Calponin

Apr 21, 2026 - 23:30
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Calponin

Added Image of chicken gizzard cross section

← Previous revision Revision as of 17:59, 21 April 2026
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| LocusSupplementaryData = -p21
| LocusSupplementaryData = -p21
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[[File:Chicken Gizzard Cross-Section.svg|thumb|Cross-section of a chicken gizzard, a smooth muscle organ where calponin was first identified.]]

== Introduction ==
== Introduction ==
'''Calponin''' is an-actin binding [[protein]] involved in regulation of smooth muscle contraction and cytoskeletal establishment.{{Cite journal |last=Hsieh |first=Tzu-Bou |last2=Jin |first2=J.-P. |date=2023-06-08 |title=Evolution and function of calponin and transgelin |url=https://www.frontiersin.org/journals/cell-and-developmental-biology/articles/10.3389/fcell.2023.1206147/full |journal=Frontiers in Cell and Developmental Biology |language=English |volume=11 |doi=10.3389/fcell.2023.1206147 |issn=2296-634X}} Calponin was first identified in smooth muscle from chicken gizzard and later characterized as an actin associated filament protein with around 300 [[Amino acid|amino acids]]. {{Cite journal |last=Liu |first=Rong |last2=Jin |first2=J. -P. |date=2016-07-01 |title=Calponin isoforms CNN1, CNN2 and CNN3: Regulators for actin cytoskeleton functions in smooth muscle and non-muscle cells |url=https://www.sciencedirect.com/science/article/pii/S0378111916301238 |journal=Gene |volume=585 |issue=1 |pages=143–153 |doi=10.1016/j.gene.2016.02.040 |issn=0378-1119 |pmc=5325697 |pmid=26970176}} Calponin functions as a calcium binding protein that inhibits ATPase activity of myosin in smooth muscle. Phosphorylation of calponin by a protein kinase releases this inhibition of the smooth muscle ATPase, which is depended on calcium binding calmodulin.
'''Calponin''' is an-actin binding [[protein]] involved in regulation of smooth muscle contraction and cytoskeletal establishment.{{Cite journal |last=Hsieh |first=Tzu-Bou |last2=Jin |first2=J.-P. |date=2023-06-08 |title=Evolution and function of calponin and transgelin |url=https://www.frontiersin.org/journals/cell-and-developmental-biology/articles/10.3389/fcell.2023.1206147/full |journal=Frontiers in Cell and Developmental Biology |language=English |volume=11 |doi=10.3389/fcell.2023.1206147 |issn=2296-634X}} Calponin was first identified in smooth muscle from chicken gizzard and later characterized as an actin associated filament protein with around 300 [[Amino acid|amino acids]]. {{Cite journal |last=Liu |first=Rong |last2=Jin |first2=J. -P. |date=2016-07-01 |title=Calponin isoforms CNN1, CNN2 and CNN3: Regulators for actin cytoskeleton functions in smooth muscle and non-muscle cells |url=https://www.sciencedirect.com/science/article/pii/S0378111916301238 |journal=Gene |volume=585 |issue=1 |pages=143–153 |doi=10.1016/j.gene.2016.02.040 |issn=0378-1119 |pmc=5325697 |pmid=26970176}} Calponin functions as a calcium binding protein that inhibits ATPase activity of myosin in smooth muscle. Phosphorylation of calponin by a protein kinase releases this inhibition of the smooth muscle ATPase, which is depended on calcium binding calmodulin.
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