Biochimie openPub Date : 2015-01-01DOI: 10.1016/j.biopen.2015.10.002
Riad El Kebbaj , Pierre Andreoletti , Hammam I. El Hajj , Youssef El Kharrassi , Joseph Vamecq , Stéphane Mandard , Fatima-Ezzahra Saih , Norbert Latruffe , M'Hammed Saïd El Kebbaj , Gérard Lizard , Boubker Nasser , Mustapha Cherkaoui-Malki
{"title":"Argan oil prevents down-regulation induced by endotoxin on liver fatty acid oxidation and gluconeogenesis and on peroxisome proliferator-activated receptor gamma coactivator-1α, (PGC-1α), peroxisome proliferator-activated receptor α (PPARα) and estrogen related receptor α (ERRα)","authors":"Riad El Kebbaj , Pierre Andreoletti , Hammam I. El Hajj , Youssef El Kharrassi , Joseph Vamecq , Stéphane Mandard , Fatima-Ezzahra Saih , Norbert Latruffe , M'Hammed Saïd El Kebbaj , Gérard Lizard , Boubker Nasser , Mustapha Cherkaoui-Malki","doi":"10.1016/j.biopen.2015.10.002","DOIUrl":"10.1016/j.biopen.2015.10.002","url":null,"abstract":"<div><p>In patients with sepsis, liver metabolism and its capacity to provide other organs with energetic substrates are impaired. This and many other pathophysiological changes seen in human patients are reproduced in mice injected with purified endotoxin (lipopolysaccharide, LPS). In the present study, down-regulation of genes involved in hepatic fatty acid oxidation (FAOx) and gluconeogenesis in mice exposed to LPS was challenged by nutritional intervention with Argan oil. Mice given a standard chow supplemented or not with either 6% (w/w) Argan oil (AO) or 6% (w/w) olive oil (OO) prior to exposure to LPS were explored for liver gene expressions assessed by mRNA transcript levels and/or enzyme activities. AO (or OO) food supplementation reveals that, in LPS-treated mice, hepatic expression of genes involved in FAOx and gluconeogenesis was preserved. This preventive protection might be related to the recovery of the gene expressions of nuclear receptors peroxisome proliferator-activated receptor α (PPARα) and estrogen related receptor α (ERRα) and their coactivator peroxisome proliferator-activated receptor gamma coactivator-1α, (PGC-1α). These preventive mechanisms conveyed by AO against LPS-induced metabolic dysregulation might add new therapeutic potentialities in the management of human sepsis.</p></div>","PeriodicalId":92004,"journal":{"name":"Biochimie open","volume":"1 ","pages":"Pages 51-59"},"PeriodicalIF":0.0,"publicationDate":"2015-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.biopen.2015.10.002","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"35990545","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Biochimie openPub Date : 2015-01-01DOI: 10.1016/j.biopen.2015.05.002
Vaibhav Sharma , Nimesha Patel , Julian F. Dye , Lilian Hook , Chris Mason , Elena García-Gareta
{"title":"Albumin removal from human fibrinogen preparations for manufacturing human fibrin-based biomaterials","authors":"Vaibhav Sharma , Nimesha Patel , Julian F. Dye , Lilian Hook , Chris Mason , Elena García-Gareta","doi":"10.1016/j.biopen.2015.05.002","DOIUrl":"10.1016/j.biopen.2015.05.002","url":null,"abstract":"<div><p>Commercially available two component human fibrin sealants are commonly used to manufacture human fibrin-based biomaterials. However, this method is costly and allows little room for further tuning of the biomaterial. Human fibrinogen solutions offer a more cost-effective and versatile alternative to manufacture human fibrin-based biomaterials. Yet, human fibrinogen is highly unstable and contains certain impurities like human albumin. Within the context of biomaterials and tissue engineering we offer a simple yet novel solution based on classical biochemical techniques to significantly reduce albumin in human fibrinogen solutions. This method can be used for various tissue engineering and biomedical applications as an initial step in the manufacturing of human fibrin-based biomaterials to optimise their regenerative application.</p></div>","PeriodicalId":92004,"journal":{"name":"Biochimie open","volume":"1 ","pages":"Pages 6-10"},"PeriodicalIF":0.0,"publicationDate":"2015-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.biopen.2015.05.002","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"35990540","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Proline substitutions in a Mip-like peptidyl-prolyl cis-trans isomerase severely affect its structure, stability, shape and activity","authors":"Soumitra Polley , Devlina Chakravarty , Gopal Chakrabarti , Rajagopal Chattopadhyaya , Subrata Sau","doi":"10.1016/j.biopen.2015.07.001","DOIUrl":"10.1016/j.biopen.2015.07.001","url":null,"abstract":"<div><p>FKBP22, an <em>Escherichia coli</em>-specific peptidyl-prolyl <em>cis</em>-<em>trans</em> isomerase, shows substantial homology with the Mip-like virulence factors. Mip-like proteins are homodimeric and possess a V-shaped conformation. Their N-terminal domains form dimers, whereas their C-terminal domains bind protein/peptide substrates and distinct inhibitors such as rapamycin and FK506. Interestingly, the two domains of the Mip-like proteins are separated by a lengthy, protease-susceptible α-helix. To delineate the structural requirement of this domain-connecting region in Mip-like proteins, we have investigated a recombinant FKBP22 (rFKBP22) and its three point mutants I65P, V72P and A82P using different probes. Each mutant harbors a Pro substitution mutation at a distinct location in the hinge region. We report that the three mutants are not only different from each other but also different from rFKBP22 in structure and activity. Unlike rFKBP22, the three mutants were unfolded by a non-two state mechanism in the presence of urea. In addition, the stabilities of the mutants, particularly I65P and V72P, differed considerably from that of rFKBP22. Conversely, the rapamycin binding affinity of no mutant was different from that of rFKBP22. Of the mutants, I65P showed the highest levels of structural/functional loss and dissociated partly in solution. Our computational study indicated a severe collapse of the V-shape in I65P due to the anomalous movement of its C-terminal domains. The α-helical nature of the domain-connecting region is, therefore, critical for the Mip-like proteins.</p></div>","PeriodicalId":92004,"journal":{"name":"Biochimie open","volume":"1 ","pages":"Pages 28-39"},"PeriodicalIF":0.0,"publicationDate":"2015-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.biopen.2015.07.001","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"35990542","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Biochimie openPub Date : 2015-01-01DOI: 10.1016/j.biopen.2015.06.001
Mototeru Yamane
{"title":"Palmitoyl-ceramide accumulation with necrotic cell death in A549 cells, followed by a steep increase in sphinganine content","authors":"Mototeru Yamane","doi":"10.1016/j.biopen.2015.06.001","DOIUrl":"10.1016/j.biopen.2015.06.001","url":null,"abstract":"<div><p>Ceramides (Cers) have recently been identified as key signaling molecules that mediate biological functions such as cell growth, differentiation, senescence, apoptosis, and autophagy. However, the functions of Cer accumulation in necrotic cell death remain unknown. The aim of this study was to clarify the relationship between Cer accumulation with inhibition of the conversion pathway of Cer and concomitant necrotic cell death. In order to minimize the effect of apoptosis against necrotic cell death, A549 cells having the inhibiting effect of caspase 9 by survivin were used in this study. Consequently, Cer accumulation in A549 cells would likely be associated with a pathway other than the mitochondrial caspase-dependent pathway of apoptosis. Here, we showed that the dual addition of a glucosyl-Cer synthase inhibitor and a ceramidase inhibitor to A549 cell culture induced palmitoyl-Cer accumulation with Cer synthase 5 expression and necrotic cell death with lysosomal rupture together with leakage of cathepsin B/alkalization after 2–3 h, although it is unknown in this study whether the necrotic cell death was caused by the lysosomal rupture. This Cer accumulation was followed by a steep increase in sphinganine base levels via the activation of serine palmitoyltransferase activity brought about by the increase in palmitoyl-coenzyme A concentration as a substrate after 5–6 h. The increase in palmitoyl-coenzyme A concentration was achieved by activation of the fatty acid synthetic pathway from acetyl coenzyme A.</p></div>","PeriodicalId":92004,"journal":{"name":"Biochimie open","volume":"1 ","pages":"Pages 11-27"},"PeriodicalIF":0.0,"publicationDate":"2015-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.biopen.2015.06.001","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"35990541","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Biochimie openPub Date : 2015-01-01DOI: 10.1016/j.biopen.2015.10.001
Vaibhav Sharma , Keith A. Blackwood , David Haddow , Lilian Hook , Chris Mason , Julian F. Dye , Elena García-Gareta
{"title":"Method for estimating protein binding capacity of polymeric systems","authors":"Vaibhav Sharma , Keith A. Blackwood , David Haddow , Lilian Hook , Chris Mason , Julian F. Dye , Elena García-Gareta","doi":"10.1016/j.biopen.2015.10.001","DOIUrl":"10.1016/j.biopen.2015.10.001","url":null,"abstract":"<div><p>Composite biomaterials made from synthetic and protein-based polymers are extensively researched in tissue engineering. To successfully fabricate a protein-polymer composite, it is critical to understand how strongly the protein binds to the synthetic polymer, which occurs through protein adsorption. Currently, there is no cost-effective and simple method for characterizing this interfacial binding. To characterize this interfacial binding, we introduce a simple three-step method that involves: 1) synthetic polymer surface characterisation, 2) a quick, inexpensive and robust novel immuno-based assay that uses protein extraction compounds to characterize protein binding strength followed by 3) an in vitro 2D model of cell culture to confirm the results of the immuno-based assay. Fibrinogen, precursor of fibrin, was adsorbed (test protein) on three different polymeric surfaces: silicone, poly(acrylic acid)-coated silicone and poly(allylamine)-coated silicone. Polystyrene surface was used as a reference. Characterisation of the different surfaces revealed different chemistry and roughness. The novel immuno-based assay showed significantly stronger binding of fibrinogen to both poly(acrylic acid) and poly(allylamine) coated silicone. Finally, cell studies showed that the strength of the interaction between the protein and the polymer had an effect on cell growth. This novel immuno-based assay is a valuable tool in developing composite biomaterials of synthetic and protein-based polymers with the potential to be applied in other fields of research where protein adsorption onto surfaces plays an important role.</p></div>","PeriodicalId":92004,"journal":{"name":"Biochimie open","volume":"1 ","pages":"Pages 40-50"},"PeriodicalIF":0.0,"publicationDate":"2015-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.biopen.2015.10.001","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"35990543","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}