-Olive-oil-one-of-the-oldest-vegetable-oils-consumed-without-any-refining-is-associated-with-a-reduced-risk-of-a-number-of-common-cancers-y

Minor constituents of virgin olive oil have been suggested to be among the major chemopreventive components. A brief overview is presented of recent findings concerning the bioavailability of certain important olive oil minor components including efficient antioxidant polyphenols, the triterpene hydrocarbon squalene and beta-sitosterol, considered as putative nutritional biomarkers, in relation to Comparative study on acid-soluble and pepsin-soluble collagens from skin and swim bladder of grass carp (Ctenopharyngodon idella).BACKGROUND: Collagen has a wide range of applications in food, biomedical and RESULTS: The collagens in grass carp (Ctenopharyngodon idella) skin and swim bladder were extracted using acetic acid and pepsin. Higher yield of pepsin-soluble collagen (PSC) was obtained from skin (178 g kg(-1)) than from swim bladder (114 g kg(-1)). Not surprisingly, yields of PSC from skin and swim bladder were also higher than those of acid-soluble collagen (ASC) from the same organs (89 and 51 g kg(-1)). Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) profiles showed that ASC and PSC were type I collagens, with PSC containing a higher proportion of α components than ASC.

Fourier transform infrared spectra revealed that ASC and PSC were very similar in their protein secondary structures. Scanning electron micrographs showed that the collagens had a spongy structure, with more pores being obtained in swim bladder than in skin collagens. The collagens showed high solubility in the acidic pH range. However, their solubility decreased in the presence of NaCl at CONCLUSION: Collagens were successfully extracted from the skin and swim bladder of grass carp. These fish by-products could serve as an alternative source of collagens for a wide variety of applications in the food and nutraceutical A cysteine-based molecular code informs collagen C-propeptide assembly.Massachusetts Avenue, Cambridge, MA, 02139, USA.Fundamental questions regarding collagen biosynthesis, especially with respect to the molecular origins of homotrimeric versus heterotrimeric assembly, remain unanswered.

Here, we demonstrate that the presence or absence of a single cysteine in type-I collagen's C-propeptide domain is a key factor governing the ability of a given collagen polypeptide to stably homotrimerize. ergothioneine mushrooms identify a critical role for Ca2+ in non-covalent collagen C-propeptide trimerization, thereby priming the protein for disulfide-mediated covalent immortalization. The resulting cysteine-based code for stable assembly provides a molecular model that can be used to predict, a priori, the identity of not just collagen homotrimers, but also naturally occurring 2:1 and 1:1:1 heterotrimers. Moreover, the code applies across all of the sequence-diverse fibrillar collagens. These results provide new insight into how evolution leverages disulfide networks to fine-tune protein assembly, and will inform the ongoing development of designer proteins that assemble into specific oligomeric Conflict of interest statement: The authors declare no competing interests.Umbelliferone aminoalkyl derivatives, a new class of squalene-hopene cyclase The synthesis is described of several aminoalkyl derivatives of coumarin, obtained in good yields under microwave or high-intensity ultrasound irradiation. These compounds proved uniformly active as inhibitors of squalene-hopene cyclase (SHC) from Alicyclobacillus acidocaldarius.

Their design stemmed from our recent finding that the umbelliferone nucleus acquires inhibitory properties towards SHC when functionalized with a suitable chain such as the omega-epoxyfarnesyl group. Under ergothioneine and glutathione , such as 7-(4'-allylmethylamino-but-2-ynyloxy)chromen-2-one (IC(50) 05 mM), approached the potency of anticholesteremic drug Ro 48-8071 (IC(50) 05 mM), an effective inhibitor of both squalene- and oxidosqualene-cyclases (OSC). Tests are in progress to determine their efficacy on different eukaryotic Collagen synthesis by cultured cardiac fibroblasts obtained from cardiomyopathic The aim of the present study was to clarify myocardial collagen metabolism in cardiomyopathic hamsters and the effects of the angiotensin converting enzyme inhibitor, captopril, on collagen synthesis. Cardiac fibroblasts from Bio 14 cardiomyopathic hamsters and from non-cardiomyopathic Flb hamsters were cultured and used in the 4th passage. The synthetic activity of collagenous protein from the two types of hamsters was determined by measuring 3H-proline uptake, and the collagen type was subsequently analyzed by SDS-PAGE in cultured cardiac fibroblasts. Also studied were the effects of the angiotensin converting enzyme inhibitor captopril (1 microM) on collagen synthesis by cardiac fibroblasts from cardiomyopathic hamsters. Twenty five-week-old Bio 14 hamsters had significantly higher synthetic activity of collagenous protein and rate of collagen synthesis compared with 13-week-old Bio 14 hamsters or 25-week-old Flb hamsters [Bio 14(25-week); 12 +/- 1, Bio 14(13-week); 4 +/- 0, Flb (25-week); 8 +/- 0 cpm/cell, Bio 14(25-week); 11 +/- 0, Bio 14(13-week); 3 +/- 0, F1b (25-week); 4 +/- 0%, p < 05].