Caldesmon

Caldesmon

Caldesmon 1, also known as CALD1, is a human gene.cite web | title = Entrez Gene: CALD1 caldesmon 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=800| accessdate = ]

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

PBB_Summary
section_title =
summary_text = 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.cite web | title = Entrez Gene: CALD1 caldesmon 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=800| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*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=
*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=
*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=
*cite journal | author=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=
*cite journal | author=Hayashi K, Yano H, Hashida T, "et al." |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=
*cite journal | author=Humphrey MB, Herrera-Sosa H, Gonzalez G, "et al." |title=Cloning of cDNAs encoding human caldesmons. |journal=Gene |volume=112 |issue= 2 |pages= 197–204 |year= 1992 |pmid= 1555769 |doi=
*cite journal | author=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=
*cite journal | author=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 |year= 1991 |pmid= 1885618 |doi=
*cite journal | author=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=
*cite journal | author=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=
*cite journal | author=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 | author=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=
*cite journal | author=Graether SP, Heinonen TY, Raharjo WH, "et al." |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
*cite journal | author=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=
*cite journal | author=Adam L, Vadlamudi R, Mandal M, "et al." |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=
*cite journal | author=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=
*cite journal | author=Nimmrich I, Erdmann S, Melchers U, "et al." |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=
*cite journal | author=Hisaoka M, Wei-Qi S, Jian W, "et al." |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=

External links

*

PBB_Controls
update_page = yes
require_manual_inspection = no
update_protein_box = yes
update_summary = no
update_citations = yes


Wikimedia Foundation. 2010.

Игры ⚽ Нужно решить контрольную?

Look at other dictionaries:

  • caldesmon — Protein originally isolated from smooth muscle (h caldesmon; 120 150 kD on gels but 88.7 kD from sequence) also found in non muscle cells (l caldesmon; 70 80 kD on gels but 58.8 kD from sequence). Normally dimeric, binds to F actin blocking the… …   Dictionary of molecular biology

  • Caldesmon-phosphatase — In enzymology, a caldesmon phosphatase (EC number|3.1.3.55) is an enzyme that catalyzes the chemical reaction:caldesmon phosphate + H2O ightleftharpoons caldesmon + phosphateThus, the two substrates of this enzyme are caldesmon phosphate and H2O …   Wikipedia

  • caldesmon — An F actin cross linking protein that, at low or absent calcium levels, binds to tropomyosin and actin and prevents myosin binding. [calcium + G. desmos, bond, fr. deo, to bind] * * * cal·des·mon (kal dezґmən) a calcium binding protein… …   Medical dictionary

  • CDK — caldesmon kinase; cell division kinase; climatic droplet keratopathy; cyclin dependent kinase * * * cyclin dependent kinase …   Medical dictionary

  • CDK — • caldesmon kinase; • cell division kinase; • climatic droplet keratopathy; • cyclin dependent kinase …   Dictionary of medical acronyms & abbreviations

  • Muscle contraction — See also: Twitch and Tremor Top down view of skeletal muscle Muscle fiber generates tension through the action of actin and myosin cross bridge cycling. While under tension, the muscle may lengthen, shorten, or …   Wikipedia

  • Smooth muscle tissue — Smooth muscle …   Wikipedia

  • Smooth muscle — is a type of non striated muscle, found within the tunica media layer of large and small arteries and veins, the bladder, uterus, male and female reproductive tracts, gastrointestinal tract, respiratory tract, the ciliary muscle, and iris of the… …   Wikipedia

  • Actin-binding protein — Actin binding proteins (also known as ABP) are proteins that bind to actin. This may mean ability to bind actin monomers, or polymers, or both.Many actin binding proteins, including α actinin, β spectrin, dystrophin, utrophin and fimbrin, do this …   Wikipedia

  • List of EC numbers (EC 3) — This list contains a list of EC numbers for the third group, EC 3, hydrolases, placed in numerical order as determined by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology.EC 3.1: Acting on Ester BondsEC… …   Wikipedia

Share the article and excerpts

Direct link
… Do a right-click on the link above
and select “Copy Link”