Effect of lead on cytoskeletal protein stability in crucian carp Carassius auratus

Jia Cheng; Dongyi Zhang; Wuying Chu; Fang Liu; Zhen Liu; Ruixue Zhou; Tao Meng; Jianshe Zhang

doi:10.1007/s00343-008-0400-1

Your Location：

Home >

Browse articles >

Effect of lead on cytoskeletal protein stability in crucian carp Carassius auratus

OriginalPaper | Updated：2023-05-16

- Effect of lead on cytoskeletal protein stability in crucian carp Carassius auratus
- Effect of lead on cytoskeletal protein stability in crucian carp Carassius auratus
- 海洋湖沼学报（英文） 2008年26卷第4期页码：400-406
- Affiliations：
  
  1. Department of Bioengineering and Environmental Science Changsha University
  2. Core Facilities of Biotechnology Central South University of Forestry and Technology
- Author bio：
- Funds：
  
  Supported by National Natural Science Foundation of China (No. 30571414, No 30640015) and Changsha Municipal Project of Science and Technology (No. K051127-72).
- DOI：10.1007/s00343-008-0400-1
  中图分类号：
- 网络首发：2009-01-23，
  
  纸质出版：2008
- Accepted：
Scan QR Code
Effect of lead on cytoskeletal protein stability in crucian carp Carassius auratus[J]. 海洋湖沼学报（英文）, 2008,26(4):400-406.

Cheng, J., Zhang, D., Chu, W. et al. Effect of lead on cytoskeletal protein stability in crucian carp Carassius auratus, ., Chin. J. Ocean. Limnol. 26, 400–406 (2008). https://doi.org/10.1007/s00343-008-0400-1
Effect of lead on cytoskeletal protein stability in crucian carp Carassius auratus[J]. 海洋湖沼学报（英文）, 2008,26(4):400-406. DOI： 10.1007/s00343-008-0400-1.

Cheng, J., Zhang, D., Chu, W. et al. Effect of lead on cytoskeletal protein stability in crucian carp Carassius auratus, ., Chin. J. Ocean. Limnol. 26, 400–406 (2008). https://doi.org/10.1007/s00343-008-0400-1 DOI：

摘要

Abstract

Inorganic lead (Pb) is one of the most common environmental pollutants. Much evidence indicates that Pb exposure could directly affect fish growth and development. In this study

we investigated the cytotoxic effects of Pb on cytoskeletal protein stability at both protein and mRNA level in crucian carp Carassius auratus. Pb(NO3)2 treatment in concentration of 100 μmol/L resulted in decreased expression of both α- and β-tubulin but γ-tubulin as assayed with SDS-PAGE

Western Blot

and ELISA. In vivo and in vitro analyses on protein expression of tubulins are consistent. The effect of Pb on mRNA expression varied among different tissues. Our results suggest that cytotoxicity of Pb at protein translation level is stronger than at mRNA expression level.

关键词

Keywords

references

Alfano, D. P. and T. L. Petit, 1982. Neonatal lead exposure alters the dendritic development of hippocampal dentate granule cells. Exp. Neurol. 75: 275–299.

Bonacker, D., T. Stoiber, K. J. Bohm, M. Wang, E. Unger, R. Their, H. M. Bolt and G. H. Gegen, 2005. Genotoxicity of inorganic lead salts and disturbance of microtubule function. Environ. Mol. Mutagen. 45(4): 346–353.

Burger, J., E. F. Orlando, M. Gochfeld, G. A. Binczik and L. J. Guillette, 2004. Metal levels in tissues of Florida gar (Lepisosteus platyhicus) from Lake Okeechobee. Environ. Monit. Assess. 90(1–3): 187–201.

Cline, H. T., S. Witte and K. W. Jones, 1996. Low lead level stunt neuronal growth in reversible manner. Proc. Natl. Acad. Sci. U. S. A. 93: 9 915–9 920.

Eun, S. O., H. S. Youn and Y. Lee, 2000. Lead disturbs microtubule organization in the root meristem of Zea mays. Physiol. Plant 110: 357–365.

Farrell, K. W. and R. G. Burns, 1975. Inability to detect Chlayodomonas microtubule assembly in vitro: possible implication to the in vivo regulation of microtubule assembly. J. Cell Sci. 17(3): 669–681.

Gerber, G. B., A. Leonard and P. Jacquet, 1980. Toxicity, mutagenecity and teratogenicity of lead. Mutat. Res. 76: 115–141.

Janssen, C. R., D. G. Heijerick, K. A. de Schamphelaere and H. E. Allen, 2003. Environmental risk assessment of metals: tools for incorporating bioavailability. Environ. Int. 28(8): 793–800.

Johnson, F. M., 1998. The genetic effects of environmental lead. Mutat. Res. 410: 123–140.

Kim, S. G. and J. C. Kang, 2004. Effect of dietary copper exposure on accumulation, growth and hematological parameters of the juvenile rockfish, Sebastes schlegeli. Mar. Environ. Res. 58(1): 65–82.

Lorton, D. and W. J. Anderson, 1986. Altered pyramidal cell dendritic development in the motor cortex of lead intoxicated neonatal rats: A Golgi study. Neurobehav. Toxicol. Teratol. 8: 45–50.

MacRae, H. T., 1992. Towards and understanding of microtubule function and cell organization: an overview. Biochem. Cell Biol. 70: 835–841.

Palus, J., K. Rydzynski, E. Dziubaltowska, K. Wyszynska, A. T. Natarajam and R. Nilsson, 2003. Genotoxic effects of occupational exposure to lead and calcium. Mutat. Res. 540: 19–28.

Riggio, M., S. Filosa, E. Parisi and R. Scudiero, 2003. Changes in zinc, copper and metallonthionein contents during oocyte growth and early development of the teleost Danio rerio (Zebrafish). Comp. Biochem. Physiol. C. Toxicol. Pharmarcol. 135(2): 191–196.

Sambrook, J. and D. W. Russell, 2002. Molecular cloning: a laboratory manual, 3rd ed. Science press, Beijing China. p. 752–770. (in Chinese)

Scortegagna, M., E. Chikhale and I. Hanbauer, 1998. Effect of lead on cytoskeletal proteins expressed in E14 mesencephalic primary cultures. Neurochem. Int. 32: 353–359.

Stoiber, T., D. Bonacker, K. J. Bohm, H. M. Bolt, R. Their, G. H. Degen and E. Unger, 2004. Disturbed microtubule function and induction of micronuclei by chelate complexes of mercury (II). Mutat. Res. 3: 97–106.

Towbin, H., T. Staehlin and J. Gordon, 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedures and some applications. Proc. Natl. Acad. Sci. U. S. A. 76: 4 350–4 354.

Vaglenov, A., A. Creus, S. Laltchev, S. Petkova and R. Marcos, 2001. Occupational exposure to lead and induction of genetic damage. Environ. Health Prespect 109: 295–298.

Vallee, R. B., 1990. Molecular characterization of high molecular weight microtubule-associated proteins: some answers, many questions. Cell Motil. Cytoskeleton 15: 204–209.

Vosyliene, M. Z., N. Kazlauskiene and G. Svecevicius, 2003. Effect of a heavy metal model mixture on biological parameters of rainbow trout Oncorhynchus mykiss. Environ. Sci. Pollut. Res. Int. 10(2): 103–107.

Weng, J., W. Ma, D. Mitchell, J. Zhang and M. Liu, 2005. Transcriptional regulation of human prostate-specific G-protein coupled receptor, PSGR, by two distinct promoters and growth factors. J. Cell. Biochem. 96(5): 1 034–1 038.

Wiche, G., 1989. High microtubule-associated proteins: properties and functions. Biochem. J. 259(1): 1–12.

Xia, C., W. Ma, L. J. Scafford, W. C. Xiong and M. Liu, 2001. Regulation of the p21-activated kinase (PAK) by a human Gbeta -like WD-repeat protein, hPIP1. Proc. Natl. Acad. Sci. U. S. A. 98: 6 174–6 179.

Yamazaki, Y., M. Tseruga, D. Zhou, Y. Fujita, X. Shang, Y. Dang, K. Kawasaki and S. Oka, 2000. Cytoskeletal disruption accelerates caspase-3 activation and alters the intracellular membrane reorganization in DNA damage-induced apoptosis. Exp. Cell Res. 259: 64–78.

Zhang, J., C. Kong, H. Xie, P. McPherson, S. Grinstein and W. S. Trimble, 1999. Phosphatidylinositol polyphosphate binding to the mammalian septin H5 is modulated by GTP. Curr. Biol. 9(24): 1 458–1 567.

Zhang, J. and T. H. MacRae, 1992. A novel 49-kilodalton protein from Artemia crosslinks microtubules in vitro. Biochem. Cell Biol. 70: 1 055–1 063.

浏览量

Downloads

CSCD

文章被引用时，请邮件提醒。

Submit

工具集

关联资源

Expression profile of long non-coding RNAs in the intestine of black rockfish Sebastes schlegelii in response to Edwardsiella tarda infection

Kinetics of lead adsorption by Xiamen Bay sediments

Digestive enzyme activity and mRNA level of trypsin in embryonic redclaw crayfish, Cherax quadricarnatus

Comparison of ciliature microtubule organelles in three hypotrichous ciliate species

导流锥结构参数对燃气弹射筒内压力冲击平滑效果影响研究