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1.
Parkinsonism Relat Disord ; 11 Suppl 1: S25-9, 2005 Jun.
Article in English | MEDLINE | ID: mdl-15885624

ABSTRACT

Involuntary movements, or dyskinesia, represent a debilitating complication of levodopa therapy for Parkinson's disease. Taking advantage of a monkey brain bank constituted to study the pathophysiology of levodopa-induced dyskinesia, we here report the changes affecting D1, D2 and D3 dopamine receptors within the striatum of four experimental groups of non-human primates: normal, parkinsonian, parkinsonian treated with levodopa without or with dyskinesia. We also report the possible role of arrestin and G protein-coupled receptor kinases.


Subject(s)
Antiparkinson Agents/adverse effects , Dyskinesia, Drug-Induced/etiology , Levodopa/adverse effects , Parkinson Disease/drug therapy , Receptors, Dopamine D1/physiology , Receptors, Dopamine D2/physiology , Dyskinesia, Drug-Induced/physiopathology , Humans , Parkinson Disease/physiopathology , Receptors, Dopamine D3
2.
Biotechnol Appl Biochem ; 32(1): 41-51, 2000 08.
Article in English | MEDLINE | ID: mdl-10918037

ABSTRACT

A soluble form of L-selectin was recombinantly produced, which might be an effective therapeutic agent in inflammatory disorders, acting as an inhibitor for leucocyte endothelium adhesion. In the present study the oligosaccharide structures of soluble human L-selectin, recombinantly expressed in baby-hamster kidney cells, were determined. The N-linked glycans were enzymically released and fluorescently labelled with 2-aminobenzamide. Sialylation of the N-glycans was analysed by anion-exchange chromatography followed by rechromatography of the resulting fractions on amino-phase HPLC after release of the sialic acid residues. Desialylated oligosaccharides were separated using two-dimensional HPLC and characterized by digestion with exoglycosidases and MS. More than 30 oligosaccharide structures representing at least 95% of the overall glycosylation of this protein were determined. The results revealed that recombinant soluble human L-selectin carries bi-, tri- and tetra-antennary sugar chains, which are fucosylated on the innermost residue of N-acetylglucosamine. The number of sialic acid residues linked to these glycans ranges from 0 (neutral glycans) to 4 (tetrasialylated oligosaccharides). The sialic acid is found exclusively in the alpha 2-3 linkage to galactose. In addition to the main glycans, different minor structures containing terminal N-acetylgalactosamine, or the H (O) blood-group determinant were also identified. O-Glycosylation of mucin-type sugar chains was not detected in recombinant soluble human L-selectin.


Subject(s)
Carbohydrates/genetics , Kidney/cytology , L-Selectin/genetics , Oligosaccharides/analysis , Animals , Carbohydrate Conformation , Carbohydrate Sequence , Cell Line , Cricetinae , Humans , L-Selectin/chemistry , L-Selectin/metabolism , Oligosaccharides/chemistry , Polysaccharides/chemistry , Polysaccharides/isolation & purification , Recombinant Proteins/genetics , Recombinant Proteins/metabolism , Sequence Analysis , Solubility
3.
FEBS Lett ; 450(1-2): 111-6, 1999 Apr 30.
Article in English | MEDLINE | ID: mdl-10350067

ABSTRACT

In the present study we show that the H (0) blood group determinant Fuc alpha1-2Gal beta1-4GlcNAc beta1-R is present on N-linked glycans of soluble human L-selectin recombinantly expressed in baby hamster kidney (BHK) cells. The glycans were isolated using complementary HPLC techniques and characterized by a combination of exoglycosidase digestion and mass spectrometry. The linkage of the fucose residues was determined by incubation of the glycans with specific fucosidases. The H blood determinant Fuc alpha1-2Gal beta1-4GlcNAc beta1 was detected for bi-, 2,4 branched tri- and tetraantennary structures. To our knowledge, the proposed oligosaccharide structures represent a new glycosylation motif for recombinant glycoproteins expressed on BHK cells.


Subject(s)
ABO Blood-Group System/immunology , Epitopes/analysis , L-Selectin/chemistry , ABO Blood-Group System/chemistry , Animals , Carbohydrate Conformation , Carbohydrate Sequence , Cells, Cultured , Cricetinae , Glycoproteins/chemistry , Humans , Infant, Newborn , Kidney/metabolism , Molecular Sequence Data , Monosaccharides/analysis , Oligosaccharides/chemistry , Oligosaccharides/immunology , Sequence Analysis , Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
4.
Pediatr Pol ; 71(7): 595-8, 1996 Jul.
Article in Polish | MEDLINE | ID: mdl-8803462

ABSTRACT

CRP was measured in cord blood of 41 neonates born by healthy mothers and those with either risk of infection or its obvious clinical symptoms, and in sera of 122 newborn babies from infection risk group. Results excluded cord blood as a possible specimen for CRP estimation, because of very low values, at lower limit of sensitivity of the immunoturbidimetric method, and showed a correlation of serum CRP and clinical condition and its usefulness in monitoring of anti-bacterial therapy.


Subject(s)
C-Reactive Protein/analysis , Fetal Blood/chemistry , Infections/blood , Pregnancy Complications, Infectious/blood , Adult , Biomarkers/analysis , Female , Humans , Infant, Newborn , Infections/diagnosis , Pregnancy , Reference Values
6.
Acta Haematol Pol ; 22(1): 149-53, 1991.
Article in Polish | MEDLINE | ID: mdl-1823957

ABSTRACT

The management is described of 12 pregnant patients with idiopathic thrombocytopenia. In no case perinatal haemorrhage developed. All labor took place through the genital canal. No perinatal injuries were observed in the newborns.


Subject(s)
Labor, Obstetric/blood , Postpartum Hemorrhage/prevention & control , Pregnancy Complications, Hematologic/blood , Thrombocytopenia/blood , Adult , Female , Humans , Platelet Count , Pregnancy , Prenatal Care
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