No abstract

Abstract. Adult mouse brain contains at least two distinct spectrin subtypes, both consisting of 240-kD and 235-kD subunits. Brain spectrin(240/235) is found in neuronal axons, but not dendrites, when immunohistochemistry is performed with antibody raised against brain spectrin isolated from enriched synaptic/axonal membranes. A second spectrin subtype, brain spectrin(240/235E), is exclusively recognized by red blood cell spectrin antibody. Brain spectrin(240/235E) is confined to neuronal cell bodies and dendrites, and some glial cells, but is not present in axons or presynaptic terminals.

Donahue RN, McLaughlin PJ, Zagon IS. Cell proliferation of human ovarian cancer is regulated by the opioid growth factoropioid growth factor receptor axis.

No abstract

We have demonstrated the existence of a spectrin-like protein in a variety of nonerythroid cultured cells. Indirect immunofluorescence studies with monospecific antispectrin IgG indicated the presence ofproteins that have common antigenic determinants to spectrin in embryonic chicken cardiac myocytes, mouse fibroblast lines (3T3, simian virus 40-transformed 3T3), and rat hepatoma lines (HTC, HMOA). Two spectrin-like peptides of 240,000 and 230,000 daltons were immunoprecipitated from octyl glucoside-solubilized embryonic chicken cardiac myocytes, along with associated cytoskeletal proteins. Immunoautoradiographic characterization of the myocyte immunoprecipitate showed that only the spectrin-like 240,000-and 230,000-daltonmpeptides were stained with monospecific antispectrin IgG and ' I-labeled protein A. One-dimensional partial proteolytic mapping of the myocyte 240,000-and 230,000-dalton peptides showed that these peptides share substantial sequence homology with embryonic chicken erythrocyte spectrin 240,000-and 220,000-dalton peptides. Spectrin is the major component of a cytoskeletal protein network that is attached to the cytoplasmic surface of the erythrocyte membrane (1) through a high-affinity association with the syndeins (bands 2.1-2.6) (2-4). Spectrin, which constitutes 25-30% of the total erythrocyte membrane protein (5), appears to play a key role in the maintenance ofthe discoid shape ofthe membrane (for review, see ref. 6) and in restricting the lateral mobility of its macromolecules (for review, see ref. 7).Spectrin has been found in all mammalian and avian red cells studied but has not been detected previously in nonerythroid cell types. Earlier attempts to demonstrate the presence of spectrin in nonerythroid cells by complement fixation (8) and radioimmunoassay (9) ECCMs growing in culture on glass coverslips were processed for immunofluorescence experiments using antispectrin IgG as follows: cells were fixed either by immersion in absolute acetone at -20°C for 5 min or by treatment with 3% paraformaldehyde in Pi/NaCl for 2 min at 20°C, washed extensively with Pi/NaCl (aldehyde-fixed cells were also washed with 0

Ulcers and erosions of the corneal epithelium, as well as delays in resurfacing of the cornea after wounding, are major causes of ocular morbidity and visual loss in diabetes. To study whether intervention by the opioid antagonist naltrexone (NTX; 30 mg/kg, twice daily) can restore reepithelialization in diabetic cornea, we induced diabetes in rats by intravenous injection of 65 mg/kg streptozotocin. After confirmation of diabetes, 5-mm-diameter epithelial defects that did not include the limbus were created by mechanical scraping of the cornea. At 4 and 8 weeks, corneal reepithelialization was markedly subnormal, with delays ranging from 11% to 17-fold in the diabetic animals compared with control counterparts. Rats that were diabetic for 8 weeks also had a significant decrease in the incidence of complete wound closure. At 4 and 8 weeks, diabetic animals that were receiving NTX had an acceleration in reepithelialization compared with diabetic animals that were receiving vehicle and even surpassed controls. DNA synthesis in the corneal epithelium of diabetic rats was decreased up to 90% of control levels, and NTX exposure of diabetic subjects elevated the labeling index by up to eightfold from diabetic animals that were receiving vehicle. Opioid growth factor and opioid growth factor receptor distribution were comparable in diabetic and control animals. These results indicate a delay in reepithelialization that is dependent on the duration of diabetes and that intervention of endogenous opioidreceptor interfacing with an opioid antagonist can facilitate the process of wound healing. Diabetes 51: 3055-3062, 2002

No abstract

LDN therapy appears effective and safe in subjects with active Crohn's disease. Further studies are needed to explore the use of this compound.