Nasal changes after presurgical nasoalveolar molding (PNAM) in the unilateral cleft lip nose.

PURPOSE: Nasal reconstruction for patients with unilateral cleft lip and palate (UCLP) is a challenge for the reconstructive surgeon. Presurgical nasoalveolar molding (PNAM) was introduced to reshape the cleft nasal structures prior to lip repair. This study analyzed two-dimensional nasal changes before and after PNAM in patients with complete UCLP. METHODS: Thirty UCLP patients (19 males; 11 females) who received PNAM before lip repair were included in this study. PNAM was applied for 100 days. Nasal casts were obtained before and after PNAM. Frontal and 45° standardized digital photographs were taken from all casts, and a photogrammetric analysis (16 linear, six angular, and two area measurements) was performed. Paired Student's t tests were used to search for differences by time, and time versus side (cleft versus noncleft). RESULTS: Significant reduction of cleft columella deviation with an increase in columella length, nostril height, and axial inclination on the cleft side were recorded. This resulted in an increase in the projection of the nasal tip. The noncleft measurements remained without significant changes. The cleft nostril area increased significantly more than the noncleft side by 90% with PNAM treatment. Significant normal growth changes were observed in nasal width and nasal height. CONCLUSION: A favorable reshaping of the nose after PNAM was achieved, resulting in an improvement in form before lip surgery. These changes lead to improved nasal symmetry before primary lip and nasal reconstruction in UCLP patients.

A novel terminal web-like structure in cortical lens fibers: architecture and functional assessment.

This study describes a novel cytoskeletal array in fiber cells of the ocular lens of the rat and shows its relationship to the classical terminal web of other epithelial tissues. Naive adult Sprague-Dawley rats (n = 28) were utilized. F-actin, fodrin, myosin IIA, and CP49 distribution was assessed in anterior and posterior polar sections. For functional analysis, lenses were cultured with or without cytochalasin-D for 3 hr, then processed for confocal microscopy or assessed by laser scan analysis along sutures. Phalloidin labeling demonstrated a dense mesh of F-actin adjacent to posterior sutural domains to a subcapsular depth of 400 µm. Anterior polar sections revealed a comparable actin structure adjacent to anterior suture branches however, it was not developed in superficial fibers. Fodrin and myosin were localized within the web-like actin apparatus. The data was used to construct a model showing that the cytoskeletal array is located within the blunt, variable-width fiber ends that abut at sutures such that the "terminal web" flanks the suture on either side. Treatment with cytochalasin-D resulted in partial disassembly of the "terminal web" and perturbed cellular organization. Laser scan analysis revealed that cytochalasin-D treated lenses had significantly greater focal variability than control lenses (P = 0.020). We conclude that cortical fibers of rat lenses contain a bipolar structure that is structurally and compositionally analogous to classical terminal webs. The results indicate that the lens "terminal web" functions to stabilize lens fiber ends at sutures thus minimizing structural disorder, which in turn, promotes the establishment and maintenance of lens transparency.

Aberrant basal fiber end migration underlies structural malformations in a streptozotocin-induced diabetic rat model.

This study characterized early structural changes at posterior fiber ends in the crystalline lens after diabetic induction. Wistar rats (n = 49), randomized into one naïve control group and four experimental groups, were rendered diabetic via streptozotocin injection. Animals were euthanized at 1 week intervals, blood glucose levels recorded and lenses were evaluated grossly, by SEM and by confocal microscopy. Scoring Indices were developed to assess structural alterations and for statistical correlations between the scores and the duration of hyperglycemic exposure as well as blood glucose levels. Average blood glucose levels increased progressively from 98.5 mg/dL (controls) to 331.4 mg/dL (4 weeks). Diabetic lenses displayed abnormal suture sub-branches and opacity formation beginning late in the first week post-injection and rapidly progressing in severity through four weeks. SEM analyses showed gradual elongation of fiber ends and filopodia which comprised a disorganized configuration and a loss of recognizable migration patterns. Structural alterations culminated in foci of fiber degeneration by the third to fourth weeks. The F-actin distribution at basal fiber ends was significantly altered as compared to naïve controls. Cadherin distribution was altered as compared to controls, but largely at later time points. The grading system clearly shows increased structural compromise with elevated blood glucose levels in streptozotocin-induced diabetes. Further, although the initial rise in blood glucose levels was associated with pathological changes, their progression depended to a larger extent on continued hyperglycemic exposure. The data suggests that hyperglycemia initially disrupts fiber end migration, resulting in structural alterations and eventual fiber degeneration.

Distribution of basal membrane complex components in elongating lens fibers.

PURPOSE: To localize specific components of the Basal Membrane Complex (BMC) of elongating lens fibers at defined points in their migration to the posterior sutures. METHODS: Normal, juvenile (4-6 week old) Sprague-Dawley rat lenses (n=46) were utilized. Lenses were either decapsulated to obtain whole mounts of lens capsules or sectioned with a vibrating knife microtome. Sections (100 microm thick) were cut parallel to the equatorial plane, beginning at the posterior pole. On both sections and whole mounts, F-actin was localized using phalloidin-FITC while myosin, cadherins, and beta1 integrin were localized using immunofluorescent labeling. Specimens were visualized on a laser scanning confocal microscope. RESULTS: F-actin labeling in the equatorial and peri-sutural regions was predominately localized to the periphery of basal fiber ends (consistent with our prior results). At sutures, labeling for F-actin in the BMC was rearranged into numerous small profiles. Furthermore, labeling intensity for F-actin was increased at sutures. Myosin was present in the BMC in all locations examined as a diffuse plaque at fiber ends. Similarly, beta1 integrin was also distributed throughout the BMC within the actin-rich borders in all regions except adjacent to and at the suture branches. In that location immunofluorescence for beta1 integrin appeared to be reduced. In the equatorial, lateral-posterior, and peri-sutural regions, cadherin showed strong localization around the periphery of basal fiber ends. However, cadherin labeling was markedly reduced in the BMC as fibers detached from the capsule and abutted to form sutures (i.e. in the sutural region). Cadherin was concentrated along the short faces of elongating fiber mid-segments. CONCLUSIONS: It appears that F-actin, cadherin and beta1 integrin components of the BMC undergo controlled rearrangements in the final stages of migration and detachment from the capsule.

Age-related compaction of lens fibers affects the structure and optical properties of rabbit lenses.

BACKGROUND: The goal of this investigation was to correlate particular age-related structural changes (compaction) to the amount of scatter in rabbit lenses and to determine if significant fiber compaction occurred in the nuclear and inner cortical regions. METHODS: New Zealand White rabbits at 16-20 months old (adult; n = 10) and at 3.5-4 years old (aged; n = 10) were utilized for this study. Immediately after euthanising, scatter was assessed in fresh lenses by low power helium-neon laser scan analysis. Scatter data was analyzed both for whole lenses and regionally, to facilitate correlation with morphometric data. After functional analysis, lenses were fixed and processed for scanning electron microcopy (SEM; right eyes) and light microscopy (LM; left eyes). Morphometric analysis of SEM images was utilized to evaluate compaction of nuclear fibers. Similarly, measurements from LM images were used to assess compaction of inner cortical fibers. RESULTS: Scatter was significantly greater in aged lenses as compared to adult lenses in all regions analyzed, however the difference in the mean was slightly more pronounced in the inner cortical region. The anterior and posterior elliptical angles at 1 mm (inner fetal nucleus) were significantly decreased in aged vs. adult lenses (anterior, p = 0.040; posterior, p = 0.036). However, the average elliptical angles at 2.5 mm (outer fetal nucleus) were not significantly different in adult and aged lenses since all lenses examined had comparable angles to inner fetal fibers of aged lenses, i.e. they were all compacted. In cortical fibers, measures of average cross-sectional fiber area were significantly different at diameters of both 6 and 7 mm as a function of age (p = 0.011 and p = 0.005, respectively). Accordingly, the estimated fiber volume was significantly decreased in aged as compared to adult lenses at both 6 mm diameter (p = 0.016) and 7 mm diameter (p = 0.010). CONCLUSION: Morphometric data indicates that inner cortical fibers undergo a greater degree of age-related compaction than nuclear fibers. Increased scatter appears to be only tentatively correlated with regions of fiber compaction, suggesting that it is simply one of an array of factors that contribute to the overall decreased transparency in aged rabbit lenses.