Size-dependent magnetic properties of γ-Fe2O3 nanocrystallites.

A route for synthesizing monodisperse magnetic nanocrystallites of maghemite, [Formula: see text]-Fe2O3, with various sizes has been revisited. A systematic investigation of three [Formula: see text]-Fe2O3 nanocrystalline samples by different techniques has been performed to characterize their size-dependent magnetic properties. Zero-field-cooled and field-cooled magnetization measurements reveal that the superparamagnetic blocking temperatures are around 230 K, 170 K, and 50 K for the 15.0 nm, 11.8 nm, and 6.1 nm nanocrystallites, respectively. Low-temperature Mössbauer spectra show that all three nanocrystallites have the maghemite structure with all the vacancies in the B-sites. Furthermore, detailed analysis shows that there are more vacancies on the B-sites for the 6.1 nm nanocrystallites compared to 0.33 for the bulk maghemite.

Inhibition of membrane-bound carbonic anhydrase enhances subretinal fluid absorption and retinal adhesiveness.

BACKGROUND: The clinical use of currently available carbonic anhydrase (CA) inhibitors is limited by systemic side-effects, thought to result from the inhibition of intracellular CA isoenzymes. This study investigates how benzolamide, a carbonic anhydrase inhibitor which does not readily penetrate cell membranes, modulates retinal pigment epithelium functions relative to acetazolamide, which diffuses into the cytosol. METHODS: Small retinal detachments were made in Dutch rabbits by injecting saline into the subretinal space. Detachment height was measured using a dual He-Ne beam YAG laser focusing system, and the fluid absorption rate was calculated before and after intravenous injections of saline, acetazolamide or benzolamide. Retinal adhesiveness was determined by peeling the retina from the RPE and measuring the amount of adherent pigment. RESULTS: The baseline fluid absorption rate of 0.04 microl/mm(2)/h was unchanged after injection of 0.9% NaCl or low-dose benzolamide (5 mg/kg). The absorption increased to about 0.14 microl/mm(2)/h after higher benzolamide doses (20-40 mg/kg) and to 0.13 microl/mm(2)/h after acetazolamide (20 mg/kg). Both acetazolamide and benzolamide significantly slowed the post-enucleation failure of retinal adhesiveness. CONCLUSION: Since benzolamide had effects similar to acetazolamide, inhibition of membrane-bound CA appears to be sufficient to enhance subretinal fluid absorption and retinal adhesiveness. Membrane-specific CA inhibitors may therefore be of clinical value if they minimize side-effects from intracellular CA inhibition.

Developmental expression of the rat rod photoreceptor cGMP-gated cation channel.

The appearance of cGMP-gated cation channel protein in the postnatal rat retina has been studied by fluorescence immunocytochemistry of radial retinal sections and immunoblots of retinal membrane proteins. Channel immunoreactivity was first detectable with RCNGC1-7H2 monoclonal antibody at postnatal day 7 (PN7) by both methods. Immunocytochemical label in retinal sections was localized to the outer segments, and immunoreactivity increased with increasing age. We also compared the developmental appearance of the cGMP-gated cation channel to that of other phototransduction proteins and developmental markers. RET-P2, a monoclonal antibody recognizing the 39-kDa rds/peripherin disc protein, first labeled outer segments at PN7, coincident with cGMP-gated cation channel expression. Double labeling of the same section of PN7 rat retina with RET-P2 and R309 (a polyclonal antiserum against the rod cGMP-gated cation channel) revealed identical patterns of labelling. Similarly, double labeling with RCNGC1-7H2 and an antibody against the rod cGMP-phosphodiesterase gave coincident labeling, suggesting coordinate expression mechanisms of phototransduction proteins with each other and with outer segment structural proteins.

Cytochalasin D reversibly weakens retinal adhesiveness.

This study asks whether retinal adhesiveness is affected by cytochalasin D, a drug that is known to alter the apical morphology of the retinal pigment epithelium (RPE). Cytochalasin D was injected intravitreally in Dutch rabbits and retinal adhesiveness measured 0.5 to 72 h later by two methods: in vitro peeling of the retina from retinal pigment epithelium to observe the amount of adherent pigment, and in vivo measurement of the pressure needed to achieve retinal separation. Electroretinograms were recorded, and RPE apical morphology was examined by scanning electron microscopy. The injection of 60 microM cytochalasin D caused in vitro retinal adhesiveness to fall within 3 h to 10% of normal although the electroretinogram (a, b, and c-waves) remained normal. Smaller doses of cytochalasin D had a lesser effect. The RPE apical surface at 3 h showed large bullet-like microvilli, swollen cone sheaths, and an absence of filamentous microvilli. The severity of these changes was dose-related. At 72 h after cytochalasin D, retinal adhesiveness had largely recovered, and RPE apical morphology appeared normal again. Thus, cytochalasin D weakens retinal adhesiveness acutely but reversibly, and both the initial effect and recovery correlate with changes in RPE microvillar morphology. This suggests that actin microfilaments may be involved in mechanisms of retinal adhesion.