Effects of hypophysectomy and growth hormone infusion on rat hepatic carbonic anhydrases

Jeffery, Stephen; Wilson, Catherine; Mode, Agneta; Gustafsson, Jan‐Åke; Carter, N. D.

doi:10.1677/joe.0.1100123

Cited by 38 publications

(13 citation statements)

References 15 publications

(18 reference statements)

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“…cytochrome P-450 Kato, Yamazoe, Shimada et al 1986;Noshiro & Negishi, 1986), car¬ bonic anhydrase (Jeffery, Wilson, Mode et al 1986) and a2u-globulin (Chatterjee, Demyan, Gustafsson et al 1986;Murty, Rao, Chung & Roy, 1987).…”

Section: Discussionmentioning

confidence: 99%

Differential secretory rhythm of growth hormone controls the number of hepatic epidermal growth factor receptors in the rat

Kashimata¹,

Hiramatsu²,

Minami³

1989

Journal of Endocrinology

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The effect of human GH (hGH) on hepatic epidermal growth factor (EGF) receptors in the rat was investigated. Continuous administration of hGH through an osmotic minipump, mimicking the female pattern of GH secretion, to normal male rats reduced the binding of 125I-labelled EGF to hepatic membranes to the normal female levels. The same treatment of hGH applied to hypophysectomized males had no apparent effect on EGF binding. Intermittent s.c. administration of hGH twice a day (every 12 h), mimicking the male pattern of GH secretion, to hypophysectomized male and/or normal female rats, caused a significant increase in EGF binding to the levels of normal male rats. Scatchard analysis of the binding data clearly showed that the change in EGF binding was due to a change in the number of EGF receptors. The results on the affinity labelling and phosphorylation of EGF receptors were in good agreement with those showing differences in the number of EGF receptors among the experimental groups. These results indicate that the number of hepatic EGF receptors in the rat is regulated by the differential secretory rhythm of pituitary GH between the sexes.

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Section: Discussionmentioning

confidence: 99%

Differential secretory rhythm of growth hormone controls the number of hepatic epidermal growth factor receptors in the rat

Kashimata¹,

Hiramatsu²,

Minami³

1989

Journal of Endocrinology

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“…An unusual situation occurs in rat tissues where CAIII is expressed in liver as well as skeletal muscle. In the liver the CAIII protein levels exhibit a sexual dimorphism which is apparently regulated by growth hormone (Jeffery et al 1986). …”

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confidence: 99%

Human muscle carbonic anhydrase: gene structure and DNA methylation patterns in fetal and adult tissues.

Lloyd¹,

Brownson²,

Tweedie³

et al. 1987

Genes Dev.

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We report the isolation and analysis of genomic clones comprising the entire gene coding for the human muscle carbonic anhydrase, CAIII. The gene spans 10.3 kb and has a seven-exon/six-intron structure. A noncanonical TATA box, a CCAAT motif, and two CCGCCC elements are present in the sequences upstream of exon 1. Although the expression of CAIII shows strict tissue specificity, the gene exhibits a number of features normally associated with housekeeping enzymes. For example, there is 48% homology with a 25-bp consensus sequence between the TATA box and the cap site and there is a CpG-rich island spanning a 469-bp sequence near to the origin of transcription. Methylation studies suggest that some CCGG sites clustered in the CpG-rich island are undermethylated in DNA from fetal and adult muscle and in other tissues irrespective of CAIII expression. In contrast, several nonclustered CCGG sites show a methylation pattern that correlates with gene expression. However DNA from differentiated type II adult muscle fibers is undermethylated at these sites even though CAIII is not expressed.

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“…High levels of CAIII have also been found in rodent liver, where it appears that its expression level is at least partially subject to hormonal regulation (13). The linkage relationship of this isozyme with that of the other CAs is not yet known.…”

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confidence: 99%

Nucleotide sequence, tissue-specific expression, and chromosome location of human carbonic anhydrase III: the human CAIII gene is located on the same chromosome as the closely linked CAI and CAII genes.

Wade¹,

Gunning²,

Eddy³

et al. 1986

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

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The carbonic anhydrases (CA) are a class of metalloenzymes that catalyze the reversible hydration of carbon dioxide. The genes for the carbonic anhydrase isozymes are members of a multigene family that are differentially expressed in a number of cell types. We have isolated a full-length representative of a CAIII mRNA transcript from an adult human muscle cDNA library, and we present the complete nucleotide sequence of this cDNA clone. RNA blots demonstrate that CAIII messages can be detected in a variety of cell types but that high-level expression is limited to human fetal and adult skeletal muscle and to rodent slow skeletal muscle and liver. In addition, we have used a panel of human-mouse cell hybrids to localize the human CAIII gene to chromosome 8. Previous reports have established the CAI and CAII isozyme genes to be closely linked on chromosome 8, and the assignment of the CAIII gene to the same chromosome raises the possibility that these genes may all be linked at a single complex locus.

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Effects of hypophysectomy and growth hormone infusion on rat hepatic carbonic anhydrases

Cited by 38 publications

References 15 publications

Differential secretory rhythm of growth hormone controls the number of hepatic epidermal growth factor receptors in the rat

Differential secretory rhythm of growth hormone controls the number of hepatic epidermal growth factor receptors in the rat

Human muscle carbonic anhydrase: gene structure and DNA methylation patterns in fetal and adult tissues.

Nucleotide sequence, tissue-specific expression, and chromosome location of human carbonic anhydrase III: the human CAIII gene is located on the same chromosome as the closely linked CAI and CAII genes.

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