Disease relevance of GPR124

• Three other multi-resistant enterobacteria were isolated during the outbreak: an Escherichia coli that had acquired the 160 kb resistance plasmid from the epidemic klebsiella, a Citrobacter isolated from one of the patients with the klebsiella but which did not produce SHV-5, and a TEM-5-producing Enterobacter [1].

High impact information on GPR124

• Here, we report that TEM5 is expressed on the surface of endothelial cells [2].
• The PDZ domains of hDlg bound the C-terminal PDZ-binding motif of TEM5 [3].
• Direct binding of the human homologue of the Drosophila disc large tumor suppressor gene to seven-pass transmembrane proteins, tumor endothelial marker 5 (TEM5), and a novel TEM5-like protein [3].
• A method using TEM-5-beta-lactamase to assay imipenem [4].
• Except for TEM-10 for which the IC50s of the two antibiotics were the same, imipenem showed significantly greater activity than latamoxef against TEM-3 and TEM-5 [5].

Chemical compound and disease context of GPR124

• Specific-pathogen-free mice, decontaminated with ampicillin and ceftazidime, were given multi-resistant K. pneumoniae CF504, CF514 or E. coli CF604, or CF614 carrying CAZ-1/TEM-5 plasmid by oral inoculation [6].

Biological context of GPR124

• Apart from broad spectrum beta-lactamases like SHV 2 or TEM 5 the presence of plasmid coded beta-lactamases in Esch. coli and H. influenzae did not affect the antibacterial activity of cefpodoxime proxetil [7].
• Two other patients had multi-resistant klebsiellas, one of them an SHV-5 producer and one a TEM-5 producer, but these could be distinguished from each other and from the outbreak strain by serological and RAPD typing and by the genetics and mechanisms of their resistances [1].

Anatomical context of GPR124

• These results suggest that hDlg localizes at the plasma membrane through TEM5 and TEM5-like and furthermore scaffolds these GPCRs in endothelial cells during tumor angiogenesis and neoangiogenesis [3].

Associations of GPR124 with chemical compounds

• The in-vitro 50% inhibitory concentrations (IC50s) of latamoxef and imipenem against a set of plasmid-mediated beta-lactamases including TEM-1, TEM-3, TEM-5 and TEM-10 were determined by an enzymatic method using nitrocefin as substrate [5].

Other interactions of GPR124

• GPR124 and GPR125 have a leucine rich repeat (LRR), an immunoglobulin (Ig) domain, and a hormone-binding domain (HBD) [8].

Analytical, diagnostic and therapeutic context of GPR124

• Plasmids carrying three types of TEM-type extended-spectrum beta-lactamase (ESBL) genes, encoding TEM-3, TEM-5, and TEM-9, respectively, were constructed by site-directed mutagenesis [9].

References