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词条 Caldesmon
释义

  1. Immunochemistry

  2. References

  3. Further reading

  4. External links

{{Infobox_gene}}Caldesmon is a protein that in humans is encoded by the CALD1 gene.[1][2]

Caldesmon is a calmodulin binding protein. Like calponin, caldesmon tonically inhibits the ATPase activity of myosin in smooth muscle.

This gene encodes a calmodulin- and actin-binding protein that plays an essential role in the regulation of smooth muscle and nonmuscle contraction. The conserved domain of this protein possesses the binding activities to Ca++-calmodulin, actin, tropomyosin, myosin, and phospholipids. This protein is a potent inhibitor of the actin-tropomyosin activated myosin MgATPase, and serves as a mediating factor for Ca++-dependent inhibition of smooth muscle contraction. Alternative splicing of this gene results in multiple transcript variants encoding distinct isoforms.[2]


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Immunochemistry

In diagnostic immunochemistry, caldesmon is a marker for smooth muscle differentiation.

References

1. ^{{cite journal |vauthors=Novy RE, Lin JL, Lin JJ | title = Characterization of cDNA clones encoding a human fibroblast caldesmon isoform and analysis of caldesmon expression in normal and transformed cells | journal = J Biol Chem | volume = 266 | issue = 25 | pages = 16917–24 |date=Oct 1991 | pmid = 1885618 | pmc = | doi = }}
2. ^{{cite web | title = Entrez Gene: CALD1 caldesmon 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=800| accessdate = }}

Further reading

{{refbegin | 2}}
  • {{cite journal | author=Huber PA |title=Caldesmon |journal=Int. J. Biochem. Cell Biol. |volume=29 |issue= 8–9 |pages= 1047–51 |year= 1998 |pmid= 9415999 |doi=10.1016/S1357-2725(97)00004-6 }}
  • {{cite journal | author=Gusev NB |title=Some properties of caldesmon and calponin and the participation of these proteins in regulation of smooth muscle contraction and cytoskeleton formation |journal=Biochemistry Mosc. |volume=66 |issue= 10 |pages= 1112–21 |year= 2002 |pmid= 11736632 |doi=10.1023/A:1012480829618 }}
  • {{cite journal | author=Wang CL |title=Caldesmon and smooth-muscle regulation |journal=Cell Biochem. Biophys. |volume=35 |issue= 3 |pages= 275–88 |year= 2002 |pmid= 11894847 |doi=10.1385/CBB:35:3:275 }}
  • {{cite journal |vauthors=Mani RS, McCubbin WD, Kay CM |title=Calcium-dependent regulation of caldesmon by an 11-kDa smooth muscle calcium-binding protein, caltropin |journal=Biochemistry |volume=31 |issue= 47 |pages= 11896–901 |year= 1992 |pmid= 1445920 |doi=10.1021/bi00162a031 }}
  • {{cite journal | author=Hayashi K |title=Genomic structure of the human caldesmon gene |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 24 |pages= 12122–6 |year= 1993 |pmid= 1465449 |doi=10.1073/pnas.89.24.12122 | pmc=50710 |name-list-format=vanc| author2=Yano H | author3=Hashida T | display-authors=3 | last4=Takeuchi | first4=R | last5=Takeda | first5=O | last6=Asada | first6=K | last7=Takahashi | first7=E | last8=Kato | first8=I | last9=Sobue | first9=K }}
  • {{cite journal | author=Humphrey MB |title=Cloning of cDNAs encoding human caldesmons |journal=Gene |volume=112 |issue= 2 |pages= 197–204 |year= 1992 |pmid= 1555769 |doi=10.1016/0378-1119(92)90376-Z |name-list-format=vanc| author2=Herrera-Sosa H | author3=Gonzalez G | display-authors=3 | last4=Lee | first4=Robyn | last5=Bryan | first5=Joseph }}
  • {{cite journal |vauthors=Adam LP, Gapinski CJ, Hathaway DR |title=Phosphorylation sequences in h-caldesmon from phorbol ester-stimulated canine aortas |journal=FEBS Lett. |volume=302 |issue= 3 |pages= 223–6 |year= 1992 |pmid= 1601129 |doi=10.1016/0014-5793(92)80446-N }}
  • {{cite journal |vauthors=Horiuchi KY, Chacko S |title=Interaction between caldesmon and tropomyosin in the presence and absence of smooth muscle actin |journal=Biochemistry |volume=27 |issue= 22 |pages= 8388–93 |year= 1989 |pmid= 3242591 |doi=10.1021/bi00422a014 }}
  • {{cite journal |vauthors=der Terrossian E, Deprette C, Lebbar I, Cassoly R |title=Purification and characterization of erythrocyte caldesmon. Hypothesis for an actin-linked regulation of a contractile activity in the red blood cell membrane |journal=Eur. J. Biochem. |volume=219 |issue= 1–2 |pages= 503–11 |year= 1994 |pmid= 8307018 |doi=10.1111/j.1432-1033.1994.tb19965.x }}
  • {{cite journal |vauthors=Surgucheva I, Bryan J |title=Over-expression of smooth muscle caldesmon in mouse fibroblasts |journal=Cell Motil. Cytoskeleton |volume=32 |issue= 3 |pages= 233–43 |year= 1996 |pmid= 8581978 |doi= 10.1002/cm.970320307 }}
  • {{cite journal |vauthors=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery |journal=Genome Res. |volume=6 |issue= 9 |pages= 791–806 |year= 1997 |pmid= 8889548 |doi=10.1101/gr.6.9.791 }}
  • {{cite journal | author=Graether SP |title=Tryptophan residues in caldesmon are major determinants for calmodulin binding |journal=Biochemistry |volume=36 |issue= 2 |pages= 364–9 |year= 1997 |pmid= 9003189 |doi= 10.1021/bi962008k |name-list-format=vanc| author2=Heinonen TY | author3=Raharjo WH | display-authors=3 | last4=Jin | first4=Jian-Ping | last5=Mak | first5=Alan S. }}
  • {{cite journal |vauthors=Wang Z, Danielsen AJ, Maihle NJ, McManus MJ |title=Tyrosine phosphorylation of caldesmon is required for binding to the Shc.Grb2 complex |journal=J. Biol. Chem. |volume=274 |issue= 47 |pages= 33807–13 |year= 1999 |pmid= 10559276 |doi=10.1074/jbc.274.47.33807 }}
  • {{cite journal | author=Adam L |title=Regulation of microfilament reorganization and invasiveness of breast cancer cells by kinase dead p21-activated kinase-1 |journal=J. Biol. Chem. |volume=275 |issue= 16 |pages= 12041–50 |year= 2000 |pmid= 10766836 |doi=10.1074/jbc.275.16.12041 |name-list-format=vanc| author2=Vadlamudi R | author3=Mandal M | display-authors=3 | last4=Chernoff | first4=J | last5=Kumar | first5=R }}
  • {{cite journal |vauthors=Hall SM, Hislop AA, Pierce CM, Haworth SG |title=Prenatal origins of human intrapulmonary arteries: formation and smooth muscle maturation |journal=Am. J. Respir. Cell Mol. Biol. |volume=23 |issue= 2 |pages= 194–203 |year= 2000 |pmid= 10919986 |doi= 10.1165/ajrcmb.23.2.3975}}
  • {{cite journal | author=Nimmrich I |title=Seven genes that are differentially transcribed in colorectal tumor cell lines |journal=Cancer Lett. |volume=160 |issue= 1 |pages= 37–43 |year= 2000 |pmid= 11098082 |doi=10.1016/S0304-3835(00)00553-X |name-list-format=vanc| author2=Erdmann S | author3=Melchers U | display-authors=3 | last4=Finke | first4=Ulrich | last5=Hentsch | first5=Sebastian | last6=Moyer | first6=Mary Pat | last7=Hoffmann | first7=Ingrid | last8=Müller | first8=Oliver }}
  • {{cite journal | author=Hisaoka M |title=Specific but variable expression of h-caldesmon in leiomyosarcomas: an immunohistochemical reassessment of a novel myogenic marker |journal=Appl. Immunohistochem. Mol. Morphol. |volume=9 |issue= 4 |pages= 302–8 |year= 2003 |pmid= 11759055 |doi=10.1097/00022744-200112000-00003 |name-list-format=vanc| author2=Wei-Qi S | author3=Jian W | display-authors=3 | last4=Morio | first4=Takashi | last5=Hashimoto | first5=Hiroshi }}
  • {{cite journal |vauthors=Sobue K, Muramoto Y, Fujita M, Kakiuchi S | title = Purification of a calmodulin-binding protein from chicken gizzard that interacts with F-actin | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 78 | issue = 9 | pages = 5652–5 |date=Sep 1981 | doi = 10.1073/pnas.78.9.5652| pmid = 6946503 | pmc=348816}}
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External links

  • {{MeshName|Caldesmon}}
{{gene-7-stub}}

1 : Proteins

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