Place Work on a Scale: What Do We Know About the Association Between Employment Status and Weight Loss Outcomes After Bariatric Surgery?

Despite the initial successful weight loss after bariatric surgery, a significant amount of patients experience weight loss failure and weight regain. Several factors are known to contribute to this, though the impact of employment status is unknown. The objective of this systematic review was to examine the impact of employment status on post-surgical weight loss outcomes. Eight studies were included with a follow-up ranging between 2 and 10 years. Employed patients seemed to present more weight loss (9.0-11.0% EWL, 1.3-1.6% BMI loss) compared to unemployed patients, but none of these numbers were statistically significant. Moreover, there were contrasting findings in terms of weight regain. This review may highlight the importance of working status after bariatric surgery and warrants further investigation on this topic.

Preliminary state of development of prediction models for primary care physical therapy: a systematic review.

OBJECTIVE: To summarize the methodological quality and developmental stage of prediction models for musculoskeletal complaints that are relevant for physical therapists in primary care. STUDY DESIGN AND SETTING: A systematic literature search was carried out in the databases of Medline, Embase, and Cinahl. Studies on prediction models for musculoskeletal complaints that can be used by primary care physical therapists were included. Methodological quality of the studies was assessed and relevant study characteristics were extracted. RESULTS: The search retrieved 4,702 references of which 29 studies were included in this review. The study quality of the included studies showed substantial variation. The studied populations consisted mostly of back (n=10) and neck pain (n=6) patients, and patients with knee complaints (n=4). Most studies (n=22) used "perceived recovery" as primary outcome. Most prediction models (n=18) were at the derivation level of development. CONCLUSIONS: Many prediction models are available for a wide range of patient populations. The developmental stage of most models is preliminary and the study quality is often moderate. We do not recommend physiotherapist to use these models yet. All models reviewed here are in the developmental stage and need validation and impact evaluation before using them in daily practice.

Laser mutagenesis of protoplasts of Penicillium sp. PT95 for the enhancement of carotenoid yield.

AIMS: To isolate the protoplasts from Penicillium sp. PT95 and carry out laser mutagenesis to attain high-yield mutant strain for carotenoid production. METHODS AND RESULTS: The mycelial pellets of PT95 strain were digested with the lytic enzyme for 3 h in order to attain protoplasts. The prepared protoplasts were irradiated using helium neon (He-Ne) laser. Among all regenerated colonies isolated from irradiated protoplasts, five colonies proved to be able to form sclerotia. The five colonies were named as strains L01, L02, L03, L04 and L05, respectively. Whereas, among all regenerated colonies isolated from no-irradiated protoplasts, no colonies were found to form sclerotia. Strains L01, L02, L03, L04 and L05 showed higher carotenoid yield than the original strain in Czapek's agar medium. Strain L05 gave the highest pigment yield of 381 microg per plate, which was 2.54 times higher than that of original strain. CONCLUSIONS: These results suggest that PT95 strain may be mutagenized using laser-irradiation to obtain higher-yield mutant strains for carotenoid production. SIGNIFICANCE AND IMPACT OF THE STUDY: These data prompted us to consider that several attempts should be made to improve carotenoid production in PT95 by strain selection using classical screening and mutagenesis techniques.

Sclerotial biomass and carotenoid yield of Penicillium sp. PT95 under oxidative growth conditions and in the presence of antioxidant ascorbic acid.

AIMS: To determine the effect of oxidative stress and exogenous ascorbic acid on sclerotial biomass and carotenoid yield of Penicillium sp. PT95. METHODS: In this experiment, high oxidative stress was applied by the inclusion of FeSO(4) in the growth medium and exposure to light. Low oxidative stress was applied by omitting iron from the growth medium and by incubation in the dark. Supplementation of exogenous ascorbic acid (as antioxidant) to the basal medium caused a concentration-dependent delay of sclerotial differentiation (up to 48 h), decrease of sclerotial biomass (up to 40%) and reduction of carotenoid yield (up to 91%). On the contrary, the exogenous ascorbic acid also caused a concentration-dependent decrease of lipid peroxidation in colonies of this fungus. CONCLUSIONS: Under high oxidative stress growth condition, the sclerotial biomass and carotenoid yield of PT95 strain in each plate culture reached 305 mg and 32.94 microg, which were 1.23 and 3.71 times higher, respectively, than those at low oxidative stress growth condition. These data prompted us to consider that in order to attain higher sclerotial biomass and pigment yield, the strain PT95 should be grown under high oxidative stress and in the absence of antioxidants. SIGNIFICANCE AND IMPACT OF THE STUDY: These results suggest that strain PT95 may be used for solid-state fermentation of carotenoid production under high oxidative stress growth conditions.

Assembly of disperse red 1 molecules in the channels of AlPO4-5 single crystals for second-harmonic generation.

Disperse red 1 (DR1) molecules have been successfully incorporated into the one-dimensional channels of AlPO4-5 single crystals by means of vapor-phase diffusion. Polarizing microscope and SHG results indicate that the DR1 molecules are well aligned in a preferred direction along the crystal channels. The p-polarization (parallel to the c-axis of AlPO4-5 crystal) SH intensity (Ip-ex), and s-polarization (perpendicular to the c-axis of AlPO4-5 crystal) SH intensity (Is-ex) of DR1-loaded AlPO4-5 single crystals can be well fitted as a function of input polarization angle (alpha): Ip-ex = 0.69 cos4 alpha + 0.37 sin4 alpha - 0.17, Is-ex = 0.69 cos2 alpha sin2 alpha + 0.06, respectively. This polarization angle dependence can be well explained by three different SHG processes of Ip (0 degrees), Ip (90 degrees), and Is (45 degrees), originated from different combinations of two polarized photons.

Solid-state fermentation of cornmeal with the basidiomycete Ganoderma lucidum for degrading starch and upgrading nutritional value.

AIMS: The objective of this research was to study the ability of the basidiomycete Ganoderma lucidum to degrade starch and upgrade nutritional value of cornmeal during solid-state fermentation (SSF). METHODS AND RESULTS: On the basal medium that consisted of cornmeal and salt solution, alpha-amylase activity of G. lucidum reached its maximum value of 267 U g(-1) of culture on day 20 after inoculation. Prolongation of fermentation time from 10 to 25 days increased significantly the degradation rate of starch and ergosterol yield (a kind of physiologically active substances of G. lucidum, also as an indicator of mycelial biomass) (P < 0.01). Supplementation of glucose, sucrose or maltose to the basal medium also caused a significant increase in either the degradation rate of starch or the ergosterol yield as compared with control (P < 0.01). Among five kinds of nitrogen sources supplemented, yeast extract, casamino acid and peptone were more effective than (NH4)2SO4 and NH4NO3, and yeast extract gave the highest degradation rate of starch and ergosterol yield, followed by peptone. Through orthogonal experiments, the theoretical optimum culture medium for SSF of this fungus was the following: 100 g cornmeal, ground to 30-mesh powder, moistened with 67 ml of nutrient salt solution supplemented with 3 g yeast extract and 7.5 g glucose per litre. CONCLUSIONS: Under the optimum culture condition, the degradation rate of starch reached its maximum values of 70.4%; the starch content of the fermented product decreased from 64.5 to 25.3%, while the reducing sugar content increased from 4.2 to 20.6%. SSF also produced a significant increase (P < 0.01) from 11.0 to 16.5% in protein content. SIGNIFICANCE AND IMPACT OF THE STUDY: After SSF by G. lucidum, the digesting and absorbing ratio of cornmeal was strikingly increased and some active substances originated from G. lucidum remained in the fermented product. This implied that cornmeal could be processed into many kinds of special functional foods by SSF of G. lucidum.

Effect of oxidative stress and exogenous beta-carotene on sclerotial differentiation and carotenoid yield of Penicillium sp. PT95.

AIMS: To determine the effect of oxidative stress and exogenous beta-carotene on sclerotial differentiation and carotenoid yield of Penicillium sp. PT95. METHODS AND RESULTS: In this experiment, high oxidative stress was applied by inclusion of FeCl(3) (10 micromol l(-1)) in the growth medium and by light exposure. Low oxidative stress was applied by omitting iron from the growth medium and by incubation in the dark. Supplementation of exogenous beta-carotene (as antioxidant) to the basal medium caused a concentration-dependent delay of sclerotial differentiation (up to 72 h), decrease of sclerotial biomass (up to 43%) and reduction of carotenoid yield (up to 92%). On the contrary, the exogenous beta-carotene also caused a concentration-dependent decrease of lipid peroxidation in colonies of this fungus. CONCLUSIONS: Under high oxidative stress growth condition, the sclerotial biomass and carotenoid yield of PT95 strain in each plate culture reached 141 mg and 30.03 microg, which were 1.53 and 3.51 times higher respectively, than that at low oxidative stress growth condition. SIGNIFICANCE AND IMPACT OF THE STUDY: These data prompted us to consider that in order to attain higher sclerotial biomass and pigment yield, the strain PT95 should be grown under high oxidative stress and in the absence of antioxidants.

Testis/brain RNA-binding protein attaches translationally repressed and transported mRNAs to microtubules.

We have previously identified a testicular phosphoprotein that binds to highly conserved sequences (Y and H elements) in the 3' untranslated regions (UTRs) of testicular mRNAs and suppresses in vitro translation of mRNA constructs that contain these sequences. This protein, testis/brain RNA-binding protein (TB-RBP) also is abundant in brain and binds to brain mRNAs whose 3' UTRs contain similar sequences. Here we show that TB-RBP binds specific mRNAs to microtubules (MTs) in vitro. When TB-RBP is added to MTs reassembled from either crude brain extracts or from purified tubulin, most of the TB-RBP binds to MTs. The association of TB-RBP with MTs requires the assembly of MTs and is diminished by colcemid, cytochalasin D, and high levels of salt. Transcripts from the 3' UTRs of three mRNAs that contain the conserved sequence elements (transcripts for protamine 2, tau protein, and myelin basic protein) are linked by TB-RBP to MTs, whereas transcripts that lack the conserved sequences do not bind TB-RBP. We conclude that TB-RBP serves as an attachment protein for the MT association of specific mRNAs. Considering its ability to arrest translation in vitro, we propose that TB-RBP functions in the storage and transportation of mRNAs to specific intracellular sites where they are translated.

Testis-brain RNA-binding protein, a testicular translational regulatory RNA-binding protein, is present in the brain and binds to the 3' untranslated regions of transported brain mRNAs.

Previous studies have demonstrated that a phosphoprotein in testis binds to transcript c, a sequence containing two highly conserved elements, Y and H, in the 3' untranslated region (UTR) of mouse protamine 2 mRNA (mP2) and represses its translation in vitro. When gel-retardation assays were performed with cytoplasmic extracts prepared from seven different mouse tissues, we found that brain in addition to testis contains a protein that binds to transcript c. Both the testis and brain proteins are found exclusively in the nonpolysomal fractions of their postmitochondrial extracts. The testis and brain proteins appear to be identical according to numerous criteria: the complexes they form with transcript c have identical mobility in native gels, identical optimal pH, identical lability to increased salt concentrations, identical chromatographic properties, identical molecular sizes as judged from UV crosslinking, and identical peptide mapping as revealed by V8 digestion of the UV crosslinked protein-RNA complexes. In addition to binding to the same conserved sequence in the 3'UTR of mP2, the phosphoprotein from testis and brain, hereafter called testis-brain RNA-binding protein (TB-RBP), also specifically binds to a similar sequence in the 3'UTR of brain Tau mRNA. Since TB-RBP binds to the 3'UTRs of several translationally regulated mRNAs in testis and since numerous transported brain mRNAs also contain the same conserved binding elements, we propose that TB-RBP plays a role in mRNA storage, translocation, and/or localization in brain and testis.

Identification of a putative tyrosine-O-sulphate (TyrS) receptor possibly functioning in the biosynthetic transport of tyrosine-sulphated proteins in Madin-Darby canine kidney cells.

By employing an affinity-gel fractionation technique coupled to Western-blot analysis, we have identified a 175 kDa tyrosine-O-sulphate (TyrS)-binding protein present in Madin-Darby canine kidney (MDCK) cells. The binding of this TyrS-binding protein to TyrS covalently bonded to Sepharose gel was found to be pH-dependent, being strong from pH 8.0 down to pH 6.5 and increasingly weak at pH 6.0 and below. Results obtained from Triton X-114 temperature-induced phase separation and sodium carbonate buffer (pH 11) extraction experiments indicated that the TyrS-binding protein is an integral membrane protein. This 175 kDa TyrS-binding protein was found to be present in association with a major tyrosine-sulphated protein, the apically secreted 80 kDa glycoprotein (gp 80), in cell lysate prepared from MDCK cells maintained under normal growth conditions. When the cell lysate used was prepared from MDCK cells pretreated with 20 mM sodium chlorate, a metabolic sulphation inhibitor, the complex formed between the two proteins could no longer be detected, indicating that the binding of the TyrS-binding protein is through the TyrS residue(s) of gp 80. Both cell-surface biotinylation and cell-surface trypsinization studies demonstrated the predominantly, if not exclusively, intracellular location of the TyrS-binding protein. Furthermore, radioactive pulse-chase experiments revealed that the newly synthesized radiolabelled fibronectin and gp 80 were present in complexes with the TyrS-binding protein in MDCK cells pulse-labelled with [35S]methionine or [35S]sulphate. Exogenous [35S]methionine-labelled gp 80 added to the medium, on the other hand, was not found to be present in association with the TyrS-binding protein in MDCK cells over a 2-h time course. These results strongly suggested the identity of the 175 kDa TyrS-binding protein as a putative 'TyrS receptor', possibly functioning in the biosynthetic transport of tyrosine-sulphated proteins in MDCK cells.

Isolation and characterization of a novel microsomal membrane-bound phenol sulfotransferase from bovine liver.

A novel phenol sulfotransferase (PST) was detected in bovine liver microsomal membrane fraction. The enzyme was found to be capable of catalyzing the sulfation of simple phenolic compounds, with 3'-phosphoadenosine-5'-phosphosulfate as the sulfate donor. Detergent extracted PST showed a pH optimum of 5.7 and, among the simple phenols tested, the PST exhibited highest activity toward alpha-naphthol. No activities were detected when tyrosine and its derivatives were used as substrates. Both 2,6-dichloro-4-nitrophenol and chlorpromazine were capable of inhibiting the activity of the PST toward p-nitrophenol with inhibition Coefficient50 values of 100 nM and 4 mM, respectively.

Polarized secretion of tyrosine-sulphated proteins and free tyrosine O-sulphate by filter-grown Madin-Darby canine kidney (MDCK) cells.

Filter-grown Madin-Darby canine kidney (MDCK) cells labelled for 24 h with [35S]sulphate were found to secrete macromolecules [35S]sulphated on their carbohydrate moieties predominantly into the basolateral medium, whereas the tyrosine-[35S]sulphated proteins synthesized were predominantly secreted into the apical medium. In contrast with the predominant apical secretin of tyrosine-[35S]sulphated proteins, the free tyrosine O-[35S]sulphate (Tyr[35S]) was released mostly into the basolateral medium. A time-lapse study using prelabelled MDCK cells incubated in fresh medium revealed that, during the 48 h time course monitored, the release of tyrosine-[35S]sulphated proteins into the apical medium was faster and quantitatively greater than that into the basolateral medium. During the same time there was a concomitant release, predominantly into the basolateral medium, of the free Tyr[35S] derived from the degradation of tyrosine-[35S]sulphated proteins. An endocytotic degradation experiment was performed to demonstrate the endocytosis of tyrosine-sulphated proteins and their degradation to generate free TyrS. It was found that free Tyr[35S] was generated and released when an apically secreted (or basolaterally secreted) tyrosine-[35S]sulphated protein preparation was added to the apical medium (or the basolateral medium) of unlabelled filter-grown MDCK cells. In both cases, the free Tyr[35S] generated was predominantly released into the basolateral medium similar to the results obtained in the time-lapse study.

Purification and characterization of the apically secreted 80 KDa glycoprotein from Madin-Darby canine kidney (MDCK) cells.

An 80 KDa glycoprotein (gp 80), known to be released predominantly from the apical surface by filter-grown Madin-Darby canine kidney cells, was purified to electrophoretic homogeneity. Purified gp 80 was found to have a disulfide-bonded dimeric structure, and appeared to exist in two molecular forms, a major (high-molecular weight) form consisting of a 46 KDa subunit and a 39 KDa subunit and a minor (low-molecular weight) form consisting of a 46 KDa subunit and a 33 KDa subunit. Upon de-glycosylation by N-glycanase treatment, the 46 KDa subunit was converted to a 25.6 KDa form, whereas both the 39 KDa and the 33 KDa subunit gave rise to a 21.1 KDa form. V8 protease mapping of deglycosylated polypeptides revealed the 39 KDa and the 33 KDa subunit to have nearly identical band patterns, which also exhibited a high degree of homology to that derived from the 46 KDa subunit. Radioimmunoassays revealed that the binding of the purified gp 80 to fibrinogen (or heparin) was dependent on both pH and divalent cations. Furthermore, binding of gp 80 to immobilized fibrinogen (or heparin) was inhibited in the presence of free fibrinogen (or heparin) added in the assay mixture.

Post-translational modifications and binding properties of the apically secreted 80-kDa glycoprotein from Madin-Darby canine kidney cells: similarities to the C-terminal portion of the basolaterally secreted fibronectin.

Apically secreted 80-kDa glycoprotein (gp 80) from Madin-Darby canine kidney cells was found to be immunoprecipitated by the polyclonal antiserum against fibronectin or a monoclonal antibody specific for the fibronectin C-terminal fibrin binding domain. Upon sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), gp 80 migrated as a doublet band under nonreducing conditions. Under reducing conditions, gp 80 was resolved into three distinct bands, respectively of 45-, 40-, and 35-kDa molecular mass. Analysis by two-dimensional SDS-PAGE revealed that gp 80 exists in two molecular forms: one consisting of a 45-kDa subunit and a 40-kDa subunit, and one consisting of a 45-kDa subunit and a 35-kDa subunit. V-8 protease mapping indicated the 40 and 35-kDa subunits as being of the same homologous group and also as bearing partial homology to the 45-kDa subunit. Radioactive labeling revealed that labeled gp 80 was subjected to covalent modifications by sulfation and phosphorylation. Sulfate analysis showed that [35S]sulfate-labeled gp 80 contained ca. 2.45 +/- 0.07% tyrosine-bound [35S]sulfate with the rest being presumably carbohydrate-bound. [32P]-Phosphate-labeled gp 80, on the other hand, was found to contain serine-O-phosphate as the predominant phosphorylated amino acid residue. Employing the affinity gel fractionation technique, it was shown that gp 80 exhibited binding affinities toward heparin and fibrin. Binding of gp 80 to heparin-agarose or fibrin-Sepharose, however, was inhibited in the presence of added fibronectin or the monoclonal antibody. Tryptic peptide mapping revealed common peptide spots between fibronectin and the three subunits of gp 80. Furthermore, Western blot analysis showed that fibronectin could be recognized and bound by anti-gp 80 antibodies. These results indicate that gp 80 bears both structural and functional similarities to the C-terminal portion of the fibronectin molecule.

Purification and characterization of a membrane-bound tyrosine-O-sulfate-binding protein from bovine liver.

A membrane-bound 175-kDa tyrosine-O-sulfate (TyrS)-binding protein from bovine liver was purified to electrophoretic homogeneity. The purified protein exhibited an apparent molecular weight of 175,000 as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) under reducing conditions. Upon SDS-PAGE under nonreducing conditions, the TyrS-binding protein migrated considerably faster than the dimeric fibronectin, indicating its presence in the monomeric form and therefore the absence of a disulfide-bonded subunit structure. The purified TyrS-binding protein was found to bind concanavalin A-Sepharose and yielded a positive reaction toward periodic acid-Schiff (PAS) staining, indicating its glycoprotein nature. The purified TyrS-binding protein displayed strong binding to TyrS, but not the unmodified tyrosine, covalently bonded to Sepharose. Using a tyrosine-sulfated cholecystokinin octapeptide (CCK-8) as the ligand in a radioimmunoassay, it was found that the binding of the TyrS-binding protein was pH-dependent, being strong from pH 8.0 down through 6.5, and becoming dramatically weaker at pH below 6.0. Divalent cations, added in the assay mixture, exerted significant promoting effects on the binding in the order Mn+2 greater than Ca2+ greater than Mg2+. Western blot analysis clearly showed that the purified TyrS-binding protein was capable of forming complexes with two tyrosine-sulfated proteins, fibronectin and fibrinogen, but not two non-tyrosine-sulfated proteins, transferrin and albumin. These results provided support to a role of the TyrS-binding protein being a putative receptor for tyrosine-sulfated proteins.

Identification of complexes between the tyrosine-O-sulphate-binding protein and tyrosine-sulphated proteins in bovine liver membrane lysates.

Rabbit antiserum against electrophoretically purified bovine liver tyrosine-O-sulphate (TyrS)-binding protein was prepared. Affinity-purified antibodies from the antiserum were found to be capable of immunoprecipitating the TyrS-binding protein from the sodium choleate extract of a bovine liver microsomal membrane fraction. Using purified specific antibodies as the probe, Western blot analysis for the presence of TyrS-binding protein/tyrosine-sulphated protein complexes in bovine liver membrane lysates was performed. It was found that the TyrS-binding protein co-precipitated with three tyrosine-sulphated proteins (fibronectin, fibrinogen and complement C4) immunoprecipitated by their respective antibodies. In contrast, for the two non-tyrosine-sulphated proteins (haptoglobin and transferrin) tested, co-precipitation of the TyrS-binding protein was not observed. On employing an affinity gel fractionation technique, it was shown that partially purified TyrS-binding protein exhibited binding affinity towards Sepharose gels covalently bonded to fibronectin or fibrinogen, but not towards Sepharose gels bonded to albumin or transferrin. These results indicate that the TyrS-binding protein formed complexes with tyrosine-sulphated proteins both in vivo and in vitro, and thus provide support for the putative role of the former being the receptor of the latter.

[Clinical and experimental study of treating aplastic anemia with fetal liver cell suspension and fetal liver cell-free suspension].

Fresh fetal liver obtained from 3- to 6-month fetus was prepared. Fetal liver cell suspension (FLC) or fetal liver cell-free suspension (FLCF) were then transfused into two groups of patient of aplastic anemia. 15 of 21 patients of aplastic anemia treated with FLC showed reconstitution of haemopoietic function or improvement of peripheral blood pictures, while 27 of 30 patients treated with FLCF showed reconstitution or improvement. It is verified that there is a stimulating factor for CFU-CM, BFU-E, and CFU-E and also a immunologic stimulant for improving the nonspecific immunologic function of the organism as shown by clinical analysis and experimental study. It is obvious that the therapeutic effect of FLCF is much better than that of the FLC.