Miroslava Jankovic

Dr. Miroslava Jankovic


Research Focus & Metrics

Academic Career Length

37Years (1990-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

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1 March 1998 in Human Reproduction
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Journal Article
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LVL. Vicovac
L. Vicovac
MJMiroslava Jankovic
Miroslava Jankovic
MCM. Cuperlovic
M. Cuperlovic
The beta-galactoside-binding proteins galectin-1 and -3 are thought to modulate cell-extracellular matrix interactions in cell adhesion and migration. In this study, their occurrence in human trophoblast has been investigated. In the first trimester placenta galectin-1 is expressed in the cytotrophoblast of the mid and distal cell columns, but absent from the villous and proximal column cytotrophoblast. The villous syncytiotrophoblast was also positive. Galectin-3, on the other hand, was uniformly localized in the villous cytotrophoblast and mid and distal cell columns. Immunolocalization of these proteins in placental bed tissue has shown that galectin-1 and -3 are not present in cytokeratin-positive interstitially migrating cytotrophoblast. The co-localization of galectin-1 with extracellular laminin in cultures of cytotrophoblast, choriocarcinoma or decidual stromal cells is consistent with a role in the organization of extracellular matrix and the regulation of cell motility.

1 September 2014 in BioTechniques
Verified
Journal Article
Open access
MKMaja Kosanović
Maja Kosanović
MJMiroslava Jankovic
Miroslava Jankovic
Urine is a readily available source of relatively large quantities of extracellular vesicles (EVs). However, the isolation of urinary EVs (uEVs) is complicated by the presence of Tamm-Horsfall protein (THP), which polymerizes and...

18 February 2008 in Cancer Biomarkers
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Journal Article
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MJMiroslava Jankovic
Miroslava Jankovic
BMBojana S. Milutinovic
Bojana S. Milutinovic
CA125, a coelomic epithelium-related antigen, is expressed in both normal and pathological conditions. In this study, we compared the glycosylation of CA125 antigen from amniotic fluid and the ovarian carcinoma cell line OVCAR-3, in order to detect p


19 May 2005 in Human Reproduction
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Journal Article
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MJMiroslava Jankovic
Miroslava Jankovic
BTBojana S. Tapuskovic
Bojana S. Tapuskovic
BACKGROUND: The cancer antigen CA125 has a very complex molecular architecture in terms of both protein backbone and oligosaccharide chains. In this study, we examined the molecular forms and microheterogeneity of oligosaccharide chains of pregnancy-associated CA125, as a first step towards gaining an insight into its possible involvement as a ligand in carbohydrate-dependent interactions. The glycobiochemical properties of CA125 may be of diagnostic and biomedical importance as specific markers of physiological and pathological conditions of early pregnancy, as well as targets in different therapeutic procedures. METHODS: Pregnancy-associated CA125 was characterized by gel filtration and ion-exchange chromatography, followed by lectin-affinity chromatography with a panel of plant lectins as ligands. RESULTS: CA125 antigen isolated from first trimester placental extract was found to be heterogeneous in respect to molecular mass and the existence of different glyco-isoforms. Thus, elution profiles from the lectin-affinity columns demonstrated molecular subpopulations bound with low, intermediate and high affinity. Under the applied experimental conditions, CA125 bound most strongly to Triticum vulgaris agglutinin (WGA) and Ricinus communis agglutinin (RCA), but low affinity interactions occurred with the other lectins tested. CONCLUSIONS: The assessment of the carbohydrate composition of N- and O-glycans of pregnancy-associated CA125 was in general agreement with available data on CA125 of cancer origin. The main difference was observed in reactivity to Canavaliaensiformis agglutinin (ConA) and Phaseolusvulgaris erythroagglutinin (PHA-E) binding.

1 January 2008 in Disease Markers
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Journal Article
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MJMiroslava Jankovic
Miroslava Jankovic
MKMaja Kosanović
Maja Kosanović
Fibronectin (FN) is a multifunctional glycoprotein involved in cell‐matrix interactions. It exhibits a complex pattern of forms differing in respect to aminoacid and oligosaccharide composition. In this study we examined glycobiochemical and functional properties of the FN in benign prostatic hyperplasia (BPH) and prostatic cancer (PCa), attempting to resolve disease‐related differences. Two BPH sera pools and three PCa sera pools were used as the FN source. The affinity‐purified molecule was characterized by SDS‐PAGE, immuno‐ and lectin blot, lectin‐affinity chromatography and adhesion assay. BPH FN existed as intact molecule, giving the main immunoreactive band at 220 kDa. In contrast, PCa FN comprised three main immunoreactive fragments of 140, 110 and 90 kDa. As for glycosylation the ratio of altogether lectin‐reactive PCa FN was different from that of BPH FN manifested as a decrease of Con A‐ and an increase of LCA‐reactive moieties. Fibroblasts adhered to both FN preparations in a concentration dependent manner, but with a significantly lower efficiency to PCa FN. The results obtained showing distinct structural characteristics of PCa FN compared to BPH FN could be important for modulation of its ligand and recognition properties expressed as gain or loss of functions or as specific markers of its origin.