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Function of Prothymosin α in Chromatin Decondensation and Expression of Thymosin β‐4 Linked to Angiogenesis and Synaptic Plasticity
Author(s) -
GÓMEZMÁRQUEZ JAIME
Publication year - 2007
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1196/annals.1415.020
Subject(s) - chromatin , microbiology and biotechnology , thymosin , histone , biology , function (biology) , synaptic plasticity , angiogenesis , histone h1 , chromatin remodeling , neuroscience , chemistry , genetics , biochemistry , receptor , dna
:  Prothymosin α (ProTα) is an abundant highly acidic protein found in the nuclei of virtually all mammalian cells. The expression of this protein is increased in proliferating mammalian cells. However, the function of this molecule is still controversial. Here I present a model explaining the role of this protein in chromatin decondensation through its interaction with histone H1. β‐thymosins are a family of small actin‐binding peptides widely distributed in eukaryotic cells. Here I will focus on thymosin β‐4, the most abundant member of this family. In particular, I will discuss its expression in the mammalian development of cardiovascular and nervous systems as well as its implications in neuronal plasticity.

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