Perinatal development of the liver in rat and spiny mouse

Lamers, W. H.; Mooren, P.G.; Graaf, A. De; Charles, R.

doi:10.1111/j.1432-1033.1985.tb08675.x

Cited by 49 publications

(33 citation statements)

References 23 publications

(11 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Liver-type arginase (arginase I) is expressed almost exclusively in the liver and catalyzes the final step of urea synthesis. Arginase I activity (12) and mRNA (13) in rat liver increase markedly in the perinatal period, in coordination with other urea cycle enzymes. The enzyme is regulated by dietary protein (14) and hormones (15).…”

Section: Nitric Oxide (No)mentioning

confidence: 99%

Coinduction of Nitric-oxide Synthase and Arginase I in Cultured Rat Peritoneal Macrophages and Rat Tissues in Vivo by Lipopolysaccharide

Sawada

Nagasaki

Gotoh

et al. 1997

Journal of Biological Chemistry

200

101

View full text Add to dashboard Cite

Nitric oxide is synthesized by nitric-oxide synthase from arginine, a common substrate of arginase. Rat peritoneal macrophages were cultured in the presence of bacterial lipopolysaccharide (LPS), and expression of the inducible isoform of nitric-oxide synthase (iNOS) and liver-type arginase (arginase I) was analyzed. mRNAs for iNOS and arginase I were induced by LPS in a dose-dependent manner. iNOS mRNA appeared 2 h after LPS treatment and increased to a near maximum at 8 -12 h. On the other hand, arginase I mRNA that was undetectable prior to the treatment began to increase after 4 h with a lag time and reached a maximum at 12 h. Immunoblot analysis showed that iNOS and arginase I proteins were also induced. mRNA for arginase II, an arginase isozyme, was not detected in the LPS-activated peritoneal cells. mRNA for CCAAT/enhancer-binding protein ␤ (C/EBP␤), a transactivator of the arginase I gene, was also induced, and the induction was more rapid than that of arginase I mRNA. Changes in iNOS and arginase I mRNAs were also examined in LPS-injected rats in vivo. iNOS mRNA increased rapidly in the lung and spleen, reached a maximum 2-6 h after the LPS treatment, and decreased thereafter. Arginase I mRNA was induced markedly and more slowly in both tissues, reaching a maximum in 12 h. Thus, arginase I appears to have an important role in down-regulating nitric oxide synthesis in murine macrophages by decreasing the availability of arginine, and the induction of arginase I is mediated by C/EBP␤. Nitric oxide (NO)1 is a major molecule regulating blood vessel dilatation and immune response and functions as a neurotransmitter in the brain and peripheral nervous system (see Refs. 1-3 for reviews). NO is synthesized from arginine by nitric-oxide synthase (NOS), generating citrulline. Cellular NO production is absolutely dependent on the availability of arginine. This amino acid can be obtained from exogenous sources via the blood circulation, from intracellular protein degradation, or by the endogenous synthesis of arginine. Major sites of arginine synthesis in ureotelic animals are the liver, where arginine generated in the urea cycle (ornithine cycle) is rapidly converted to urea and ornithine by arginase, and the kidney, where arginine is synthesized from citrulline and released into the blood circulation (see Ref. 4 for a review). In other tissues and cell types, arginine can be generated from citrulline, which is produced as a coproduct of the NOS reaction, forming a cycle that is composed of NOS, argininosuccinate synthetase, and argininosuccinate lyase and that is termed the "citrulline-NO cycle" (5-10). The inducible isoform of NOS (iNOS) and argininosuccinate synthetase are coinduced in activated murine macrophage-like RAW 264.7 cells (8), in cultured vascular smooth muscle cells (9), and in vivo (10, 11). Argininosuccinate lyase is also induced in vivo (10, 11).On the other hand, arginine is utilized for both the arginase and NOS reactions. Thus, these two enzymes compete for arginine. At least two isoforms of ...

show abstract

Section: Nitric Oxide (No)mentioning

confidence: 99%

Coinduction of Nitric-oxide Synthase and Arginase I in Cultured Rat Peritoneal Macrophages and Rat Tissues in Vivo by Lipopolysaccharide

Sawada

Nagasaki

Gotoh

et al. 1997

Journal of Biological Chemistry

200

101

View full text Add to dashboard Cite

show abstract

“…As a model of viral illness appropriate to second-trimester pregnancy in women, we have used the spiny mouse (Acomys cahirinus) , an animal whose brain development is more advanced by the time of birth [26]. Indeed, the spiny mouse may be said to be precocial in that organogenesis is largely complete by the time of birth, and the neonates are capable of motor activity and thermoregulation [27,28,29,30,31]. In addition, the spiny mouse secretes cortisol as the major circulating glucocorticoid (cf.…”

Section: Introductionmentioning

confidence: 99%

Prenatal Exposure to the Viral Mimetic Poly I:C Alters Fetal Brain Cytokine Expression and Postnatal Behaviour

et al. 2014

View full text Add to dashboard Cite

An increased incidence of mental illness disorders is found in children and adolescents born to mothers who experienced an infection-based illness during pregnancy. Animal models to study the prenatal origin of such outcomes of pregnancy have largely used conventional rodents, which are immature (altricial) at birth compared with the human neonate. In this study, we used the precocial spiny mouse (Acomys cahirinus), whose offspring have completed organogenesis at birth, and administered a single subcutaneous injection of a 5 mg/kg dose of the viral mimetic poly I:C (polyriboinosinic-polyribocytidylic acid) at mid gestation (20 days; term is 39 days). Prenatal exposure to poly I:C caused a transient weight loss in the pregnant dam, produced a downregulation of the proinflammatory cytokine tumour necrosis factor-α in the fetal brain, and resulted in abnormalities in sensorimotor gating and reduced social interaction, memory and learning in juvenile offspring. No changes in exploratory activity or anxiety and fear behaviours were found between the treatment groups. This study provides evidence that, in a rodent model that more closely resembles human brain development, prenatal infection can lead to behavioural abnormalities in postnatal life.

show abstract

“…Arginase has been purified from rat (1)(2)(3), rabbit (4), and human (5) liver and consists of three subunits (6) ofMr 35,000. Arginase activity in the rat (7) and human (8,9) liver increases markedly in the perinatal period, in coordination with other urea cycle enzymes. The activities of arginase and of other urea cycle enzymes are regulated by dietary protein (1) and hormones (10,11).…”

mentioning

confidence: 99%

Molecular cloning and nucleotide sequence of cDNA for human liver arginase.

Haraguchi¹,

Takao²,

Amaya³

et al. 1987

Proc. Natl. Acad. Sci. U.S.A.

122

View full text Add to dashboard Cite

Arginase (EC 3.5.3.1) catalyzes the last step of the urea cycle in the liver of ureotelic animals. Inherited deficiency of the enzyme results in argininemia, an autosomal recessive disorder characterized by hyperammonemia. To facilitate investigation of the enzyme and gene structures and to elucidate the nature of the mutation in argininemia, we isolated cDNA clones for human liver arginase. Oligo(dT)-primed and random primer human liver cDNA libraries in Xgtll were screened using isolated rat arginase cDNA as a probe. Two of the positive clones, designated XhARG6 and XhARG109, contained an overlapping cDNA sequence with an open reading frame encoding a polypeptide of 322 amino acid residues (predicted Mr, 34,732), a 5'-untranslated sequence of 56 base pairs, a 3'-untranslated sequence of423 base pairs, and a poly(A) segment. Arginase activity was detected in Escherichia coli cells transformed with the plasmid carrying XhARG6 cDNA insert. RNA gel blot analysis of human liver RNA showed a single mRNA of 1.6 kilobases. The predicted amino acid sequence of human liver arginase is 87% and 41% identical with those of the rat liver and yeast enzymes, respectively. There are several highly conserved segments among the human, rat, and yeast enzymes.Arginase (EC 3.5.3.1) is an enzyme involved in the urea cycle in the liver of ureotelic animals catalyzing the conversion of arginine to urea and ornithine. Arginase has been purified from rat (1-3), rabbit (4), and human (5) liver and consists of three subunits (6) ofMr 35,000. Arginase activity in the rat (7) and human (8, 9) liver increases markedly in the perinatal period, in coordination with other urea cycle enzymes. The activities of arginase and of other urea cycle enzymes are regulated by dietary protein (1) and hormones (10, 11). The arginase isozymes that differ from the liver enzyme in catalytic, molecular, and immunological properties, are present in the kidney, small intestine, and lactating mammary gland (12)(13)(14). A deficiency in human liver arginase results in argininemia, an inherited autosomal recessive disorder accompanied by hyperammonemia. Molecular cloning of cDNA sequences should facilitate studies on the enzyme and gene structures and on hormonal and developmental regulation and aid in determining the nature of mutation in argininemia. We isolated cDNA clones for rat liver arginase and determined the size and abundance of arginase mRNA in rat tissues (15). We now report the isolation of human liver arginase cDNAs and the complete amino acid sequence ofthe enzyme, predicted from the nucleotide sequence. The amino acid sequence is compared with sequences of the rat and yeast enzymes. MATERIALS AND METHODS

show abstract

Perinatal development of the liver in rat and spiny mouse

Cited by 49 publications

References 23 publications

Coinduction of Nitric-oxide Synthase and Arginase I in Cultured Rat Peritoneal Macrophages and Rat Tissues in Vivo by Lipopolysaccharide

Coinduction of Nitric-oxide Synthase and Arginase I in Cultured Rat Peritoneal Macrophages and Rat Tissues in Vivo by Lipopolysaccharide

Prenatal Exposure to the Viral Mimetic Poly I:C Alters Fetal Brain Cytokine Expression and Postnatal Behaviour

Molecular cloning and nucleotide sequence of cDNA for human liver arginase.

Contact Info

Product

Resources

About