Distribution of α1-adrenoceptor subtype proteins in different tissues of neonatal and adult rats

2000 ◽  
Vol 78 (3) ◽  
pp. 237-243 ◽  
Author(s):  
Hao Shen ◽  
Krishna G Peri ◽  
Xing-Fei Deng ◽  
Sylvain Chemtob ◽  
Daya R Varma
Keyword(s):  
Vas Deferens ◽  
Polyclonal Antibodies ◽  
Receptor Subtype ◽  
Receptor Subtypes ◽  
Rat Tissues ◽  
Adult Rats ◽  
Adult Rat ◽  
Old Rats ◽  
Kidney Liver ◽  
The Brain

Distribution of α1-adrenoceptor (α1AR) subtype (α1A, α1B, α1D) proteins in brain, heart, kidney, and liver of 1-week-old rats and in brain, heart, aorta, kidney, liver, vas deferens, prostate, and adrenal glands of adult rats was investigated by Western analysis, using receptor subtype specific polyclonal antibodies. High levels of immunoreactive α1AAR and α1DAR in brain and heart and of α1BAR in liver and heart of neonatal rats were detected. In adult rat tissues, the abundance of α1AAR protein was most marked in the brain, intermediate in heart, aorta, liver, vas deferens, and adrenals, and minimal in the kidney and prostate; relative to other tissues, the expression of α1BAR was higher in brain and heart and that of α1DAR in brain. All the three receptor subtypes increased with age in the brain cortex, whereas the abundance of α1BAR increased in the heart but decreased in the liver; α1AAR and α1DAR in liver, kidney, and heart were not affected by age. It is concluded that α1AR subtypes are widely expressed in different neonatal and adult rat tissues.Key words: α1A-adrenoceptors, α1B-adrenoceptors, α1D-adrenoceptors, α1-adrenoceptor proteins.

Erythropoietin production in the rat: additive role of kidney and liver

1976 ◽  
Vol 230 (3) ◽  
pp. 845-848 ◽  
Author(s):  
C Peschle ◽  
G Marone ◽  
A Genovese ◽  
C Magli ◽  
M Condorelli
Keyword(s):  
Sham Operation ◽  
Progressive Decrease ◽  
Adult Rats ◽  
Adult Rat ◽  
Erythropoietin Production ◽  
Significant Difference ◽  
Old Rats ◽  
Subtotal Hepatectomy ◽  
First Time

Erythropoietin (Ep) levels were evaluated in serum of neonate, weanling, or adult rats subjected to 1) sham operation, nephrectomy, and/or subtotal hepatectomy and 2) a standard bout of hypoxia (0.45 atm air/6 h, starting 1 h after the operation). Ep activity was quantitated by means of strictly controlled assays in exhypoxic polycythemic mice. The sum of Ep titers in the serum of nephrectomized or hepatectomized rats was compared to Ep levels in sham-operated animals of corresponding age levels, with the exception of 1-wk-old rats: it is relevance that no significant difference is apparent between these Ep production curves. Thus, evidence is presented indicating for the first time that Ep derives from two functionally distinct and additive sources, i.e., the kidney and the liver. Liver Ep, although prevalent in neonatal animals, is obscured in the weanling adult rat by both gradual initiation of massive renal Ep production and progressive decrease of hepatic Ep activity.

scholarly journals Differential effects of D-cycloserine and amantadine on motor behavior and D2/3 receptor binding in the nigrostriatal and mesolimbic system of the adult rat

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Susanne Nikolaus ◽  
Hans-Jörg Wittsack ◽  
Frithjof Wickrath ◽  
Anja Müller-Lutz ◽  
Hubertus Hautzel ◽  
...  
Keyword(s):  
Nucleus Accumbens ◽  
Motor Behavior ◽  
Small Animal ◽  
Exploratory Activity ◽  
Reference Region ◽  
Post Challenge ◽  
Adult Rats ◽  
Adult Rat ◽  
Agonist And Antagonist ◽  
The Brain

Abstract D-cycloserine (DCS) and amantadine (AMA) act as partial NMDA receptor (R) agonist and antagonist, respectively. In the present study, we compared the effects of DCS and AMA on dopamine D2/3R binding in the brain of adult rats in relation to motor behavior. D2/3R binding was determined with small animal SPECT in baseline and after challenge with DCS (20 mg/kg) or AMA (40 mg/kg) with [123I]IBZM as radioligand. Immediately post-challenge, motor/exploratory behavior was assessed for 30 min in an open field. The regional binding potentials (ratios of the specifically bound compartments to the cerebellar reference region) were computed in baseline and post-challenge. DCS increased D2/3R binding in nucleus accumbens, substantia nigra/ventral tegmental area, thalamus, frontal, motor and parietal cortex as well as anterodorsal and posterior hippocampus, whereas AMA decreased D2/3R binding in nucleus accumbens, caudateputamen and thalamus. After DCS, ambulation and head-shoulder motility were decreased, while sitting was increased compared to vehicle and AMA. Moreover, DCS increased rearing relative to AMA. The regional elevations of D2/3R binding after DCS reflect a reduction of available dopamine throughout the mesolimbocortical system. In contrast, the reductions of D2/3R binding after AMA indicate increased dopamine in nucleus accumbens, caudateputamen and thalamus. Findings imply that, after DCS, nigrostriatal and mesolimbic dopamine levels are directly related to motor/exploratory activity, whereas an inverse relationship may be inferred for AMA.

scholarly journals Effect of phenylpyruvate on enzymes involved in fatty acid synthesis in rat brain

1973 ◽  
Vol 134 (2) ◽  
pp. 545-555 ◽  
Author(s):  
John M. Land ◽  
John B. Clark
Keyword(s):  
Fatty Acid ◽  
Citrate Synthase ◽  
Mitochondrial Protein ◽  
Fatty Acid Synthetase ◽  
Acetyl Coa Carboxylase ◽  
Acetyl Coa ◽  
Adult Rats ◽  
Malonyl Coa ◽  
Old Rats ◽  
The Brain

1. The activities of, and the effects of phenylpyruvate on, citrate synthase (EC 4.1.3.7), acetyl-CoA carboxylase (EC 6.4.1.2) and fatty acid synthetase derived from the brains of 14-day-old and adult rats were investigated. 2. The brain citrate synthase from 14-day-old rats had a Km for oxaloacetate of 2.38μm and for acetyl-CoA of 16.9μm, and a Vmax. of 838nmol of acetyl-CoA incorporation/min per mg of mitochondrial protein. From adult rat brain this enzyme had a Km for oxaloacetate of 2.5μm and for acetyl-CoA of 16.6μm and a Vmax. of 1070nmol of acetyl-CoA incorporated/min per mg of mitochondrial protein. Phenylpyruvate inhibited the enzyme from adult and young rat brains in a competitive fashion with respect to acetyl-CoA, with a Ki of 700μm. 3. The brain acetyl-CoA carboxylase from 14-day-old rats had a Km for acetyl-CoA of 21μm and a Vmax. of 0.248nmol/min per mg of protein, and from adult rats a Km for acetyl-CoA of 21μm and a Vmax. of 0.173nmol/min per mg of protein. The enzyme from young and adult rats required citrate (Ka=3mm) for activation and were inhibited non-competitively by phenylpyruvate, with a Ki of 10mm. 4. The brain fatty acid synthetase from 14-day-old rats had a Km for acetyl-CoA of 7.58μm and a Vmax. of 1.1 nmol of malonyl-CoA incorporated/min per mg of protein, and from adult rats a Km for acetyl-CoA of 4.9μm and a Vmax. of 0.48nmol of malonyl-CoA incorporated/min per mg of protein. Phenylpyruvate acted as a competitive inhibitor with respect to acetyl-CoA with a Ki of 250μm for the enzyme from 14-day-old rats. 5. These results are discussed with respect to phenylketonuria, and it is suggested that the inhibition of the brain fatty acid synthetase and possibly the citrate synthetase by phenylpyruvate could explain the defective myelination characteristic of this condition.

scholarly journals Expression of P2X and P2Y receptors in the intramural parasympathetic ganglia of the cat urinary bladder

2006 ◽  
Vol 290 (5) ◽  
pp. F1143-F1152 ◽  
Author(s):  
Huai Zhen Ruan ◽  
Lori A. Birder ◽  
Zhenghua Xiang ◽  
Bikramjit Chopra ◽  
Tony Buffington ◽  
...  
Keyword(s):  
Urinary Bladder ◽  
Polyclonal Antibodies ◽  
Imaging Techniques ◽  
Cholinergic Neurons ◽  
P2x Receptor ◽  
Receptor Subtype ◽  
Receptor Subtypes ◽  
P2y Receptor ◽  
Parasympathetic Ganglia ◽  
Intramural Ganglia

The distribution and function of P2X and P2Y receptor subtypes were investigated on intact or cultured intramural ganglia of the cat urinary bladder by immunocytochemistry and calcium-imaging techniques, respectively. Neurons were labeled by all seven P2X receptor subtype antibodies and antibodies for P2Y2, P2Y4, P2Y6, and P2Y12 receptor subtypes with a staining intensity of immunoreactivity in the following order: P2X3=P2Y2=P2Y4=P2Y6=P2Y12>P2X1=P2X2=P2X4>P2X5=P2X6=P2X7. P2Y1 receptor antibodies labeled glial cells, but not neurons. P2X3 and P2Y4 polyclonal antibodies labeled ∼95 and 40% of neurons, respectively. Double staining showed that 100, 48.8, and 97.4% of P2X3 receptor-positive neurons coexpressed choline acetyl transferase (ChAT), nitric oxide synthase (NOS), and neurofilament 200 (NF200), respectively, whereas 100, 59.2, and 97.6% of P2Y4 receptor-positive neurons coexpressed ChAT, NOS, and NF200, respectively. Application of ATP, α,β-methylene ATP, and uridine triphosphate elevated intracellular Ca2+ concentration in a subpopulation of dissociated cultured cat intramural ganglia neurons, demonstrating the presence of functional P2Y4 and P2X3 receptors. This study indicates that P2X and P2Y receptor subtypes are expressed by cholinergic parasympathetic neurons innervating the urinary bladder. The neurons were also stained for NF200, usually regarded as a marker for large sensory neurons. These novel histochemical properties of cholinergic neurons in the cat bladder suggest that the parasympathetic pathways to the cat bladder may be modulated by complex purinergic synaptic mechanisms.

scholarly journals Regional Brain Blood Flow, Blood Volume, and Haematocrit Values in the Adult Rat

1983 ◽  
Vol 3 (2) ◽  
pp. 254-256 ◽  
Author(s):  
Jill E. Cremer ◽  
Malcolm P. Seville
Keyword(s):  
Blood Flow ◽  
Blood Volume ◽  
Brain Regions ◽  
Adult Rats ◽  
Adult Rat ◽  
Systemic Artery ◽  
Significant Difference ◽  
Total Body ◽  
The Brain ◽  
Made In

Measurements of red cell volume, plasma volume, and tissue haematocrit (Hct) were made in 14 brain regions in adult rats using 51Cr-tagged red cells and 125I-labeled human serum albumin. The mean large vessel (systemic artery) Hct was 41.8, total body Hct was 35.3, and of the brain regions, the lowest value (septal nucleus) was 25.91 and the highest (visual cortex) was 32.05. The lowest blood volume was 6.29 μl g−1 (caudate putamen) and the highest was 14.44 μl g−1 (inferior colliculus). There was a significant difference between regions in both blood volume and tissue blood Hct. When brain regions were ranked in order of blood volume, this did not coincide with the order for blood flow.

scholarly journals Expression level of adenosine kinase in rat tissues. Lack of phosphate effect on the enzyme activity.

2001 ◽  
Vol 48 (3) ◽  
pp. 745-754 ◽  
Author(s):  
M Sakowicz ◽  
M Grdeń ◽  
T Pawełczyk
Keyword(s):  
Polyclonal Antibodies ◽  
Rat Kidney ◽  
Mrna Level ◽  
Kinetic Studies ◽  
Immunoblot Analysis ◽  
Adenosine Kinase ◽  
Cloning And Expression ◽  
Rat Tissues ◽  
Phosphate Ions ◽  
Kidney Liver

In this report we describe cloning and expression of rat adenosine kinase (AK) in Esccherichaia coli cells as a fusion protein with 6xHis. The recombinant protein was purified and polyclonal antibodies to AK were generated in rabbits. Immunoblot analysis of extracts obtained from various rat tissues revealed two protein bands reactive with anti-AK IgG. The apparent molecular mass of these bands was 48 and 38 kDa in rat kidney, liver, spleen, brain, and lung. In heart and muscle the proteins that react with AK antibodies have the molecular masses of 48 and 40.5 kDa. In order to assess the relative AK mRNA level in rat tissues we used the multiplex PCR technique with beta-actin mRNA as a reference. We found the highest level of AK mRNA in the liver, which decreased in the order kidney > spleen > lung > heart > brain > muscle. Measurement of AK activity in cytosolic fractions of rat tissues showed the highest activity in the liver (0.58 U/g), which decreased in the order kidney > spleen > lung > brain > heart > skeletal muscle. Kinetic studies on recombinant AK as well as on AK in the cytosolic fraction of various rat tissues showed that this enzyme is not affected by phosphate ions. The data presented indicate that in the rat tissues investigated at least two isoforms of adenosine kinase are expressed, and that the expression of the AK gene appears to have some degree of tissue specificity.

Expression of GFRα-1, receptor for GDNF, in rat brain capillary during postnatal development of the BBB

2000 ◽  
Vol 279 (2) ◽  
pp. C361-C368 ◽  
Author(s):  
Hiroyuki Utsumi ◽  
Hideki Chiba ◽  
Yasuhiro Kamimura ◽  
Makoto Osanai ◽  
Yo Igarashi ◽  
...  
Keyword(s):  
Postnatal Development ◽  
Evans Blue ◽  
Brain Cortex ◽  
Reciprocal Relation ◽  
Adult Rats ◽  
Brain Capillary ◽  
Old Rats ◽  
Porcine Endothelial Cells ◽  
The Brain ◽  
Junction Proteins

It is well known that the blood-brain barrier (BBB) matures at ∼2 wk after birth in the rat. Recently, we showed that glial cell line-derived neurotrophic factor (GDNF) enhances the barrier function of porcine endothelial cells forming the BBB in culture. In the present study, we examined the relation between permeability of the BBB, using Evans blue as a tracer, and expression of the GDNF family receptor (GFRα-1) during postnatal development of the BBB. Morphometric analysis showed that exudation of Evans blue from capillaries of the cerebral cortex progressively decreased until postnatal day 21. Inversely, immunohistochemical examinations showed expression of GFRα-1 in the capillaries at postnatal day 3 and expression that reached the same levels as observed in adult rats by postnatal day 10. However, c- ret, which is thought to mediate a signal evoked by binding of GDNF to GFRα-1, was not expressed in the capillaries of the brain cortex in 3-mo-old rats. On the other hand, the tight junction proteins occludin and ZO-1 appeared to be fully expressed at birth. The reciprocal relation between GFRα-1 expression and the permeability of the BBB strongly suggests active participation of GDNF in postnatal development of the BBB, although the mechanism(s) involved is still veiled.

Glomerular angiotensin II receptor subtypes during development of rat kidney

1993 ◽  
Vol 265 (2) ◽  
pp. F264-F271 ◽  
Author(s):  
G. M. Ciuffo ◽  
M. Viswanathan ◽  
A. M. Seltzer ◽  
K. Tsutsumi ◽  
J. M. Saavedra
Keyword(s):  
Angiotensin Ii ◽  
Kidney Development ◽  
Developmental Stages ◽  
Rat Kidney ◽  
Receptor Subtype ◽  
Receptor Subtypes ◽  
Ang Ii ◽  
Kidney Medulla ◽  
At1 Receptors ◽  
Old Rats

We used quantitative autoradiography to investigate distribution of angiotensin II (ANG II) receptor subtypes during development of the kidney in the rat. In fetal, newborn, and 3-day-old rats, immature glomeruli in the form of comma and S-shaped bodies, located in the nephrogenic zone of the renal cortex, expressed only the angiotensin AT2 receptor subtype. Conversely, the juxtamedullary glomeruli, in more advanced developmental stages, expressed only the AT1 subtype. Similarly, maturing and fully developed glomeruli, present in 1-, 2-, and 8-wk-old rats, expressed only AT1 receptors. In the kidney medulla, there was a similar change in ANG II receptor subtype expression, with the AT2 subtype expressed earlier and the AT1 subtype later during development. Our results demonstrate a selective expression of ANG II receptor subtypes during kidney development. We have found glomerular and medullary AT1 receptors only at developmental stages when kidney function has matured. Conversely, AT2 receptors are expressed only in immature structures, suggesting that they may have a role during kidney organogenesis.

Distribution and ontogeny of thyrotropin-releasing hormone degrading enzymes in rats

1990 ◽  
Vol 259 (6) ◽  
pp. E787-E791 ◽  
Author(s):  
Y. Fuse ◽  
D. H. Polk ◽  
R. W. Lam ◽  
A. L. Reviczky ◽  
D. A. Fisher
Keyword(s):  
Brain Cortex ◽  
Prolyl Endopeptidase ◽  
Rat Tissues ◽  
Peptidase Activity ◽  
Developmentally Regulated ◽  
Adult Rats ◽  
Adult Rat ◽  
Endopeptidase Activity ◽  
Low Levels ◽  
Lung And Kidney

The distribution and ontogeny of tissue prolyl endopeptidase and pyroglutamyl peptidase I activities were studied in the rat from the 7th day before birth to adulthood. While low levels of prolyl endopeptidase activity were demonstrable in many fetal tissues, activity in brain cortex, hypothalamus, lung, and kidney increased dramatically during the 2 wk after birth, gradually returning to adult levels. In adult rats, levels of tissue prolyl endopeptidase activity were highest in kidney, when compared with the intermediate levels in brain cortex, hypothalamus, and liver. Pyroglutamyl peptidase activity was widely distributed in adult rat tissues with high levels in kidney and liver that exceeded intermediate levels in brain cortex and hypothalamus. Pyroglutamyl peptidase activities in fetal gut, brain, and lung tissue were elevated above adult values. In contrast to the development changes in prolyl endopeptidase activities, pyroglutamyl peptidase activity remained elevated above adult levels only during the first week of life. These results indicate that both prolyl endopeptidase and pyroglutamyl peptidase activities in the rat are developmentally regulated.

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.

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