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Gene Review

TAGLN  -  transgelin

Homo sapiens

Synonyms: 22 kDa actin-binding protein, DKFZp686P11128, Protein WS3-10, SM22, SM22-alpha, ...
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Disease relevance of TAGLN

  • Shifted cells undergo a process of cell hypertrophy, as demonstrated by increased time of flight and forward scatter, as well as increased expression of the contractile proteins alpha-smooth muscle actin, myosin light chain kinase, and SM22 [1].
  • We performed site-directed mutagenesis to generate a series of NH(2)-terminal histidine (His)-tagged mutants of human SM22 in Escherichia coli and used these to analyze the functional importance of potential actin binding domains [2].
  • Contrary to our expectation, SM22 and smooth muscle myosin heavy chain promoter activities (but not viral murine sarcoma virus-long terminal repeat promoter activity) were decreased in long term serum-deprived myocytes by at least 8-fold [3].
  • The SMC identity of both pdSMC lines was confirmed by SM22 mRNA expression. pdSMC2 were generally diploid but with various structural and numerical alterations; pdSMC1A demonstrated several chromosomal abnormalities, most commonly -Y, +7, -13, anomalies previously reported in both primary pdSMCs and atherosclerotic tissue [4].
  • The following results were observed: The levels of liver fatty acid-binding protein, actin-binding protein/smooth muscle protein 22-alpha and cyclooxygenase 2 were downregulated in colorectal carcinoma compared to normal colon mucosa [5].

High impact information on TAGLN

  • The pattern of expression of these two genes contrasted markedly with that of calponin and SM22 alpha, genes expressed predominantly by differentiated smooth muscle cells and whose expression was generally confined to the media of the vessel [6].
  • Muscle-specific enzyme isoforms and contractile intermediate filaments including tropomyosin and smooth muscle (SM22) alpha protein were detected in the myoepithelial cells, and a large number of cytokeratin subclasses and isoforms characteristic of luminal cells were detected in this cell type [7].
  • Thus, both replicative senescence and forced expression of the WS3-10 gene sequence lead to suppression of Ca(2+)-dependent membrane currents, which suggests that a causal connection exists between these two processes [8].
  • Stable transfection of transgelin in LNCaP cells suppressed AR-mediated cell growth and prostate-specific antigen expression, whereas this suppressive effect was abolished by the addition of ARA54-small interfering RNA [9].
  • Here we describe transgelin as the first ARA54-associated negative modulator for AR [9].

Chemical compound and disease context of TAGLN

  • Among the identified proteins, there were seven over-expressed proteins in stomach cancer tissue: NSP3, transgelin, prohibitin, heat shock protein (hsp) 27 and variant, protein disulfide isomerase A3, unnamed protein product and glucose regulated protein [10].

Biological context of TAGLN


Anatomical context of TAGLN


Associations of TAGLN with chemical compounds


Regulatory relationships of TAGLN

  • Here, we investigated the effect of changes in the expression of histone acetyltransferases (HAT) or histone deacetylases (HDAC) on TGFbeta1-induced SM22 promoter activities [18].

Other interactions of TAGLN

  • Third, the steady-state level of the mRNA of three senescence-associated genes, i.e. fibronectin, osteonectin and SM22, was increased in HDFs at 72 h after three and five exposures to UVB [19].
  • It has structural homology to calponin, but how SM22 binds to actin remains unknown [2].
  • Of the three consensus protein kinase C or casein kinase II phosphorylation sites in SM22, only Ser-181 was readily phosphorylated by protein kinase C in vitro, and such phosphorylation greatly decreased actin binding [2].
  • TGFbeta1 also stimulates the association of Smad3 (a potent transactivator for the SM22 promoter) and p300 by co-immunoprecipitation assay [18].
  • DP III-1 and DP III-2 cDNA clone showed significant homology to the cDNA of alpha actin gene; DP III-3 cDNA clone showed significant homology to the cDNA of transgelin gene [20].

Analytical, diagnostic and therapeutic context of TAGLN


  1. Human bronchial smooth muscle cell lines show a hypertrophic phenotype typical of severe asthma. Zhou, L., Li, J., Goldsmith, A.M., Newcomb, D.C., Giannola, D.M., Vosk, R.G., Eves, E.M., Rosner, M.R., Solway, J., Hershenson, M.B. Am. J. Respir. Crit. Care Med. (2004) [Pubmed]
  2. Mutagenesis analysis of human SM22: characterization of actin binding. Fu, Y., Liu, H.W., Forsythe, S.M., Kogut, P., McConville, J.F., Halayko, A.J., Camoretti-Mercado, B., Solway, J. J. Appl. Physiol. (2000) [Pubmed]
  3. Physiological control of smooth muscle-specific gene expression through regulated nuclear translocation of serum response factor. Camoretti-Mercado, B., Liu, H.W., Halayko, A.J., Forsythe, S.M., Kyle, J.W., Li, B., Fu, Y., McConville, J., Kogut, P., Vieira, J.E., Patel, N.M., Hershenson, M.B., Fuchs, E., Sinha, S., Miano, J.M., Parmacek, M.S., Burkhardt, J.K., Solway, J. J. Biol. Chem. (2000) [Pubmed]
  4. Generation and characterization of human smooth muscle cell lines derived from atherosclerotic plaque. Bonin, L.R., Madden, K., Shera, K., Ihle, J., Matthews, C., Aziz, S., Perez-Reyes, N., McDougall, J.K., Conroy, S.C. Arterioscler. Thromb. Vasc. Biol. (1999) [Pubmed]
  5. Protein abundance alterations in matched sets of macroscopically normal colon mucosa and colorectal carcinoma. Stulík, J., Koupilova, K., Osterreicher, J., Knízek, J., Macela, A., Bures, J., Jandík, P., Langr, F., Dedic, K., Jungblut, P.R. Electrophoresis (1999) [Pubmed]
  6. High expression of genes for calcification-regulating proteins in human atherosclerotic plaques. Shanahan, C.M., Cary, N.R., Metcalfe, J.C., Weissberg, P.L. J. Clin. Invest. (1994) [Pubmed]
  7. Proteomic definition of normal human luminal and myoepithelial breast cells purified from reduction mammoplasties. Page, M.J., Amess, B., Townsend, R.R., Parekh, R., Herath, A., Brusten, L., Zvelebil, M.J., Stein, R.C., Waterfield, M.D., Davies, S.C., O'Hare, M.J. Proc. Natl. Acad. Sci. U.S.A. (1999) [Pubmed]
  8. Suppression of calcium-dependent membrane currents in human fibroblasts by replicative senescence and forced expression of a gene sequence encoding a putative calcium-binding protein. Liu, S., Thweatt, R., Lumpkin, C.K., Goldstein, S. Proc. Natl. Acad. Sci. U.S.A. (1994) [Pubmed]
  9. Transgelin Functions as a Suppressor via Inhibition of ARA54-Enhanced Androgen Receptor Transactivation and Prostate Cancer Cell Growth. Yang, Z., Chang, Y.J., Miyamoto, H., Ni, J., Niu, Y., Chen, Z., Chen, Y.L., Yao, J.L., di Sant'agnese, P.A., Chang, C. Mol. Endocrinol. (2007) [Pubmed]
  10. The proteomics approach to find biomarkers in gastric cancer. Ryu, J.W., Kim, H.J., Lee, Y.S., Myong, N.H., Hwang, C.H., Lee, G.S., Yom, H.C. J. Korean Med. Sci. (2003) [Pubmed]
  11. Expression and cytogenetic localization of the human SM22 gene (TAGLN). Camoretti-Mercado, B., Forsythe, S.M., LeBeau, M.M., Espinosa, R., Vieira, J.E., Halayko, A.J., Willadsen, S., Kurtz, B., Ober, C., Evans, G.A., Thweatt, R., Shapiro, S., Niu, Q., Qin, Y., Padrid, P.A., Solway, J. Genomics (1998) [Pubmed]
  12. Human SM22 alpha BAC encompasses regulatory sequences for expression in vascular and visceral smooth muscles at fetal and adult stages. Xu, R., Ho, Y.S., Ritchie, R.P., Li, L. Am. J. Physiol. Heart Circ. Physiol. (2003) [Pubmed]
  13. Fibroblast transgelin and smooth muscle SM22alpha are the same protein, the expression of which is down-regulated in many cell lines. Lawson, D., Harrison, M., Shapland, C. Cell Motil. Cytoskeleton (1997) [Pubmed]
  14. Localized adenovirus-mediated gene transfer into vascular smooth muscle in the hamster cheek pouch. Frame, M.D., Miano, J.M., Yang, J., Rivers, R.J. Microcirculation (New York, N.Y. : 1994) (2001) [Pubmed]
  15. Expression of senescence-induced protein WS3-10 in vivo and in vitro. Grigoriev, V.G., Thweatt, R., Moerman, E.J., Goldstein, S. Exp. Gerontol. (1996) [Pubmed]
  16. Investigation of early protein changes in the urinary bladder following partial bladder outlet obstruction by proteomic approach. Kim, H.J., Sohng, I., Kim, D.H., Lee, D.C., Hwang, C.H., Park, J.Y., Ryu, J.W. J. Korean Med. Sci. (2005) [Pubmed]
  17. Identification of autoantibodies elicited in a patient with prostate cancer presenting as dermatomyositis. Mooney, C.J., Dunphy, E.J., Stone, B., McNeel, D.G. International journal of urology : official journal of the Japanese Urological Association. (2006) [Pubmed]
  18. Dynamic changes in chromatin acetylation and the expression of histone acetyltransferases and histone deacetylases regulate the SM22alpha transcription in response to Smad3-mediated TGFbeta1 signaling. Qiu, P., Ritchie, R.P., Gong, X.Q., Hamamori, Y., Li, L. Biochem. Biophys. Res. Commun. (2006) [Pubmed]
  19. UVB-induced premature senescence of human diploid skin fibroblasts. Chainiaux, F., Magalhaes, J.P., Eliaers, F., Remacle, J., Toussaint, O. Int. J. Biochem. Cell Biol. (2002) [Pubmed]
  20. Identification of differential genes in ovarian cancer using representational difference analysis of cDNA. Chen, H., Wang, M., Wang, X.Y., Gao, S., Wang, J., Guan, X.M. Chin. Med. Sci. J. (2005) [Pubmed]
  21. Cyclic strain induces expression of specific smooth muscle cell markers in human endothelial cells. Cevallos, M., Riha, G.M., Wang, X., Yang, H., Yan, S., Li, M., Chai, H., Yao, Q., Chen, C. Differentiation (2006) [Pubmed]
  22. Purification, characterization, and partial sequence analysis of a new 25-kDa actin-binding protein from bovine aorta: a SM22 homolog. Kobayashi, R., Kubota, T., Hidaka, H. Biochem. Biophys. Res. Commun. (1994) [Pubmed]
  23. Calponin and SM 22 as differentiation markers of smooth muscle: spatiotemporal distribution during avian embryonic development. Duband, J.L., Gimona, M., Scatena, M., Sartore, S., Small, J.V. Differentiation (1993) [Pubmed]
  24. Mechanical regulation of matrix reorganization and phenotype of smooth muscle cells and mesenchymal stem cells in 3D matrix. Liao, S., Hida, K., Park, J., Li, S. Conference proceedings : ... Annual International Conference of the IEEE Engineering in Medicine and Biology Society. IEEE Engineering in Medicine and Biology Society. Conference (2004) [Pubmed]
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