Stanniocalcin (STC) is a hormone that was originally identified in fish, where it inhibits calcium uptake by the gills and gut and stimulates phosphate adsorption by the kidney. Recently, two mammalian homologues of stanniocalcin were identified. The first (STC1) shows 61% identity to the fish stanniocalcins and appears to have a function similar to that of the fish stanniocalcins. The second homologue (STC2) is 30-38% identical to the fish stanniocalcins, and is characterized by unique cysteine and histidine motifs that are not found in the other stanniocalcins. We purified both the native hamster and recombinant human STC2 proteins and obtained a partial amino acid sequence of the hamster protein. Both proteins behave as a disulfide bonded homodimer, which undergoes post-translational modification(s). The STC2 gene was localized to human chromosome 5q35. Northern blot analysis revealed that the primary site of human STC2 production is the pancreas, and immunostaining localized the STC2 protein to a subpopulation of cells in the islet. Double immunostaining for STC2 and either insulin or glucagon revealed that STC2 protein is found in the alpha cells, but not the beta cells. We speculate that STC2 may play a role in glucose homeostasis.
Sansanmycins, members of the uridyl peptide antibiotics, are assembled by nonribosomal peptide synthetases (NRPSs), the substrate promiscuity of which results in the diversity of products. Further exploration of the NRPSs' substrate promiscuity by reinvestigating sansanmycin producer strain led to the isolation and structural elucidation of eight new uridyl peptides, sansanmycins H-O (1-8). Among them, sansanmycin L, containing a 6-OH-bicyclic residue and Phe3 first found at the position AA3, exhibited activity against M. tuberculosis H37Rv with an MIC value of 2 μg/mL, 8-fold more potent than that of the major compound, sansanmycin A (MIC = 16 μg/mL).
Background: Adjacent segment disease (ASD) is a well-known complication after interbody fusion. Pedicle screwrod revision possesses sufficient strength and rigidity. However, is a surgical segment with rigid fixation necessary for ASD reoperation? This study aimed to investigate the biomechanical effect of different instrumentation on lateral lumbar interbody fusion (LLIF) for ASD treatment. Methods: A validated L2~5 finite element (FE) model was modified for simulation. ASD was considered the level cranial to the upper-instrumented segment (L3/4). Bone graft fusion in LLIF with bilateral pedicle screw (BPS) fixation occurred at L4/5. The ASD segment for each group underwent a) LLIF + posterior extension of BPS, b) PLIF + posterior extension of BPS, c) LLIF + lateral screw, and d) stand-alone LLIF. The L3/4 range of motion (ROM), interbody cage stress and strain, screw-bone interface stress, cage-endplate interface stress, and L2/3 nucleus pulposus of intradiscal pressure (NP-IDP) analysis were calculated for comparisons among the four models. Results: All reconstructive models displayed decreased motion at L3/4. Under each loading condition, the difference was not significant between models a and b, which provided the maximum ROM reduction (73.8 to 97.7% and 68.3 to 98.4%, respectively). Model c also provided a significant ROM reduction (64.9 to 77.5%). Model d provided a minimal restriction of the ROM (18.3 to 90.1%), which exceeded that of model a by 13.1 times for flexion-extension, 10.3 times for lateral bending and 4.8 times for rotation. Model b generated greater cage stress than other models, particularly for flexion. The maximum displacement of the cage and the peak stress of the cageendplate interface were found to be the highest in model d under all loading conditions. For the screw-bone interface, the stress was much greater with lateral instrumentation than with posterior instrumentation.
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