 2+ is normally sequestered (isolated) in a specialized form of endoplasmic reticulum (ER) called sarcoplasmic reticulum (SR). It is a Ca 2+ ATPase that transfers Ca 2+ from the cytosol of the cell to the lumen of the SR at the expense of ATP hydrolysis during muscle relaxation. In the skeletal muscles the calcium ...

  9. Calcium buffering - Wikipedia

    en.wikipedia.org/wiki/Calcium_buffering

    When calcium is added to or removed from the cytoplasm by transport across the cell membrane or sarcoplasmic reticulum, calcium buffers minimise the effect on changes in cytoplasmic free calcium concentration by binding calcium to or releasing calcium from intracellular proteins. As a result, 99% of the calcium added to the cytosol of a ...