Acquired Diverticulosis of the Entire Colon in a Cadaver.

Diverticulosis involving the entire colon is rare in Western society. During a routine dissection of a 74-year-old Caucasian female cadaver, who died from vascular disease complications, diverticula were observed in the ascending, transverse, and descending colon. A total of 413 diverticula were manually counted. The majority of diverticula arose from the right and transverse colon, which is atypical of the disease in Western society. Histological examination of sections from sample diverticula reveals morphology consistent with pseudodiverticula, suggestive of acquired disease. Pancolonic diverticulosis may be associated with systemic diseases such as collagen disorders, vascular complications, and increased risk of recurrent diverticulitis. This case is an example of a rare manifestation of diverticular disease that is important for clinicians to recognize when evaluating and treating patients with gastrointestinal symptoms.

Glycine N-acyltransferase-like 3 is responsible for long-chain N-acylglycine formation in N18TG2 cells.

Long-chain fatty acid amides are signaling lipids found in mammals and other organisms; however, details of the metabolic pathways for the N-acylglycines and primary fatty acid amides (PFAMs) have remained elusive. Heavy-labeled precursor and subtraction lipidomic experiments in mouse neuroblastoma N18TG2 cells, a model cell line for the study of fatty acid amide metabolism, establish the biosynthetic pathways for the N-acylglycines and the PFAMs. We provide evidence that the N-acylglycines are formed by a long-chain specific glycine-conjugating enzyme, glycine N-acyltransferase-like 3 (GLYATL3). siRNA knockdown of GLYATL3 in the N18TG2 cells resulted in a decrease in the levels of the N-acylglycines and the PFAMs. This is the first report of an enzyme responsible for long-chain N-acylglycine production in cellula. The production of the PFAMs in N18TG2 cells was reported to occur by the oxidative cleavage of the N-acylglycines, as catalyzed by peptidylglycine α-amidating monooxygenase (PAM). siRNA knockdown of PAM resulted in an accumulation of [(13)C18]N-oleoylglycine and decreased levels of [(13)C18]oleamide when the N18TG2 cells were grown in the presence of [(13)C18]oleic acid. The addition of [1-(13)C]palmitate to the N18TG2 cell growth media led to the production of a family of [1-(13)C]palmitoylated fatty acid amides, consistent with the biosynthetic pathways detailed herein.