Disease relevance of LYCAT

• The ALCAT test--inappropriate in testing for food allergy in clinical practice [1].

High impact information on LYCAT

• Immunocytohistochemical analysis showed that the ALCAT1 enzyme is localized in the endoplasmic reticulum, which is supported by a significant ALCAT activity in isolated liver and heart microsomes [2].
• A novel cardiolipin-remodeling pathway revealed by a gene encoding an endoplasmic reticulum-associated acyl-CoA:lysocardiolipin acyltransferase (ALCAT1) in mouse [2].
• In contrast, no significant increases in acyltransferase activities by the recombinant ALCAT1 were detected against either glycerol-3-phosphate or a variety of other lysophospholipids as substrates, including lysophosphatidylcholine, lysophosphatidylethanolamine, and lysophosphatidylserine [2].
• The recombinant ALCAT1 enzyme recognizes both monolysocardiolipin and dilysocardiolipin as substrates with a preference for linoleoyl-CoA and oleoyl-CoA as acyl donors [2].
• The new ALCAT test, a procedure utilizing electronic hematology instrumentation and computerized data analysis, is designed for monitoring changes in cell volumes in response to antigen stimulation in vitro [3].

Anatomical context of LYCAT

• ALCAT1 represents the first identified cardiolipin-remodeling enzyme from any living organism; its identification implies a novel role for the endoplasmic reticulum in cardiolipin metabolism [2].

Analytical, diagnostic and therapeutic context of LYCAT

• Northern blot analysis indicates that the mouse ALCAT1 is widely distributed, with the highest expression in heart and liver [2].
• By contrast, a number of unproven tests have been proposed for evaluating allergic patients including cytotoxic food testing, ALCAT test, bioresonance, electrodermal testing (electroacupuncture), reflexology, applied kinesiology a.o. There is little or no scientific rationale for these methods [4].

References