Publication:

Proteomic database mining opens up avenues utilizing extracellular protein phosphorylation for novel therapeutic applications

Loading...
Thumbnail Image

Open/View Files

Date

2015

Journal Title

Journal ISSN

Volume Title

Publisher

BioMed Central
The Harvard community has made this article openly available. Please share how this access benefits you.

Research Projects

Organizational Units

Journal Issue

Citation

Yalak, Garif, and Bjorn R Olsen. 2015. “Proteomic database mining opens up avenues utilizing extracellular protein phosphorylation for novel therapeutic applications.” Journal of Translational Medicine 13 (1): 125. doi:10.1186/s12967-015-0482-4. http://dx.doi.org/10.1186/s12967-015-0482-4.

Abstract

Summary Recent advances in extracellular signaling suggest that extracellular protein phosphorylation is a regulatory mechanism outside the cell. The list of reported active extracellular protein kinases and phosphatases is growing, and phosphorylation of an increasing number of extracellular matrix molecules and extracellular domains of trans-membrane proteins is being documented. Here, we use public proteomic databases, collagens – the major components of the extracellular matrix, extracellular signaling molecules and proteolytic enzymes as examples to assess what the roles of extracellular protein phosphorylation may be in health and disease. We propose that novel tools be developed to help assess the role of extracellular protein phosphorylation and translate the findings for biomedical applications. Furthermore, we suggest that the phosphorylation state of extracellular matrix components as well as the presence of extracellular kinases be taken into account when designing translational medical applications. Electronic supplementary material The online version of this article (doi:10.1186/s12967-015-0482-4) contains supplementary material, which is available to authorized users.

Description

Research Data

Keywords

Extracellular matrix, Extracellular protein phosphorylation, Secreted kinases, Ectokinase, Exokinase, Collagens, BMPs, MMPs

Terms of Use

This article is made available under the terms and conditions applicable to Other Posted Material (LAA), as set forth at Terms of Service

Endorsement

Review

Supplemented By

Related Stories