Comprehensive characterization of protein 4.1 expression in epithelium of large intestine

Zhang, Jingxin and Yang, Shaomin and An, Chao and Wang, Jie and Yan, Hongxia and Huang, Yumin and Song, Jinlei and Yin, Changcheng and Baines, Anthony J. and Mohandas, Narla and An, Xiuli (2014) Comprehensive characterization of protein 4.1 expression in epithelium of large intestine. Histochemistry and Cell Biology, 142 (5). pp. 529-539. ISSN 0948-6143. E-ISSN 1432-119X. (doi:https://doi.org/10.1007/s00418-014-1224-z) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided)

The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided. (Contact us about this Publication)
Official URL
http://dx.doi.org/10.1007/s00418-014-1224-z

Abstract

The protein 4.1 family consists of four members, 4.1R, 4.1N, 4.1B and 4.1G, each encoded by a distinct gene. All 4.1 mRNAs undergo extensive alternative splicing. Functionally, they usually serve as adapters that link actin-based cytoskeleton to plasma membrane proteins. It has been reported that 4.1 proteins are expressed in most animal cell types and tissues including epithelial cells and epithelial tissues. However, the expression of 4.1 proteins in large intestine has not been well characterized. In the present study, we performed RT-PCR, western blot and immunohistochemistry analysis to characterize the transcripts, the protein expression and cellular localization of 4.1 proteins in the epithelia of mouse large intestine. We show that multiple transcripts derive from each gene, including eight 4.1R isoforms, four 4.1N isoforms, four 4.1B isoforms and six 4.1G isoforms. However, at the protein level, only one or two major bands were detected, implying that not all transcripts are translated and/or the proteins do not accumulate at detectable levels. Immunohistochemistry revealed that 4.1R, 4.1N and 4.1B are all expressed at the lateral membrane as well as cytoplasm of epithelial cells, suggesting a potentially redundant role of these proteins. Our findings not only provide new insights into the structure of protein 4.1 genes but also lay the foundation for future functional studies.

Item Type: Article
Subjects: Q Science
Divisions: Faculties > Sciences > School of Biosciences
Depositing User: Sue Davies
Date Deposited: 20 Oct 2014 13:59 UTC
Last Modified: 20 Jul 2015 09:03 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/43516 (The current URI for this page, for reference purposes)
  • Depositors only (login required):