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- calmodulin-binding protein
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出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2015/11/07 04:41:56」(JST)
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Caldesmon 1 |
Identifiers |
Symbols |
CALD1 ; CDM; H-CAD; HCAD; L-CAD; LCAD; NAG22 |
External IDs |
OMIM: 114213 HomoloGene: 137424 GeneCards: CALD1 Gene |
Gene ontology |
Molecular function |
• actin binding
• calmodulin binding
• tropomyosin binding
• myosin binding
|
Cellular component |
• cytosol
• cytoskeleton
• plasma membrane
• actin cytoskeleton
• myofibril
• actin cap
|
Biological process |
• movement of cell or subcellular component
• muscle contraction
|
Sources: Amigo / QuickGO |
|
RNA expression pattern |
|
|
|
More reference expression data |
Orthologs |
Species |
Human |
Mouse |
Entrez |
800 |
n/a |
Ensembl |
ENSG00000122786 |
n/a |
UniProt |
Q05682 |
n/a |
RefSeq (mRNA) |
NM_004342 |
n/a |
RefSeq (protein) |
NP_004333 |
n/a |
Location (UCSC) |
Chr 7:
134.74 – 134.97 Mb |
n/a |
PubMed search |
[1] |
n/a |
|
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]
Contents
- 1 Immunochemistry
- 2 References
- 3 Further reading
- 4 External links
Immunochemistry
In diagnostic immunochemistry, caldesmon is a marker for smooth muscle differentiation.
References
- ^ Novy RE, Lin JL, Lin JJ (Oct 1991). "Characterization of cDNA clones encoding a human fibroblast caldesmon isoform and analysis of caldesmon expression in normal and transformed cells". J Biol Chem 266 (25): 16917–24. PMID 1885618.
- ^ a b "Entrez Gene: CALD1 caldesmon 1".
Further reading
- Huber PA (1998). "Caldesmon". Int. J. Biochem. Cell Biol. 29 (8–9): 1047–51. doi:10.1016/S1357-2725(97)00004-6. PMID 9415999.
- Gusev NB (2002). "Some properties of caldesmon and calponin and the participation of these proteins in regulation of smooth muscle contraction and cytoskeleton formation". Biochemistry Mosc. 66 (10): 1112–21. doi:10.1023/A:1012480829618. PMID 11736632.
- Wang CL (2002). "Caldesmon and smooth-muscle regulation". Cell Biochem. Biophys. 35 (3): 275–88. doi:10.1385/CBB:35:3:275. PMID 11894847.
- Mani RS, McCubbin WD, Kay CM (1992). "Calcium-dependent regulation of caldesmon by an 11-kDa smooth muscle calcium-binding protein, caltropin". Biochemistry 31 (47): 11896–901. doi:10.1021/bi00162a031. PMID 1445920.
- Hayashi K, Yano H, Hashida T, et al. (1993). "Genomic structure of the human caldesmon gene". Proc. Natl. Acad. Sci. U.S.A. 89 (24): 12122–6. doi:10.1073/pnas.89.24.12122. PMC 50710. PMID 1465449.
- Humphrey MB, Herrera-Sosa H, Gonzalez G, et al. (1992). "Cloning of cDNAs encoding human caldesmons". Gene 112 (2): 197–204. doi:10.1016/0378-1119(92)90376-Z. PMID 1555769.
- Adam LP, Gapinski CJ, Hathaway DR (1992). "Phosphorylation sequences in h-caldesmon from phorbol ester-stimulated canine aortas". FEBS Lett. 302 (3): 223–6. doi:10.1016/0014-5793(92)80446-N. PMID 1601129.
- Horiuchi KY, Chacko S (1989). "Interaction between caldesmon and tropomyosin in the presence and absence of smooth muscle actin". Biochemistry 27 (22): 8388–93. doi:10.1021/bi00422a014. PMID 3242591.
- der Terrossian E, Deprette C, Lebbar I, Cassoly R (1994). "Purification and characterization of erythrocyte caldesmon. Hypothesis for an actin-linked regulation of a contractile activity in the red blood cell membrane". Eur. J. Biochem. 219 (1–2): 503–11. doi:10.1111/j.1432-1033.1994.tb19965.x. PMID 8307018.
- Surgucheva I, Bryan J (1996). "Over-expression of smooth muscle caldesmon in mouse fibroblasts". Cell Motil. Cytoskeleton 32 (3): 233–43. doi:10.1002/cm.970320307. PMID 8581978.
- Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
- Graether SP, Heinonen TY, Raharjo WH, et al. (1997). "Tryptophan residues in caldesmon are major determinants for calmodulin binding". Biochemistry 36 (2): 364–9. doi:10.1021/bi962008k. PMID 9003189.
- Wang Z, Danielsen AJ, Maihle NJ, McManus MJ (1999). "Tyrosine phosphorylation of caldesmon is required for binding to the Shc.Grb2 complex". J. Biol. Chem. 274 (47): 33807–13. doi:10.1074/jbc.274.47.33807. PMID 10559276.
- Adam L, Vadlamudi R, Mandal M, et al. (2000). "Regulation of microfilament reorganization and invasiveness of breast cancer cells by kinase dead p21-activated kinase-1". J. Biol. Chem. 275 (16): 12041–50. doi:10.1074/jbc.275.16.12041. PMID 10766836.
- Hall SM, Hislop AA, Pierce CM, Haworth SG (2000). "Prenatal origins of human intrapulmonary arteries: formation and smooth muscle maturation". Am. J. Respir. Cell Mol. Biol. 23 (2): 194–203. doi:10.1165/ajrcmb.23.2.3975. PMID 10919986.
- Nimmrich I, Erdmann S, Melchers U, et al. (2000). "Seven genes that are differentially transcribed in colorectal tumor cell lines". Cancer Lett. 160 (1): 37–43. doi:10.1016/S0304-3835(00)00553-X. PMID 11098082.
- Hisaoka M, Wei-Qi S, Jian W, et al. (2003). "Specific but variable expression of h-caldesmon in leiomyosarcomas: an immunohistochemical reassessment of a novel myogenic marker". Appl. Immunohistochem. Mol. Morphol. 9 (4): 302–8. doi:10.1097/00022744-200112000-00003. PMID 11759055.
- Sobue K, Muramoto Y, Fujita M, Kakiuchi S (Sep 1981). "Purification of a calmodulin-binding protein from chicken gizzard that interacts with F-actin". Proc. Natl. Acad. Sci. U.S.A. 78 (9): 5652–5. doi:10.1073/pnas.78.9.5652. PMC 348816. PMID 6946503.
External links
- Caldesmon at the US National Library of Medicine Medical Subject Headings (MeSH)
UpToDate Contents
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English Journal
- Potentially neuroprotective gene modulation in an in vitro model of mild traumatic brain injury.
- Di Pietro V, Amorini AM, Tavazzi B, Hovda DA, Signoretti S, Giza CC, Lazzarino G, Vagnozzi R, Lazzarino G, Belli A.SourceNeuropharmacology and Neurobiology Section, School of Clinical and Experimental Medicine, College of Medical and Dental Sciences, University of Birmingham, Birmingham, UK.
- Molecular and cellular biochemistry.Mol Cell Biochem.2013 Mar;375(1-2):185-98. doi: 10.1007/s11010-012-1541-2. Epub 2012 Dec 15.
- In this study, we investigated the hypothesis that mild traumatic brain injury (mTBI) triggers a controlled gene program as an adaptive response finalized to neuroprotection, similar to that found in hibernators and in ischemic preconditioning. A stretch injury device was used to produce an equi-bia
- PMID 23242602
- Epstein-Barr virus-associated smooth muscle tumor-report of 3 tumors including 1 intracerebral case with a prominent intratumoral B-lymphocytic component and plasma cells.
- Petersson F.SourceDepartment of Pathology, National University Health System, Singapore. fredrikpetersson@live.se
- Annals of diagnostic pathology.Ann Diagn Pathol.2013 Feb;17(1):91-8. doi: 10.1016/j.anndiagpath.2012.07.007. Epub 2012 Sep 27.
- Three Epstein-Barr virus-associated smooth muscle tumors (intracranial, endobronchial, and paraspinal) in 2 patients are presented. The patient with the intracranial tumor had no concurrent or previous manifestation of this neoplasm and was immunosuppressed because of a renal transplant. The other p
- PMID 23022018
- Gene expression signatures differentiate uterine endometrial stromal sarcoma from leiomyosarcoma.
- Davidson B, Abeler VM, Hellesylt E, Holth A, Shih IeM, Skeie-Jensen T, Chen L, Yang Y, Wang TL.SourceDepartment of Pathology, Norwegian Radium Hospital, Oslo University Hospital, N-0424 Oslo, Norway; The Medical Faculty, University of Oslo, N-0316 Oslo, Norway. Electronic address: bend@medisin.uio.no.
- Gynecologic oncology.Gynecol Oncol.2013 Feb;128(2):349-55. doi: 10.1016/j.ygyno.2012.11.021. Epub 2012 Nov 21.
- OBJECTIVE: Endometrial stromal sarcoma (ESS) and leiomyosarcoma (LMS) are the two most common uterine sarcomas, but both are rare tumors. The aim of the present study was to compare the global gene expression patterns of ESS and LMS.METHODS: Gene expression profiles of 7 ESS and 13 LMS were analyzed
- PMID 23178314
Japanese Journal
- 肝および副腎合併切除を行った下大静脈原発平滑筋肉腫の1例
- 日本臨床外科学会雑誌 = The journal of the Japan Surgical Association 74(9), 2428-2433, 2013-09-25
- NAID 10031203131
Related Links
- (Gene:7q33;CALD1,CDM,CAD ともいう) Caldesmonにはisoformがあり、この抗体(clone:TD107)は約80kDaの血小板由来のCaldesmonを免疫源としているが、約140kDaの平滑筋高分子caldesmon(heavy caldesmon ...
- heavy-caldesmon, h-caldesmon 札幌医科大学医学部病理診断学 長谷川 匡先生 クローン:h-CD メーカー: Dako 希釈倍率: ×50、抗原賦活化法: オートクレーブ (札幌医科大学病理診断学での条件) 推奨陽性コントロール: 何でも ...
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