RESUMO
OBJECTIVE: To investigate the impact of resident participation in cataract surgery on operative time and cost. DESIGN: Retrospective chart review. PARTICIPANTS: All patients who underwent phacoemulsification cataract surgery by an attending or resident surgeon of the Penn State Hershey Eye Center between July 1, 2004, and June 30, 2007. METHODS: Operating room records of all phacoemulsification surgeries performed at a single academic center between July 1, 2004, and June 30, 2007, were reviewed. MAIN OUTCOME MEASURES: Operative case length in minutes and cost of operating room time. RESULTS: The primary surgeon was an attending physician in 474 cases and a senior resident physician in 473 cases. Phacoemulsification surgeries took an average of 12 minutes 41 seconds longer per eye when performed by a senior resident compared with an attending surgeon (95% confidence interval [CI], 1 minute 48 seconds to 23 minutes 35 seconds; P = 0.027). Resident cases averaged 63 minutes in July, and decreased to an average of 27 minutes in June. Every month from July through December of the academic year, the monthly mean operative case length for resident cases was significantly longer than the mean operative case length for attending cases (P<0.05), except November, when the difference was borderline significant (95% CI, -23 seconds to 23 minutes 9 seconds; P = 0.057). From January through June, there was no difference. Using the nonsupply cost of running the operating room at our institution ($8.30 per operating minute), resident participation added $105.40 to the average phacoemulsification case. This cost totaled $8293.23 per resident per year. CONCLUSIONS: Resident participation is associated with significantly increased phacoemulsification operative times and costs during the first half, but not the second half, of the academic year. The time and cost per resident may be important to consider when allocating resources for preclinical training. FINANCIAL DISCLOSURE(S): The authors have no proprietary or commercial interest in any of the materials discussed in this article.
Assuntos
Educação de Pós-Graduação em Medicina/economia , Internato e Residência/economia , Salas Cirúrgicas/economia , Oftalmologia/educação , Facoemulsificação/economia , Competência Clínica , Alocação de Custos , Recursos em Saúde , Custos Hospitalares , Humanos , Implante de Lente Intraocular/economia , Alocação de Recursos , Estudos Retrospectivos , Fatores de TempoRESUMO
PURPOSE: The durability of the ubiquitin proteasome pathway in the mammalian lens makes this enzyme system a potential contributor to certain cataracts and posterior capsular opacification (PCO). The present study addresses proteasome involvement in TGF-beta induced, cataract-associated gene activation in human lens cells. METHODS: HLE B-3 cells were treated with TGF-beta, in combination with the proteasome inhibitors MG-132 or lactacystin. TGF-beta target gene expression was measured by semiquantitative RT-PCR. Annexin-FITC staining and flow cytometry were used to assess apoptosis levels. Western blot analyses were performed with anti-SnoN and anti-Smad2 antibodies. RESULTS: TGF-beta induced the expression of alpha-smooth muscle actin, fibronectin, and TGF-beta-inducible gene mRNA in HLE B-3 cells and primary cultured human lens cells from donor tissues. TGF-beta also induced a time-dependent decrease in the level of the Smad repressor SnoN. Gamma-glutamyl-cysteine synthetase (gamma-GCS) mRNA levels decreased in the presence of TGF-beta. Proteasome inhibitor cotreatment blocked the induction of alpha-SMA mRNA, the loss of SnoN protein, the decrease in gamma-GCS mRNA, and TGF-beta-induced apoptosis. CONCLUSIONS: The HLE B-3 cell line and primary cultured human lens cells respond similarly to TGF-beta treatments by activating cataract-related gene expression. This response in both of these model systems is blocked by inhibiting the proteasome. This suggests that the proteasome can mediate cataract and PCO-associated changes and therefore is a novel target of medical therapy.
Assuntos
Células Epiteliais/efeitos dos fármacos , Regulação da Expressão Gênica/fisiologia , Cristalino/efeitos dos fármacos , Complexo de Endopeptidases do Proteassoma/fisiologia , Transdução de Sinais/fisiologia , Fator de Crescimento Transformador beta/farmacologia , Acetilcisteína/análogos & derivados , Acetilcisteína/farmacologia , Actinas/genética , Anexinas/metabolismo , Western Blotting , Catarata/genética , Células Cultivadas , Inibidores de Cisteína Proteinase/farmacologia , Células Epiteliais/metabolismo , Fibronectinas/genética , Citometria de Fluxo , Técnica Indireta de Fluorescência para Anticorpo , Glutamato-Cisteína Ligase/genética , Humanos , Peptídeos e Proteínas de Sinalização Intracelular/metabolismo , Cristalino/citologia , Cristalino/metabolismo , Leupeptinas/farmacologia , Proteínas Proto-Oncogênicas/metabolismo , RNA Mensageiro/metabolismo , Reação em Cadeia da Polimerase Via Transcriptase Reversa , Proteína Smad2/metabolismo , Ativação TranscricionalRESUMO
PURPOSE: The purpose of this study is to compare the protein composition of the B-3 line of transformed human lens epithelial (HLE) cells to that of freshly dissected HLE cells. This provides baseline data on lens cell proteins from fresh lens cells and from the B-3 cell line, which is often used as a model system for the lens. METHODS: Human lens epithelial cells adherent to the lens capsule were dissected into central (undifferentiated) and peripheral (partially differentiated) populations. Fully differentiated human lens fiber cells were isolated from the outer cortical layers of the lens. HLE B-3 cells were analyzed at several passage levels. Extracts were prepared from each cell type and the proteins resolved by two-dimensional polyacrylamide gel electrophoresis (2-DE). Representative gel patterns were visually compared, spots excised, and trypsin digests prepared. The peptide compositions of the digests were analyzed using either liquid chromatography electrospray ionization tandem mass spectrometry or atmospheric pressure-matrix-assisted laser desorption ionization mass spectrometry, using a liquid chromatography classic ion trap (LCQ) mass spectrometer. RESULTS: Two-DE patterns were obtained for fresh and cultured cell types. Similar patterns were observed between central and peripheral HLE cells, both of which contained high levels of alphaA-, alphaB-, and betaB2-crystallins; alpha-enolase; and aldehyde dehydrogenase. HLE B-3 cultured cells were characterized by a marked loss of crystallins and a relatively higher level of noncrystallin proteins--most notably, high molecular weight, acidic proteins. Whereas subunit d of adenosine triphosphate (ATP) synthase, alphaB-crystallin, galectin, glyceraldehyde-3-phosphate dehydrogenase, alpha-enolase, actin, peptidylprolyl isomerase A, phosphatidylethanolamine-binding protein, and vimentin were present in both fresh and cultured lens epithelium, only the high abundance of alpha-enolase, galectin-1, and vimentin suggested that B-3 cells were lens derived. CONCLUSIONS: Freshly dissected noncultured HLE cells from both central and peripheral regions contain a high concentration of crystallins that mask the detection of less abundant proteins by 2-DE. Transformation and culture of HLE cells causes a loss of these crystallins and an increase in the relative concentration of other proteins. However, most of these noncrystallin proteins were different from those observed in noncultured HLE cells. These results suggest that transformation markedly alters the protein expression pattern in immortalized HLE cells and that caution should be exercised when using them to study properties of HLE cells in vivo.
Assuntos
Cristalinas/análise , Células Epiteliais/química , Cristalino/química , Proteoma/análise , Idoso , Diferenciação Celular , Linhagem Celular Transformada , Cromatografia Líquida de Alta Pressão , Cristalinas/isolamento & purificação , Eletroforese em Gel Bidimensional , Humanos , Pessoa de Meia-Idade , Peso Molecular , Proteoma/isolamento & purificação , Espectrometria de Massas por Ionização e Dessorção a Laser Assistida por MatrizRESUMO
A 28-year-old woman with a 6-year history of optic neuropathy and 8 years of hearing loss had enhancing dural lesions around the brain stem and in both internal auditory canals on MRI. Histopathology from cranial procedures performed in 1990 and 1993 was originally interpreted as inflammatory meningioma, now known as lymphoplasmacyte-rich meningioma (LRM). Because the clinical course was more consistent with a relapsing process, the original surgical specimens were restudied with additional immunocytochemical stains. The review led to a pathologic diagnosis of idiopathic hypertrophic pachymeningitis (IHP). IHP and LRM can be confused on both imaging and histopathologic grounds.