PubMed Health⌕ Search

Biomedical subjects

G Jeserich

Publications and source records attributed to G Jeserich.

At least 37 records · Page 2Linked to original sources
PubMed1992

Voltage-dependent potassium currents in cultured trout oligodendrocytes.

Ionic currents were recorded in cultured oligodendrocytes from the brain of trout using the whole-cell configuration of the patch-clamp technique. Outward currents were evoked at membrane potentials more positive than -40 mV, which could be separated into two components according to their kinetic parameters and their sensitivity to the holding potential: a fast inactivating current which was completely suppressed by 4-aminopyridine and reduced by tetraethylammonium and a slow steady-state conductance which was similarly sensitive to both potassium channel blockers. The current reversal potential was close to the potassium equilibrium potential. In contrast to mammalian oligodendrocytes but in similarity with cultured Schwann cells, trout oligodendrocytes did not exhibit any inwardly rectifying currents at hyperpolarized membrane potentials.

4-Aminopyridine↗
PubMed1992

Myelination of regenerated axons in goldfish optic nerve by Schwann cells.

This study uses immunohistochemistry and EM to examine the site of injury in goldfish optic nerve during axonal regeneration. Within seven days of nerve crush axons begin to regrow and a network of GFAP+ reactive astrocytes appears in the nerve on either side of the injury. However, the damaged area remains GFAP-. By 42 days after nerve crush, the sheaths of new axons acquire myelin marker 6D2, and the crush area becomes populated by a mass of longitudinally-orientated S-100+ cells. Ultrastructurally, the predominant cells in the crush area bear a strong resemblance to peripheral nerve Schwann cells; they display a one-to-one association with myelinated axons, have a basal lamina and are surrounded by collagen fibres. It is proposed that these cells are Schwann cells which enter the optic nerve as a result of crush, where they become confined to the astrocyte-free crush area.

Animals↗
PubMed1991

Soluble factor(s) produced in injured fish optic nerve regulate the postinjury number of oligodendrocytes: possible role of macrophages.

Mammalian central nervous system (CNS) axons are virtually incapable of regenerating after injury. However, CNS neurons of lower vertebrates, such as fish and amphibians, are endowed with a high regenerative capacity. Lately, the glial cells have been credited with the regenerative ability of any specific CNS. We have previously demonstrated that many oligodendrocytes are recovered in cultures of injured rat optic nerve, while only a few oligodendrocytes are recovered from injured fish optic nerve in culture. We further demonstrated that medium conditioned by regenerating fish optic nerves (CM), which has been shown to cause axonal elongation in injured rabbit optic nerves, causes a decrease in the number of oligodendrocytes in rat glial cultures. In the present study, we demonstrate that soluble factors in the CM are capable of reducing the number of fish oligodendrocytes in fish optic nerve cultures. In addition, an inverse relationship was found between the number of macrophages and the number of oligodendrocytes. These results thus suggest that macrophages and/or activated resident microglial cells are directly or indirectly responsible for the presence of these soluble factor(s) that regulate the postinjury number of oligodendrocytes in the fish optic nerves.

Animals↗
PubMed1990

Developmental expression of myelin proteins by oligodendrocytes in the CNS of trout.

Using immunohistochemical techniques, the pattern of cytoplasmic staining and the temporal order of expression of 5 major myelin components of oligodendrocytes were studied in the developing central nervous system of trout. The two myelin glycoproteins, IP1 and IP2, in the cytoplasm of glial cells showed a granular pattern of immunostaining, whereas the 36K protein was homogeneously distributed. Analysis of freshly dissociated cells during early stages of myelinogenesis revealed a constant chronological sequence of expression of myelin proteins by the oligodendrocytes: glycoprotein IP2 was the first protein to appear during glial development together with the galactocerebroside GalC at stage 28 followed by the 36K at stage 30 and finally IP1 at stage 32. The deposition of myelin proteins into the nascent myelin sheath occurred in the same chronological order as their expression by oligodendrocytes. Moreover myelin basic protein, which was not detectable in glial cells, on tissue sections was found to appear in parallel with IP2.

Animals↗
PubMed1990

Cell cultures enriched in oligodendrocytes from the central nervous system of trout in terms of phenotypic expression exhibit parallels with cultured rat Schwann cells.

Oligodendrocytes were isolated from the white matter of young trout by Percoll density centrifugation of enzymatically dissociated tissue and cultured on poly-D-lysine-coated petri dishes. Using antisera recognizing myelin-specific compounds of fish CNS (36K, IP2) up to 72% of the isolated cells could be identified as oligodendrocytes with an average yield of 4 x 10(6) cells per gram of wet tissue. Taken in culture, the cells rapidly regenerated their processes and soon acquired a morphology closely resembling mammalian oligodendrocytes in vitro. On the other hand, in terms of phenotypic expression, interesting parallels were revealed with the known in vitro behavior of Schwann cells: Galactocerebroside, which in mammalian oligodendrocytes is persistently expressed over longer periods of time in vitro, rapidly disappeared from the surface of cultured trout oligodendrocytes. In contrast, the fish CNS myelin glycoprotein IP2, which like IP1 is immunologically related to the major myelin product of Schwann cells, P0, was continuously expressed over several weeks in culture. Two other myelin protein constituents, 36K and IP1, transiently declined in vitro, but later on fully reappeared in the glial cells of trout. The present cell culture system offers an experimental model for studying in vitro the factors underlying oligodendroglial regeneration and remyelination in the fish CNS.

Animals↗
PubMed1990

Glial response to axonal injury: in vitro manifestation and implication for regeneration.

Crushed fish optic axons readily regenerate, while similarly injured rat optic axons do not; the reasons for the differences in regeneration ability may lie in differences in the environment of the axons. We have cultured glial cells from previously crushed optic nerves of fish and rat to determine whether a relationship exists between the ability to regenerate and the nature of the responses of the associated nonneuronal cells to injury. The glial cells were examined using indirect immunofluorescence with antibodies to known glial markers. In the rat cultures, mature GalC oligodendrocytes, which are known to be nonpermissive for axonal growth, were abundant. In contrast, in the fish cultures mature oligodendrocytes were rare, but A2B5 positive cells were abundant. The high number of A2B5 positive cells in the fish may suggest a high number of immature cells. This interpretation, however, should wait until evidence for glial cell lineage of the fish is available. Additional indication is provided also in the present study that the number of mature oligodendrocytes in the fish is regulated by elements external to the nerve. This study thus demonstrates an important difference between rat and fish optic nerves in the response of glial cells to the optic nerve injury.

Animals↗
PubMed1987

Antigenic sites common to major fish myelin glycoproteins (IP) and to major tetrapod PNS myelin glycoprotein (Po) reside in the amino acid chains.

The major myelin glycoproteins in the CNS and PNS of trout (IP) were enzymatically deglycosylated with endoglycosidase F (Endo F) and examined by electro-immunoblotting. Following carbohydrate removal and loss of concanavalin A affinity each of the four IP components underwent a similar reduction in molecular size, corresponding to approximately 3,000 daltons. Immunological cross-reactivities with anti-bovine Po or anti-trout IP2 antibodies, were however fully retained by the Endo F cleavage products. This strongly implies that the antigenic sites shared by the mammalian Po protein and the various intermediate glycoproteins of trout CNS and PNS are located in the protein portion. Immunoblot analysis of the PNS myelin proteins from various species of the major vertebrate classes with anti-trout IP2 antiserum revealed striking differences in the immunological properties of the individual Po components which were not detected when anti-bovine Po antiserum was used as a probe.

Animals↗
PubMed1986

Characterization of antibodies against major fish CNS myelin proteins: immunoblot analysis and immunohistochemical localization of 36K and IP2 proteins in trout nerve tissue.

Antisera against the trout CNS myelin proteins 36K and IP2 were prepared in rabbits and characterized by immunoblot analysis and immunohistochemistry. The anti-36K antiserum exclusively stained its corresponding antigen from trout CNS myelin but failed to recognize any myelin polypeptide from either trout PNS or mammalian CNS and PNS. Antibodies against the IP2 glycoprotein specifically cross-reacted with related intermediate proteins (IP) of both CNS and PNS myelin from trout but only faintly labeled the PO protein of mouse peripheral nerve. Immunohistochemical localization of both antigens in the CNS of young trout was confined to the myelin sheath, except that anti-36K antiserum also stained oligodendrocytes. Nodes of Ranvier, neuronal cell bodies, and dendrites, as well as other glial elements, were negative. Specificity of the immunofluorescent reaction was established by crossed immunoadsorption experiments. Whereas on adjacent sections through trout brain both antigens exhibited a nearly identical distribution pattern, immunostaining in peripheral nerves was seen only with anti-IP2 antibodies.

Animals↗
PubMed1986

Myelin lipids: a phylogenetic study.

The lipid composition of CNS and PNS myelin was studied in rat, Xenopus, trout and Torpedo. The main difference lay in the proportion of cerebrosides, which decreased in the sequence rat greater than Xenopus greater than Torpedo greater than trout. In addition Torpedo CNS and PNS myelins were extremely rich in sulfatides. In some respects, Torpedo appeared closer to tetrapods than trout. Otherwise the proportion of the different lipid classes did not reveal any clear evolutionary trends. The presence of hydroxylated galactolipids in CNS myelin was investigated in several additional species. Considerable amounts were found in Torpedo, Polypterus, Protopterus, lizard, and chicken, with the highest values in rat and anurans. Only very small amounts of hydroxylated cerebrosides were detected in trout and in axolotl, while newt had none. This parameter appears therefore of doubtful usefulness for phylogenetic studies. In contrast to myelin proteins, myelin lipids are of limited value for establishing phylogenetic relationships among vertebrates.

Amphibians↗
PubMed1986

Central nervous system myelin of teleosts: comparative electrophoretic analysis of its proteins by staining and immunoblotting.

CNS myelin was isolated from 24 teleostean fishes and the proteins were analyzed by staining and immunoblotting. All species showed a 36 K protein, two or more glycosylated hydrophobic intermediate protein (IP) components and several myelin basic protein bands (BP). The 36 K protein was specific for teleostean fishes. The IP and BP components displayed substantial variations in their proportions as well as in molecular sizes when comparing the different teleosts. This contrasts with CNS myelin proteins which appear more stable in terrestrial vertebrates.

Animals↗
PubMed1986

Major central nervous system myelin glycoprotein of the African lungfish (Protopterus dolloi) cross-reacts with myelin proteolipid protein antibodies, indicating a close phylogenetic relationship with amphibians.

CNS myelin was isolated from the spinal cord of the African lungfish Protopterus dolloi. Its proteins consisted of (1) two basic proteins (16,000 and 18,500 apparent Mr) that reacted with anti-human CNS myelin basic protein antibodies and (2) a major protein (29,000 apparent Mr) that stained with concanavalin A-horseradish peroxidase and bound to anti-rat CNS myelin proteolipid protein (PLP) antibodies. This dominant 29,000 Mr protein showed no reaction with antibodies against the major bovine PNS myelin glycoprotein P0. Following treatment with endoglycosidase F the 29,000 Mr protein was reduced in size to a 26,000 apparent Mr component that no longer bound concanavalin A but retained the anti-PLP reactivity. These results agree with a concanavalin A-binding oligosaccharide linked through asparagine to a protein backbone of PLP homology. The major 29,000 Mr lungfish CNS myelin protein was therefore termed g-PLP (glycosylated proteolipid protein). This is the first report demonstrating the occurrence of a PLP-cross-reactive protein in CNS myelin of a fish. It attests to the close phylogenetic relationship of lungfishes to amphibians. Amphibians were previously recognized as the oldest class bearing PLP in its CNS myelin.

Amphibians↗
PubMed1986

Bony fish myelin: evidence for common major structural glycoproteins in central and peripheral myelin of trout.

Peripheral nervous system (PNS) myelin from the rainbow trout (Salmo gairdneri) banded at a density of 0.38 M sucrose. The main myelin proteins consisted of (1) two basic proteins, BPa and BPb (11,500 and 13,000 MW, similar to those of trout central nervous system (CNS) myelin proteins BP1 and BP2), and (2) two glycosylated components, IPb (24,400 MW) and IPc (26,200 MW). IPc comigrated with trout CNS myelin protein IP2 in sodium dodecyl sulfate-polyacrylamide gel electrophoresis, whereas trout CNS myelin protein IP1 had a lower molecular weight (23,000). Following two-dimensional separation, however, both IPb and IPc from PNS showed two components; the more acidic component of IPc comigrated with IP2 from CNS. PNS tissue autolysis led to the formation of IPa (20,000 MW), consisting of two components in isoelectric focusing of which again the more acidic one comigrated with the CNS autolysis product IP0. Limited enzymatic digestion of isolated IP proteins from PNS and CNS led to closely similar degradation patterns, being most pronounced in the case of IP2 and IPc. Immunoblotting revealed that all IP components from trout PNS and CNS myelins reacted with antibodies to trout IP1 (CNS) and bovine P0 protein (PNS) whereas antibodies to rat PLP (CNS) were entirely unreactive. All BP components from trout PNS and CNS myelins bound to antibodies against human myelin basic protein. On the basis of these studies trout PNS and CNS myelins contain at least one common IP glycoprotein, whereas other members of the IP myelin protein family appear closely related. In the CNS myelin of trout the IP components appear to replace PLP.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1985

Immunohistochemical localization of myelin basic protein in the developing optic system of trout.

Immunofluorescent localization of basic protein (BP) in the CNS of trout was performed using a heterologous antiserum raised against human BP. Bright specific fluorescence was confined to the myelin sheath of axons in most regions of the brain, whereas neuronal pericarya and dendrites as well as glial cells were entirely negative. In the tectum immunofluorescence was characteristically distributed in two rows of horizontally aligned patches, most evidently reflecting the orderly array of myelinated fiber bundles in the stratum opticum and stratum album. During development of the retino-tectal pathway, the appearance of BP followed a distinct rostro-caudal gradient firstly reaching the anterior ventral border of the tectum by larval stage 34. Furthermore, on cross sections through the optic nerve a specifically organized pattern of myelin formation was revealed by immunohistochemistry, which strikingly coincided with the pattern of fiber outgrowth.

Animals↗
PubMed1984

Biochemical characterization of the central nervous system myelin proteins of the rainbow trout, Salmo gairdneri.

Central nervous system myelin isolated from the rainbow trout (Salmo gairdneri) displays a very low median density on zonal gradient centrifugation, banding at approximately 0.32 M sucrose. Its proteins consist of a 36 K (36,000 mol.wt.) component, two Concanavalin A-reactive intermediate proteins IP1 (23,000 mol.wt.) and IP2 (26,200 mol.wt.), and two basic proteins BP1 and BP2, of which the latter co-migrates with rat SBP while BP1 is of slightly smaller size. The trout myelin proteins electrofocus at pH positions similar to those of their mammalian counterparts. Immunoblotting shows that antibodies against rat PNS myelin P0 glycoprotein are bound by IP1 and IP2, but not by 36K. None of the trout myelin proteins react with anti-rat CNS myelin proteolipid protein (PLP) antiserum. The basic proteins BP1 and BP2 bind strongly to antibodies directed against human myelin basic protein. In vivo injection of tritiated fucose or palmitate leads to radiolabeling of IP1 and IP2. Under autolytic in situ conditions the appearance of a glycosylated 20,000 mol.wt. component (IP0) is noted, with parallel reduction of both IP1 and IP2, indicating sequence homologies between IP1 and IP2. The 36K protein is not affected by autolysis.

Animals↗
PubMed1983

Protein analysis of myelin isolated from the CNS of fish: developmental and species comparisons.

The protein composition of myelin isolated from the CNS of four different fish species (trout, goldfish), eel, Tilapia) was analysed by SDS-polyacrylamide gel electrophoresis and compared with that of pig and rat brain. Thereby the following features were found typical to the myelin of fish: (1) a basic protein of particular low molecular weight, (2) the entire absence of Wolfgram protein, (3) the appearance of an additional major component of medium molecular weight (around 36,000) and (4) a strong Con A-affinity exhibited by the intermediate proteins, being most clearly discernible in trout and eel myelin. During development of the trout brain, in particular, a myelin fraction could first be isolated from the brainstem at 14 days after hatching and the myelin yield steadily increased during the first year of life. In tectum and cerebellum main myelin accumulation was stated during the third and seventh month. Concomitantly marked changes in the relative distribution of major myelin proteins were observed: especially the IP1-protein showed a marked increase during the first half year, while the relative amount of the 36-K protein was gradually declining during the same time.

Aging↗
PubMed1982

Ingrowth of optic nerve fibers and onset of myelin ensheathment in the optic tectum of the trout (Salmo gairdneri).

The early differentiation of the optic pathway of the trout was studied by means of autoradiography, silver impregnation and electron microscopy. Ingrowth of the optic nerve fibers into the optic tectum was consistently shown by tracer application and Golgi studies to occur at stage 28, about one week before hatching. Fibers being arranged in discrete bundles were rapidly growing through the longitudinal axis of tectum and at stage 33 reached its posterior end. Cross sections of these fiber bundles at different positions revealed myelin ensheatment to be initiated at the end of stage 34 at the anterior pole of the tectum. Since in the optic nerve of the trout the onset of myelination occurred even earlier (stage 33), it is assumed that this differentiation process follows a rostro-caudal gradient during development of the optic pathway.

Animals↗
PubMed1981

Effect of exogenous gangliosides on synaptosomal membrane ATPase activity.

Changes in the activity of (Na+, K+)-ATPase of synaptosomal membranes induced by exogenous gangliosides were studied. Depending on the ganglioside-protein ratio, the enzyme activity was finally reduced to 40% when the ratio was about 1. By analysis of the reaction kinetics the effect was characterized as a noncompetitive inhibition. Moreover the ganglioside effect was clearly dependent on the incubation temperature. Since exogenous gangliosides thereby caused a shifting in the optimum temperature of (Na+, K+)-ATPase, the effect is discussed in terms of changes of the membrane properties. In preincubation experiments it was revealed that the interaction of the glycolipids with synaptosomal membranes itself was temperature dependent and enhanced by ATP. It is suggested that ganglioside micelles might have been incorporated by the membranes in a way comparable to a fusion process.

Adenosine Triphosphate↗