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Protein extremes gain relevance in massive proteomic studies
Date:6/15/2010

ute of Biotechnology and Biomedicine and the Department of Biochemistry and Molecular Biology).

In other words, it is now possible to use massive proteomic methods to study maturing processes of proteins which often include breaks in their linear sequence both internally and at their N- and C-termini. Therefore, it will be possible to assess the specific role of these regions in the processes mentioned and in other related functions such as generation, activation and deactivation of hormones, growth factors, neuropeptides, enzymes, membrane receptors and many other proteins with important biological roles. The strategy developed can be carried out ex-vivo (in cell extracts) or in-vivo (by transfection and proteomic analysis). In addition, protein extremes are commonly involved in essential functions, such as locating and directing cells-tissues, triggering the start of three-dimensional folding, joining other biomolecules and macrostructures, post-generation chemical modifications of proteins, etc.

This publication completes previous studies (e.g. on N-terminal regions) carried out by the Flemish research group, leader in the field of general proteomics, as well as by researchers at Universitat Autnoma de Barcelona, leaders in the field of enzymes processing and maturing C-terminal proteins (carboxypeptidases), who recently published an article on the processing of C-terminal peptides in the Journal of Biological Chemistry, by S. Tanco, J. Lorenzo and F. X. Aviles, of UAB, and Ll. Fricker et. al. of Albert Einsten College of Medicine of New York.


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Contact: Maria Jesus Delgado
MariaJesus.Delgado@uab.cat
34-935-814-049
Universitat Autonoma de Barcelona
Source:Eurekalert  

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