Metalloproteinases in disease: identification of biomarkers of tissue damage through proteomics

被引:16
作者
Herrera, Cristina [1 ]
Escalante, Teresa [2 ]
Rucavado, Alexandra [2 ]
Fox, Jay W. [3 ]
Maria Gutierrez, Jose [2 ]
机构
[1] Univ Costa Rica, Fac Farm, San Jose, Costa Rica
[2] Univ Costa Rica, Fac Microbiol, Inst Clodomiro Picado, San Jose, Costa Rica
[3] Univ Virginia, Sch Med, Charlottesville, VA 22959 USA
关键词
Metalloproteinases; mass spectrometry; proteomics; wound exudate; terminomics; matrix metalloproteinases (MMPs); ADAMs; ADAMTS; snake venom; proteolytic signature; SNAKE-VENOM METALLOPROTEINASES; CROTALUS-ATROX VENOM; MATRIX METALLOPROTEINASES; EXTRACELLULAR-MATRIX; SKELETAL-MUSCLE; BASEMENT-MEMBRANES; HEMORRHAGIC TOXINS; CELL-MIGRATION; IV COLLAGEN; PATHOLOGY;
D O I
10.1080/14789450.2018.1538800
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Introduction: Metalloproteinases play key roles in health and disease, by generating novel proteoforms with variable structure and function. Areas covered: This review focuses on the role of endogenous [a Disintegrin and Metalloproteinase (ADAMs), ADAMs with thrombospondin motifs (ADAMTS), and matrix metalloproteinases (MMPs)] and exogenous metalloproteinases in various disease conditions, and describes the application of mass spectrometry-based proteomics to detect qualitative and quantitative changes in protein profiles in tissues and body fluids in disease. Emphasis is placed on the proteomic analysis of exudates collected from affected tissues, including methods that enrich newly generated protein fragments derived from proteolysis in cells, stroma, or extracellular matrix. The use of proteomic analysis of exudates in the study of the local tissue damage induced by metalloproteinases derived from viperid snake venoms is discussed, particularly in relation to extracellular matrix degradation and to the overall pathology of these envenomings. Expert commentary: The information provided by these proteomics approaches is paving the way for the identification of biomarkers based on particular proteolytic signatures associated with different pathologies. Together with other methodological approaches, a comprehensive view of the mechanisms and dynamics of diseases can be achieved. Such basis of knowledge allows for the design of novel diagnostic and therapeutic approaches within the frame of 'precision' or 'personalized' medicine.
引用
收藏
页码:967 / 982
页数:16
相关论文
共 103 条
[91]   Interactions between extracellular matrix and growth factors in wound healing [J].
Schultz, Gregory S. ;
Wysocki, Annette .
WOUND REPAIR AND REGENERATION, 2009, 17 (02) :153-162
[92]   Function of the cysteine-rich domain of the haernorrhagic metalloproteinase atrolysin A: targeting adhesion proteins collagen I and von Willebrand factor [J].
Serrano, SMT ;
Jia, LG ;
Wang, DY ;
Shannon, JD ;
Fox, JW .
BIOCHEMICAL JOURNAL, 2005, 391 :69-76
[93]  
SHANNON JD, 1989, J BIOL CHEM, V264, P11575
[94]   Immunodepletion of high-abundant proteins from acute and chronic wound fluids to elucidate low-abundant regulators in wound healing [J].
Steinsträer L. ;
Jacobsen F. ;
Hirsch T. ;
Kesting M. ;
Chojnacki C. ;
Krisp C. ;
Wolters D. .
BMC Research Notes, 3 (1)
[95]   ADAM and ADAMTS Family Proteins and Snake Venom Metalloproteinases: A Structural Overview [J].
Takeda, Soichi .
TOXINS, 2016, 8 (05)
[96]  
Tian SY, 2014, INT J CLIN EXP PATHO, V7, P3752
[97]   BMP-1/tolloid-like proteinases synchronize matrix assembly with growth factor activation to promote rnorphogenesis and tissue remodeling [J].
Vadon-Le Goff, Sandrine ;
Hulmes, David J. S. ;
Moali, Catherine .
MATRIX BIOLOGY, 2015, 44-46 :14-23
[98]   Adamalysins in biology and disease [J].
van Goor, Harry ;
Melenhorst, Wynand B. W. H. ;
Turner, Anthony J. ;
Holgate, Stephen T. .
JOURNAL OF PATHOLOGY, 2009, 219 (03) :277-286
[99]   Extracellular regulation of VEGF: Isoforms, proteolysis, and vascular patterning [J].
Vempati, Prakash ;
Popel, Aleksander S. ;
Mac Gabhann, Feilim .
CYTOKINE & GROWTH FACTOR REVIEWS, 2014, 25 (01) :1-19
[100]   Catalytic Domain Architecture of Metzincin Metalloproteases [J].
Xavier Gomis-Rueth, F. .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2009, 284 (23) :15353-15357