Antimicrobial peptide derived from insulin‐like growth factor‐binding protein 5 activates mast cells via Mas‐related G protein‐coupled receptor X2

Allergy ◽  
2019 ◽  
Vol 75 (1) ◽  
pp. 203-207 ◽  
Author(s):  
François Niyonsaba ◽  
Pu Song ◽  
Hainan Yue ◽  
Nutda Sutthammikorn ◽  
Yoshie Umehara ◽  
...  
Keyword(s):  
Growth Factor ◽  
Mast Cells ◽  
Antimicrobial Peptide ◽  
G Protein ◽  
Binding Protein ◽  
Insulin Like Growth Factor ◽  
G Protein Coupled Receptor ◽  
Factor Binding ◽  
G Protein Coupled

scholarly journals Mas-related Gene X2 (MrgX2) Is a Novel G Protein-coupled Receptor for the Antimicrobial Peptide LL-37 in Human Mast Cells

2011 ◽  
Vol 286 (52) ◽  
pp. 44739-44749 ◽  
Author(s):  
Hariharan Subramanian ◽  
Kshitij Gupta ◽  
Qiang Guo ◽  
Ryan Price ◽  
Hydar Ali
Keyword(s):  
Mast Cells ◽  
Antimicrobial Peptide ◽  
G Protein ◽  
Related Gene ◽  
G Protein Coupled Receptor ◽  
Human Mast Cells ◽  
G Protein Coupled

scholarly journals Arthropod IGF, relaxin and gonadulin, putative orthologs of Drosophila insulin-like peptides 6, 7 and 8, likely originated from an ancient gene triplication

PeerJ ◽  
2020 ◽  
Vol 8 ◽  
pp. e9534 ◽  
Author(s):  
Jan A. Veenstra
Keyword(s):  
Growth Factors ◽  
Growth Factor ◽  
Insulin Receptor ◽  
G Protein ◽  
Insulin Like Growth Factor ◽  
G Protein Coupled Receptor ◽  
Insulin Receptor Tyrosine Kinase ◽  
Putative Orthologs ◽  
G Protein Coupled ◽  
Insulin Like Growth Factors

Background Insects have several genes coding for insulin-like peptides and they have been particularly well studied in Drosophila. Some of these hormones function as growth hormones and are produced by the fat body and the brain. These act through a typical insulin receptor tyrosine kinase. Two other Drosophila insulin-like hormones are either known or suspected to act through a G-protein coupled receptor. Although insulin-related peptides are known from other insect species, Drosophila insulin-like peptide 8, one that uses a G-protein coupled receptor, has so far only been identified from Drosophila and other flies. However, its receptor is widespread within arthropods and hence it should have orthologs. Such putative orthologs were recently identified in decapods and have been called gonadulins. Methodology In an effort to identify gonadulins in other arthropods public genome assemblies and short-read archives from insects and other arthropods were explored for the presence of genes and transcripts coding insulin-like peptides and their putative receptors. Results Gonadulins were detected in a number of arthropods. In those species for which transcriptome data from the gonads is available insect gonadulin genes are expressed in the ovaries and at least in some species also in the testes. In some insects differences in gonadulin expression in the ovary between actively reproducing and non-reproducing females differs more than 100-fold. Putative orthologs of Drosophila ilp 6 were also identified. In several non-Dipteran insects these peptides have C-terminally extensions that are alternatively spliced. The predicted peptides have been called arthropod insulin-like growth factors. In cockroaches, termites and stick insects genes coding for the arthropod insulin-like growth factors, gonadulin and relaxin, a third insulin-like peptide, are encoded by genes that are next to one another suggesting that they are the result of a local gene triplication. Such a close chromosomal association was also found for the arthropod insulin-like growth factor and gonadulin genes in spiders. Phylogenetic tree analysis of the typical insulin receptor tyrosine kinases from insects, decapods and chelicerates shows that the insulin signaling pathway evolved differently in these three groups. The G-protein coupled receptors that are related to the Drosophila ilp 8 receptor similarly show significant differences between those groups. Conclusion A local gene triplication in an early ancestor likely yielded three genes coding gonadulin, arthropod insulin-like growth factor and relaxin. Orthologs of these genes are now commonly present in arthropods and almost certainly include the Drosophila insulin-like peptides 6, 7 and 8.

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