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Biomedical subjects

H G Bernstein

Publications and source records attributed to H G Bernstein.

At least 73 records · Page 4Linked to original sources
PubMed1988

Ornithine decarboxylase in the inner ear of the guinea pig.

L-Ornithine decarboxylase, the rate limiting enzyme of polyamine synthesis and a possible marker enzyme for tissue proliferation and maturation, has been found in the developing guinea pig cochlea using the unlabelled horseradish-peroxidase-antiperoxidase technique. Ornithine decarboxylase-like immunoreactive material was detected in the neurons of the Ganglion spirale and in their axonal and/or dendritic fibers. The location of the enzyme and the possible functional role of ornithine decarboxylase plays in the development and maturation of the auditory organ and of the hearing process are discussed.

Aging↗
PubMed1988

Immunohistochemical analysis of thiol: protein disulfide oxidoreductase in hypothalamic neurons of Brattleboro rat.

The immunolocalization of thiol: protein disulfide oxidoreductase (TPO) in CNS of Wistar rats and homozygous Brattleboro rats was investigated by use of monospecific antiserum and Sternberger's unlabelled immunoenzyme technique. It was revealed that TPO is present in hypothalamic neurons belonging to nucleus supraopticus and paraventricularis. The number of immunopositive nerve cells was reduced in Brattleboro rats as compared to Wistar rats. It was concluded that TPO must have tasks in CNS unrelated to the management of vasopressin production and/or processing.

Animals↗
PubMed1988

Cathepsin B immunoreactivity is widely distributed in the rat brain.

The cellular localization and regional distribution of cathepsin B within rat CNS was revealed by immunohistochemistry using a monospecific antiserum. Cathepsin B protein was found to be widely but unevenly distributed throughout rat brain. Neurons were always cathepsin B immunoreactive. Glial elements were only occasionally immunostained. The distribution of the enzyme resembles largely that of cathepsin D.

Animals↗
PubMed1987

Immunolocalization of dipeptidyl aminopeptidase (DAP IV) in the developing human brain.

By means of immunohistochemical techniques we have investigated the presence of dipeptidyl aminopeptidase IV immunoreactivity in brain material derived from human fetuses, newborns and aged persons. It was revealed that the enzyme protein is abundantly present in the immature human CNS. On the contrary the adult human brain contains much less dipeptidyl aminopeptidase immunoreactivity. It is speculated that the enzyme might play an important role in neuronal proliferation and/or differentiation especially with regard to its possible action on certain neuronotrophic peptides (IGF II, growth hormone).

Aged↗
PubMed1987

Immunohistochemical localization of L-ornithine decarboxylase in developing rat brain.

L-Ornithine decarboxylase, the rate limiting enzyme of polyamine biosynthesis and a marker enzyme of tissue proliferation and maturation, was localized immunocytochemically in the developing rat central nervous system. It can be noted that the distribution of the enzyme protein underlies temporal alterations. Conclusions are drawn from the localization of the enzyme and possible functional roles played by ornithine decarboxylase in discrete brain areas.

Animals↗
PubMed1987

Immunohistochemical detection of cathepsin D in human neuroontogenesis.

An antiserum against rat liver cathepsin D, which was previously found to cross-react with human brain cathepsin(s) D, was used to immunolocalize the enzyme in developing CNS man. Cathepsin D protein was found in neurons as well as in glial cells. The aerliest occurrence of cathepsin D was observed in neuroblasts at the 12th gestational week. During pre-, peri-, and postnatal neuroontogenesis, there is a strong increase in the amount of immunoreactive material.

Brain↗
PubMed1987

Proteolytic degradation of insulin and glucagon in rat brain during ontogenesis.

The degradation of insulin and glucagon was investigated in rat brain, kidney, and liver during postnatal ontogenesis. It was found that a maximal activity around 13 d is unique for CNS and differs remarkably from time-course in liver and kidney. It is concluded that this result supports the hypothesis of a growth promoting role of insulin in developing rat brain.

Aging↗
PubMed1986

Immunocytochemical detection of peptides in the guinea pig cochlea.

The cochleae of juvenile guinea pigs were investigated for the presence of several neuropeptides. Glucagon, insulin, CCK and beta-endorphin immunoreactive neurons and nerve fibers as well as hair cells were demonstrated by the peroxidase antiperoxidase technique. Small amounts of substance P were also found in different sites in the inner ear. In contrast, prolactin-like material could not be found at all. These findings have significance with regard to the putative role of neuropeptides in neuromodulation.

Animals↗
PubMed1986

Proctolin immunoreactive neurons in the human brain stem.

Using the peroxidase-antiperoxidase (PAP) technique it could be established that a variety of nerve cells of human Pons and Medulla oblongata contain proctolin-like material. These neurons belong to the Nuc. olivaris caudalis, Nuc. originis n. hypoglossi, Nuc. raphes dorsalis and the Nuc. ambiguus. Furthermore, proctolin immunoreactive peptide was found to be contained in certain fiber systems (Lemniscus medialis and fiber tracts near the Raphe).

Aging↗
PubMed1986

Neuropeptides in macula utriculi and macula sacculi of guinea pig labyrinth. An immunohistochemical study.

The neuropeptides Substance P, beta-Endorphin, Prolactin, Cholecystokinin, and Glucagon were investigated by means of Sternbergers PAP technique in the neuroepithelium of the Maculae utriculi and sacculi of the labyrinth of newborn guinea pigs. This brief report will show the localization of some neuropeptides in the neuroepithelium of the Maculae utriculi and sacculi. We could not find information about similar studies on this topic in the literature. In connection with investigations of the sensory apparatus of the inner ear we have recently presented neuropeptides evidence for the presence of certain peptides in the Ggl. spirale and the hair cells of the organ of Corti. With this paper we continue to report on neuropeptides in the labyrinth of the juvenile guinea pig as revealed by immunohistochemistry (Nowak et al., in press).

Acoustic Maculae↗
PubMed1986

Immunohistochemical demonstration of ornithine decarboxylase in tissues. A preliminary study.

Using the unlabeled immunoenzyme technique, ornithine decarboxylase immunoreactivity was demonstrated in rat prostate gland and kidney. Three types of prostate epithelial cells could be revealed, displaying different strength of ODC immunoreactivity. In rat kidneys, ODC was found in proximal and distal tubules of immature tissue. Both tissues served as paradigms to optimize the immunohistochemical approach for ODC localization.

Animals↗
PubMed1986

Postnatal changes in thiol: protein-disulfide oxidoreductase immunoreactivity of rat brain.

Thiol: Protein-disulfide oxidoreductase (TPO) was localized in the brain of juvenile and adult rats by use of the unlabeled immunoperoxidase technique. In the brain of adult animals, TPO protein was revealed in neurons of Nucc. supraopticus and paraventricularis as well as in the subcommissural organ. In the developing rat, TPO seems to be a constituent of almost all neurons. The roles played by the enzyme remain to be elucidated, however.

Aging↗
PubMed1986

Cathepsins B and D in rat brain glia during experimentally induced neuropathological defects. An immunocytochemical approach.

The lysosome-associated cathepsins B and D were localized by means of immunocytochemistry (peroxidase-antiperoxidase technique) in glial cells of rat brain. A specific reaction pattern of hippocampal neuroglia could be observed after intracerebroventricular application of the neurotoxin kainic acid. After the induction of a focal epilepsy in rats by the implantation of cobalt pellets there was a pronounced immunoreaction of glia near the primary focus as well as the mirror focus. It is concluded that both cathepsins are useful immunocytochemical markers to trace functionally activated glia.

Animals↗
PubMed1986

Immunohistochemical analysis of the distribution of cathepsin D throughout human nervous system with reference to developmental aspects.

The aspartic endopeptidase cathepsin D was demonstrated in post mortem human brain by means of the peroxidase-antiperoxidase technique. The enzyme protein was found to be present in multiple neurons as well as in some glial cells. In embryonic nervous tissue cathepsin D was detected as early as at the 12th gestational week. During neuroontogenesis there was a continuous increase in cathepsin D immunoreactivity.

Aged↗