The Ontogeny of Apolipoprotein Expression in Rat Liver. mRNA Levels in Developing Liver and Cultured Fetal Rat Hepatocytes

Hall, Graham P.; Redgrave, Trevor G.; Yeoh, George

doi:10.1111/j.1432-1033.1995.tb20268.x

Cited by 3 publications

(4 citation statements)

References 18 publications

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“…Figure 3 shows Northern blot analyses of the differentially expressed proteins identified on 2-D gels from their main sites of production, i.e., liver, intestine, and white adipose tissues in fed, P2 and P3 rats. As already reported [24], two apo A-IV transcripts were found in liver. Compared to the fed state, hepatic apo A-IV mRNA levels were significantly lower in P2 (1.7-fold) and P3 (3.7-fold) while apo E gene expression was increased in SC in P3 (1.7-fold) and in EPI both in P2 (1.7-fold) and P3 (2.3-fold).…”

Section: Profiles and Identification Of Plasma Proteins On 2-d Gels Asupporting

confidence: 83%

A proteomic approach to identify differentially expressed plasma proteins between the fed and prolonged fasted states

et al. 2008

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Prolonged fasting is characterized by consecutive phases, a short period of adaptation (phase 1), phase 2 (P2) characterized by fat oxidation, and phase 3 (P3) during which energy requirements are mostly derived from increased protein utilization. At this latter stage, food seeking behavior is induced. Very few circulating biomolecules have been identified that are involved in the response to prolonged fasting. To this end, rat plasma samples were compared by a proteomic approach, using 2-DE. The results revealed a selective variation of the levels of apolipoprotein A-IV, A-I, and E, haptoglobin, transthyretin, plasma retinol binding-protein, and vitamin D binding-protein in P2 and P3. The variations in protein levels were confirmed by ELISA. Changes in mRNA levels encoding these proteins did not systematically correlate well with protein concentrations, and tissue-specific regulation of mRNA expression was observed, underlining the complex metabolic regulation in response to food deprivation. In late fasting, the marked reduction of apolipoprotein A-IV levels could contribute to the alarm signal that triggers refeeding. The variations of the other differentially expressed proteins are more likely related to lipid metabolism and insulin signaling alterations.

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Section: Profiles and Identification Of Plasma Proteins On 2-d Gels Asupporting

confidence: 83%

A proteomic approach to identify differentially expressed plasma proteins between the fed and prolonged fasted states

et al. 2008

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“…33 Glucagon can activate adenylate cyclase and stimulate cAMP production, 34 and it can also increase ApoA1 mRNA expression in cultured rat hepatocytes. 35 Therefore, cAMP and ApoA1 could be the downstream effectors of glucagon in regulating eye growth.…”

Section: Discussionmentioning

confidence: 99%

Cyclic Adenosine Monophosphate Activates Retinal Apolipoprotein A1 Expression and Inhibits Myopic Eye Growth

Chun

Shan

Lam

et al. 2015

Invest. Ophthalmol. Vis. Sci.

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“…Similar to humans, the levels of HDL in rodents also decline with age (10,11). Ontogeny studies showed that expression of apoA-I mRNA is highest around the time of birth (10)(11)(12). Soon after birth, there is an induction of apoA-I mRNA until day 19, followed by a steady decline.…”

Section: Transcription Factors and Age-related Decline In Apolipoprotein A-i Expressionmentioning

confidence: 94%

“…Soon after birth, there is an induction of apoA-I mRNA until day 19, followed by a steady decline. The observed induction and then decline in the levels of apoA-I mRNA correlate with weaning and the abundance of endogenous hormones such as glucocorticoid, insulin, and thyroxine (10,12). Given the pivotal role of apoA-I protein in the protection against CAD, we have studied the mechanisms that regulate expression of this gene (13 -16).…”

Section: Transcription Factors and Age-related Decline In Apolipoprotein A-i Expressionmentioning

confidence: 99%

Transcription factors and age-related decline in apolipoprotein A-I expression

Nakamura¹,

Fox‐Robichaud

Kikkawa³

et al. 1999

Journal of Lipid Research

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Apolipoprotein (apo)A-I alone or as a component of high density lipoprotein particles has antiatherogenic properties. The age-dependent decline in abundance of this protein may underlie the higher risk for developing occlusive coronary artery disease (CAD) in older individuals. Similar to humans, expression of rat apoA-I also declines with age. Results in rats showed that levels of serum apoA-I protein, hepatic mRNA, and transcription of the gene were decreased to 39%, 18%, and 38%, respectively, in 180-day-old animals compared to those of newborn rats. These findings suggest that a nuclear mechanism(s) may account for the decline in apoA-I expression. Accordingly, we examined hepatic nuclear binding activity to four specific cis -acting elements of the rat apoA-I promoter. There were age-dependent changes of binding activity to two proximal sites, B and C, but not to the more distal elements, IRCE and A. Decreased B-site binding activity correlated with lower mRNA levels encoding the activator, HNF-3 ␤ . The age-dependent change in the pattern of binding to site C was due to a switch from the activator, HNF-4, to the repressor, ARP-1. In summary, the age-related decline in apoA-I expression may arise from a reduction in the activity of both cis-acting elements, B and

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The Ontogeny of Apolipoprotein Expression in Rat Liver. mRNA Levels in Developing Liver and Cultured Fetal Rat Hepatocytes

Cited by 3 publications

References 18 publications

A proteomic approach to identify differentially expressed plasma proteins between the fed and prolonged fasted states

A proteomic approach to identify differentially expressed plasma proteins between the fed and prolonged fasted states

Cyclic Adenosine Monophosphate Activates Retinal Apolipoprotein A1 Expression and Inhibits Myopic Eye Growth

Transcription factors and age-related decline in apolipoprotein A-I expression

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