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Biomedical subjects

M R Morris

Publications and source records attributed to M R Morris.

At least 19 recordsLinked to original sources

Osmotically induced cytosolic free Ca(2+) changes in human neutrophils.

Cytosolic free Ca(2+) concentration in neutrophils was measured by ratiometric fluorometry of intracellular fura2. Increasing the extracellular osmolarity, by either NaCl (300-600 mM) or sucrose (600-1200 mM), caused a rise in cytosolic free Ca(2+) (Delta(max) approximately equal to 600 nM). This was not due to cell lysis as the cytosolic free Ca(2+) concentration was reversed by restoration of isotonicity and a second rise in cytosolic free Ca(2+) could be provoked by repeating the change in extracellular osmolarity. Furthermore, the rise in cytosolic free Ca(2+) concentration occurred in the absence of extracellular Ca(2+), demonstrating that release of intracellular fura2 into the external medium did not occur. The osmotically-induced rise in cytosolic free Ca(2+) was not inhibited by either the phospholipase C-inhibitor U73122, or the microfilament inhibitor cytochalasin B, suggesting that neither signalling via inositol tris-phosphate or the cytoskeletal system were involved. However, the rise in cytosolic free Ca(2+) may have resulted from a reduction in neutrophil water volume in hyperosmotic conditions. As these rises in cytosolic Ca(2+) (Delta(max) approximately equal to 600 nM) were large enough to provoke changes in neutrophil activity, we propose that conditions which removes cell water may similarly elevate cytosolic free Ca(2+) to physiologically important levels.

Calcium↗

Properties of CFTR activated by the xanthine derivative X-33 in human airway Calu-3 cells.

The pharmacological activation of the cystic fibrosis gene protein cystic fibrosis transmembrane conductance regulator (CFTR) was studied in human airway epithelial Calu-3 cells, which express a high level of CFTR protein as assessed by Western blot and in vitro phosphorylation. Immunolocalization shows that CFTR is located in the apical membrane. We performed iodide efflux, whole cell patch-clamp, and short-circuit recordings to demonstrate that the novel synthesized xanthine derivative 3, 7-dimethyl-1-isobutylxanthine (X-33) is an activator of the CFTR channel in Calu-3 cells. Whole cell current activated by X-33 or IBMX is linear, inhibited by glibenclamide and diphenylamine-2-carboxylate but not by DIDS or TS-TM calix[4]arene. Intracellular cAMP was not affected by X-33. An outwardly rectifying Cl(-) current was recorded in the absence of cAMP and X-33 stimulation, inhibited by DIDS and TS-TM calix[4]arene. With the use of short-circuit recordings, X-33 and IBMX were able to stimulate a large concentration-dependent CFTR transport that was blocked by glibenclamide but not by DIDS. Our results show that manipulating the chemical structure of xanthine derivatives offers an opportunity to identify further specific activators of CFTR in airway cells.

1-Methyl-3-isobutylxanthine↗

Onlay bone augmentation with an osteoinductive implant.

The repair of contour defects of craniofacial bone can be accomplished by several methods, including autogenous bone grafts, demineralized bone, and alloplastic materials. The objective of this study was to assess a biodegradable, xenogeneic, osteoinductive implant for craniofacial onlay bone augmentation. Twelve New Zealand White rabbits each had craniofacial onlays consisting of three experimental materials: 1) autograft; 2) allogeneic, demineralized block implant; and 3) partially purified osteoinductive protein (osteogenin) with allogeneic collagen and 50:50 poly (DL-lactide-co-glycolide). Implants with host bone were recovered after 20 weeks and assessed by histomorphometric methods. There was no evidence of adverse local reaction to the three treatments. No significant difference in bone replacement or bone density resulting from each of the implant types was demonstrated. In conclusion, the osteoinductive implants were well tolerated, and over the 20-week period they appeared to maintain their contour as onlays.

Animals↗