-
Something wrong with this record ?
Gamma-glutamyltransferase-associated glycoprotein patterns in human seminal plasma of normozoospermic men: a new aspect of biomarker heterogeneity
T. Jankovic, J. Danilovic Lukovic, S. Goc, N. Mitic, L. Hajdukovic, M. Jankovic
Language English Country Czech Republic
Document type Journal Article
NLK
Directory of Open Access Journals
from 2001
Free Medical Journals
from 1998
Medline Complete (EBSCOhost)
from 2007-06-01
ROAD: Directory of Open Access Scholarly Resources
from 2001
PubMed
37465893
DOI
10.5507/bp.2023.031
Knihovny.cz E-resources
- MeSH
- Biomarkers * metabolism MeSH
- Adult MeSH
- gamma-Glutamyltransferase * metabolism MeSH
- Glycoproteins * metabolism MeSH
- Humans MeSH
- Semen * metabolism chemistry MeSH
- Check Tag
- Adult MeSH
- Humans MeSH
- Male MeSH
- Publication type
- Journal Article MeSH
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.
References provided by Crossref.org
- 000
- 00000naa a2200000 a 4500
- 001
- bmc24022789
- 003
- CZ-PrNML
- 005
- 20250521143042.0
- 007
- ta
- 008
- 241205s2024 xr da f 000 0|eng||
- 009
- AR
- 024 7_
- $a 10.5507/bp.2023.031 $2 doi
- 035 __
- $a (PubMed)37465893
- 040 __
- $a ABA008 $b cze $d ABA008 $e AACR2
- 041 0_
- $a eng
- 044 __
- $a xr
- 100 1_
- $a Jankovic, Tamara $u Department for Immunochemistry and Glycobiology, Institute for the Application of Nuclear Energy, INEP, University of Belgrade, Belgrade, Serbia
- 245 10
- $a Gamma-glutamyltransferase-associated glycoprotein patterns in human seminal plasma of normozoospermic men: a new aspect of biomarker heterogeneity / $c T. Jankovic, J. Danilovic Lukovic, S. Goc, N. Mitic, L. Hajdukovic, M. Jankovic
- 520 9_
- $a 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.
- 650 _2
- $a lidé $7 D006801
- 650 _2
- $a mužské pohlaví $7 D008297
- 650 12
- $a gama-glutamyltransferasa $x metabolismus $7 D005723
- 650 12
- $a biologické markery $x metabolismus $7 D015415
- 650 12
- $a sperma $x metabolismus $x chemie $7 D012661
- 650 12
- $a glykoproteiny $x metabolismus $7 D006023
- 650 _2
- $a dospělí $7 D000328
- 655 _2
- $a časopisecké články $7 D016428
- 700 1_
- $a Danilovic Lukovic, Jelena $u Department for Immunochemistry and Glycobiology, Institute for the Application of Nuclear Energy, INEP, University of Belgrade, Belgrade, Serbia
- 700 1_
- $a Goc, Sanja $u Department for Immunochemistry and Glycobiology, Institute for the Application of Nuclear Energy, INEP, University of Belgrade, Belgrade, Serbia
- 700 1_
- $a Mitic, Ninoslav $u Department for Immunochemistry and Glycobiology, Institute for the Application of Nuclear Energy, INEP, University of Belgrade, Belgrade, Serbia
- 700 1_
- $a Hajdukovic, Ljiljana $u Department for Immunochemistry and Glycobiology, Institute for the Application of Nuclear Energy, INEP, University of Belgrade, Belgrade, Serbia
- 700 1_
- $a Jankovic, Miroslava $u Department for Immunochemistry and Glycobiology, Institute for the Application of Nuclear Energy, INEP, University of Belgrade, Belgrade, Serbia
- 773 0_
- $w MED00012606 $t Biomedical papers of the Medical Faculty of the University Palacky, Olomouc, Czechoslovakia $x 1804-7521 $g Roč. 168, č. 4 (2024), s. 319-325
- 856 41
- $u https://pubmed.ncbi.nlm.nih.gov/37465893 $y Pubmed
- 910 __
- $a ABA008 $b A 1502 $c 958 $y p $z 0
- 990 __
- $a 20241205 $b ABA008
- 991 __
- $a 20250521143040 $b ABA008
- 999 __
- $a ok $b bmc $g 2324814 $s 1234794
- BAS __
- $a 3
- BAS __
- $a PreBMC-MEDLINE
- BMC __
- $a 2024 $b 168 $c 4 $d 319-325 $e 20230717 $i 1804-7521 $m Biomedical papers of the Medical Faculty of the University Palacky, Olomouc, Czechoslovakia $n Biomed Pap Med Fac Univ Palacky Olomouc Czech Repub $x MED00012606
- LZP __
- $b NLK124 $a Pubmed-20241205