Disease relevance of LRG1

• System members share physical associations, leucine-rich glycoprotein (LRG) structures, and a congenital deficiency state, Bernard-Soulier syndrome [1].
• Sequence variation in two ipaH genes of Shigella flexneri 5 and homology to the LRG-like family of proteins [2].
• Histology did not show venous stasis, ischemic lesions, or differences in the degree of edema between groups SRG and LRG [3].

High impact information on LRG1

• Mature GP V is a 544-amino acid transmembrane protein with a 504-amino acid extracellular domain that encompasses a set of 15 tandem LRG repeats in a "flank-LRG center-flank" array [Roth, G. J. (1991) Blood 77, 5-19] along with eight putative N-linked glycosylation sites and cleavage sites for thrombin and calpain [1].
• The amino-terminal region of the beta chain contains a leucine-rich sequence of 24 amino acids that is similar to a sequence that occurs as seven tandem repeats in the alpha chain of GPIb and nine tandem repeats in leucine-rich alpha 2-glycoprotein [4].
• The leucine-rich sequence in the beta chain of GPIb is flanked on both sides by amino acid sequences that are similar to those flanking the leucine-rich tandem repeats of the alpha chain of GPIb and leucine-rich alpha 2-glycoprotein [4].
• Cloning of the alpha chain of human platelet glycoprotein Ib: a transmembrane protein with homology to leucine-rich alpha 2-glycoprotein [5].
• The determined sequence of the alpha chain of glycoprotein Ib contains a region (residues 29-193) with seven repeats, which is indicative of gene duplication and is highly homologous to human leucine-rich alpha 2-glycoprotein [6].

Biological context of LRG1

• Overall, the amino acid sequence of LRG is not significantly homologous to the continuous sequence of any protein in the current data base [7].
• The hLRG gene was localized to chromosome 19p13.3, a region to which the genes for several neutrophil granule enzymes also map [8].
• The extracytoplasmic domain of the alpha subunit of GPIb contains several noteworthy structural features, including a region of seven tandem repeats of 24 amino acids that are homologous with those present in leucine-rich alpha 2-glycoprotein [5].
• G protein-coupled receptors form a ternary complex of ligand, receptor, and G protein heterotrimer (LRG) during signal transduction from the outside to the inside of a cell [9].
• The 702 bp partial cDNA encoded an amino acid sequence for a putative member of the leucine-rich glycoprotein (LRG) family known to be involved in cell adhesion/recognition [10].

Anatomical context of LRG1

• These results suggest that LRG is a novel marker for early neutrophilic granulocyte differentiation [8].
• LRG transcripts were also detected in human neutrophils and progenitor cells but not in peripheral blood mononuclear cells [8].
• Notably, LRG expression was up-regulated during neutrophilic differentiation of human MPD and HL-60 cells but down-regulated during monocytic differentiation of HL-60 cells [8].

Associations of LRG1 with chemical compounds

• Periodicity of leucine and tandem repetition of a 24-amino acid segment in the primary structure of leucine-rich alpha 2-glycoprotein of human serum [7].
• These are: 1) the ternary complex of ligand, receptor, and G protein (LRG); 2) the rapidly dissociating occupied receptor (ligand-receptor complex (LR]; and 3) a desensitized slowly dissociating guanine nucleotide-insensitive receptor (desensitized ligand-receptor complex ("LRX"] [11].
• Equilibrium studies showed that GTP [S] caused a loss of binding affinity of approximately two orders of magnitude, from approximately 0.04 nM (LRG) to approximately 3 nM (LR), respectively [12].

Other interactions of LRG1

• Mouse CD14 showed 13 building blocks, of which internal nine blocks have a conserved leucine motif and significant homology with human leucine-rich alpha 2-glycoprotein [13].

Analytical, diagnostic and therapeutic context of LRG1

References