Caldesmon

CALD1
Identifiers
Aliases	CALD1 , CDM, H-CAD, HCAD, L-CAD, LCAD, NAG22, caldesmon 1, h-CD
External IDs	OMIM: 114213; HomoloGene: 137424; GeneCards: CALD1; OMA:CALD1 - orthologs
Gene location (Human) Chr. Chromosome 7 (human) [1] Band 7q33 Start 134,744,252 bp [1] End 134,970,729 bp [1]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in saphenous vein tail of epididymis seminal vesicula tendon of biceps brachii urethra superficial temporal artery visceral pleura parietal pleura stromal cell of endometrium right coronary artery n/a More reference expression data BioGPS More reference expression data
Gene ontology Molecular function myosin binding actin binding tropomyosin binding protein binding calmodulin binding cadherin binding Cellular component cytoplasm cytosol plasma membrane myofibril cytoskeleton actin cytoskeleton intracellular membrane-bounded organelle membrane actin cap Biological process muscle contraction Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 800 n/a Ensembl ENSG00000122786 n/a UniProt Q05682 n/a RefSeq (mRNA) NM_004342 NM_033138 NM_033139 NM_033140 NM_033157 n/a RefSeq (protein) NP_004333 NP_149129 NP_149130 NP_149131 NP_149347 n/a Location (UCSC) Chr 7: 134.74 – 134.97 Mb n/a PubMed search [2] n/a
Wikidata
View/Edit Human

Caldesmon is a protein that in humans is encoded by the CALD1 gene. ^{[3] [4]}

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 ${\displaystyle {\text{Ca}}^{2+}}$-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 ${\displaystyle {\text{Ca}}^{2+}}$-dependent inhibition of smooth muscle contraction. Alternative splicing of this gene results in multiple transcript variants encoding distinct isoforms. ^[4]

Immunochemistry

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

References

1. GRCh38: Ensembl release 89: ENSG00000122786 – Ensembl, May 2017
2. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
3. 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. doi: 10.1016/S0021-9258(18)55390-4 . PMID   1885618.
4. "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. S2CID   310781.
• Wang CL (2002). "Caldesmon and smooth-muscle regulation". Cell Biochem. Biophys. 35 (3): 275–88. doi:10.1385/CBB:35:3:275. PMID   11894847. S2CID   195271255.
• 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. S2CID   46129878.
• 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. S2CID   25653139.
• 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. Bibcode:1981PNAS...78.5652S. doi: 10.1073/pnas.78.9.5652 . PMC   348816 . PMID   6946503.

External links

• Caldesmon at the U.S. National Library of Medicine Medical Subject Headings (MeSH)