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The Mouse Thymosin Beta15 Gene Family Displays Unique Complexity and Encodes A Functional Thymosin Repeat

Stien Dhaese UGent, Klaas Vandepoele UGent, DAVY WATERSCHOOT, Berlinda Vanloo UGent, Joël Vandekerckhove, Christophe Ampe UGent and Marleen Van Troys UGent (2009) JOURNAL OF MOLECULAR BIOLOGY. 387(4). p.809-825
abstract
We showed earlier that human beta -thymosin 15 (Th15) is up-regulated in prostate cancer, confirming Studies from others that propagated Tb15 as a prostate cancer biomarker. In this first report on mouse Tb15, we show that, unlike in humans, four Tb15-like isoforms are present in Mouse. We used phylogenetic analysis of deuterostome beta-thymosins to show that these four new isoforms cluster within the vertebrate Tb15-clade. Intriguingly, one of these Mouse beta-thymosins, Th15r, consists of two beta-thymosin domains. The existence of such a repeat beta-thymosin is so far unique in vertebrates, though common in lower eukaryotes. Biochemical data indicate that Tb15r potently sequesters actin. In a cellular context, Tb15r behaves as a bona fide beta-thymosin, lowering central stress fibre content. We reveal that a complex genomic organization underlies Tb15r expression: Tb15r results from read-through transcription and alternative splicing of two tandem duplicated mouse Tb15 genes. Transcript profiling of all Mouse beta-thymosin isoform (Th15s, Tb4 and Tb10) reveals that two isoform switches occur between embryonic and adult tissues, and indicates Th15r as the major mouse Tb15 isoform in adult cells. Tb15r is present also in mouse prostate cancer cell lines. This insight into the mouse Tb15 family is fundamental for future studies on Tb15 in mouse (prostate) cancer models.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
keyword
BINDING-SITE, MOLECULAR-CLONING, URINARY BIOMARKER, actin, thymosin, read-through transcript, phylogeny, qRT-PCR, KeyWords Plus: ACTIN NUCLEATION FACTOR, HUMAN PROSTATE-CANCER, CELL-LINES, RAT THYMOSIN-BETA-15, STRUCTURAL-CHARACTERIZATION, PROTEINS, BETA-15
journal title
JOURNAL OF MOLECULAR BIOLOGY
J. Mol. Biol.
volume
387
issue
4
pages
809 - 825
publisher
ACADEMIC PRESS LTD ELSEVIER SCIENCE LTD
place of publication
24-28 OVAL RD, LONDON NW1 7DX, ENGLAND
Web of Science type
Article
Web of Science id
000265302700003
JCR category
BIOCHEMISTRY & MOLECULAR BIOLOGY
JCR impact factor
3.871 (2009)
JCR rank
81/281 (2009)
JCR quartile
2 (2009)
ISSN
0022-2836
DOI
10.1016/j.jmb.2009.02.026
language
English
UGent publication?
yes
classification
A1
id
665101
handle
http://hdl.handle.net/1854/LU-665101
date created
2009-05-25 16:31:24
date last changed
2017-01-02 09:55:43
@article{665101,
  abstract     = {We showed earlier that human beta -thymosin 15 (Th15) is up-regulated in prostate cancer, confirming Studies from others that propagated Tb15 as a prostate cancer biomarker. In this first report on mouse Tb15, we show that, unlike in humans, four Tb15-like isoforms are present in Mouse. We used phylogenetic analysis of deuterostome beta-thymosins to show that these four new isoforms cluster within the vertebrate Tb15-clade. Intriguingly, one of these Mouse beta-thymosins, Th15r, consists of two beta-thymosin domains. The existence of such a repeat beta-thymosin is so far unique in vertebrates, though common in lower eukaryotes. Biochemical data indicate that Tb15r potently sequesters actin. In a cellular context, Tb15r behaves as a bona fide beta-thymosin, lowering central stress fibre content. We reveal that a complex genomic organization underlies Tb15r expression: Tb15r results from read-through transcription and alternative splicing of two tandem duplicated mouse Tb15 genes. Transcript profiling of all Mouse beta-thymosin isoform (Th15s, Tb4 and Tb10) reveals that two isoform switches occur between embryonic and adult tissues, and indicates Th15r as the major mouse Tb15 isoform in adult cells. Tb15r is present also in mouse prostate cancer cell lines. This insight into the mouse Tb15 family is fundamental for future studies on Tb15 in mouse (prostate) cancer models.},
  author       = {Dhaese, Stien and Vandepoele, Klaas and WATERSCHOOT, DAVY and Vanloo, Berlinda and Vandekerckhove, Jo{\"e}l and Ampe, Christophe and Van Troys, Marleen},
  issn         = {0022-2836},
  journal      = {JOURNAL OF MOLECULAR BIOLOGY},
  keyword      = {BINDING-SITE,MOLECULAR-CLONING,URINARY BIOMARKER,actin,thymosin,read-through transcript,phylogeny,qRT-PCR,KeyWords Plus: ACTIN NUCLEATION FACTOR,HUMAN PROSTATE-CANCER,CELL-LINES,RAT THYMOSIN-BETA-15,STRUCTURAL-CHARACTERIZATION,PROTEINS,BETA-15},
  language     = {eng},
  number       = {4},
  pages        = {809--825},
  publisher    = {ACADEMIC PRESS LTD ELSEVIER SCIENCE LTD},
  title        = {The Mouse Thymosin Beta15 Gene Family Displays Unique Complexity and Encodes A Functional Thymosin Repeat},
  url          = {http://dx.doi.org/10.1016/j.jmb.2009.02.026},
  volume       = {387},
  year         = {2009},
}

Chicago
Dhaese, Stien, Klaas Vandepoele, DAVY WATERSCHOOT, Berlinda Vanloo, Joël Vandekerckhove, Christophe Ampe, and Marleen Van Troys. 2009. “The Mouse Thymosin Beta15 Gene Family Displays Unique Complexity and Encodes A Functional Thymosin Repeat.” Journal of Molecular Biology 387 (4): 809–825.
APA
Dhaese, Stien, Vandepoele, K., WATERSCHOOT, D., Vanloo, B., Vandekerckhove, J., Ampe, C., & Van Troys, M. (2009). The Mouse Thymosin Beta15 Gene Family Displays Unique Complexity and Encodes A Functional Thymosin Repeat. JOURNAL OF MOLECULAR BIOLOGY, 387(4), 809–825.
Vancouver
1.
Dhaese S, Vandepoele K, WATERSCHOOT D, Vanloo B, Vandekerckhove J, Ampe C, et al. The Mouse Thymosin Beta15 Gene Family Displays Unique Complexity and Encodes A Functional Thymosin Repeat. JOURNAL OF MOLECULAR BIOLOGY. 24-28 OVAL RD, LONDON NW1 7DX, ENGLAND: ACADEMIC PRESS LTD ELSEVIER SCIENCE LTD; 2009;387(4):809–25.
MLA
Dhaese, Stien, Klaas Vandepoele, DAVY WATERSCHOOT, et al. “The Mouse Thymosin Beta15 Gene Family Displays Unique Complexity and Encodes A Functional Thymosin Repeat.” JOURNAL OF MOLECULAR BIOLOGY 387.4 (2009): 809–825. Print.