Quality of Life 1 Year After Laparoscopic Sleeve Gastrectomy Versus Laparoscopic Roux-en-Y Gastric Bypass: a Randomized Controlled Trial Focusing on Gastroesophageal Reflux Disease

Introduction: Bariatric surgery is the only treatment option that achieves sustained weight loss in obese patients and that also has positive effects on obesity-related comorbidities. Laparoscopic sleeve gastrectomy (LSG) seems to achieve equal weight loss as laparoscopic Roux-en-Y gastric bypass (LRYGB), but there is still much debate about the quality of life (QOL) after LSG, mainly concerning the association with gastroesophageal reflux. Our hypothesis is that QOL after LSG is comparable with QOL after LRYGB. Materials and Methods: Between February 2013 and February 2014, 150 patients were randomized to undergo either LSG or LRYGB in our clinic. Differences in QOL were compared between groups by using multiple QOL questionnaires at follow-up moments preoperatively and 2 and 12 months after surgery. Results: After 12 months of follow-up, 128 patients had returned the questionnaires. Most QOL questionnaires showed significant improvement in scores between the preoperative moment and after 12 months of follow-up. The Gastroesophageal Reflux Disease Questionnaire (GerdQ) score deteriorated in the LSG group after 2 months, but recovered again after 12 months. After 2 months of follow-up, the mean GerdQ score was 6.95 ± 2.14 in the LSG group versus 5.50 ± 1.49 in the LRYGB group (p < 0.001). After 1 year, the mean GerdQ score was 6.63 ± 2.26 in the LSG group and 5.60 ± 1.07 in the LRYGB group (p = 0.001). Conclusion: This randomized controlled trial shows that patients who underwent LSG have significantly higher GerdQ scores at both 2 and 12 months postoperatively than patients who underwent LRYGB, whereas overall QOL did not differ significantly

Substrate specificities of 3-oxoacyl-CoA thiolase A and sterol carrier protein 2/3-oxoacyl-CoA thiolase purified from normal rat liver peroxisomes - Sterol carrier protein 2/3-oxoacyl-CoA thiolase is involved in the metabolism of 2-methyl-branched fatty acids and bile acid intermediates

The two main thiolase activities present in isolated peroxisomes from normal rat liver were purified to near homogeneity. On sodium dodecyl sulfate-polyacrylamide gel electrophoresis, the first enzyme preparation displayed a single band of 41 kDa that was identified as 3-oxoacyl-CoA thiolase A (thiolase A) by N-terminal amino acid sequencing, The second enzyme preparation consisted of a 58- and a 46-kDa band, The 58-kDa polypeptide reacted with antibodies raised against either sterol carrier protein 2 or the thiolase domain of sterol carrier protein 2/3-oxoacyl-CoA thiolase (SCP-2/thiolase), formerly also called sterol carrier protein X, whereas the 46-kDa polypeptide reacted only with the antibodies raised against the thiolase domain, Internal peptide sequencing confirmed that the 58-kDa polypeptide is SCP-2/thiolase and that the 46-kDa polypeptide is the thiolase domain of SCP-2/thiolase. Thiolase A catalyzed the cleavage of short, medium, and long straight chain 3-oxoacyl-CoAs, medium chain 3-oxoacyl-CoAs being the best substrates, The enzyme was inactive with the 2-methyl-branched 3-oxo-2-methylpalmitoyl-CoA and with the bile acid intermediate 24-oxo-trihydroxycoprostanoyl-CoA. SCP-2/thiolase was active with medium and long straight chain 3-oxoacyl-CoAs but also with the 2-methyl-branched 3-oxoacyl-CoA and the bile acid intermediate. In peroxisomal extracts, more than 90% of the thiolase activity toward straight chain 3-oxoacyl-CoAs was associated with thiolase A. Kinetic parameters (K-m and V-max) were determined for each enzyme with the different substrates. Our results indicate the following: 1) the two (main) thiolases present in peroxisomes from normal rat liver are thiolase A and SCP-2/thiolase; 2) thiolase A is responsible for the thiolytic cleavage of straight chain 3-oxoacyl-CoAs; and 3) SCP-2/thiolase is responsible for the thiolytic cleavage of the 3-oxoacyl-CoA derivatives of 2-methyl-branched fatty acids and the side chain of cholesterol

Synthesis and 29-14C-labeling of 3 alpha,7alpha,12alpha-trihydroxy-27-carboxymethyl-5beta-cholestan-26-oic acid, a bile acid occurring in peroxisomal diseases

The synthesis and 14C-labeling of 3 alpha, 7 alpha, 12 alpha-trihydroxy-27-carboxymethyl-5 beta-cholestan-26-oic acid by two different approaches is described. One of them involves chain elongation of cholic acid via Wittig-Horner condensation of its formylated 24-aldehyde with tetraethyl phosphonoglutarate. The resulting cholestenoate, on deprotection and hydrogenation, affords the unusual C29 bile acid in good yield. An alternative procedure consists in a malonic ester synthesis starting from the formylated 24-alcohol which, after conversion into a mesylate, is reacted with sodium salt of 2-carboethoxy-gamma-butyrolactone. Alkaline hydrolysis, decarboxylation, esterification with diazomethane and selective tosylation of the newly introduced primary hydroxyl function give a C28 precursor, which is easily chain-elongated into a labeled or unlabeled C29 bile acid by reaction with cyanide and hydrolysis. Due to the easy lactonization of some of the C28 intermediates, the latter method provides a better way for introducing a C-29 label than the sequence usually employed for carboxyl labeling of bile acids and consisting in a decarboxylative halogenation of the parent acid followed by substitution of the norhalogenide with [14C]cyanide and hydrolysis. The structure of the synthesized acid or its dimethyl ester is confirmed by 13C nuclear magnetic resonance spectroscopy and mass spectrometry, and is also shown by gas liquid chromatography to be identified with an authentic sample of biosynthetic C29 dioic bile acid extracted from body fluids of Zellweger patients.status: publishe