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J Parkkinen

Publications and source records attributed to J Parkkinen.

17 recordsLinked to original sources
PubMed1992

Image processing for the study of brain structure and function: problems and programs.

Fundamental problems in the analysis of functional and structural imaging data include data transport, boundary identification (including manual tracing, edge detection, and tissue segmentation), volume estimation, three-dimensional reconstruction and display, surface and volume rendering, shape analysis, and image overlay. These problems require that research investigators have access to suitable methods of image analysis, implemented on a set of software programs, in order to conduct neuroimaging research. The authors describe a group of software programs designed to provide a comprehensive solution for these problems.

Brain↗
PubMed1991

Interactions of plasminogen and tissue plasminogen activator (t-PA) with amphoterin. Enhancement of t-PA-catalyzed plasminogen activation by amphoterin.

The heparin-binding p30 protein amphoterin is proposed to mediate adhesive interactions of the advancing plasma membrane in migrating and differentiating cells. Since the NH2-terminal part of amphoterin is exceptionally rich in lysine residues, we have studied its interactions with plasminogen and tissue plasminogen activator (t-PA). On immunostaining of N18 neuroblastoma cells, amphoterin and t-PA showed a close co-localization in the filopodia of the leading membrane and in the substrate-attached material. In purified systems, both t-PA and plasminogen bound to immobilized amphoterin, and their binding was inhibited by the lysine analogue epsilon-aminocaproic acid. Plasminogen bound to immobilized amphoterin was activated by t-PA, and this resulted in effective degradation of the immobilized amphoterin. Correspondingly, amphoterin-bound t-PA activated plasminogen. In solution amphoterin accelerated t-PA-catalyzed plasminogen activation maximally 46-fold. The results indicate that t-PA and plasminogen form through their lysine-binding sites a complex with amphoterin, which results in acceleration of plasminogen activation and effective degradation of amphoterin. We suggest that local acceleration of t-PA-catalyzed plasminogen activation by amphoterin at the leading membrane enhances the penetration of growing cytoplasmic processes through extracellular materials during cell migration, differentiation and regeneration. The amphoterin-mediated adhesion at the leading membrane may be transient in nature, because the protein also enhances its own breakdown by accelerating t-PA-catalyzed plasminogen activation.

Binding Sites↗
PubMed1991

Enhancement of tissue plasminogen activator-catalyzed plasminogen activation by Escherichia coli S fimbriae associated with neonatal septicaemia and meningitis.

The effect of Escherichia coli strains isolated from blood and cerebrospinal fluid of septic infants on plasminogen activation was studied. These strains typically carry a filamentous surface protein, S fimbria, that has formerly been shown to bind to endothelial cells and interact with plasminogen. The bacteria effectively promoted plasminogen activation by tissue plasminogen activator (t-PA) which was inhibited by epsilon-aminocaproic acid. A recombinant strain expressing S fimbriae accelerated t-PA-catalyzed plasminogen activation to a similar extent as did the wild-type strains whereas the nonfimbriate recipient strain had no effect. After incubation with t-PA and plasminogen, the S-fimbriate strain displayed bacterium-bound plasmin activity whereas the nonfimbriate strain did not. Bacterium-associated plasmin generation was also observed with a strain expressing mutagenized S fimbriae that lack the cell-binding subunit SfaS but not with a strain lacking the major subunit SfaA. Both t-PA and plasminogen bound to purified S fimbriae in a lysine-dependent manner and purified S fimbriae accelerated t-PA-catalyzed plasminogen activation. The results indicate that E. coli S fimbriae form a complex with t-PA and plasminogen which enhances the rate of plasminogen activation and generates bacterium-bound plasmin. This may promote bacterial invasion and persistence in tissues and contribute to the systemic activation of fibrinolysis in septicaemia.

Amino Acid Sequence↗
PubMed1989

Binding of plasminogen to Escherichia coli adhesion proteins.

Immobilization of plasminogen via its lysine-binding sites is regarded as a prerequisite for its activation and function in fibrinolysis and pericellular proteolysis. In the present study, the interaction of plasminogen with fimbriae found on Escherichia coli strains causing invasive human infections was studied. Plasminogen displayed concentration-dependent and saturable binding to immobilized type 1 fimbriae and, several fold lower binding to P and S fimbriae. The binding to fimbriae was effectively inhibited by epsilon-aminocaproic acid indicating that it was mediated by the lysine-binding sites of plasminogen. Binding studies with mutated fimbriae and inhibition tests indicated that the interaction was not dependent on the lectin subunit of the fimbriae. These results indicate the existence of a novel type of host-microbe interaction which may be important in the invasion by bacteria of host tissues.

Adhesins, Escherichia coli↗
PubMed1989

A lectin-immunofluorometric assay using an immobilized Bandeiraea simplicifolia II lectin for the determination of galactosylation variants of glycoproteins.

The sandwich-type immunometric assay was modified by replacing the solid phase-bound antibody with a lectin for the determination of glycoproteins carrying terminal N-acetylglucosamine residues. Microwells were coated with Bandeiraea simplicifolia II lectin and incubated with glycosylation variants of human serum glycoproteins. The bound glycoproteins were detected by time-resolved fluorometry using europium-labeled antibodies. Agalacto-derivatives of alpha 1-acid glycoprotein and transferrin obtained by neuraminidase and beta-galactosidase treatment bound to the immobilized lectin, whereas the native or desialylated glycoproteins showed no binding. The measuring range of the method for agalacto-alpha 1-acid glycoprotein was 0.01 to 10 micrograms/ml and for agalacto-transferrin 1 to 300 micrograms/ml. The binding of the agalacto-glycoproteins was totally inhibited with 1 to 10 mM N-acetylglucosamine which confirmed the specificity of the method for glycoproteins containing terminal N-acetylglucosamine residues. The results indicate that the novel lectin-immunofluorometric method is sensitive and has a wide measuring range for the determination of glycosylation variants of glycoproteins.

Acetylglucosamine↗
PubMed1989

Binding of Escherichia coli S fimbriae to cultured human endothelial cells.

The binding of Escherichia coli adhesins to human umbilical vein endothelial cells was studied by a cell monolayer enzyme-linked immunosorbent assay. S fimbriae displayed a concentration-dependent and saturable binding to the endothelial cells which was mediated by their sialylgalactoside-specific lectin activity. P fimbriae exhibited only low binding, and type 1 fimbriae exhibited no binding to these cells.

Adhesins, Escherichia coli↗
PubMed1989

Aberrant lectin-binding activity of immunoglobulin G in serum from rheumatoid arthritis patients.

Structural studies of oligosaccharide chains of immunoglobulin G (IgG) in serum have revealed a specific galactosylation deficiency associated with rheumatoid arthritis (RA). Using a two-site lectin-immunofluorometric assay, I studied the interaction of IgG with immobilized lectins. Compared with control IgG, IgG purified from RA patients' sera bound up to 40-fold more strongly to immobilized Bandeiraea simplicifolia agglutinin II, a lectin that specifically binds agalacto forms of other glycoproteins. However, inhibition studies and treatment of IgG with glycosidase suggested that only a minor part of this binding was mediated by agalacto oligosaccharides of IgG. Furthermore, these IgG samples bound even more intensively to some other immobilized lectins, including Ricinus communis agglutinin (RCA). The binding to RCA was not inhibited by lactose, a hapten sugar of RCA, whereas other lectin species in solution effectively inhibited it. Compared with intact RA IgG, isolated F(ab')2 fragments displayed only low RCA-binding activity. These results indicate the existence of a carbohydrate-nondependent interaction between RA IgG and different plant lectins. With use of immobilized RCA, the lectin-immunofluorometric assay was rapid and reproducible for measuring the aberrant lectin-binding activity of IgG directly in diluted serum samples.

Arthritis, Rheumatoid↗
PubMed1988

A N-acetyllactosamine-specific cell-binding activity in a plant pathogen, Erwinia rhapontici.

A strain of the phytopathogenic bacterial species, Erwinia rhapontici, was found to cause hemagglutination of human erythrocytes that was specifically inhibited by beta-galactosides. Of the monosaccharides tested, N-acetyl galactosamine and galactose efficiently inhibited the hemagglutination. The most potent inhibitor identified was Ga1 beta 1-4GlcNAc that was 30-100-fold more potent than Ga1 beta 1-3GlcNac or Ga1 beta 1-3GalNAc. Fetuin had no effect on the hemagglutination whereas asialofetuin was inhibitory. No blood group specificity was found for the hemagglutinin. These findings indicate that the E. rhapontici strain possesses a novel bacterial cell-binding activity with specificity for terminal N-acetyllactosamine residues.

Acetylgalactosamine↗
PubMed1988

Binding characteristics of Escherichia coli adhesins in human urinary bladder.

We studied domains in the human bladder that acted as receptors for Escherichia coli P, S, type 1, type 1C, and O75X fimbriae or adhesin and domains in the human kidneys that were receptors for E. coli type 1C fimbriae. Binding sites in frozen tissue sections were localized by direct staining with fluorochrome-labeled recombinant strains and by indirect immunofluorescence with the purified adhesins. In the bladder, the P and S fimbriae showed closely similar binding to the epithelial and muscular layers, and the S fimbriae also bound to the connective tissue elements. Type 1 fimbriae bound to vascular walls and to muscle cells, whereas the O75X adhesin bound avidly to connective tissue elements and to some extent to epithelial and muscle cells of the bladder. The type 1C fimbriae bound to distal tubules and collecting ducts of the kidney and to vascular endothelial cells in both the kidney and bladder. The binding of all adhesin types was inhibited by specific receptor analogs or Fab fragments. The results reveal a possible mechanism by which the type 1C fimbriae may help invasion of E. coli in the kidneys but do not support a pathogenetic role for type 1 fimbriae. Similar tissue specificity of P and S fimbriae in the human urinary tract indicates that the presence of binding sites on uroepithelia does not fully explain the virulence properties of P fimbriae in human urinary tract infections.

Adhesins, Escherichia coli↗
PubMed1988

Identification of factors in human urine that inhibit the binding of Escherichia coli adhesins.

Earlier studies on the binding of Escherichia coli adhesins to the human urinary tract have indicated that the ability to recognize binding sites on the urinary tract epithelial cells is not a characteristic for P fimbriae only, but is also shared by some other adhesins that are not associated with pyelonephritis, especially S fimbriae. In the present study we have investigated whether human urine contains inhibitors of the binding of E. coli adhesins. Normal human urine was found to inhibit hemagglutination by S and type 1 fimbriae but not P fimbriae. The major inhibitor of S fimbriae in normal urine was identified as Tamm-Horsfall glycoprotein, and the interaction with S fimbriae is probably mediated by its sialyloligosaccharide chains. No significant variation was observed in the inhibitory effect of T-H glycoprotein preparations originating from different individuals. In contrast to S fimbriae, the major inhibitors of type 1 fimbriae in urine were identified as low-molecular-weight compounds. Gel filtration and ion-exchange chromatography and alpha-mannosidase treatment indicated that they were neutral alpha-mannosides, probably manno-oligosaccharides with three to five saccharides. Studies of urine samples collected from several individuals indicated the common occurrence of these inhibitory alpha-mannosides. Type 1 fimbriae bound to immobilized T-H glycoprotein, but, unlike S fimbriae, their binding was poorly inhibited by soluble T-H glycoprotein. Some urine samples were also found to contain low-molecular-weight inhibitors for the O75X adhesin of E. coli. These results emphasize that to function as a virulence factor in human urinary tract infections, an adhesin must evidently recognize such receptor structures at the infection sites that are not excreted in soluble form in urine. This prerequisite is filled by P fimbriae but not by type 1 or S fimbriae.

Adhesins, Escherichia coli↗
PubMed1988

Binding sites in the rat brain for Escherichia coli S fimbriae associated with neonatal meningitis.

Escherichia coli strains that cause sepsis and meningitis in neonatal infants carry S fimbriae that bind to sialyl galactoside units of cell surface glycoproteins. To investigate the possible role of S fimbriae in determining the tissue tropism of neonatal meningitis, we have studied the presence of binding sites for S fimbriae in different tissues of the neonatal rat which is susceptible to meningitis caused by S-fimbriated E. coli. Purified S fimbriae were incubated on cryostat sections of different rat organs and their binding was assessed by indirect immunofluorescence. In the brain of the neonatal rat, S fimbriae specifically bound to the luminal surfaces of the vascular endothelium and of the epithelium lining the choroid plexuses and brain ventricles. The binding was completely inhibited by the trisaccharide NeuAc alpha 2-3Gal beta 1-4Glc, a receptor analogue of S fimbriae, and by a preceding neuraminidase treatment of the sections. A recombinant E. coli strain expressing S fimbriae adhered in large numbers to the same tissue sites in the neonatal brain sections as did the purified fimbriae, whereas the non-fimbriated host strain and a recombinant strain expressing P fimbriae did not adhere to brain tissues. The results suggest that adhesion of S-fimbriated bacteria to the binding sites observed in the neonatal brain has a pathogenetic role during bacterial invasion from circulation into the cerebrospinal fluid.

Animals↗
PubMed1986

Identification of the O-linked sialyloligosaccharides of glycophorin A as the erythrocyte receptors for S-fimbriated Escherichia coli.

The erythrocyte receptors for S-fimbriated Escherichia coli, which causes sepsis and meningitis in newborn infants, were investigated. Neuraminidase and trypsin treatments of erythrocytes abolished the hemagglutination ability of the bacteria. To identify the receptor glycoproteins, we separated erythrocyte membrane proteins by gel electrophoresis, blotted them to nitrocellulose, and incubated them with 125I-labeled bacteria. The only bacterium-binding bands identified corresponded to glycophorin A dimer and monomer, and the binding was abolished by neuraminidase treatment of the blot. Radiolabeled bacteria also bound to purified glycophorin A adsorbed to polyvinyl chloride microwells, and the binding was inhibited by other sialoglycoproteins and isolated sialyloligosaccharides containing the NeuAc alpha 2-3Gal sequence. Oligosaccharides which contain the NeuAc alpha 2-3Gal beta 1-3GalNAc and NeuAc alpha 2-3Gal beta 1-3(NeuAc alpha 2-6)GalNAc sequence and which are identical to the O-linked saccharides of glycophorin A were twofold more effective inhibitors of binding than were other oligosaccharides containing the NeuAc alpha 2-3Gal sequence. The replacement of sialic acid in asialoerythrocytes with a purified Gal beta 1-3GalNAc alpha 2-3 sialyltransferase, which forms the O-linked NeuAc alpha 2-3Gal beta 1-3GalNAc sequence in asialoglycophorins, restored bacterial hemagglutination. These results indicated that the major erythrocyte receptor for S-fimbriated E. coli is the NeuAc alpha 2-3Gal beta 1-3GalNAc sequence of the O-linked oligosaccharide chains of glycophorin A.

Bacterial Adhesion↗
PubMed1986

Binding of Escherichia coli S fimbriae to human kidney epithelium.

Purified S fimbriae and an Escherichia coli strain carrying the recombinant plasmid pANN801-4 that encodes S fimbriae were tested for adhesion to frozen sections of human kidney. The fimbriae and the bacteria bound to the same tissue domains, and in both cases the binding was specifically inhibited by the receptor analog of S fimbria, sialyl(alpha 2-3)lactose. S fimbriae bound specifically to the epithelial elements in the kidneys; to the epithelial cells of proximal and distal tubules as well as of the collecting ducts and to the visceral and parietal glomerular epithelium. In addition, they bound to the vascular endothelium of glomeruli and of the renal interstitium. No binding to connective tissue elements was observed. The results suggest that the biological function of S fimbriae is to mediate the adhesion of E. coli to human epithelial and vascular endothelial cells.

Adenocarcinoma↗
PubMed1985

Serotypes, hemolysin production, and receptor recognition of Escherichia coli strains associated with neonatal sepsis and meningitis.

Sixty-three Escherichia coli strains isolated from neonatal sepsis or meningitis were studied and compared with previous data on fecal or urinary pyelonephritis-associated isolates from children. Characteristics significantly associated with neonatal infection were capsular type K1 (54%), O group 18 (27%), rough-type lipopolysaccharide together with K1 capsule (19%), and S fimbriae (29%). Within the neonatal infection group, the K1 capsule and rough lipopolysaccharide were most common among the youngest infants (0 to 21 days old) and in meningitis. Hemolysin production, P fimbriae, and X adhesions (adhesions not identifiable as type 1, P, or S) were significantly more common in the two materials from infections as compared with the fecal isolates. One large clone of 11 strains (O18:K1:H7, with both type 1 and S fimbriae) and three smaller ones (O7:K1:H1 and O6:K2:H1, both with type 1 and P fimbriae and X adhesions; and R:K1:H33 with no adhesions) were identified among the strains from neonatal infections. Only O6:K2:H1 strains were also common among the strains from pyelonephritis.

Adhesins, Escherichia coli↗