Pore-forming bacterial toxins and antimicrobial peptides as modulators of ADAM function

被引:15
作者
Reiss, Karina [1 ]
Bhakdi, Sucharit [2 ]
机构
[1] Univ Kiel, Dept Dermatol, D-24098 Kiel, Germany
[2] Johannes Gutenberg Univ Mainz, Inst Med Microbiol & Hyg, D-55131 Mainz, Germany
关键词
Bacterial toxins; Antimicrobial peptides; Metalloproteinase; ADAMs; EGFR; ALPHA-CONVERTING-ENZYME; GROWTH-FACTOR-RECEPTOR; ESCHERICHIA-COLI HEMOLYSIN; ACTIVATED PROTEIN-KINASE; CELL-CELL ADHESION; P2X(7) RECEPTOR; L-SELECTIN; EGF RECEPTOR; TNF-ALPHA; MAMMALIAN-CELLS;
D O I
10.1007/s00430-012-0260-3
中图分类号
R392 [医学免疫学]; Q939.91 [免疫学];
学科分类号
100102 ;
摘要
Membrane-perturbating proteins and peptides are widespread agents in biology. Pore-forming bacterial toxins represent major virulence factors of pathogenic microorganisms. Membrane-damaging peptides constitute important antimicrobial effectors of innate immunity. Membrane perturbation can incur multiple responses in mammalian cells. The present discussion will focus on the interplay between membrane-damaging agents and the function of cell-bound metalloproteinases of the ADAM family. These transmembrane enzymes have emerged as the major proteinase family that mediate the proteolytic release of membrane-associated proteins, a process designated as "shedding". They liberate a large spectrum of functionally active molecules including inflammatory cytokines, growth factor receptors and cell adhesion molecules, thereby regulating such vital cellular functions as cell-cell adhesion, cell proliferation and cell migration. ADAM activation may constitute part of the cellular recovery machinery on the one hand, but likely also promotes inflammatory processes on the other. The mechanisms underlying ADAM activation and the functional consequences thereof are currently the subject of intensive research. Attention here is drawn to the possible involvement of purinergic receptors and ceramide generation in the context of ADAM activation following membrane perturbation by membrane-active agents.
引用
收藏
页码:419 / 426
页数:8
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