Molecular cloning and sequence analysis of cDNA for human transferrin

Uzan, Georges; Frain, Monique; Park, Insoo; Besmond, Claude; Maessen, G.D.F.; Trepat, JoséSala; Zakin, Mario M.; Kahn, Axel

doi:10.1016/0006-291x(84)91648-6

Cited by 54 publications

(20 citation statements)

References 25 publications

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“…The multiple sequence alignment was generated by using the GAP program of the University of Wisconsin Genetics Computer Group package. The sequences used in the gapping program were hemiferrin, human transferrin (humtf [23,27]), and rat transferrin (rattf [13]). The transferrin sequences were obtained from the GenBank database release 60.0.…”

Section: Resultsmentioning

confidence: 99%

“…Transferrin is a major protein secreted by cultured rat Sertoli cells (20,26) and is an important component in mediating the delivery of iron to the germ cells. Transferrin mRNA has been cloned and sequenced from a number of species (3,6,7,13,23,27), and its expression has been localized to a discrete number of tissues including the liver, brain, mammary gland, and testis. While analyzing transferrin mRNA by Northern (RNA) blot analysis, we detected a novel transcript present in rat testicular tissue which cross-hybridized with authentic rat transferrin cDNA.…”

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confidence: 99%

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A transferrinlike (hemiferrin) mRNA is expressed in the germ cells of rat testis.

Stallard¹,

Collard²,

Griswold³

1991

Mol. Cell. Biol.

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In the testis, germ cells which are separated from the serum by the blood-testis barrier rely primarily on the Sertoli cell to obtain nutrients. For example, transferrin synthesized by the Sertoli cell is important in delivering iron from the serum to the developing germ cells. Because of its role in the testis, Sertoli cell transferrin protein and mRNA have been extensively studied. By using RNA blot analysis of rat testicular tissue, we detected a transcript of 2.6 kb which is attributed to transferrin. In addition, we detected a novel mRNA of 0.9 kb which had sequence similarity to the 3' end of transferrin. This 0.9-kb mRNA was present in germ cells, but not Sertoli cells, liver, or brain. The primary source of this mRNA in the testis was round spermatids. Sequence analysis of a cDNA clone showed that this mRNA encoded a protein with sequence similarity to the carboxy terminus of transferrin. Polysome analysis indicated that this transcript was translated and may therefore have importance in the iron metabolism of germ cells. The evolutionary implications between the transferrinlike mRNA germ cells and the gene duplication event which resulted in the diferric binding of transferrin are discussed.

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Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

A transferrinlike (hemiferrin) mRNA is expressed in the germ cells of rat testis.

Stallard¹,

Collard²,

Griswold³

1991

Mol. Cell. Biol.

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“…Hybridization of northern blots containing HepG2 and nontransgenic mouse liver RNA as controls for human and mouse apo A-I mRNA, respectively, revealed no cross-hybridization between human and mouse apo A-I under the hybridization and washing conditions used. An acyl CoA oxidase (ACO) cDNA probe (38) was used as a control for PPAR mediated transcriptional activation by fibrates (20), and a transferrin probe was used as a control probe for primary cultures of human hepatocytes (39). All probes were labeled by random primed labeling (rediprime kit; Amersham International, Buckinghamshire, UK).…”

Section: Methodsmentioning

confidence: 99%

Opposite regulation of human versus mouse apolipoprotein A-I by fibrates in human apolipoprotein A-I transgenic mice.

Berthou¹,

Duverger²,

Emmanuel³

et al. 1996

J. Clin. Invest.

239

158

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The regulation of liver apolipoprotein (apo) A-I gene expression by fibrates was studied in human apo A-I transgenic mice containing a human genomic DNA fragment driving apo A-I expression in liver. Treatment with fenofibrate (0.5% wt/wt) for 7 d increased plasma human apo A-I levels up to 750% and HDL-cholesterol levels up to 200% with a shift to larger particles. The increase in human apo A-I plasma levels was time and dose dependent and was already evident after 3 d at the highest dose (0.5% wt/wt) of fenofibrate. In contrast, plasma mouse apo A-I concentration was decreased after fenofibrate in nontransgenic mice. The increase in plasma human apo A-I levels after fenofibrate treatment was associated with a 97% increase in hepatic human apo A-I mRNA, whereas mouse apo A-I mRNA levels decreased to 51%. In nontransgenic mice, a similar down-regulation of hepatic apo A-I mRNA levels was observed. Nuclear run-on experiments demonstrated that the increase in human apo A-I and the decrease in mouse apo A-I gene expression after fenofibrate occurred at the transcriptional level. Since part of the effects of fibrates are mediated through the nuclear receptor PPAR (peroxisome proliferator-activated receptor), the expression of the acyl CoA oxidase (ACO) gene was measured as a control of PPAR activation. Both in transgenic and nontransgenic mice, fenofibrate induced ACO mRNA levels up to sixfold. When transgenic mice were treated with gemfibrozil (0.5% wt/wt) plasma human apo A-I and HDL-cholesterol levels increased 32 and 73%, respectively, above control levels. The weaker effect of this compound on human apo A-I and HDL-cholesterol levels correlated with a less pronounced impact on ACO mRNA levels (a threefold increase) suggesting that the level of induction of human apo A-I gene is related to the PPAR activating potency of the fibrate used. Treatment of human primary hepatocytes with fenofibric acid (500 M) provoked an 83 and 50% increase in apo A-I secretion and mRNA levels, respectively, supporting that a direct action of fibrates on liver human apo A-I production leads to the observed increase in plasma apo A-I and HDLcholesterol. ( J. Clin. Invest. 1996. 97:2408-2416.)

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“…The blank (non-recombined plasmids), usually <50 c.p.m., was subtracted. Plasmid DNA samples The clones were generous gifts from: A.Kahn for rat aldolase B and pyruvate kinase L (Simon et al, 1983) actin, transferrin (Uzan et al, 1984) and liverspecific 3F1, J.Sala-Trepat for rat serum albumin (Sargent et al, 1979).…”

Section: Methodsmentioning

confidence: 99%

Dependence of hepatocyte-specific gene expression on cell-cell interactions in primary culture.

Fraslin¹,

Kneip²,

Vaulont³

et al. 1985

The EMBO Journal

144

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In co-culture with non-parenchymal liver epithelial cells, rat hepatocytes show a marked increase in albumin and total protein synthesis when compared with cells maintained as pure populations in which an early decline in albumin secretion takes place. Analysis of the relative amounts of different mRNA sequences, determined by hybridization, indicated that the increase in protein synthesis resulted essentially from an increased level of the corresponding mRNAs. In addition, when cell-cell contacts were established between the two cell types several days after the seeding of hepatocytes, the stimulation of albumin secretion was similarly observed with a significant increase of the corresponding mRNA on days 10-14 of culture. Transcriptional assays, in which isolated nuclei were used for the study of RNA synthesis, showed that liverspecific gene transcription was significantly increased and maintained for at least 2 weeks. These results demonstrate for the first time long-term stabilization and reversibility of various specific mRNAs at high levels by adult hepatocytes in primary culture. They suggest that establishment of cellcell contacts between hepatocytes and liver epithelial cells are essential for the maintenance of a high rate of transcription of the liver-specific genes.

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Molecular cloning and sequence analysis of cDNA for human transferrin

Cited by 54 publications

References 25 publications

A transferrinlike (hemiferrin) mRNA is expressed in the germ cells of rat testis.

A transferrinlike (hemiferrin) mRNA is expressed in the germ cells of rat testis.

Opposite regulation of human versus mouse apolipoprotein A-I by fibrates in human apolipoprotein A-I transgenic mice.

Dependence of hepatocyte-specific gene expression on cell-cell interactions in primary culture.

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