Overexpression of <i>YKL-39</i> Gene in Glial Brain Tumors

Kavsan, Vadym; Dmitrenko, Vladimir; Boyko, Oxana; Filonenko, Valery; Avdeev, Stanislav; Areshkov, Pavel; Marusyk, Andriy; Malisheva, Tatiana; Rozumenko, Vladimir; Zozulya, Yury

doi:https://doi.org/10.3814/2008/814849

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Volume 2008 | Article ID 814849 | https://doi.org/10.3814/2008/814849

Overexpression of YKL-39 Gene in Glial Brain Tumors

Vadym Kavsan,¹Vladimir Dmitrenko,¹Oxana Boyko,¹Valery Filonenko,¹Stanislav Avdeev,¹Pavel Areshkov,¹Andriy Marusyk,¹Tatiana Malisheva,²Vladimir Rozumenko,²and Yury Zozulya²

Received23 Jun 2008

Revised09 Sept 2008

Accepted22 Sept 2008

Published23 Oct 2008

Abstract

More than forty genes with considerably increased expression in glioblastoma as compared to normal human brain were identified by SAGE. One of the most prominent among them was CHI3L2 (YKL-39) gene, which encodes 39 kDa chitinase-like protein. Northern blot hybridization confirmed the data of SAGE for the majority of glioblastomas. Anaplastic astrocytomas could be divided on two groups: in one of them the YKL-39 expression was completely undetectable, but in the other group quite high contents of YKL-39 mRNA were detected. In this study, preliminary data show that patients with undetectable expression of YKL-39 in anaplastic astrocytomas did not have recurrent tumors quite long (more than 2-3 years) period of time. YKL-39 RNA has not been detected in diffuse astrocytomas and in all (but one) samples of normal brain. Increased expression of YKL-39 gene in glioblastomas was shown also at the protein level. Western blots did not shown simultaneous production of YKL-39 and YKL-40, in spite of having high degree of their sequence identity. Increased expression of YKL-39 in subsets of patients with glial tumors, reported here for the first time, together with abnormal increase of the YKL-40 gene expression may be a novel molecular marker for glial tumors.

References

G. Reifenberger and V. P. Collins, “Pathology and molecular genetics of astrocytic gliomas,” Journal of Molecular Medicine, vol. 82, no. 10, pp. 656–670, 2004.
View at: Publisher Site | Google Scholar
Y. Cheng, H.-K. Ng, M. Ding, S.-F. Zhang, J. C.-S. Pang, and K.-W. Lo, “Molecular analysis of microdissected de novo glioblastomas and paired astrocytic tumors,” Journal of Neuropathology and Experimental Neurology, vol. 58, no. 2, pp. 120–128, 1999.
View at: Google Scholar
V. Kavsan, K. Shostak, V. Dmitrenko, Y. Zozulya, V. Rozumenko, and J. Demotes-Mainard, “Characterization of genes with increased expression in human glioblastomas,” Tsitology and Genetics, vol. 39, no. 6, pp. 37–49, 2005.
View at: Google Scholar
B. Hu, K. Trinh, W. F. Figueira, and P. A. Price, “Isolation and sequence of a novel human chondrocyte protein related to mammalian members of the chitinase protein family,” The Journal of Biological Chemistry, vol. 271, no. 32, pp. 19415–19420, 1996.
View at: Publisher Site | Google Scholar
D. N. Louis, H. Ohgaki, O. D. Wiestler et al., “The 2007 WHO classification of tumours of the central nervous system,” Acta Neuropathologica, vol. 114, no. 2, pp. 97–109, 2007.
View at: Publisher Site | Google Scholar
K. Boon and G. J. Riggins, “SAGE as a strategy to isolate cancer-related genes,” Methods in Molecular Biology, vol. 222, pp. 463–479, 2003.
View at: Publisher Site | Google Scholar
V. Kavsan, V. Dmitrenko, K. Shostak et al., “Comparison of microarray and SAGE techniques in gene expression analysis of human glioblastoma,” Tsitology and Genetics, vol. 41, no. 1, pp. 36–55, 2007.
View at: Google Scholar
V. Dmitrenko, O. I. Bojko, K. Shostak et al., “Characterization of genes, down-regulated in human glioma, potential tumor suppressor genes,” Biopolymers and Cell, vol. 23, no. 4, pp. 347–362, 2007.
View at: Google Scholar
P. Chomczynski and N. Sacchi, “Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction,” Analytical Biochemistry, vol. 162, no. 1, pp. 156–159, 1987.
View at: Publisher Site | Google Scholar
L. L. Sidorik, O. I. Gudzera, V. A. Dragovoz, M. A. Tukalo, and S. F. Beresten, “Immuno-chemical non-cross-reactivity between eukaryotic and prokaryotic seryl-tRNA synthetases,” FEBS Letters, vol. 292, no. 1-2, pp. 76–78, 1991.
View at: Publisher Site | Google Scholar
M. M. Bradford, “A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding,” Analytical Biochemistry, vol. 72, no. 1-2, pp. 248–254, 1976.
View at: Publisher Site | Google Scholar
W. N. Burnette, ““Western blotting”: electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A,” Analytical Biochemistry, vol. 112, no. 2, pp. 195–203, 1981.
View at: Publisher Site | Google Scholar
F. Fusetti, T. Pijning, K. H. Kalk, E. Bos, and B. W. Dijkstra, “Crystal structure and carbohydrate-binding properties of the human cartilage glycoprotein-39,” The Journal of Biological Chemistry, vol. 278, no. 39, pp. 37753–37760, 2003.
View at: Publisher Site | Google Scholar
R. G. Boot, G. H. Renkema, A. Strijland, A. J. van Zonneveld, and J. M. F. G. Aerts, “Cloning of a cDNA encoding chitotriosidase, a human chitinase produced by macrophages,” The Journal of Biological Chemistry, vol. 270, no. 44, pp. 26252–26256, 1995.
View at: Publisher Site | Google Scholar
B. E. Hakala, C. White, and A. D. Recklies, “Human cartilage gp-39, a major secretory product of articular chondrocytes and synovial cells, is a mammalian member of a chitinase protein family,” The Journal of Biological Chemistry, vol. 268, no. 34, pp. 25803–25810, 1993.
View at: Google Scholar
H. M. Jin, N. G. Copeland, D. J. Gilbert, N. A. Jenkins, R. B. Kirkpatrick, and M. Rosenberg, “Genetic characterization of the murine Ym1 gene and identification of a cluster of highly homologous genes,” Genomics, vol. 54, no. 2, pp. 316–322, 1998.
View at: Publisher Site | Google Scholar
E. B. Arias, H. G. Verhage, and R. C. Jaffe, “Complementary deoxyribonucleic acid cloning and molecular characterization of an estrogen-dependent human oviductal glycoprotein,” Biology of Reproduction, vol. 51, no. 4, pp. 685–694, 1994.
View at: Google Scholar
J. Kzhyshkowska, S. Mamidi, A. Gratchev et al., “Novel stabilin-1 interacting chitinase-like protein (SI-CLP) is up-regulated in alternatively activated macrophages and secreted via lysosomal pathway,” Blood, vol. 107, no. 8, pp. 3221–3228, 2006.
View at: Publisher Site | Google Scholar
J. J. Rejman and W. L. Hurley, “Isolation and characterization of a novel 39 kilodalton whey protein from bovine mammary secretions collected during the nonlactating period,” Biochemical and Biophysical Research Communications, vol. 150, no. 1, pp. 329–334, 1988.
View at: Google Scholar
S. W. Krause, M. Rehli, M. Kreutz, L. Schwarzfischer, J. D. Paulauskis, and R. Andreesen, “Differential screening identifies genetic markers of monocyte to macrophage maturation,” Journal of Leukocyte Biology, vol. 60, no. 4, pp. 540–545, 1996.
View at: Google Scholar
C. Cintin, J. S. Johansen, I. J. Christensen, P. A. Price, S. Sørensen, and H. J. Nielsen, “Serum YKL-40 and colorectal cancer,” British Journal of Cancer, vol. 79, no. 9-10, pp. 1494–1499, 1999.
View at: Publisher Site | Google Scholar
J. S. Johansen, C. Cintin, M. Jørgensen, C. Kamby, and P. A. Price, “Serum YKL-40: a new potential marker of prognosis and location of métastases of patients with recurrent breast cancer,” European Journal of Cancer, vol. 31, no. 9, pp. 1437–1442, 1995.
View at: Publisher Site | Google Scholar
M. K. Tanwar, M. R. Gilbert, and E. C. Holland, “Gene expression microarray analysis reveals YKL-40 to be a potential serum marker for malignant character in human glioma,” Cancer Research, vol. 62, no. 15, pp. 4364–4368, 2002.
View at: Google Scholar
K. Shostak, V. Labunskyy, V. Dmitrenko et al., “HC gp-39 gene is upregulated in glioblastomas,” Cancer Letters, vol. 198, no. 2, pp. 203–210, 2003.
View at: Publisher Site | Google Scholar
T. Knorr, F. Obermayr, E. Bartnik, A. Zien, and T. Aigner, “YKL-39 (chitinase 3-like protein 2), but not YKL-40 (chitinase 3-like protein 1), is up regulated in osteoarthritic chondrocytes,” Annals of the Rheumatic Diseases, vol. 62, no. 10, pp. 995–998, 2003.
View at: Publisher Site | Google Scholar

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Copyright © 2008 Vadym Kavsan et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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