Redox-linked signal transduction pathways for protein tyrosine kinase activation

被引:108
作者
Nakashima, I [1 ]
Kato, M [1 ]
Akhand, AA [1 ]
Suzuki, H [1 ]
Takeda, K [1 ]
Hossain, K [1 ]
Kawamoto, Y [1 ]
机构
[1] Nagoya Univ, Grad Sch Sci, Dept Immunol, Showa Ku, Nagoya, Aichi 4668550, Japan
关键词
D O I
10.1089/15230860260196326
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The signaling for activation of protein tyrosine kinases (PTKs) is usually started by binding of ligands to cell-surface receptors. However, recent evidence suggests the presence of ligand binding-independent signaling pathways that are mediated by oxidative stress. Oxidation and reduction of protein cysteine sulfhydryl (SH) groups may work as a molecular switch to start or to stop the signaling. It is known that oxidation of cysteine SH groups on protein tyrosine phosphatases switches off the action of protein tyrosine phosphatases. This event may not, however, signal for initial autophosphorylation of previously unphosphorylated PTKs, whereas it certainly prevents dephosphorylation of once-phosphorylated PTKs. We have suggested new mechanisms for oxidative stress-mediated PTK activation. First, cell-surface glycosylphosphatidylinositol-anchoring proteins and a phosphoglycolipid/cholesterol-enriched membrane microdomain termed a "raft" can be the direct targets of oxidative stress for inducing their clustering through an S-S-bonded or S-X-S-bonded crosslinking of cell-surface proteins and subsequent activation of raft-associating Src family PTKs. Second, intracellular specific cysteine SH groups on PTK proteins can be another target of oxidative stress for inducing a conformational change necessary for initial activation of PTKs. A possible relationship between cell-surface and intracellular events is that the former frequently induces superoxide production as the second messenger for the latter.
引用
收藏
页码:517 / 531
页数:15
相关论文
共 110 条
[71]   DIRECT EVIDENCE OF INVOLVEMENT OF GLYCOSYLPHOSPHATIDYLINOSITOL-ANCHORED PROTEINS IN THE HEAVY METAL-MEDIATED SIGNAL DELIVERY INTO T-LYMPHOCYTES [J].
PU, MY ;
MA, L ;
OHKUSU, K ;
ISOBE, KI ;
TAGUCHI, R ;
IKEZAWA, H ;
HAMAGUCHI, M ;
NAKASHIMA, I .
FEBS LETTERS, 1995, 361 (2-3) :295-298
[72]  
Pu MY, 1996, ONCOGENE, V13, P2615
[73]   Involvement of receptor aggregation and reactive oxygen species in osmotic stress-induced Syk activation in B cells [J].
Qin, SF ;
Ding, JY ;
Takano, T ;
Yamamura, H .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1999, 262 (01) :231-236
[74]   REDOX-LINKED LIGAND-INDEPENDENT CELL-SURFACE TRIGGERING FOR EXTENSIVE PROTEIN TYROSINE PHOSPHORYLATION [J].
RAHMAN, SMJ ;
PU, MY ;
HAMAGUCHI, M ;
IWAMOTO, T ;
ISOBE, K ;
NAKASHIMA, I .
FEBS LETTERS, 1993, 317 (1-2) :35-38
[75]   Exclusion of CD45 inhibits activity of p56(lck) associated with glycolipid-enriched membrane domains [J].
Rodgers, W ;
Rose, JK .
JOURNAL OF CELL BIOLOGY, 1996, 135 (06) :1515-1523
[76]   Low levels of ionic mercury modulate protein tyrosine phosphorylation in lymphocytes [J].
Rosenspire, AJ ;
Bodepudi, S ;
Mathews, M ;
McCabe, MJ .
INTERNATIONAL JOURNAL OF IMMUNOPHARMACOLOGY, 1998, 20 (12) :697-707
[77]   Ultraviolet light and osmotic stress: Activation of the JNK cascade through multiple growth factor and cytokine receptors [J].
Rosette, C ;
Karin, M .
SCIENCE, 1996, 274 (5290) :1194-1197
[78]   INVOLVEMENT OF GROWTH-FACTOR RECEPTORS IN THE MAMMALIAN UVC RESPONSE [J].
SACHSENMAIER, C ;
RADLERPOHL, A ;
ZINCK, R ;
NORDHEIM, A ;
HERRLICH, P ;
RAHMSDORF, HJ .
CELL, 1994, 78 (06) :963-972
[79]   ACTIVATION OF RET AS A DOMINANT TRANSFORMING GENE BY GERMLINE MUTATIONS OF MEN2A AND MEN2B [J].
SANTORO, M ;
CARLOMAGNO, F ;
ROMANO, A ;
BOTTARO, DP ;
DATHAN, NA ;
GRIECO, M ;
FUSCO, A ;
VECCHIO, G ;
MATOSKOVA, B ;
KRAUS, MH ;
DIFIORE, PP .
SCIENCE, 1995, 267 (5196) :381-383
[80]  
SCHIEVEN GL, 1994, J BIOL CHEM, V269, P20718