TY  - JOUR
AU  - Nyitrayné Pap, Erna
AU  - Pállinger, Éva
AU  - Falus, András
AU  - Kiss, AA
AU  - Kittel, Ágnes
AU  - Kovacs, P
AU  - Buzás, Edit Irén
TI  - T Lymphocytes are Targets for Platelet- and Trophoblast-Derived Microvesicles During Pregnancy
JF  - PLACENTA
J2  - PLACENTA
VL  - 29
PY  - 2008
IS  - 9
SP  - 826
EP  - 832
PG  - 7
SN  - 0143-4004
DO  - 10.1016/j.placenta.2008.06.006
UR  - https://m2.mtmt.hu/api/publication/109957
ID  - 109957
N1  - Megjegyzés-21253630
PubMed ID: 18684502
Chemicals/CAS: P-Selectin; Platelet Glycoprotein GPIb-IX Complex
AB  - Microvesicles (MVs) can derive from several cell types and their membranes contain cell surface elements. Their role is increasingly recognized in cell-to-cell communication, as they act as both paracrine and remote messengers, occurring in circulating form as well as in plasma. Successful pregnancy requires a series of interactions between the maternal immune system and the implanted fetus, such that the semi-allograft will not be rejected. These interactions occur at the materno-placental interface and/or at a systemic level. In the present study we identified for the first time the in vivo plasma pattern of the MVs of third-trimester, healthy pregnant women, their cellular origin, and their target cells using flow cytometry and confocal laser microscopy. We searched for the cellular target molecules of thrombocyte-derived MVs with the help of neutralizing antibodies. We examined the in vitro effects of MVs on STAT3 phosphorylation of primary lymphocytes and Jurkat cells. We found that both placental trophoblast-derived and maternal thrombocyte-derived MVs bind to circulating peripheral T lymphocytes, but not to B lymphocytes or NK cells. We were able to show that the P-selectin (CD62P)-PSGL-1 (CD162) interaction is one mechanism binding platelet-derived MVs to T cells. We were also able to demonstrate that MV-lymphocyte interactions induce STAT3 phosphorylation in T cells. Our findings indicate that both thrombocyte- and trophoblast-derived MVs may play an important role in the immunomodulation of pregnancy. We suggest that the transfer of different signals via MVs represents a novel form of communication between the placenta and the maternal immune system, and that MVs contribute to the establishment of stable immune tolerance to the semi-allograft fetus.
LA  - English
DB  - MTMT
ER  - 

TY  - JOUR
AU  - Glant, TT
AU  - Mikecz, K
AU  - Roughley, PJ
AU  - Buzás, Edit Irén
AU  - Poole, AR
TI  - Age-related changes in protein-related epitopes of human articular-cartilage proteoglycans.
JF  - BIOCHEMICAL JOURNAL
J2  - BIOCHEM J
VL  - 236
PY  - 1986
IS  - 1
SP  - 71
EP  - 75
PG  - 5
SN  - 0264-6021
DO  - 10.1042/bj2360071
UR  - https://m2.mtmt.hu/api/publication/1392708
ID  - 1392708
AB  - Monoclonal antibodies were prepared that recognize different age-related epitopes on proteoglycan subunits of high buoyant density isolated from human epiphysial and articular cartilages. Antibody EFG-4 (IgG1) recognizes a proteinase-sensitive segment associated with the core protein. Antibody BCD-4 (IgG1) reacts with keratan sulphate bound to core protein. Both epitopes are minimally expressed in foetal cartilage and increase with age after birth to become maximally expressed in adult cartilage by about 30 years of age. In contrast, monoclonal antibody alpha HFPG-846 (IgM) recognizes a core-protein-related epitope that is maximally expressed in young foetal cartilage, declines up to birth and thereafter and is almost absent after about 30 years of age. Antibody alpha HFPG-846 was used to isolate by immuno-affinity chromatography two subpopulations of proteoglycan subunits from a 16-year-old-human cartilage proteoglycan subunit preparation. Only the antibody-unbound population showed a significant reaction with antibodies EGF-4 and BCD-4. The amino acid and carbohydrate compositions of these proteoglycan fractions were different, and one (antibody-bound) resembled those of foetal and the other (antibody-unbound) resembled those of adult proteoglycans isolated from 24-27-week-old-foetal and 52-56-year-old-adult cartilage respectively. These observations demonstrate that human cartilages contain at least two chemically and immunochemically distinct populations of proteoglycans, the proportions and content of which are age-dependent. It is likely that these populations represent the products of different genes, though their heterogeneity may be compounded by the result of different post-translation modifications.
LA  - English
DB  - MTMT
ER  -