Proteome of human T lymphocytes with treatment of cyclosporine and polysaccharopeptide: Analysis of significant proteins that manipulate T cells proliferation and immunosuppression
Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
Standard
Proteome of human T lymphocytes with treatment of cyclosporine and polysaccharopeptide : Analysis of significant proteins that manipulate T cells proliferation and immunosuppression. / Lee, Cheuk Lun; Jiang, Ping Ping; Sit, Wai Hung; Wan, Jennifer Man Fan.
I: International Immunopharmacology, Bind 7, Nr. 10, 10.2007, s. 1311-1324.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
Harvard
APA
Vancouver
Author
Bibtex
}
RIS
TY - JOUR
T1 - Proteome of human T lymphocytes with treatment of cyclosporine and polysaccharopeptide
T2 - Analysis of significant proteins that manipulate T cells proliferation and immunosuppression
AU - Lee, Cheuk Lun
AU - Jiang, Ping Ping
AU - Sit, Wai Hung
AU - Wan, Jennifer Man Fan
N1 - Funding Information: This work was supported in part by RGC Grants# HKU 7511/03M obtained from The University of Hong Kong and partially supported by the Hong Kong Association for Health Care, Hong Kong, SAR. P.R. China.
PY - 2007/10
Y1 - 2007/10
N2 - The aberrant activation of T lymphocyte proliferation is one of the key events in organ transplant recipients and autoimmune disorders. The present study adopted a gel-based proteomics approach to define the proteins representative of the T cell proliferation and to discover the molecules that play critical roles during the suppression of T cell proliferation. Human T lymphocytes were isolated from healthy donors and primed with phytohemagglutinin (PHA) to undergo proliferation. Two medical fungal products with specific T cell activation inhibitory properties, cyclosporine A (CsA) and polysaccharopeptide (PSP), were used to study the proteins that manipulate T cell proliferation. After demonstrating their similar effects on cell proliferation, cell survival and interleuklin-2 (IL-2) secretion, significant quantitative protein alterations were detected between the CsA- and PSP-treated T cell proteome. These altered proteins were identified by MALDI-TOF and classified into 3 categories: (i) proteins affected by both CsA and PSP, (ii) proteins affected by CsA alone, and (iii) proteins affected by PSP alone. Most of these altered proteins have functional significance in protein degradation, the antioxidant pathway, energy metabolism and immune cell regulation.
AB - The aberrant activation of T lymphocyte proliferation is one of the key events in organ transplant recipients and autoimmune disorders. The present study adopted a gel-based proteomics approach to define the proteins representative of the T cell proliferation and to discover the molecules that play critical roles during the suppression of T cell proliferation. Human T lymphocytes were isolated from healthy donors and primed with phytohemagglutinin (PHA) to undergo proliferation. Two medical fungal products with specific T cell activation inhibitory properties, cyclosporine A (CsA) and polysaccharopeptide (PSP), were used to study the proteins that manipulate T cell proliferation. After demonstrating their similar effects on cell proliferation, cell survival and interleuklin-2 (IL-2) secretion, significant quantitative protein alterations were detected between the CsA- and PSP-treated T cell proteome. These altered proteins were identified by MALDI-TOF and classified into 3 categories: (i) proteins affected by both CsA and PSP, (ii) proteins affected by CsA alone, and (iii) proteins affected by PSP alone. Most of these altered proteins have functional significance in protein degradation, the antioxidant pathway, energy metabolism and immune cell regulation.
KW - Coriolus versicolor
KW - Cyclosporine A
KW - Human T lymphocytes
KW - Polysaccharopeptide
KW - Proteomics
KW - Two dimensional gel electrophoresis
UR - http://www.scopus.com/inward/record.url?scp=34547153230&partnerID=8YFLogxK
U2 - 10.1016/j.intimp.2007.05.013
DO - 10.1016/j.intimp.2007.05.013
M3 - Journal article
C2 - 17673146
AN - SCOPUS:34547153230
VL - 7
SP - 1311
EP - 1324
JO - International Immunopharmacology
JF - International Immunopharmacology
SN - 1567-5769
IS - 10
ER -
ID: 299106662