Disease relevance of Orm1

• These studies suggest that the synthesis of specific C/EBP alpha and C/EBP beta isoforms is induced by hyperthermia, and that the regulation of the AGP-1 and AGP-2 genes during heat stress may involve one of these isoforms [1].
• Alpha-1-acid (AAG, orosomucoid) glycoprotein: interaction with bacterial lipopolysaccharide and protection from sepsis [2].
• Desialised orosomucoid (alpha-1-acidic glycoprotein) was coupled to Pseudomonas 7A glutaminase-asparaginase by glutaraldehyde, iodinated and injected into mice [3].
• alpha 1-acid glycoprotein (alpha 1-AGP), or orosomucoid, is shown to be inducible by glucocorticoids in HTC rat hepatoma cells [4].

High impact information on Orm1

• To explore the possibility that the behavior of immune complexes can, under some circumstances, be directed by the antigen, we have studied the behavior of complexes of identical size made with the glycoproteins, orosomucoid (OR), and ceruloplasmin: or with their desialylated derivatives, asialo-orosomucoid (ASOR) and asialo-ceruloplasmin [5].
• Assay of galactosyl transferase activity using ovalbumin, desialylated degalactosylated orosomucoid, and N-acetylglucosamine as galactose acceptors showed that the Golgi fraction was enriched in specific activity over the homogenate [6].
• By using perfusions and bolus administration, coupled with postembedding immunocytochemical procedures, we have identified the structures involved in the transport of derivatized orosomucoid (alpha1-acidic glycoprotein) across the continuous microvascular endothelium of the murine myocardium [7].
• Because, by size and shape, the orosomucoid qualifies as a preferential probe for the postulated small pore system, our results are discussed in relation to the pore theory of capillary permeability [7].
• The third pattern, revealed by surveying their expression across 76 hepatic and extra-hepatic tissues, uncovered a restricted temporospatial pattern of liver overexpression for CD14, orosomucoid 1, hepcidin, Spi 2.1, Ith3, and Tim-44 [8].

Biological context of Orm1

• Polymorphism in the structure of AGP-1 among strains was used to map the structural gene, Agp-1, to chromosome 4 near the b locus [9].
• Detailed mapping and analysis of the Orm gene cluster in both normal and whirler mice indicates the presence of a <48-kb deletion in whirler mice that disrupts the Orm1 locus [10].
• DNase I footprinting assays revealed multiple protein binding domains in the mouse AGP-1 promoter region [11].
• The hemagglutination was inhibited by N-acetyl-glucosamine, N-acetylgalactosamine and glyco-proteins, such as fetuin and orosomucoid, but not by N-acetylneuraminic acid (NeuNAc) in saccharides and asialo-transferrin in glycoproteins [12].
• Kinetics of uptake and activity in mouse liver of glutaminase coupled to desialated orosomucoid [3].

Anatomical context of Orm1

• In SVEC4-10 cells, a mouse lymphoid endothelial cell line, orosomucoid, albumin, insulin and LDL were transcytosed from the apical (luminal) to basal (abluminal) side by a receptor-mediated pathway [13].

Associations of Orm1 with chemical compounds

• Molecular cloning of cDNAs corresponding to two genes of alpha 1-acid glycoprotein and characterization of two alleles of AGP-1 in the mouse [14].
• The atomic force microscope (AFM) was used to assay the extent of DNA condensation in approximately 100 different complexes of DNA with polylysine (PL) or PL covalently attached to the glycoproteins asialoorosomucoid (AsOR) or orosomucoid (OR) [15].

Other interactions of Orm1

• In the interspecific backcross, wi was found to be non-recombinant with Orm1, 0.12 cM distal of D4Mit87 and Ambp, and 0.12 cM proximal of CD301 [16].
• In the intraspecific backcross, wi was found to be non-recombinant with Orm1 and D4Mit244, 0.3 cM distal of Mup1, and 0.6 cM proximal of Tnc [16].
• No recombinants were identified in 124 animals between Lv and Orm-1 [17].
• Two alpha 1-acid glycoproteins, termed AGP-1 and AGP-2, differing in size and charge, were found in all mice and appear to derive from distinct yet closely related mRNAs [9].
• The liver is the major site of heavy metal induction of AGP and SAA genes; Hg induces AGP-1 and 2, and SAA-1 and 2 only in the liver [18].

Analytical, diagnostic and therapeutic context of Orm1

• In a genetic cross, electrophoretic polymorphisms for the two alpha 1-acid glycoproteins, AGP-1 and AGP-2, co-segregated in 58 backcross progeny, indicating that either a single gene or two tightly-linked genes on chromosome 4 encode the AGPs [19].

References