{"title":"Effect of essential fatty acids on proliferation of two neural tumor lines.","authors":"E Yavin, Z Yavin, J H Menkes","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>A combination of linoleic and linolenic acids has been shown to be able to partly replace serum in maintaining cell division of neural tumor lines. Addition of essential fatty acids to C-6 rat astrocytoma cells grown in serum-deprived medium increased the rate of cell proliferation and restored morphological appearance. Essential fatty acids also restored the rate of 3H-thymidine uptake by N-18 neuroblastoma cells grown in a serum-deprived medium. In the complete absence of serum, neuroblastoma cells were unable to proliferate despite addition of essential fatty acids. These studies indicate the importance of essential fatty acids in controlling the rate of neural tumor proliferation.</p>","PeriodicalId":19126,"journal":{"name":"Neurobiology","volume":"5 4","pages":"214-20"},"PeriodicalIF":0.0,"publicationDate":"1975-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12354598","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Sialoglycoprotein synthesis in developing rat brain.","authors":"D H van den Eijnden, W van Dijk, P A Roukema","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The postnatal developmental profiles of the protein-bound sialic acid content and the activities of CMP-N-acetylneuraminic acid (CMP-AcNeu) synthetase (EC 2.7.7.43) and glycoprotein sialyltransferase, enzymes involved in sialoglycoprotein biosynthesis, were estimated in the rat brain. The sialoglycoprotein level appeared to increase 2-fold from birth to about 20 days of age, which correlates with the outgrowth of the cell processes in this period. In contrast, the activities per g wet tissue of the enzymes were highest at birth and showed decreasing tendencies during maturation. This revealed that, at least at a certain stage during development, the sialyltransferase is present in structures other than synaptic membranes, since the new-born rat brain is devoid of these membranes. The developmental profile of the endogenous, sialic acid accepting molecules was very similar to that of the sialoglycoproteins. It was concluded that cerebral sialoglycoprotein biosynthesis during postnatal development is not limited by the activities of the synthetase and the transferase, but may largely depend on the production of the endogenous acceptors, which are presumed to be the natural precursors for the sialoglycoproteins.</p>","PeriodicalId":19126,"journal":{"name":"Neurobiology","volume":"5 4","pages":"221-7"},"PeriodicalIF":0.0,"publicationDate":"1975-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12354599","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Morphological changes of astrocyte-like cells induced by serum beta-lipoprotein in brain cell culture.","authors":"H Offner, G Konat, J Clausen","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>When added to brain cell cultures of newborn rats, serum and, in particular, its beta-lipoprotein fraction caused significant morphological transformations of astrocyte-like cells present in the culture. The changes were instantaneous as they appeared within 1 min after addition of beta-lipoprotein and they were characterized by swelling and loss of cellular processes of all astrocyte-like cells present. The lipoprotein effect was reversed after a period of about 7 h. Since the blood-brain and blood-spinal fluid barrier in multiple sclerosis is decreased towards serum macromolecules, i.e. the serum beta-lipoprotein, this protein may enter the central nervous system and thereby initiate a demyelinating process.</p>","PeriodicalId":19126,"journal":{"name":"Neurobiology","volume":"5 3","pages":"192-6"},"PeriodicalIF":0.0,"publicationDate":"1975-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11388515","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Separation of brain-RNA by micro-electrophoresis on agarose-acrylamide gels.","authors":"A Cupello, H Hydén","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>A simple method is described for RNA fractionation on the microscale (10(-8) to 10(-7) g). The optimal conditions for electrophoretic separation of low molecular weight RNA (4S-16S) on such a scale have been determined running a standard mixture of 4S, 5S and 16S E. coli RNAs on agarose-polyacrylamide gels at three different concentrations of acrylamide. The separations were evaluated for resolution of the different species and for linearity in the relationship between mobility and logarithm of molecular weight. A straight linear relationship and good resolution was obtained on a 3.48 per cent polyacrylamide - 0.7 per cent agarose gel. When a sample of 10(-2) O.D.U.260 of macroextracted cerebral RNA was separated on such a gel, six unusual RNA bands were detected between 5A and 18S. To find out optimal conditions for RNA fractionation in the 16S-28S range a standard mixture of 16S, 18S, 23S and 28S RNA was run on gels of three different acrylamide concentrations. The separations were again evaluated with regard to both the resolution and the linearity of the relationship between the logarithms of the molecular weights and the mobilities of the standard RNA species. A 0.7 per cent agarose - 2.5 per cent polyacrylamide gel appeared to be quite suitable with regard to both. The fractionation of a microsample of RNA macroextracted from whole rat brain is presented. We also present the fractionation of the RNA microextracted from 1 mg of the CA3 region of rat hippocampus.</p>","PeriodicalId":19126,"journal":{"name":"Neurobiology","volume":"5 3","pages":"129-36"},"PeriodicalIF":0.0,"publicationDate":"1975-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12282107","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
C Blomstrand, A Hamberger, A Sellström, O Steinwall
{"title":"Protein bound radioactivity in neuronal and glial fractions following intra-carotid 3H-leucine perfusion.","authors":"C Blomstrand, A Hamberger, A Sellström, O Steinwall","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Brain proteins in one cerebral hemisphere were labeled by means of intracarotid perfusion with 3H-leucine by a 40 s pulse. Recirculating precursor contributed little to the protein bound radioactivity. This radioactivity reached a peak level 30 min after perfusion. Fractions enriched in neuronal perikarya and glial cells showed a similar time course of labeling, but the neuronal fraction demonstrated the highest level of protein bound radioactivity. Subcellular fractions from whole brain were studied by the same system. The highest protein bound radioactivity was observed in the nuclear and microsomal fractions. The brain entry of the precursor by means of a controlled intracarotid pulse of short duration offers particular advantages in short-term experiments since the systemic metabolism of the labeled precursor is largely avoided. The easily achieved high labeling of proteins facilitates assay of the radio-activities in different cellular and subcellular fractions and also allows analyses of relative turnover rates in electrophoretically separated proteins.</p>","PeriodicalId":19126,"journal":{"name":"Neurobiology","volume":"5 3","pages":"178-87"},"PeriodicalIF":0.0,"publicationDate":"1975-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12354790","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Fractionation of protein carried by axoplasmic transport. II. Comparison in the rat of proteins carried to the optic relay nuclei.","authors":"L G Siegel, W O McClure","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Proteins carried in the fast (200 mm/day) axoplasmic flow of retinal ganglion cells in albino rats were labeled with intraocular injections of radioactive L-methionine. Transported proteins which accumulated in the lateral geniculate nuclei (LGN) and superior colliculi (SC) 4 1/2 hours after injection were extracted with media of increasing solubilizing power. Over 70 percent of the transported material is soluble only in media possessing detergents such as Triton X-100 and sodium dodecyl sulfate. Specific activities of the transported proteins exceeded 7000 dpm/mg. With specific activities this high, further fractionation could be carried out under conditions of high resolution. Separations of solubilized proteins on polyacrylamide gels, either with or without detergents, showed that a large number (60-100) of polypeptides are transported. Using a double labeling procedure which employed L-[35S]methionine and L-[methyl-3H]methionine, material transported to the LGN was compared with that transported to the SC. No statistically significant differences were seen in the polypeptides transported by the retinal ganglion cells to the two major optic relay nuclei.</p>","PeriodicalId":19126,"journal":{"name":"Neurobiology","volume":"5 3","pages":"167-77"},"PeriodicalIF":0.0,"publicationDate":"1975-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11274020","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"The effect of pre- and postnatal undernutrition on the development of the cerebellar cortex in the rat. II. Histochemical observations.","authors":"L Persson, A Sima","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The effect of pre- and postnatal undernutrition on the neuronal enzymatic maturation of the neocerebellar hemispheral lobules VI b, VI c and VII (according to Larsell 1952) was studied. Postnatally oxidative enzyme histochemistry (LDH, SDH, NADH, NADPH, G6PDH) revealed a delayed enzymatic development in the cerebellum between days 8 and 22, as an effect of pre- and postnatal undernutrition. In the Purkinje cell apical cone a delayed increase in enzyme activities could be seen at days 8 to 11 as well as a delayed decrease in Purkinje cell perikaryal enzyme activities at days 11 to 14 post-partum. The retarded enzymatic development seemed to parallel the retarded morphological development (cf. Sima & Persson 1975).</p>","PeriodicalId":19126,"journal":{"name":"Neurobiology","volume":"5 3","pages":"151-66"},"PeriodicalIF":0.0,"publicationDate":"1975-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11455029","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Measurement of protein in cultures of nervous tissue grown on collagen substrate.","authors":"T H Oh, S U Kim, D D Johnson","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The microchemical method of Bonting & Jones was found to detect the amount of protein present in tissue culture explants without measuring protein of collagen substrate. The protein contents of chick spinal cord explants at different points during a 1-month culture period were studied using this method.</p>","PeriodicalId":19126,"journal":{"name":"Neurobiology","volume":"5 3","pages":"188-91"},"PeriodicalIF":0.0,"publicationDate":"1975-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12354791","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Disease-inducing activity of different parts of bovine encephalitogenic protein in guinea-pigs.","authors":"J Lindh, H Bergstrand","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The encephalitogenic activity of different parts of bovine encephalitogenic protein (BEP) has been tested in guinea-pigs, mainly at a dose equimolar to 32 mug of intact protein. A high activity was found with complete protein and with region 89-169; both peptide 43-115, tyr (modified at the tyrosine residue 67) and HNB-89-169 (modified at the tryptophan residue 115) showed a moderate but clear-cut activity, whereas that of peptide 1-42 was very faint. No qualitative differences in the disease induced by the different peptides could be found; in only one animal out of 139 were clinical signs observed without evidence of histological disease. Slight histological changes, similar to those seen at EAE, were found in four out of 19 animals injected with Freund's complete adjuvant only.</p>","PeriodicalId":19126,"journal":{"name":"Neurobiology","volume":"5 3","pages":"137-50"},"PeriodicalIF":0.0,"publicationDate":"1975-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11274019","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Brain proteins in undernourished rats during learning.","authors":"H Hydén, P W Lange","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The effect of protein calorie undernourishment was studied in the hippocampus, the visual and the sensory-motor cortex of rats, subjected to a reversal learning test, with respect to protein fractions containing the acid proteins S-100 and 14-3-2. These proteins are brain specific and are confined to the nervous system of vertebrates and invertebrates. The 14-3-2 protein is localized in the fractions 4 and 5 counted from the anodal front in an acrylamide electrophoretic separation. Incorporation of 1-14-C-leucine and 3-H-leucine was determined in single and double-labeling experiments. The rats learned to discriminate between dark and light in a reversal and in a final re-reversal test. Extinction rats served as a comparison to trained rats although we stress the comparison trained, undernourished versus trained, fully fed rats. Behaviorally, the undernourished rats showed lower acquisition expressed as number of correct responses per trial block, but a somewhat higher rate of acquisition compared to the fully fed rats. In the untrained rats (undernourished versus fully fed) the following was found: a decreased amount of S100 in the visual cortex; an increased amount of S100 in the sensory-motor cortex. Significant differences existed in the biochemical response between the two groups of rats in the learning test (trained, undernourished versus trained, fully fed rats): decreased relative specific activities of the hippocampal S100, 4 and 5 proteins, and the 4 protein of the visual cortex; but increased relative specific activities of the 4 and 5 proteins of the sensory-motor cortex. Evidence is presented that these protein changes are specific. The changed response of the undernourished rats is interpreted as an adaption of the central nervous system to the stress on the organism induced by the protein calorie deficiency.</p>","PeriodicalId":19126,"journal":{"name":"Neurobiology","volume":"5 2","pages":"84-100"},"PeriodicalIF":0.0,"publicationDate":"1975-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11994012","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}