Enzymhistochemische Befunde im subependymalen Glialager während der Entwicklung des Rattenhirns

Zusammenfassung Die prä- bzw. postnatale enzymtopochemische Differenzierung des subependymalen Glialagers in der lateralen Wand des Vorderhornes wurde bei der SpragueDawley-Ratte untersucht. Während der pränatalen Entwicklungsphase des Rattenhirns zeichnet sich die Subependymschicht, beim Nachweis der wichtigsten hydrolytischen und oxydativen Enzyme, im allgemeinen durch eine geringe enzymatische Aktivität aus. Die Ergänzung der enzymatischen Ausstattung dieser Zellschicht erfolgt erst während der postnatalen Hirnentwicklung und zwar in den ersten 2 Lebenswochen. Eine Ausnahme von dieser Regel wurde beim Nachweis der Phosphomonoesterase-I festgestellt, welche in der prä- bzw. perinatalen Entwicklungsphase die höchste Aktivität zeigte. Die erhobenen enzymtopochemischen Befunde deuten darauf hin, daß in der subependymalen Zellschicht eine vom übrigen Hirn vor allem zeitlich abweichende topochemische Differenzierung stattfindet, welche im wesentlichen während der ersten 2 Lebenswochen abgeschlossen ist.

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Enzyme topochemical findings of the subependymal cell layer in the developing rat brain

Summary The pre- and postnatal enzyme topochemical differentiation of the subependymal glial layer of the lateral ventricle was examined in the Sprague-Dawley rat. During the prenatal development phase of the subependymal layer, weak enzymatic activity of the most important hydrolytic and oxidative enzymes is demonstrated. The completion of the enzyme activity of this cell layer follows in the postnatal brain development period, and certainly within the first two weeks of life. An exception to this rule has been found in the case of phosphomonoesterase-I which showed the greatest activity in the pre- and perinatal development phases. The observed enzyme topochemical findings indicate that the subependymal cell layer, in contrast to other parts of the brain, shows temporally deviating topochemical differentiation, which is essentially completed in the first two weeks of life.

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Mit Unterstützung durch die Deutsche Forschungsgemeinschaft (SFB 51).     

Biosynthesis of immunoglobulin A (IgA). Secretion and addition of carbohydrate to monomer and polymer forms of a mouse myeloma protein

Cell suspensions of mouse plasma-cell tumour MOPC 315 secreting predominantly IgA (immunoglobulin A) monomer and dimer were incubated with radioactive leucine, mannose, galactose and fucose for various periods of time. The amounts of secreted and intracellular immunoglobulins were measured by co-precipitation with specific antibody, and the molecular species present were assessed by electrophoresis in polyacrylamide gels. Analysis of the secreted myeloma protein demonstrated that monomer and dimer IgA molecules are identical with respect to carbohydrate composition and rate of secretion. Within the cell, the myeloma protein is almost entirely accounted for by monomer units which either leave the cell as such or are polymerized with the addition of J chain close to the time of secretion. The results support the concept of a stepwise addition of carbohydrate residues to IgA immunoglobulin during the process of secretion. Similar patterns of carbohydrate assembly were found for the monomer or dimer molecules. Mannose residues are added at an early stage, whereas fucose is added close to the time of secretion. Galactose is also added early, but some may also be incorporated at a later stage. Control of IgA polymerization is considered unlikely to reflect regulation at the level of carbohydrate addition, and it is suggested that the critical controlling factor is the J chain.