Biomedical subjects

U Kägi

Publications and source records attributed to U Kägi.

5 recordsLinked to original sources

PubMed1990

Innervation and maturation of muscular tissue in testicular teratomas in strain 129/Sv-ter mice.

In strain 129/Sv-ter mice, teratomas develop spontaneously during the 13th day of gestation. These testicular germ cell tumors exhibit characteristics of different germ layers closely resembling normal embryonic tissue. We investigated the interrelationship between nervous and muscular tissues (often found side by side) in teratomas of 4-week-old 129/Sv-ter mice. In well-differentiated mouse teratomas, histochemically and immunohistochemically distinct muscle fiber types could be distinguished, but not with all reactions. According to its aerobic oxidative capacity, teratoma muscle tissue was comparable with normal muscles. However, with respect to myosin-related properties, fiber type differentiation was incomplete. The muscle fibers - generally arranged in bundles - contained one centrally located endplate which was contacted mostly by a single nerve terminal. From this, proper endplate zones within the fiber bundles were formed. Occasionally "type grouping" was encountered, suggesting collateral axonal branching paralleled by synapse elimination. Together with the earlier in vivo observation of muscular contractions, we assume that teratoma muscle fibers are innervated by nerve cells (within the nervous tissue compartments) corresponding to spinal motoneurons. Thus, myogenesis, maturation and innervation of skeletal muscular tissue in mouse teratomas are largely comparable to normal development.

Animals↗

PubMed1990

Poly- and monoclonal antibodies against recombinant rat brain calbindin D-28K were produced to map its selective distribution in the central nervous system.

Many processes in the CNS depend on calcium. The calcium signal is transduced into an intracellular response via Ca2(+)-binding proteins, including calbindin D-28K. In many laboratories, polyclonal antibodies against chicken intestinal calbindin D-28K have been used to study its localization in the brain (normal and degenerated) of various species, including humans, but some of these antisera cross-reacted with other proteins, including calretinin. We purified recombinant rat brain calbindin D-28K to raise antisera in rabbits and purified a recombinant rat-chicken calbindin D-28K hybrid protein to immunize mice for the generation of monoclonal antibodies. These antisera were highly specific for calbindin D-28K, as demonstrated by two-dimensional Western blotting analysis. Immunohistochemical analyses combined with in situ hybridization studies demonstrated that calbindin D-28K in the Purkinje cells of the cerebellum is independent of vitamin D. The antibodies described here will be important tools for studying the regulation of expression of calbindin D-28K and its biological function in the brain and in the PNS.

Animals↗

PubMed1988

Developmental appearance of the Ca2+-binding proteins parvalbumin, calbindin D-28K, S-100 proteins and calmodulin during testicular development in the rat.

Calcium and intracellular Ca2+-binding proteins are possibly involved in hormone production and spermatogenesis in rat testis. Parvalbumin, calbindin D-28K, S-100 proteins and calmodulin were localized in the Leydig cells, which are sites of testosterone synthesis. Only the appearance of parvalbumin-immunoreactivity is closely correlated to testosterone production during development of the testes. Calbindin D-28K-immunoreactivity persisted in foetal-type Leydig cells and in adult-type Leydig cells at all stages of development. S-100-immunoreactivity was low during all foetal stages, absent between birth and puberty, and increased thereafter. Calmodulin staining is most prominent in the cytoplasm of developing spermatocytes and of maturing spermatids. All four proteins co-exist in the seminiferous tubules. The distinct localization and developmental appearance of these proteins suggests different regulatory roles in Leydig cell function and spermatogenesis.

Animals↗

PubMed1987

Ca2+-binding parvalbumin in rat testis. Characterization, localization, and expression during development.

Parvalbumin, a Ca2+-binding protein, was isolated from rat testis. This is the first demonstration of the protein in endocrine glands. By using a rat parvalbumin cDNA probe, parvalbumin mRNA was demonstrated in the testis, indicating that the protein is synthesized in this tissue and that testis parvalbumin is a product of the same gene as the one encoding for muscle parvalbumin. Parvalbumin was localized by immunohistochemical methods in the Leydig cells and in the acrosome region of maturing spermatids (stages 1-15). The expression of parvalbumin during testis development was followed. High parvalbumin protein and mRNA levels were found at stages of highest Leydig cell activity, i.e. at late fetal stages until birth and again around postnatal day 50. This suggests that parvalbumin may be involved in the production of testosterone in Leydig cells, a process which is highly dependent on calcium.

Acrosome↗

PubMed1986

Parvalbumin in cat brain: isolation, characterization, and localization.

Because of the increasing evidence that Ca2+-binding proteins have important regulating functions in nerve cells and because of the indications that there are species differences in the structures of these proteins, parvalbumin was purified from cat brain and muscle. Brain and muscle parvalbumins were found to be indistinguishable from each other in their biochemical and immunological properties. However, cat parvalbumin differs from all other mammalian parvalbumins by its apparently lower Mr on sodium dodecyl sulfate-polyacrylamide gel electrophoresis of 10-11K (compared to rat parvalbumin, 12K), and a lower pI of 4.6 (rat parvalbumin, 4.9), in the tryptic peptide maps, and in the immunological properties, indicating a distinct primary structure. With the purified parvalbumin as antigen, polyclonal antibodies were raised in rabbits and these were subsequently used for immunohistochemical localizations of parvalbumin in the cat brain. In the visual cortices of adult cats immunoreactive neurons were present throughout layers II and IV. In cerebellar cortex, Purkinje, basket, and stellate cells were immunoreactive. Comparison with staining patterns obtained with antiserum against rat parvalbumin revealed some cross-reactivity but confirmed the existence of species differences in the antigenic structure of rat and cat parvalbumin.

Amino Acids↗