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Background: Differential diagnosis of sellar masses includes adenoma, meningioma, craniopharyngioma, and metastasis. Primary paraganglioma is seldom considered. We present a case of this unique pathology, review the relevant literature, and compile a compendium of immunohistochemical characteristics for use as a resource., Case Description: A 73-year-old woman presented to the hospital with visual changes in her left hemifield. Noncontrast head computed tomography demonstrated a large sellar mass with suprasellar extension and displacement of the optic chiasm (diameter of 3.1 cm). Magnetic resonance imaging was unobtainable owing to an incompatible pacemaker. Computed tomography characterization was most consistent with a macroadenoma. Given the acute visual decline, surgical decompression via an endonasal transsphenoidal route was performed without complication. A diagnosis of paraganglioma was made based on histopathology. Following resection, the patient's visual field deficit improved. Computed tomography body imaging was negative for a metastatic origin., Conclusions: Paraganglioma is a rare but potential differential diagnosis to consider when evaluating sellar masses., (Copyright © 2019 Elsevier Inc. All rights reserved.)

Cationic peptides possessing antibacterial activity are virtually ubiquitous in nature, and offer exciting prospects as new therapeutic agents. We had previously demonstrated that such peptides could be produced by fusion protein technology in bacteria and several carrier proteins had been tested as fusion partners including glutathione-S-transferase, S. aureus protein A, IgG binding protein and P. aeruginosa outer membrane protein OprF. However these fusion partners, while successfully employed in peptide expression, were not optimized for high level production of cationic peptides (Piers, K., Brow, M. L., and Hancock, R. E. W. 1993, Gene 137, 7-13). In this paper we took advantage of a small replication protein RepA from E. coli and used its truncated version to construct fusion partners. The minimal elements required for high level expression of cationic peptide were defined as a DNA sequence encoding a fusion protein comprising, from the N-terminus, a 68 amino acid carrier region, an anionic prepro domain, a single methionine and the peptide of interest. The 68 amino acid carrier region was a block of three polypeptides consisting of a truncated RepA, a synthetic cellulose binding domain and a hexa histidine domain. The improved system showed high level expression and simplified downstream purification. The active peptide could be yielded by CNBr cleavage of the fusion protein. This novel vector was used to express three classes of cationic peptides including the alpha-helical peptide CEMA, the looped peptide bactenecin and the extended peptide indolicidin. In addition, mutagenesis of the peptide gene to produce peptide variants of CEMA and indolicidin using the improved vector system was shown to be successful.

The PufQ protein, prepared by the recombinant expression of the pufQ gene of Rhodobacter capsulatus, has been reconstituted into liposomes in the presence of the bacteriochlorophyll precursor, protochlorophyllide. The liposomes were separated from liposomes free of the PufQ protein by sucrose density gradient ultracentrifugation and analyzed for their content of protochlorophyllide, protein, and phospholipid. The results indicated a 3.5 times higher level of association of protochlorophyllide with the PufQ protein-containing liposomes than with liposomes containing either the hydrophobic protein, apolipoprotein A-I, or the water-soluble maltose-binding protein. Only the association of the protochlorophyllide with the PufQ protein corresponded to a small but reproducible shift in its fluorescence emission maximum to a lower wavelength, consistent with a change in its environment.