Bjelakovic L.,University of Sfax |
Kocic G.,Institute of Biochemistry |
Cvetkovic T.,Institute of Biochemistry |
Stojanovic D.,University of Sfax |
And 5 more authors.
Journal of Basic and Clinical Physiology and Pharmacology | Year: 2010
Arginase (L-arginine amidinohydrolase, EC 220.127.116.11) is the key enzyme in urea synthesis, hydrolyzing L-arginine into L-ornithine and urea. Arginase modulates levels of nitric oxide, creatine, and creatinine, likely by regulating intracellular L-arginine availability. The objective of the present study was to determine the arginase activity and concentration of urea and creatinine in colostrum and mature human milk obtained from nursing mothers. Our longitudinal biochemical analyses show that arginase activities and urea concentrations were the highest at the first day of lactation (colostrum). The decreasing enzyme activity and urea start at the second day, remaining at this level until the end of the first month of lactation (30th day). The concentration of creatinine in human colostrum and mature milk did not significantly change. The alteration of arginase activity between colostrum and mature milk may be a consequence of the transfer of arginase from the blood of the breast mother mammary glands into the colostrum and mature milk. The concentration of nutrients in colostrum and mature milk undergo alterations, probably to satisfy the requirements of the nursing infant for arginine, essential amino acids for human body growth, and normal physiology.
Jekic B.,Institute of Human Genetics |
Bunjevacki V.,Institute of Human Genetics |
Dobricic V.,Institute of Neurology |
Novakovic I.,Institute of Human Genetics |
And 6 more authors.
Archives of Biological Sciences | Year: 2011
Myelodysplastic syndromes (MDS) are rare in children and only a few studies have analyzed their molecular mechanisms. The NPM1 gene encodes for nucleophosmin (NPM) which regulates hematopoiesis. Mutations in exon 12 of the NPM1 cause the nucleophosmin cytoplasmic dislocation and disrupt its functions. We have analyzed mutations of the NPM1 gene in archival bone marrow samples from 17 children with MDS and detected, in one patient, transition C to T in codon 293. To the best of our knowledge, this is the first analysis of NPM1 mutations in childhood MDS and the very first missense mutation of the NPM1 gene reported so far.
Najdanovic J.G.,Institute of Biology and Human Genetics |
Cvetkovic V.J.,University of Nis |
Stojanovic S.,Institute of Biology and Human Genetics |
Vukelic-Nikolic M..,Institute of Biology and Human Genetics |
And 3 more authors.
Cellular and Molecular Bioengineering | Year: 2015
Established vascular network has a crucial importance in bone regeneration. Adipose-derived stem cells (ADSCs) can be differentiated in vitro towards endothelial cells (ECs) that give a possibility for their application in bone tissue engineering (BTE). The aim of our study was to examine the influence of ADSCs in vitro induced into ECs on vascularization and osteogenic process in subcutaneous implants. Induced ADSCs were implanted subcutaneously into BALB/c mice, in combination with the bone mineral matrix carrier (BC) and platelet-rich plasma (PRP), parallel with the implants without the cells. The combination of BC, PRP and ADSCs induced into ECs increased vascularization in subcutaneous implants that was shown through endothelial-related gene expression, high percentage of vascularization and VEGFR-2 immunoexpression. Osteocalcin immunoexpression, relative expression of osteopontin gene, and histological analysis showed that osteogenic process was more pronounced when the carrier was loaded with ADSCs induced into ECs which was associated with strong vascularization in cellularized implants. In implants without the cells vasculogenesis was initially stimulated, but vascular network was unsustainable at later observation points. Therefore, the approach that includes ADSCs in vitro induced into ECs combined with BC and PRP can be a good strategy for improving vascularization in bone regeneration and BTE. © 2015, Biomedical Engineering Society.