Protein conjugates in tissue regeneration 2 (PCTR2) is a specialized pro-resolving mediator (SPM) synthesized from docosahexaenoic acid . DHA is oxidized to 16S,17S-epoxy-protectin, which is converted to PCTR1 by glutathione S-transferase and to PCTR2 via γ-glutamyl transpeptidase. PCTR2 is found in resolving mouse exudate and in both M1 and M2 macrophages differentiated from isolated human monocytes.
Maresin conjugates in tissue regeneration 2 (MCTR2) is a specialized pro-resolving mediator (SPM) synthesized from docosahexaenoic acid in macrophages at the site of inflammation. DHA is oxidized to maresin 1 , which is converted to MCTR1 by glutathione S-transferase Mu 4 or leukotriene C4 synthase then to MCTR2 by γ-glutamyltransferase. MCTR2 accelerates tissue regeneration in planaria (1 and 100 nM). Pretreatment with MCTR2 prior to E. coli administration reduces neutrophil infiltration, shortens the inflammatory resolution period, and increases phagocytosis of E. coli by macrophages. When administered at a dose of 100 ng 12h post E. coli infection in a mouse model of peritonitis, MCTR2 selectively reduced the amount of the eicosanoids PGD2 and PGF2α in the exudate.
Maresin conjugates in tissue regeneration 3 (MCTR3) is a specialized pro-resolving mediator (SPM) synthesized from docosahexaenoic acid in macrophages. DHA is oxidized to maresin 1 , which is converted to MCTR1 by glutathione S-transferase Mu 4 or leukotriene C4 synthase, then to MCTR2 by γ-glutamyltransferase, and to MCTR3 by dipeptidase. MCTR3 accelerates tissue regeneration in planaria (1 and 100 nM) approximately as potently as MCTR2 and more potently than MCTR1. Pretreatment with MCTR3 prior to E. coli administration in mice reduces neutrophil infiltration, shortens the inflammatory resolution period, and increases phagocytosis of E. coli by macrophages. When administered at a dose of 100 ng 12h post E. coli infection in a mouse model of peritonitis, MCTR3 selectively reduces the amount of the eicosanoids PGD2 , PGE2 , PGF2α , and TXB2 in the exudate.