Structure and Expression of Mouse α<sub>1</sub>-Acid Glycoprotein Gene-3 (AGP-3)

Chang, Ching-Jin; Lai, Ming‐Yang; Chen, Ding‐Shinn; Lee, Sheng-Chung

doi:10.1089/dna.1992.11.315

Cited by 8 publications

(7 citation statements)

References 20 publications

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“…This difference in the level of expression is consistent with the order of the two tandem AGP genes (Proudfoot 1986). Table 2 summarizes the nucleotide substitutions and predicted amino acids in the ORM1 alleles and the AGP2 gene together with the sequences of animal AGP genes (Liao et al 1985;Reinke and Feigelson 1985;Stone and Maurer 1987;Lee et al 1989;Ray and Ray 1991;Chang et al 1992). The variations in the three common ORM1 alleles result from the differences in nucleotide sequence at the two polymorphic sites in exons 1 and 5.…”

Section: Discussionsupporting

confidence: 61%

“…The polymorphic sites of the mouse AGP-1 gene are different from those of humans, although a change from glutamine to arginine is detected (Lee et al 1989;Chang et al 1992). As compared with the nucleotides and predicted amino acids at the corresponding positions in animals, the replacements of glutamine with arginine and of valine with methionine are restricted to humans.…”

Section: Discussionmentioning

confidence: 90%

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Human orosomucoid polymorphism: molecular basis of the three common ORM1 alleles, ORM1F1, ORM1F2, and ORM1*S

et al. 1997

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The human orosomucoid (ORM) is controlled by two closely linked loci, ORM1 and ORM2, and two tandem genes, AGP1 and AGP2, encoding the proteins produced by the two loci, have been cloned. In this study the molecular basis of ORM1 polymorphism was investigated. For the detection of mutations the products of the six exons of each gene, amplified by the polymerase chain reaction (PCR), were screened by single-strand conformation polymorphism analysis. Subsequently, the exons with an altered migration pattern were gene-specifically amplified by nested PCR. Sequencing of the gene-specific PCR products showed that the three common ORM1 alleles result from A-->G transitions at the codons for amino acid positions 20 in exon 1 and 156 in exon 5 of the AGP1 gene: ORM1*F1 was characterized by CAG (Gln) and GTG (Val), ORM1*F2, by CAG (Gln) and ATG (Met), and ORM1*S, by CGG (Arg) and GTG (Val). The phylogenesis of the genes encoding these three ORM1 alleles is discussed.

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Section: Discussionsupporting

confidence: 61%

Section: Discussionmentioning

confidence: 90%

Human orosomucoid polymorphism: molecular basis of the three common ORM1 alleles, ORM1F1, ORM1F2, and ORM1*S

et al. 1997

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“…Mouse AGP exists in two main forms of 187 residues, which are the product of three distinct genes, AGP-1, AGP-2 and AGP-3 [36]. Five, six and three glycosylation sites have been identified in mouse AGP-1, AGP-2 and AGP-3, respectively [37].…”

Section: ) the Structure Of The Polypeptide Chainmentioning

confidence: 99%

The Acute Phase Protein α1-Acid Glycoprotein: A Model for Altered Glycosylation During Diseases

Ceciliani¹,

Pocacqua²

2007

CPPS

194

200

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Glycosylation is one of the most important post-translational modifications of proteins, and has been widely acknowledged as one of the most important ways to modulate both protein function and lifespan. The acute phase proteins are a major group of serum proteins whose concentration is altered during various pathophysiological conditions. The aim of this paper is to review the structure and functions of the alpha1-acid glycoprotein (AGP). AGP belongs to the subfamily of immunocalins, a group of binding proteins that also have immunomodulatory functions. One of the most interesting features of AGP is that its glycosylation microheterogeneity can be modified during diseases. This aspect is particularly remarkable, since both the immunomodulatory and the binding properties of AGP strongly depend on its carbohydrate composition. For these reasons, AGP can be considered an outstanding model for the study of glycan pattern modification during diseases. This review is focused on the most recent studies on the occurrence of different glycoforms in plasma and tissues and how the appearance of different oligosaccharide patterns during systemic inflammation or diseases can influence AGP's biological functions. The first part of the review will describe the structure of AGP and the several biological functions identified so far for this protein. The second part will be devoted to the post-translational modifications of the oligosaccharides micro-heterogeneity of AGP caused by pathological states. A critical evaluation of the impact of different AGP glycoforms on both its transport and anti-inflammatory features, and how the modifications of the glycan pattern can be utilized in clinical biochemistry, is also discussed.

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“…Three functional AGP genes (Agp-1, Agp-2, and Agp-3) have been isolated from the mouse genomic library (9,27). * Corresponding author.…”

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confidence: 99%

“…The nucleotide sequences corresponding to the 5'-flanking regions of these AGP genes have been determined (9) and shown to be highly homologous to the rat AGP sequence. We have identified a number of cis elements in the 5'-flanking region of the Agp-1 gene.…”

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confidence: 99%

Molecular cloning of a transcription factor, AGP/EBP, that belongs to members of the C/EBP family.

et al. 1990

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A C/EBP-like transcription factor, AGP/EBP, that binds to three distinct motifs in the 5'-flanking region of al-acid glycoprotein gene (AGP) has been identified. Here we report the cloning and properties of cDNA corresponding to mouse AGP/EBP. AGP/EBP and C/EBP share 87% amino acid sequence homology in the "leucine zipper" and its associated DNA-binding domains, while their sequences outside these domains and the sizes of their mRNAs are different. Unlike the limited expression of C/EBP in tissues and cells, AGP/EBP appears to be ubiquitously expressed in tissues like lung, spleen, kidney, heart, testis, and liver and cell lines like p388D1, 129P (hepatoma cell line of C3H/HeJ), FO (mouse myeloma), and L929. Antibody against cloned and expressed AGP/EBP which was raised in rabbits could recognize AGP/EBP from nuclear extract of a number of cells and tissues. On the basis of our findings about the structural relationship and the similarity of motif recognition, we propose that a family of C/EBP-like transcription factors exists. a,-Acid glycoprotein (AGP) is a liver-derived plasma glycoprotein which increases severalfold during acute-phase reaction (3-5, 37). AGP is transcriptionally regulated in rat, mouse, and human hepatocytes by interleukin-1 (IL-1) (31,34,36), hepatocyte-stimulating factor (beta interferon subtype 2 and IL-6) (6,13,16,24), and glucocorticoids (3,4,7,22,23,40). In the rat AGP gene, the hormonal stimulation by IL-1 and IL-6 is mediated by the distal regulatory element located at -5300 to -5150 (34), and the glucocorticoidresponsive element has been limited to positions -120 to -42 (7). The corresponding enhancer elements in the human and mouse AGP genes have not yet been defined. Unlike many glucocorticoid-responsive genes, such as those encoding the mouse mammary tumor virus (38, 40), human metallothionein (21), and tyrosine aminotransferase (33), the induction of AGP RNA by glucocorticoids is diminished in cells treated with protein synthesis inhibitor (e.g., cycloheximide) (3,22,23). It has been demonstrated that the rat AGP 5'-flanking region contains a DNA sequence (-121 to -107), exhibiting a high degree of homology to the glucocorticoid-responsive element consensus sequence 5'-GGTACAN3TGTTCT-3', which serves to specifically bind purified rat glucocorticoid receptor in vitro (22). A 15-bp oligonucleotide representing the rat AGP glucocorticoidresponsive element (5'-GGAACATTTTGTGCA-3') confers glucocorticoid responsiveness on a heterologous promoter; such regulation is not diminished by concurrent inhibition of protein synthesis. However, inclusion of the AGP sequences immediately downstream of the AGP glucocorticoid-responsive element (-106 to -42) renders the hormonal induction sensitive to inhibition of protein synthesis (22). DNase I footprinting with nuclear extracts prepared from HTC hepatoma cells indicates the presence of DNA-protein interactions spanning the region from -110 to -68 of the rat AGP gene (22).Three functional AGP genes (Agp-1, Agp-2, and Agp-3) have been isolated f...

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Structure and Expression of Mouse α₁-Acid Glycoprotein Gene-3 (AGP-3)

Cited by 8 publications

References 20 publications

Human orosomucoid polymorphism: molecular basis of the three common ORM1 alleles, ORM1F1, ORM1F2, and ORM1*S

Human orosomucoid polymorphism: molecular basis of the three common ORM1 alleles, ORM1F1, ORM1F2, and ORM1*S

The Acute Phase Protein α1-Acid Glycoprotein: A Model for Altered Glycosylation During Diseases

Molecular cloning of a transcription factor, AGP/EBP, that belongs to members of the C/EBP family.

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Structure and Expression of Mouse α1-Acid Glycoprotein Gene-3 (AGP-3)

Cited by 8 publications

References 20 publications

Human orosomucoid polymorphism: molecular basis of the three common ORM1 alleles, ORM1*F1, ORM1*F2, and ORM1*S

Human orosomucoid polymorphism: molecular basis of the three common ORM1 alleles, ORM1*F1, ORM1*F2, and ORM1*S

The Acute Phase Protein &#945;1-Acid Glycoprotein: A Model for Altered Glycosylation During Diseases

Molecular cloning of a transcription factor, AGP/EBP, that belongs to members of the C/EBP family.

Contact Info

Product

Resources

About

Structure and Expression of Mouse α₁-Acid Glycoprotein Gene-3 (AGP-3)

Human orosomucoid polymorphism: molecular basis of the three common ORM1 alleles, ORM1F1, ORM1F2, and ORM1*S

Human orosomucoid polymorphism: molecular basis of the three common ORM1 alleles, ORM1F1, ORM1F2, and ORM1*S

The Acute Phase Protein α1-Acid Glycoprotein: A Model for Altered Glycosylation During Diseases