Nitrite oxidation and tyrosine nitration by human myeloperoxidase
Yükleniyor...
Tarih
2016
Yazarlar
Dergi Başlığı
Dergi ISSN
Cilt Başlığı
Yayıncı
Wiley-Blackwell
Erişim Hakkı
info:eu-repo/semantics/closedAccess
Özet
Biomineralization is deposition of hydroxyapatite, the crystallized mineral form of calcium and phosphate, by cells to their extracellular matrix (ECM), and it is an essential mechanism of bone and teeth formation in humans. Biomineralization is especially important in adults for tissue regeneration in bone defects. ECM
molecules regulate mineral formation and provide crystal growth and nucleation. One of the most important ECM molecules, Alkaline Phosphatase (ALP), is the key enzyme in biomineralization process by the activity of converting organophosphate into
inorganic phosphate. Moreover, osteocalcin and osteopontin are small soluble noncollagenous proteins of ECM and they regulate biomineralization by binding to calcium atoms available at crystal surfaces due to their highly negative charged amino acid residues. In this study, ALP, osteocalcin and osteopontin are expressed in bacterial systems and purified to assess in vitro biomineralization. Optimization of in vitro biomineralization activities with osteocalcin and osteopontin proteins provided the
understanding of the effect of protein concentrations in crystal structure of calcium crystals. Understanding of the effect of protein concentrations will provide control over biomineralization in different cell types by designing synthetic genetic circuits. Programming non-biomineral formation cells for biomineral formation will enable differentiation free bone mineral formation. Reprogramming of non-biomineral formation cells will help to treat bone defects and bone-impairing diseases, such as osteoporosis. Consequently, it is an outstanding approach to understand the activity of bone ECM proteins and construct synthetic genetic systems that can reprogram non-mineral formation cells for biomineralization within the scope of bone tissue engineering.
Açıklama
41st FEBS Congress on Molecular and Systems Biology for a Better Life -- SEP 03-08, 2016 -- Kusadasi, TURKEY
Anahtar Kelimeler
Nitrite Oxidation, Tyrosine Nitration, Myeloperoxidase, NO2-, NO2
Kaynak
Febs Journal
WoS Q Değeri
Q2
Scopus Q Değeri
Cilt
283
