scholarly journals Enzyme activity and composition of myelin and subcellular fractions in the developing rat brain

1969 ◽  
Vol 115 (5) ◽  
pp. 1051-1062 ◽  
Author(s):  
N. L. Banik ◽  
A. N. Davison
Keyword(s):  
Enzyme Activity ◽  
Plasma Membrane ◽  
Rat Brain ◽  
Membrane Fraction ◽  
Subcellular Fractions ◽  
Aminopeptidase Activity ◽  
Adult Rat ◽  
Adult Rat Brain ◽  
Developing Rat ◽  
The Brain

1. Subcellular fractions and myelin were isolated from developing and adult rat brain. 2. Measurements of chemical composition and enzyme activities indicate the presence of a second myelin-like fraction mainly in the brain of developing rats. 3. This membrane fraction has a different lipid composition from myelin, but resembles myelin in its content of phosphohydrolase and aminopeptidase activity. 4. It is suggested that the second myelin-like fraction may be a submicrosomal contaminant or it may be derived from oligodendroglial plasma membrane during myelinogenesis.

scholarly journals Effect of phenylalanine on protein synthesis in the developing rat brain

1970 ◽  
Vol 117 (2) ◽  
pp. 325-331 ◽  
Author(s):  
H. C. Agrawal ◽  
A. H. Bone ◽  
A. N. Davison
Keyword(s):  
Amino Acids ◽  
Rat Brain ◽  
Free Amino ◽  
Myelin Proteins ◽  
Free Amino Acid Pool ◽  
Adult Rat ◽  
Adult Rat Brain ◽  
Old Rats ◽  
Developing Rat ◽  
The Brain

1. Inhibition of the rate of incorporation of [35S]methionine into protein by phenylalanine was more effective in 18-day-old than in 8-day-old or adult rat brain. 2. Among the subcellular fractions incorporation of [35S]methionine into myelin proteins was most inhibited in 18-day-old rat brain. 3. Transport of [35S]methionine and [14C]leucine into the brain acid-soluble pool was significantly decreased in 18-day-old rats by phenylalanine (2mg/g body wt.). The decrease of the two amino acids in the acid-soluble pool equalled the inhibition of their rate of incorporation into the protein. 4. Under identical conditions, entry of [14C]glycine into the brain acid-soluble pool and incorporation into protein and uptake of [14C]acetate into lipid was not affected by phenylalanine. 5. It is proposed that decreased myelin synthesis seen in hyperphenylalaninaemia or phenylketonuria may be due to alteration of the free amino acid pool in the brain during the vulnerable period of brain development. Amyelination may be one of many causes of mental retardation seen in phenylketonuria.

Expression of the mRNAs for the Kv3.1 potassium channel gene in the adult and developing rat brain

1992 ◽  
Vol 68 (3) ◽  
pp. 756-766 ◽  
Author(s):  
T. M. Perney ◽  
J. Marshall ◽  
K. A. Martin ◽  
S. Hockfield ◽  
L. K. Kaczmarek
Keyword(s):  
In Situ Hybridization ◽  
Rat Brain ◽  
K Channel ◽  
Rnase Protection ◽  
Hybridization Histochemistry ◽  
Adult Rat ◽  
In Situ Hybridization Histochemistry ◽  
Adult Rat Brain ◽  
Developing Rat

1. The gene for a mammalian Shaw K+ channel has recently been cloned and has been shown, by alternative splicing, to give rise to two different transcripts, Kv3.1 alpha and Kv3.1 beta. To determine whether these channels are associated with specific types of neurons and to determine whether or not the alternately spliced K+ channel variants are differentially expressed, we used ribonuclease (RNase) protection assays and in situ hybridization histochemistry to localize the specific subsets of neurons containing Kv3.1 alpha and Kv3.1 beta mRNAs in the adult and developing rat brain. 2. In situ hybridization histochemistry revealed a heterogeneous expression pattern of Kv3.1 alpha mRNA in the adult rat brain. Highest Kv3.1 alpha mRNA levels were expressed in the cerebellum. High levels of hybridization were also detected in the globus pallidus, subthalamus, and substantia nigra reticulata. Many thalamic nuclei, but in particular the reticular thalamic nucleus, hybridized well to Kv3.1 alpha-specific probes. A subpopulation of cells in the cortex and hippocampus, which by their distribution and number may represent interneurons, were also found to contain high levels of Kv3.1 alpha mRNA. In the brain stem, many nuclei, including the inferior colliculus and the cochlear and vestibular nuclei, also express Kv3.1 alpha mRNA. Low or undetectable levels of Kv3.1 alpha mRNA were found in the caudate-putamen, olfactory tubercle, amygdala, and hypothalamus. 3. Kv3.1 beta mRNA was also detected in the adult rat brain by both RNase protection assays and by in situ hybridization experiments. Although the beta splice variant is expressed at lower levels than the alpha species, the overall expression pattern for both mRNAs is similar, indicating that both splice variants co-expressed in the same neurons. 4. The expression of Kv3.1 alpha and Kv3.1 beta transcripts was examined throughout development. Kv3.1 alpha mRNA is detected as early as embryonic day 17 and then increases gradually until approximately postnatal day 10, when there is a large increase in the amount of Kv3.1 alpha mRNA. Interestingly, the expression of Kv3.1 beta mRNA only increases gradually during the developmental time frame examined. Densitometric measurements indicated that Kv3.1 alpha is the predominant splice variant found in neurons of the adult brain, whereas Kv3.1 beta appears to be the predominant species in embryonic and perinatal neurons. 5. Most of the neurons that express the Kv3.1 transcripts have been characterized electrophysiologically to have narrow action potentials and display high-frequency firing rates with little or no spike adaptation.(ABSTRACT TRUNCATED AT 400 WORDS)

Angiotensinase activity and angiotensin receptor binding in guinea pig aorta

1977 ◽  
Vol 55 (3) ◽  
pp. 652-657 ◽  
Author(s):  
Patrick Le Morvan ◽  
Djuro Palaic ◽  
Dragana Ferguson
Keyword(s):  
Enzyme Activity ◽  
Plasma Membrane ◽  
Guinea Pig ◽  
Membrane Fraction ◽  
Binding Capacity ◽  
Specific Binding ◽  
Mitochondrial Fraction ◽  
Subcellular Fractions ◽  
Angiotensin Receptor ◽  
Plasma Membrane Fraction

The angiotensinase (EC 3.4.99.3) activity of the subcellular fractions of guinea pig aorta has been studied in relation to their [14C]angiotensin binding capacity. The enzyme activity occurs in the following decreasing order: supernatant > plasma membrane fraction > 105 000 × g pellet > mitochondrial fraction. The specific binding of [14C]angiotensin to these fractions follows the same pattern. Pretreatment of the subcellular fractions at 47 °C for 20 min was performed in an attempt to differentiate binding of angiotensin to the pharmacological receptor from binding to the destroying enzymes. This procedure decreased the angiotensinase activity in the plasma membrane fraction only whereas the specific binding of [14C]angiotensin to this fraction was not significantly decreased, suggesting that the plasma membrane angiotensinase is a thermolabile enzyme.

Mn2+-activated aspartat aminopeptidase activity, subcellular localization in young and adult rat brain

1990 ◽  
Vol 522 (1) ◽  
pp. 165-167 ◽  
Author(s):  
Manuel Rami´rez ◽  
Garbin˜e Arechaga ◽  
Sonia Garcia ◽  
Begon˜a Sanchez ◽  
Pilar Lardelli ◽  
...  
Keyword(s):  
Subcellular Localization ◽  
Rat Brain ◽  
Aminopeptidase Activity ◽  
Adult Rat ◽  
Adult Rat Brain

scholarly journals The Transfer Coefficients for L-Valine and the Rate of Incorporation of L-[1-14C] Valine into Proteins in Normal Adult Rat Brain

1988 ◽  
Vol 8 (4) ◽  
pp. 598-605 ◽  
Author(s):  
M. Kirikae ◽  
M. Diksic ◽  
Y. L. Yamamoto
Keyword(s):  
White Matter ◽  
Rat Brain ◽  
Inferior Colliculus ◽  
Gray Matter ◽  
Transfer Coefficients ◽  
Brain Proteins ◽  
Adult Rat ◽  
Adult Rat Brain ◽  
Normal Rat ◽  
The Brain

An autoradiographic method for the measurement of the rate of valine incorporation into brain proteins is described. The transfer coefficients for valine into and out of the brain and the rate of valine incorporation into normal rat brain proteins are given. The valine incorporation and the transfer constants of valine between different biological compartments are provided for 14 gray matter and 2 white matter structures of an adult rat brain. The rate of valine incorporation varies between 0.52 ± 0.19 nmol/g/min in white matter and 1.94 ± 0.47 in inferior colliculus (gray matter). Generally, the rate of valine incorporation is about three to four times higher in the gray matter than in the white matter structures.

scholarly journals The distribution of oxytocin and the oxytocin receptor in rat brain: relation to regions active in migraine

2020 ◽  
Vol 21 (1) ◽  
Author(s):  
Karin Warfvinge ◽  
Diana Krause ◽  
Lars Edvinsson
Keyword(s):  
Rat Brain ◽  
Nerve Fibers ◽  
Adult Rat ◽  
Paraventricular Nuclei ◽  
Hypothalamic Nuclei ◽  
Calcitonin Gene ◽  
Adult Rat Brain ◽  
Central Actions ◽  
The Brain

Abstract Background Recent work, both clinical and experimental, suggests that the hypothalamic hormone oxytocin (OT) and its receptor (OTR) may be involved in migraine pathophysiology. In order to better understand possible central actions of OT in migraine/headache pathogenesis, we mapped the distribution of OT and OTR in nerve cells and fibers in rat brain with a focus on areas related to migraine attacks and/or shown previously to contain calcitonin gene related peptide (CGRP), another neuropeptide involved in migraine. Methods Distribution of OT and OTR in the adult, rat brain was qualitatively examined with immunohistochemistry using a series of well characterized specific antibodies. Results As expected, OT was extensively localized in the cell somas of two hypothalamic nuclei, the supraoptic (SO or SON) and paraventricular nuclei (Pa or PVN). OT also was found in many other regions of the brain where it was localized mainly in nerve fibers. In contrast, OTR staining in the brain was mainly observed in cell somas with very little expression in fibers. The most distinct OTR expression was found in the hippocampus, the pons and the substantia nigra. In some regions of the brain (e.g. the amygdala and the hypothalamus), both OT and OTR were expressed (match). Mismatch between the peptide and its receptor was primarily observed in the cerebral and cerebellar cortex (OT expression) and hippocampus (OTR expression). Conclusions We compared OT/OTR distribution in the CNS with that of CGRP and identified regions related to migraine. In particular, regions suggested as “migraine generators”, showed correspondence among the three mappings. These findings suggest central OT pathways may contribute to the role of the hypothalamus in migraine attacks.

scholarly journals Synthesis and turnover of cerebrosides and phosphatidylserine of myelin and microsomal fractions of adult and developing rat brain

1976 ◽  
Vol 160 (2) ◽  
pp. 195-204 ◽  
Author(s):  
L W Hayes ◽  
F B Jungalwala
Keyword(s):  
Rat Brain ◽  
Half Life ◽  
Time Course ◽  
Specific Radioactivity ◽  
Intracerebral Injection ◽  
Adult Rat ◽  
Adult Rat Brain ◽  
Kinetics Of ◽  
Developing Rat

The synthesis and turnover of cerebrosides and phospholipids was followed in microsomal and myelin fractions of developing and adult rat brains after an intracerebral injection of [U-14C]serine. The kinetics of incorporation of radioactivity into microsomal and myelin cerebrosides indicate the possibility of a precursor-product relationship between cerebrosides of these membranes. The specific radioactivity of myelin cerebrosides was corrected for the deposition of newly formed cerebrosides in myelin. Multiphasic curves were obtained for the decline in specific radioactivity of myelin and microsomal cerebrosides, suggesting different cerebroside pools in these membranes. The half-life of the fast turning-over pool of cerebrosides of myelin was 7 and 22 days for the developing and adult rat brain respectively. The half-life of the slowly turning-over pool of myelin cerebrosides was about 145 days for both groups of animals. The half-life of the rapidly turning-over microsomal cerebrosides was calculated to be 20 and 40 h for the developing and adult animals respectively. The half-life of the intermediate and slowly turning-over microsomal cerebrosides was 11 and 60 days respectively, for both groups of animals. The amount of incorporation of radioactivity into microsomal cerebrosides from L-serine was greatly decreased in the adult animals, and greater amounts of the precursor were directed towards the synthesis of phosphatidylserine. In the developing animals, considerable amounts of cerebrosides were synthesized from L-serine, besides phosphatidylserine. The time-course of incorporation indicated that a precursor-product relationship exists between microsomal and myelin phosphatidylserine. The half-life of microsomal phosphatidylserine was calculated to be about 8 h for the fast turning-over pool in both groups of animals.

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