| 1. |
|
|
| 2. |
|
|
| 3. |
- Karadima, G, et al.
(författare)
-
Nondisjunction studies in trisomy 8.
- 1997
-
Ingår i: CYTOGENETICS AND CELL GENETICS. - 0301-0171. ; 77:1-2, s. P105-P105
-
Konferensbidrag (övrigt vetenskapligt/konstnärligt)
|
|
| 4. |
|
|
| 5. |
|
|
| 6. |
|
|
| 7. |
|
|
| 8. |
|
|
| 9. |
|
|
| 10. |
|
|
| 11. |
- Li, J. Y., et al.
(författare)
-
Distribution of Rab3a in rat nervous system: comparison with other synaptic vesicle proteins and neuropeptides
- 1996
-
Ingår i: Brain Research. ; 706:1, s. 103-112
-
Tidskriftsartikel (refereegranskat)abstract
- In the present study we have investigated the distribution of Rab3a in rat peripheral nervous system and compared it with the distribution of other synaptic vesicle proteins (synaptophysin, synapsin I), neuropeptides (CGRP, SP, NPY) and tyrosine hydroxylase (TH). Rab3a immunoreactivity (-IR) was always colocalized with synaptophysin-IR and synapsin I-IR in nerve terminals of the spinal cord and peripheral nerve endings. In many cases, Rab3a-IR was also present in the same axons and terminals as peptides. In crushed sciatic nerve axons, Rab3a was colocalized, proximal to the crush, with synaptophysin-IR, synapsin I-IR, CGRP-IR, and TH-IR, but only partially co-localized with NPY-IR and SP-IR. In the area distal to the crush, Rab3a-IR was very weakly positive in a few thin axons, while larger amount of synaptophysin, CGRP, NPY and SP immunoreactivities were detected. The subcellular distribution of peptides and Rab3a differed in that peptides were observed mainly in large granular structures, while Rab3a-IR was observed mainly as diffuse, finely granular immunoreactivity, in addition to a few exceptional large granules present in some axons. The results demonstrate that Rab3a is widely distributed in different types of neurons, i.e. motor, sensory, autonomic adrenergic and cholinergic neurons, and colocalized with other synaptic vesicle proteins, suggesting that Rab3a may play an essential role in neuronal function. Furthermore, Rab3a is present in many peptide containing axons and terminals, but with an apparently different subcellular distribution, being affiliated mostly with small synaptic vesicles and only occasionally with large vesicles, that may represent peptide contained vesicles.
|
|
| 12. |
- Marques, F. M., et al.
(författare)
-
Neutrons from the breakup of C-19
- 1996
-
Ingår i: Physics Letters, Section B: Nuclear, Elementary Particle and High-Energy Physics. - 0370-2693. ; 381:4, s. 407-412
-
Tidskriftsartikel (refereegranskat)abstract
- Neutrons arising from the breakup of a 30 MeV/nucleon C-19 beam on a tantalum target have been measured using the 98 element array DEMON. A narrow, forward peaked neutron angular distribution, with a corresponding momentum spread considerably smaller than those measured simultaneously for N-21, O-22 and F-24 was observed for charged fragments with Z
|
|
| 13. |
- Munch-Petersen, C., et al.
(författare)
-
Concrete strategy for the Oresund Tunnel
- 1997
-
Ingår i: Betonwerk und Fertigteil-Technik / Concrete Precasting Plant and Technology. - 0373-4331. ; 63:11, s. 44-54
-
Tidskriftsartikel (övrigt vetenskapligt/konstnärligt)abstract
- This paper gives a short review of the most requirements for the concrete to be used for the 3.510 m long immersed tunnel from Amager (outside Copenhagen Airport) to an artificial double island south of Saltholm (in the middle of Oresund). The basis for the requirements is shortly commented.
|
|
| 14. |
|
|
| 15. |
|
|
| 16. |
- Petersen, Frank, et al.
(författare)
-
Characterization of a neutophil surfacer glycosaminoglycan responsible for binding of platelet factor 4
- 1999
-
Ingår i: Journal of Biological Chemistry. - : Elsevier BV. - 0021-9258 .- 1083-351X. ; 274:18, s. 12376-12382
-
Tidskriftsartikel (refereegranskat)abstract
- Abstract Platelet factor 4 (PF-4) is a platelet-derived α-chemokine that binds to and activates human neutrophils to undergo specific functions like exocytosis or adhesion. PF-4 binding has been shown to be independent of interleukin-8 receptors and could be inhibited by soluble chondroitin sulfate type glycosaminoglycans or by pretreatment of cells with chondroitinase ABC. Here we present evidence that surface-expressed neutrophil glycosaminoglycans are of chondroitin sulfate type and that this species binds to the tetrameric form of PF-4. The glycosaminoglycans consist of a single type of chain with an average molecular mass of ∼23 kDa and are composed of ∼85–90% chondroitin 4-sulfate disaccharide units type CSA (→4GlcAβ1→3GalNAc(4-O-sulfate)β1→) and of ∼10–15% di-O-sulfated disaccharide units. A major part of these di-O-sulfated disaccharide units are CSE units (→4GlcAβ1→3GalNAc(4,6-O-sulfate)β1→). Binding studies revealed that the interaction of chondroitin sulfate with PF-4 required at least 20 monosaccharide units for significant binding. The di-O-sulfated disaccharide units in neutrophil glycosaminoglycans clearly promoted the affinity to PF-4, which showed a K d ∼ 0.8 μm, as the affinities of bovine cartilage chondroitin sulfate A, porcine skin dermatan sulfate, or bovine cartilage chondroitin sulfate C, all consisting exclusively of monosulfated disaccharide units, were found to be 3–5-fold lower. Taken together, our data indicate that chondroitin sulfate chains function as physiologically relevant binding sites for PF-4 on neutrophils and that the affinity of these chains for PF-4 is controlled by their degree of sulfation. The activation and control of polymorphonuclear granulocytes (PMN)1 are known to play an essential role in host defense against microbial invaders as well as in chronic diseases. Several members of the α-chemokine family like interleukin-8 (IL-8), neutrophil-activating peptide 2, or melanoma growth stimulatory activity have been shown to act as potent activators of PMN by binding to common IL-8 receptors (1). Such binding elicits diverse biological responses such as chemotaxis, degranulation, or adhesion. PF-4, another member of the α-subgroup of the chemokine family, is released in high concentrations from activated platelets (2,3). The functional role of PF-4 is intriguing. Highly purified PF-4 lacks any apparent biological activity for PMN but will in the presence of tumor necrosis factor α stimulate these cells to exocytose secondary granule markers or adhere tightly to different surfaces (4). These PF-4-induced functions are not elicited through binding to IL-8 receptors but by interaction with distinct binding sites different from all other chemokine receptors known so far (4,5). The action of PF-4 on PMN was shown to be sensitive to chondroitinase ABC treatment and could be inhibited by soluble chondroitin sulfate (CS), indicating that the potential receptor is of CS proteoglycan type (5). CSs are galactosaminoglycans composed of alternating glucuronic acid and galactosamine units (→4GlcAβ1→3GalNAcβ1→)n that areO-sulfated on one or both units.2 In contrast to the glucosaminoglycans heparin and heparan sulfate (HS), they do not contain N-sulfate groups or l-iduronic acid units (except for CSB), which have been particularly implicated in protein binding to HS chains (6). The expression of glycosaminoglycans (GAGs) on neutrophils has been described previously by several authors. Pioneering work by Olsson and co-workers showed that PMN predominantly express chondroitin 4-sulfate (CSA) (7, 8), and Levitt et al. demonstrated a minor proportion of HS in these cells (9). However, as all of these analyses were done with total cell extracts, little is known about the composition and function of cell surface-expressed GAGs in PMN. Gardiner and colleagues showed that the majority of metabolically 35S-labeled compounds occurs as proteoglycans in neutrophil granules where they may enable proper storage of granule contents or exert protective functions against cellular damage (10,11). Here, we provide evidence that surface exposed CS chains serve as physiologically relevant receptors for PF-4 on PMN, and propose that this function is critically dependent on the content of sulfate groups.
|
|
| 17. |
|
|
| 18. |
|
|
| 19. |
- Stender, H, et al.
(författare)
-
Fluorescence In situ hybridization assay using peptide nucleic acid probes for differentiation between tuberculous and nontuberculous mycobacterium species in smears of mycobacterium cultures
- 1999
-
Ingår i: Journal of Clinical Microbiology. - 1098-660X. ; 37:9, s. 2760-2765
-
Tidskriftsartikel (refereegranskat)abstract
- TB PNA FISH is a new fluorescence in situ hybridization (FISH) method using peptide nucleic acid (PNA) probes for differentiation between species of the Mycobacterium tuberculosis complex (MTC) and nontuberculous mycobacteria (NTM) in acid-fast bacillus-positive (AFB+) cultures is described. The test is based on fluorescein-labelled PNA probes that target the rRNA of MTC or NTM species applied to smears of AFB+ cultures for microscopic examination. Parallel testing with the two probes serves as an internal control for each sample such that a valid test result is based on one positive and one negative reaction. TB PNA FISH was evaluated with 30 AFB+ cultures from Denmark and 42 AFB+ cultures from Thailand. The MTC-specific PNA probe showed diagnostic sensitivities of 84 and 97%, respectively, and a diagnostic specificity of 100% in both studies, whereas the NTM-specific PNA probe showed diagnostic sensitivities of 91 and 64%, respectively, and a diagnostic specificity of 100% in both studies. The low sensitivity of the NTM-specific PNA probe in the Thai study was due to a relatively high prevalence of Mycobacterium fortuitum, which is not identified by the probe. In total, 63 (87%) of the cultures were correctly identified as MTC (n = 46) or NTM (n = 17), whereas the remaining 9 were negative with both probes and thus the results were inconclusive. None of the samples were incorrectly identified as MTC or NTM; thus, the predictive value of a valid test result obtained with TB PNA FISH was 100%.
|
|
| 20. |
|
|
