ABC  Vol.4 No.1 , February 2014
Interaction of calcium- and integrin-binding protein 1 with integrin α11 and its possible involvement in pulmonary fibrosis
ABSTRACT

Integrin α11 (ITGA11) is one of the collagen-binding integrin α chains; however, its biological significance remains unknown. To determine the functions of ITGA11, we performed a yeast two-hybrid screen using the cytoplasmic domain of ITGA11 as bait and transformed an EGY48 yeast strain with the bait-containing plasmid using the plasmid from a human lung fibroblast cDNA library. This screen identified calcium- and integrin-binding protein 1 (CIB1) as prey. Recombinant ITGA11 and CIB1 were expressed in mammalian cells and used in coimmunoprecipitation experiments, which showed that full-length ITGA11 and CIB1 are also associated in vivo. Over-expression of CIB1 in the human lung myofibroblast MRC-5 cells decreased the expression of α-smooth muscle actin and fibronectin. Using a mouse model of pulmonary fibrosis (bleomycin-treatment), we detected elevated expression of CIB1 in lung tissues compared with controls. These data suggest that CIB1 may regulate pulmonary fibrosis in concert with IT-GA11.


Cite this paper
Yoshida, K. , Park, A. , Ozaki, S. and Munakata, H. (2014) Interaction of calcium- and integrin-binding protein 1 with integrin α11 and its possible involvement in pulmonary fibrosis. Advances in Biological Chemistry, 4, 59-66. doi: 10.4236/abc.2014.41009.
References
[1]   Honda, E., Yoshida, K. and Munakata, H. (2010) Transforming growth factor-β upregulates the expression of integrin and related proteins in MRC-5 human myofibroblasts. Tohoku Journal of Experimental Medicine, 220, 319-327.
http://dx.doi.org/10.1620/tjem.220.319

[2]   Border, W.A. and Noble, N.A. (1994) Transforming growth factor β in tissue fibrosis. New England Journal of Medicine, 331, 1286-1292.
http://dx.doi.org/10.1056/NEJM199411103311907

[3]   Schuppan, D., Krebs, A., Bauer, M. and Hahn, E.G. (2003) Hepatitis C and liver fibrosis. Cell Death & Differentiation, 10, S59-S67.
http://dx.doi.org/10.1038/sj.cdd.4401163

[4]   Akhmetshina, A., Palumbo, K., Dees, C., Bergmann, C., Venalis, P., Zerr, P., Horn, A., Kireva, T., Beyer, C., Zwerina, J., Schneider, H., Sadowski, A., Riener, M.O., Mac-Dougald, O.A., Distler, O., Schett, G. and Distler, J.H. (2012) Activation of canonical Wnt signalling is required for TGF-β-mediated fibrosis. Nature Communications, 3, 735.
http://dx.doi.org/10.1038/ncomms1734

[5]   Chung, H.J., Steplewski, A., Chung, K.Y., Uitto, J. and Fertala, A. (2008) Collagen fibril formation. A new target to limit fibrosis. Journal of Biological Chemistry, 283, 25879-25886.
http://dx.doi.org/10.1038/ncomms1734

[6]   Iredale, J.P., Thompson, A. and Henderson, N.C. (2013) Extracellular matrix degradation in liver fibrosis: Biochemistry and regulation. Biochimica et Biophysica Acta, 1832, 876-883.
http://dx.doi.org/10.1016/j.bbadis.2012.11.002

[7]   Honda, E., Park, A.M., Yoshida, K., Tabuchi, M. and Munakata, H. (2013) Myofibroblasts: Biochemical and proteomic approaches to fibrosis. Tohoku Journal of Experimental Medicine, 230, 67-73.
http://dx.doi.org/10.1620/tjem.230.67

[8]   Gullberg, D., Velling, T., Sjoberg, G. and Sejersen, T. (1995) Up-regulation of a novel integrin α-chain (αmt) on human fetal myotubes. Developmental Dynamics, 204, 57-65.
http://dx.doi.org/10.1002/aja.1002040108

[9]   Velling, T., Kusche-Gullberg, M., Sejersen, T. and Gullberg, D. (1999) cDNA cloning and chromosomal localization of human α11 integrin. A collagen-binding, I domain-containing, β1-associated integrin α-chain present in muscle tissues. Journal of Biological Chemistry, 274, 25735-25742.
http://dx.doi.org/10.1074/jbc.274.36.25735

[10]   Zhu, C.Q., Popova, S.N., Brown, E.R., Barsyte-Lovejoy, D., Navab, R., Shih, W., Li, M., Lu, M., Jurisica, I., Penn, L.Z., Gullberg, D. and Tsao, M.S. (2007) Integrin α11 regulates IGF2 expression in fibroblasts to enhance tumo-rigenicity of human non-small-cell lung cancer cells. Proceedings of the National Academy of Sciences of the United States of America, 104, 11754-11759.
http://dx.doi.org/10.1073/pnas.0703040104

[11]   Popov, C., Radic, T., Haasters, F., Prall, W.C., Aszodi, A., Gullberg, D., Schieker, M. and Docheva, D. (2011) Integrins α2β1 and α11β1 regulate the survival of mesenchymal stem cells on collagen I. Cell Death and Disease, 2, e186.
http://dx.doi.org/10.1038/cddis.2011.71

[12]   Popova, S.N., Barczyk, M., Tiger, C.F., Beertsen, W., Zigrino, P., Aszodi, A., Miosge, N., Forsberg, E. and Gullberg, D. (2007) α11β1 integrin-dependent regulation of periodontal ligament function in the erupting mouse incisor. Molecular and Cellular Biology, 27, 4306-4316.
http://dx.doi.org/10.1128/MCB.00041-07

[13]   Bystrom, B., Carracedo, S., Behndig, A., Gullberg, D. and Pedrosa-Domellof, F. (2009) α11 integrin in the human cornea: Importance in development and disease. Investigative Ophthalmology & Visual Science, 50, 5044-5053.
http://dx.doi.org/10.1167/iovs.08-3261

[14]   Talior-Volodarsky, I., Connelly, K.A., Arora, P.D., Gullberg, D. and McCulloch, C.A. (2012) α11 integrin stimulates myofibroblast differentiation in diabetic cardiomyopathy. Cardiovascular Research, 96, 265-275.
http://dx.doi.org/10.1093/cvr/cvs259

[15]   Barczyk, M.M., Lu, N., Popova, S.N., Bolstad, A.I. and Gullberg, D. (2013) α11β1 integrin-mediated MMP-13-dependent collagen lattice contraction by fibroblasts: Evidence for integrin-coordinated collagen proteolysis. Journal of Cellular Physiology, 228, 1108-1119.
http://dx.doi.org/10.1002/jcp.24261

[16]   Yoshida, K., Suzuki, Y., Saito, A., Fukuda, K., Hamanishi, C. and Munakata, H. (2005) Aggrecanase-1 (ADAMTS-4) interacts with α1-antitrypsin. Biochimica et Biophysica Acta, 1725, 152-159.
http://dx.doi.org/10.1016/j.bbagen.2005.06.009

[17]   Shock, D.D., Naik, U.P., Brittain, J.E., Alahari, S.K., Sondek, J. and Parise, L.V. (1999) Calcium-dependent properties of CIB binding to the integrin αIIb cytoplasmic domain and translocation to the platelet cytoskeleton. Biochemical Journal, 342, 729-735.
http://dx.doi.org/10.1016/j.bbagen.2005.06.009

[18]   Whitehouse, C., Chambers, J., Howe, K., Cobourne, M., Sharpe, P. and Solomon, E. (2002) NBR1 interacts with fasciculation and elongation protein zeta-1 (FEZ1) and calcium and integrin binding protein (CIB) and shows developmentally restricted expression in the neural tube. European Journal of Biochemistry, 269, 538-545.
http://dx.doi.org/10.1046/j.0014-2956.2001.02681.x

[19]   Naik, U.P., Patel, P.M. and Parise, L.V. (1997) Identification of a novel calcium-binding protein that interacts with the integrin αIIb cytoplasmic domain. Journal of Biological Chemistry, 272, 4651-4654.
http://dx.doi.org/10.1074/jbc.272.8.4651

[20]   Stabler, S.M., Ostrowski, L.L., Janicki, S.M. and Monteiro, M.J. (1999) A myristoylated calcium-binding protein that preferentially interacts with the Alzheimer’s disease presenilin 2 protein. Journal of Cell Biology, 145, 1277-1292.
http://dx.doi.org/10.1083/jcb.145.6.1277

[21]   Lehnert, K., Ni, J., Leung, E., Gough, S.M., Weaver, A., Yao, W.P., Liu, D., Wang, S.X., Morris, C.M. and Krissansen, G.W. (1999) Cloning, sequence analysis, and chromosomal localization of the novel human integrin α11 subunit (ITGA11). Genomics, 60, 179-187.
http://dx.doi.org/10.1006/geno.1999.5909

[22]   Leitinger, B. and Hohenester, E. (2007) Mammalian collagen receptors. Matrix Biology, 26, 146-155.
http://dx.doi.org/10.1016/j.matbio.2006.10.007

[23]   Barczyk, M., Carracedo, S. and Gullberg, D. (2010) Integrins. Cell and Tissue Research, 339, 269-280.
http://dx.doi.org/10.1007/s00441-009-0834-6

[24]   Yamodo, I.H. and Blystone, S.D. (2012) Calcium integrin binding protein associates with integrins αVβ3 and αIIbβ3 independent of β3 activation motifs. CellBio (Irvine, Calif), 1, 30-37.
http://dx.doi.org/10.4236/cellbio.2012.12004

[25]   Freeman Jr., T.C., Black, J.L., Bray, H.G., Dagliyan, O., Wu, Y.I., Tripathy, A., Dokholyan, N.V., Leisner, T.M. and Parise, L.V. (2013) Identification of novel integrin binding partners for calcium and integrin binding protein 1 (CIB1): Structural and thermodynamic basis of CIB1 promiscuity. Biochemistry, 52, 7082-7090.
http://dx.doi.org/10.1021/bi400678y

[26]   Hinz, B., Celetta, G., Tomasek, J.J., Gabbiani, G. and Chaponnier, C. (2001) α-smooth muscle actin expression upregulates fibroblast contractile activity. Molecular Biology of the Cell, 12, 2730-2741.
http://dx.doi.org/10.1091/mbc.12.9.2730

[27]   Kadler, K.E., Hill, A. and Canty-Laird, E.G. (2008) Collagen fibrillogenesis: Fibronectin, integrins, and minor collagens as organizers and nucleators. Current Opinion in Cell Biology, 20, 495-501.
http://dx.doi.org/10.1016/j.ceb.2008.06.008

[28]   Klingberg, F., Hinz, B. and White, E.S. (2013) The myofibroblast matrix: Implications for tissue repair and fibrosis. Journal of Pathology, 229, 298-309.
http://dx.doi.org/10.1002/path.4104

[29]   Heineke, J., Auger-Messier, M., Correll, R.N., Xu, J., Benard, M.J., Yuan, W., Drexler, H., Parise, L.V. and Molkentin, J.D. (2010) CIB1 is a regulator of pathological cardiac hypertrophy. Nature Medicine, 16, 872-879.
http://dx.doi.org/10.1038/nm.2181

[30]   Zayed, M.A., Yuan, W., Chalothorn, D., Faber, J.E. and Parise, L.V. (2010) Tumor growth and angiogenesis is impaired in CIB1 knockout mice. Journal of Angiogenesis Research, 2, 17.
http://dx.doi.org/10.1186/2040-2384-2-17

[31]   Moeller, A., Ask, K., Warburton, D., Gauldie, J. and Kolb, M. (2008) The bleomycin animal model: A useful tool to investigate treatment options for idiopathic pulmonary fibrosis? International Journal of Biochemistry & Cell Biology, 40, 362-382.
http://dx.doi.org/10.1016/j.biocel.2007.08.011

 
 
Top