Changes of X-prolyl dipeptidyl-aminopeptidase activity in developing rat brain

Summary We found X-prolyl dipeptidyl-aminopeptidase activity in rat brain and examined the developmental changes at various ages. The total enzyme activity per brain increased until 4 weeks of age, and then decreased during maturation. Specific activity in young rat brain was higher than that in adult rat brain. The properties of the brain enzyme were different from those of pituitary and other tissues.     

Comparison of X-prolyl dipeptidyl-aminopeptidase activity in human cerebrospinal fluid with that in serum.

X-Prolyl dipeptidyl-aminopeptidase activities in cerebrospinal fluid and serum from the same patients without neurological diseases, undergoing surgery under lumbar anesthesia, were assayed fluorometrically with a newly synthesized fluorogenic substrate, 7-glycylproline-4-methylcoumarinamide; the values were 129.1 +/- 19.5 nmoles/min/l and 54.17 +/- 3.11 mumoles/min/l (mean +/- SEM, n = 23), respectively, and there was no correlation between both activities (r = 0.0894).     

Comparison of X-prolyl dipeptidyl-aminopeptidase activity in human cerebrospinal fluid with that in serum

Summary X-Prolyl dipeptidyl-aminopeptidase activities in cerebrospinal fluid and serum from the same patients without neurological diseases, undergoing surgery under lumbar anesthesia, were assayed fluorometrically with a newly synthesized fluorogenic substrate, 7-glycylproline-4-methylcoumarinamide; the values were 129.1±19.5 nmoles/min/1 and 54.17±3.11 moles/min/1 (mean±SEM, n=23), respectively, and there was no correlation between both activities (r=0.0894).     

Reduction of serum X-prolyl dipeptidyl-aminopeptidase activity in tumour-bearing mice and reversal of reduced enzyme activity by lentinan, an anti-tumour polysaccharide.

Serum X-prolyl dipeptidyl-aminopeptidase activity which had been shown to be depressed in cancer patients was clearly reduced in mice with Ehrlich carcinoma and Sarcoma 180, and slightly reduced in mice with methylcholanthrene-induced sarcomas. The reduced enzyme activity was completely reversed during tumour regression of sarcoma 180 by administration of lentinan, which causes regression of sarcoma 180.     

Reduction of serum X-prolyl dipeptidyl-aminopeptidase activity in tumour-bearing mice and reversal of reduced enzyme activity by lentinan,an anti-tumour polysaccharide

Summary Serum X-prolyl dipeptidyl-aminopeptidase activity which had been shown to be depressed in cancer patients was clearly reduced in mice with Ehrlich carcinoma and Sarcoma 180, and slightly reduced in mice with methylcholanthrene-induced sarcomas. The reduced enzyme activity was completely reversed during tumour regression of sarcoma 180 by administration of lentinan, which causes regression of sarcoma 180.     

Studies on substrate specificity of X-prolyl dipeptidyl-aminopeptidase during new chromogenic substrates, X-Y-p-nitroanilides

Substrate specificity of X-prolyl dipeptidyl-aminopeptidase (dipeptidyl aminopeptidase IV) was examined by using newly synthesized 8 chromogenic substrates, X-Y-p-nitroanilides. Homogeneous enzyme from human submaxillary gland hydrolyzed glycylproline p-nitroanilide almost specifically, except alanylalanine p-nitroanilide which had 11% activity.     

Studies on substrate specificity of X-prolyl dipeptidyl-aminopeptidase using new chromogenic substrates,X-Y-p-nitroanilides

Summary Substrate specificity of X-prolyl dipeptidyl-aminopeptidase (dipeptidyl aminopeptidase IV) was examined by using newly synthesized 8 chromogenic substrates, X-Y-p-nitroanilides. Homogeneous enzyme from human submaxillary gland hydrolyzed glycylproline p-nitroanilide almost specifically, except alanylalanine p-nitroanilide which had 11% activity.     

Changes in transglutaminase activity in carbon tetrachloride-damaged rat liver.

A significant decrease in transglutaminase (TGase) activity was observed in the cytosol and nuclear fractions of carbon tetrachloride-damaged rat liver. The degree of decrease in TGase activity in the cytosol fraction was closely related to the serum transaminase level. Gel filtration studies revealed that TGase activity in 80 kDa fractions significantly decreased, but that in 160 kDa fractions slightly increased after carbon tetrachloride treatment.     

Differential changes in Cu,Zn and Mn superoxide dismutase activity in developing rat brain and liver

Summary The aim of our study was to assess the pattern of copper and zinc-containing superoxide dismutase (Cu, ZnSOD) and manganese-containing superoxide dismutase (MnSOD) activity from embryonic life to senescence in rat brain and liver. The two isoenzymes showed different profiles in the two organs examined. In particular, the cerebral MnSOD activity profile suggests a primary role during differentiation of this enzymatic form.     

Changes in electrical activity of the cockroachBlatta orientalis L. brain induced by anti-lobster brain antibody

Zusammenfassung Bei mit Langustenhirn immunisierten Kaninchen werden Anti-Hirn-Antikörper gebildet. Werden diese auf die Hirnoberfläche der SchabeBlatta orientalis L. gebracht, so kommt es zu erheblichen Veränderungen in der elektrischen Hirntätigkeit des Insekts.     

Glutamate decarboxylase and γ-Aminobutyrate transaminase in developing rat brain

Résumé Le décarboxylase de glutamate (GAD) et le transaminase -aminobutyro--cétoglutarique (GABAT) ont été étudiés dans le cerveau du rat pendant le développement postnatal. Le résultat le plus frappant de cette recherche a été de montrer que le rapport de ces deux enzymes est à peu près constant au cours du développement. Ce rapport (GABAT/GAD) est de 2,5 à 3,7.     

Changes in transglutaminase activity in carbon tetrachloride-damaged rat liver

Summary A significant decrease in transglutaminase (TGase) activity was observed in the cytosol and nuclear fractions of carbon tetrachloride-damaged rat liver. The degree of decrease in TGase activity in the cytosol fraction was closely related to the serum transaminase level. Gel filtration studies revealed that TGase activity in 80 kDa fractions significantly decreased, but that in 160 kDa fractions slightly increased after carbon tetrachloride treatment.     

Organophosphate-mediated inhibition of choline acetyltransferase activity in rat brain tissue

Summary Administration of the organophosphate compound soman in rats resulted in an inhibition of choline acetyltransferase activity in almost all brain regions examined. Enzyme activity was inhibited by 20–50% in various brain regions 30 min after soman injection (94–120 g/kg). Enzyme activity in two regions decreased with time to a near zero level by 3 h after injection.Research sponsored by the Air Force Office of Scientific Research/AFSC, United States Air Force, under Contract F49620-82-C-0035. This work was also supported by PHS MBRS Grant No. RR08037. The cooperation of Dr G. Goddard of the School of Aerospace Medicine, Brooks AFB, is gratefully acknowledged.     

Organophosphate-mediated inhibition of choline acetyltransferase activity in rat brain tissue

Administration of the organophosphate compound soman in rats resulted in an inhibition of choline acetyltransferase activity in almost all brain regions examined. Enzyme activity was inhibited by 20-50% in various brain regions 30 min after soman injection (94-120 micrograms/kg). Enzyme activity in two regions decreased with time to a near zero level by 3 h after injection.     

The oxygen uptake of the developing brain in the rat with intra-uterine growth retardation

Résumé Les hémisphères cérébraux des rats normaux et des rats ayant subi un retard de croissance intra-uterin ont une consommation d'oxygène identique à tous les stades du développement. Ces résultats confirment que le cerveau est épargné par l'hypotrophie provoquée pendant la vie ftale tant au point de vue pondéral que métabolique.     

Altered brain cholinergic enzymes activity in the genetically obese rat

Summary Genetically obese male Zucker rats (fa/fa) and their lean littermates (Fa/-) were used in this experiment. Fourteen-week-old obese and lean littermates were sacrificed and choline acetyltransferase (ChAT) and acetylcholinesterase (AChE) enzymes were assayed in specific brain regions. The assays of these enzymes indicate that obese animals and a significantly lower ChAT activity in the cerebellum, pons, and cerebral cortex and a significant increase in ChAT activity in the thalamus and hypothalamus. Meanwhile, the cerebral cortex, cerebellum, midbrain, thalamus and hypothalamus of the obese animals showed significantly higher AChE activity than their lean littermates. It was concluded from this study that obesity may be associated with changes in the enzymes of the brain cholinergic system.This work was supported by a grant from the National Aeronautics and Space Administration (NAG 2-411), a grant from the National Institutes of Health (NIH RR 0811), and a grant from the Division of Research Resources, National Institutes of Health (NIH Grant RR 03020).