Implementation of a Protein Profiling Platform Developed as an Academic-Pharmaceutical Industry Collaborative Effort
(2008) In Electrophoresis 29(12). p.2696-2705- Abstract
- As much attention has devoted to the proteome research during the last years, biomarker discovery has become an increasingly hot area, potentially enabling the development of new assays for diagnosis and prognosis of severe diseases. This is the field of research interest where efforts originating from both academic and industrial groups should jointly work on solutions. In this paper we would like to demonstrate the fruitful combination of both research domains where the scientific crossroads sprout fresh ideas from the basic research domain and how these are refined and tethered to industrial standards.
We will present an approach that is based on novel microfluidic devices, utilizing their benefits in processing small-volume... (More) - As much attention has devoted to the proteome research during the last years, biomarker discovery has become an increasingly hot area, potentially enabling the development of new assays for diagnosis and prognosis of severe diseases. This is the field of research interest where efforts originating from both academic and industrial groups should jointly work on solutions. In this paper we would like to demonstrate the fruitful combination of both research domains where the scientific crossroads sprout fresh ideas from the basic research domain and how these are refined and tethered to industrial standards.
We will present an approach that is based on novel microfluidic devices, utilizing their benefits in processing small-volume samples. Our biomarker discovery strategy, built around this platform, involves optimized samples processing (based on solid-phase extraction and sample enrichment) and fast MALDI-MS read-out. The identification of novel biomarkers at low abundance level has been achieved by the utilization of a miniaturized sample handling platform, which offers clean up and enrichment of proteins in one step. Complete automation has been realized in the form of a unique robotic instrumentation that is able to extract and transfer 96 samples onto standard MALDI target plates with high throughput.
The developed platform was operated with a 60 sample turnaround per hour allowing sensitivities in femtomol regions of medium and low abundant target proteins from clinical studies on tissue samples of multiple sclerosis and gastroesophageal reflux disease. Several proteins have been identified as new biomarkers from cerebrospinal fluid and esophagus epithelial cells. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1038483
- author
- organization
- publishing date
- 2008
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- microfluidics, solid-phase extraction, multiple sclerosis, piezo-dispensing, gastroesophageal reflux disease, proteomics
- in
- Electrophoresis
- volume
- 29
- issue
- 12
- pages
- 2696 - 2705
- publisher
- John Wiley & Sons Inc.
- external identifiers
-
- wos:000257481300027
- scopus:46249112656
- ISSN
- 0173-0835
- DOI
- 10.1002/elps.200700816
- language
- English
- LU publication?
- yes
- additional info
- The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Analytical Chemistry (S/LTH) (011001004), Machine Design (011027000), Biomedical Engineering (011200011)
- id
- e8cac7df-f306-4233-8b59-45a24fc55875 (old id 1038483)
- date added to LUP
- 2016-04-01 12:35:32
- date last changed
- 2023-01-03 18:42:50
@article{e8cac7df-f306-4233-8b59-45a24fc55875,
abstract = {{As much attention has devoted to the proteome research during the last years, biomarker discovery has become an increasingly hot area, potentially enabling the development of new assays for diagnosis and prognosis of severe diseases. This is the field of research interest where efforts originating from both academic and industrial groups should jointly work on solutions. In this paper we would like to demonstrate the fruitful combination of both research domains where the scientific crossroads sprout fresh ideas from the basic research domain and how these are refined and tethered to industrial standards. <br/><br>
We will present an approach that is based on novel microfluidic devices, utilizing their benefits in processing small-volume samples. Our biomarker discovery strategy, built around this platform, involves optimized samples processing (based on solid-phase extraction and sample enrichment) and fast MALDI-MS read-out. The identification of novel biomarkers at low abundance level has been achieved by the utilization of a miniaturized sample handling platform, which offers clean up and enrichment of proteins in one step. Complete automation has been realized in the form of a unique robotic instrumentation that is able to extract and transfer 96 samples onto standard MALDI target plates with high throughput. <br/><br>
The developed platform was operated with a 60 sample turnaround per hour allowing sensitivities in femtomol regions of medium and low abundant target proteins from clinical studies on tissue samples of multiple sclerosis and gastroesophageal reflux disease. Several proteins have been identified as new biomarkers from cerebrospinal fluid and esophagus epithelial cells.}},
author = {{Végvári, Ákos and Magnusson, Mattias and Wallman, Lars and Ekström, Simon and Bolmsjö, Gunnar and Nilsson, Johan and Milliotis, Tasso and Östrling, Jörgen and Kjällström, Sven and Ottervald, Jan and Franzén, Bo and Hultberg, Hans and Marko-Varga, György and Laurell, Thomas}},
issn = {{0173-0835}},
keywords = {{microfluidics; solid-phase extraction; multiple sclerosis; piezo-dispensing; gastroesophageal reflux disease; proteomics}},
language = {{eng}},
number = {{12}},
pages = {{2696--2705}},
publisher = {{John Wiley & Sons Inc.}},
series = {{Electrophoresis}},
title = {{Implementation of a Protein Profiling Platform Developed as an Academic-Pharmaceutical Industry Collaborative Effort}},
url = {{https://lup.lub.lu.se/search/files/2986320/1173013.pdf}},
doi = {{10.1002/elps.200700816}},
volume = {{29}},
year = {{2008}},
}