Goč, Sanja

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  • Goč, Sanja (2)
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Author's Bibliography

Gamma-glutamyltransferase-associated glycoprotein patterns in human seminal plasma of normozoospermic men: a new aspect of biomarker heterogeneity

Janković, Tamara; Danilović Luković, Jelena; Goč, Sanja; Mitić, Ninoslav; Hajduković, Ljiljana; Janković, Miroslava

(Faculty of Medicine and Dentistry Palacký University Olomouc, Czech Republic, 2023)

TY  - JOUR
AU  - Janković, Tamara
AU  - Danilović Luković, Jelena
AU  - Goč, Sanja
AU  - Mitić, Ninoslav
AU  - Hajduković, Ljiljana
AU  - Janković, Miroslava
PY  - 2023
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/2497
AB  - Background. Gamma-glutamyltransferase (GGT) is a well-known laboratory biomarker. In spite of high concentration
and the possible biomedical importance of estimating GGT in human seminal plasma (hSP), it has not been widely
explored in reproductive physiology. This study aimed to complement existing data on its diversity, previously obtained
on seminal extracellular vesicles, by analyzing matched soluble fraction of hSP. The GGT-associated patterns of
selected glycoproteins were analyzed in order to establish an adjunct referent parameter for differentiation between
known high molecular mass forms of GGT. Getting insight into distinct GGT-associated glycoprotein patterns should
contribute to define them together as possible multimarkers.
Methods. GGT forms in soluble, membrane-free-fraction isolated form hSP of normozoospermic men were analyzed
using gel filtration and lectin blotting using WGA (wheat germ agglutinin) and Con A (concanavalin A).
Results. Widely distributed GGT (with two to three partially resolved peaks), which may correspond to high molecular
mass aggregates, were detected. GGT-associated patterns of selected glycoproteins (at position of big, medium, and
small-GGT) all comprised high molecular mass WGA-reactive smears, but differed in the presence of Con A-reactive
glycans, as well as mucin-associated antigens CA19-9 and CA125.
Conclusions. GGT contributes to several molecular patterns that differ between the soluble and extracellular vesicle
fractions of hSP. Their glycobiochemical heterogeneity is due to difference in the presence of distinct sialylated and mannosylated
glycans. Moreover, GGT-associated glycoprotein patterns differentiate between high molecular mass forms
of GGT in the soluble fraction of hSP. They hold promise as possible targets for increasing biomarker potential of GGT.
PB  - Faculty of Medicine and Dentistry Palacký University Olomouc, Czech Republic
T2  - Biomedical papers of the Medical Faculty of the University Palacky, Olomouc, Czechoslovakia
T1  - Gamma-glutamyltransferase-associated glycoprotein patterns in human seminal plasma of normozoospermic men: a new aspect of biomarker heterogeneity
DO  - 10.5507/bp.2023.031
ER  - 
@article{
author = "Janković, Tamara and Danilović Luković, Jelena and Goč, Sanja and Mitić, Ninoslav and Hajduković, Ljiljana and Janković, Miroslava",
year = "2023",
abstract = "Background. Gamma-glutamyltransferase (GGT) is a well-known laboratory biomarker. In spite of high concentration
and the possible biomedical importance of estimating GGT in human seminal plasma (hSP), it has not been widely
explored in reproductive physiology. This study aimed to complement existing data on its diversity, previously obtained
on seminal extracellular vesicles, by analyzing matched soluble fraction of hSP. The GGT-associated patterns of
selected glycoproteins were analyzed in order to establish an adjunct referent parameter for differentiation between
known high molecular mass forms of GGT. Getting insight into distinct GGT-associated glycoprotein patterns should
contribute to define them together as possible multimarkers.
Methods. GGT forms in soluble, membrane-free-fraction isolated form hSP of normozoospermic men were analyzed
using gel filtration and lectin blotting using WGA (wheat germ agglutinin) and Con A (concanavalin A).
Results. Widely distributed GGT (with two to three partially resolved peaks), which may correspond to high molecular
mass aggregates, were detected. GGT-associated patterns of selected glycoproteins (at position of big, medium, and
small-GGT) all comprised high molecular mass WGA-reactive smears, but differed in the presence of Con A-reactive
glycans, as well as mucin-associated antigens CA19-9 and CA125.
Conclusions. GGT contributes to several molecular patterns that differ between the soluble and extracellular vesicle
fractions of hSP. Their glycobiochemical heterogeneity is due to difference in the presence of distinct sialylated and mannosylated
glycans. Moreover, GGT-associated glycoprotein patterns differentiate between high molecular mass forms
of GGT in the soluble fraction of hSP. They hold promise as possible targets for increasing biomarker potential of GGT.",
publisher = "Faculty of Medicine and Dentistry Palacký University Olomouc, Czech Republic",
journal = "Biomedical papers of the Medical Faculty of the University Palacky, Olomouc, Czechoslovakia",
title = "Gamma-glutamyltransferase-associated glycoprotein patterns in human seminal plasma of normozoospermic men: a new aspect of biomarker heterogeneity",
doi = "10.5507/bp.2023.031"
}
Janković, T., Danilović Luković, J., Goč, S., Mitić, N., Hajduković, L.,& Janković, M.. (2023). Gamma-glutamyltransferase-associated glycoprotein patterns in human seminal plasma of normozoospermic men: a new aspect of biomarker heterogeneity. in Biomedical papers of the Medical Faculty of the University Palacky, Olomouc, Czechoslovakia
Faculty of Medicine and Dentistry Palacký University Olomouc, Czech Republic..
https://doi.org/10.5507/bp.2023.031
Janković T, Danilović Luković J, Goč S, Mitić N, Hajduković L, Janković M. Gamma-glutamyltransferase-associated glycoprotein patterns in human seminal plasma of normozoospermic men: a new aspect of biomarker heterogeneity. in Biomedical papers of the Medical Faculty of the University Palacky, Olomouc, Czechoslovakia. 2023;.
doi:10.5507/bp.2023.031 .
Janković, Tamara, Danilović Luković, Jelena, Goč, Sanja, Mitić, Ninoslav, Hajduković, Ljiljana, Janković, Miroslava, "Gamma-glutamyltransferase-associated glycoprotein patterns in human seminal plasma of normozoospermic men: a new aspect of biomarker heterogeneity" in Biomedical papers of the Medical Faculty of the University Palacky, Olomouc, Czechoslovakia (2023),
https://doi.org/10.5507/bp.2023.031 . .

Extracellular vesicles in a maze of glycomic complexity

Danilović Luković, Jelena; Goč, Sanja; Mitic, Ninoslav; Janković, Tamara

(Faculty of Sciences, Department of Biology, University of Novi Sad, Serbia, 2022)

TY  - JOUR
AU  - Danilović Luković, Jelena
AU  - Goč, Sanja
AU  - Mitic, Ninoslav
AU  - Janković, Tamara
PY  - 2022
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/2476
AB  - The carbohydrate portion of proteins and lipids mediates a variety of biological processes. Revealing their
underlying principles is a challenging task that could contribute to a better understanding of many patho/physiological
conditions. On the other hand, the interest in extracellular vesicles (EVs) has increased in recent years due to their
involvement in intercellular communication leading to an array of functional and structural changes in recipient cells.
Their characterization uncovered an exceptional diversity in size, morphology, as well as in membrane and cargo content.
Monitoring/analysis of surface glycosylation of EVs originating from the prostate, termed prostasomes, revealed
their substantial contribution to the complexity of seminal plasma (SP) glycome. Heterogeneity of surface glycans confirm
the existence of several prostasome subpopulations. Presentation of surface glycans on prostasomal membrane is
strongly affected by co-localized membrane-associated glycoproteins and tetraspanins. They appear to be organized in
established/regular distribution patterns on membrane domains. Surface glycans are a component of EVs membrane
that affects its functionality and potentially a distinction marker of prostasome subpopulations. Further understanding
of the complex composition of glycans on EVs might explain the relation of their structure with functional alterations
in distinct patho/physiological conditions.
PB  - Faculty of Sciences, Department of Biology, University of Novi Sad, Serbia
T2  - Biologia Serbica
T1  - Extracellular vesicles in a maze of glycomic complexity
EP  - 32
IS  - 1
SP  - 25
VL  - 44
DO  - 10.5281/zenodo.7075050
ER  - 
@article{
author = "Danilović Luković, Jelena and Goč, Sanja and Mitic, Ninoslav and Janković, Tamara",
year = "2022",
abstract = "The carbohydrate portion of proteins and lipids mediates a variety of biological processes. Revealing their
underlying principles is a challenging task that could contribute to a better understanding of many patho/physiological
conditions. On the other hand, the interest in extracellular vesicles (EVs) has increased in recent years due to their
involvement in intercellular communication leading to an array of functional and structural changes in recipient cells.
Their characterization uncovered an exceptional diversity in size, morphology, as well as in membrane and cargo content.
Monitoring/analysis of surface glycosylation of EVs originating from the prostate, termed prostasomes, revealed
their substantial contribution to the complexity of seminal plasma (SP) glycome. Heterogeneity of surface glycans confirm
the existence of several prostasome subpopulations. Presentation of surface glycans on prostasomal membrane is
strongly affected by co-localized membrane-associated glycoproteins and tetraspanins. They appear to be organized in
established/regular distribution patterns on membrane domains. Surface glycans are a component of EVs membrane
that affects its functionality and potentially a distinction marker of prostasome subpopulations. Further understanding
of the complex composition of glycans on EVs might explain the relation of their structure with functional alterations
in distinct patho/physiological conditions.",
publisher = "Faculty of Sciences, Department of Biology, University of Novi Sad, Serbia",
journal = "Biologia Serbica",
title = "Extracellular vesicles in a maze of glycomic complexity",
pages = "32-25",
number = "1",
volume = "44",
doi = "10.5281/zenodo.7075050"
}
Danilović Luković, J., Goč, S., Mitic, N.,& Janković, T.. (2022). Extracellular vesicles in a maze of glycomic complexity. in Biologia Serbica
Faculty of Sciences, Department of Biology, University of Novi Sad, Serbia., 44(1), 25-32.
https://doi.org/10.5281/zenodo.7075050
Danilović Luković J, Goč S, Mitic N, Janković T. Extracellular vesicles in a maze of glycomic complexity. in Biologia Serbica. 2022;44(1):25-32.
doi:10.5281/zenodo.7075050 .
Danilović Luković, Jelena, Goč, Sanja, Mitic, Ninoslav, Janković, Tamara, "Extracellular vesicles in a maze of glycomic complexity" in Biologia Serbica, 44, no. 1 (2022):25-32,
https://doi.org/10.5281/zenodo.7075050 . .