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1.
J Cancer Surviv ; 9(2): 287-304, 2015 Jun.
Artigo em Inglês | MEDLINE | ID: mdl-25432632

RESUMO

PURPOSE: This study aims to examine literature on effectiveness of low-level laser therapy (LLLT) in reducing limb volume and pain in adults with breast cancer-related lymphedema (BCRL). METHODS: PubMed, PEDro, CINAHL, and Cochrane databases were searched using (lymphedema OR edema OR swelling) AND (breast cancer OR mastectomy) AND (laser OR low-level laser therapy OR LLLT OR cold laser). Intervention studies or meta-analyses reporting LLLT for BCRL were included in the search. Pooled effect sizes (ES) and 95 % confidence intervals (CI) were calculated for volume and pain. No limitations were placed on length of follow-up, publication year, or language. Final search was conducted on October 16, 2014. RESULTS: Nine studies met criteria for inclusion. Within-group pooled ES for volume (six studies) was -0.52 (-0.78, -0.25), representing a 75.7-ml reduction in limb volume after LLLT. Between-group pooled ES for volume (four studies) was -0.62 (-0.97, -0.28), representing a 90.9-ml greater reduction in volume with treatment including LLLT versus not including LLLT. Within-group pooled ES for pain reduction (three studies) was -0.62 (-1.06, -0.19), pain reduction of 13.5 mm (0-100 mm VAS). Between-group pooled ES for pain reduction (two studies) was non-significant at -1.21 (-4.51, 2.10). CONCLUSION: Moderate-strength evidence supports LLLT in the management of BCRL, with clinically relevant within-group reductions in volume and pain immediately after conclusion of LLLT treatments. Greater reductions in volume were found with the use of LLLT than in treatments without it. IMPLICATIONS FOR CANCER SURVIVORS: LLLT confers clinically meaningful reductions in arm volume and pain in women with BCRL.


Assuntos
Neoplasias da Mama/complicações , Terapia com Luz de Baixa Intensidade , Linfedema/radioterapia , Dor/radioterapia , Sobreviventes , Adulto , Neoplasias da Mama/radioterapia , Neoplasias da Mama/cirurgia , Feminino , Humanos , Linfedema/etiologia , Mastectomia/efeitos adversos , Dor/epidemiologia , Manejo da Dor/métodos , Resultado do Tratamento
2.
Proc Natl Acad Sci U S A ; 102(6): 1921-6, 2005 Feb 08.
Artigo em Inglês | MEDLINE | ID: mdl-15671163

RESUMO

The role of intracellular Ca2+ in the regulation of actin filament assembly and disassembly has not been clearly defined. We show that reduction of intracellular free Ca2+ concentration ([Ca2+]i) to <40 nM in Listeria monocytogenes-infected, EGFP-actin-transfected Madin-Darby canine kidney cells results in a 3-fold lengthening of actin filament tails. This increase in tail length is the consequence of marked slowing of the actin filament disassembly rate, without a significant change in assembly rate. The Ca2+-sensitive actin-severing protein gelsolin concentrates in the Listeria rocket tails at normal resting [Ca2+]i and disassociates from the tails when [Ca2+]i is lowered. Reduction in [Ca2+]i also blocks the severing activity of gelsolin, but not actin-depolymerizing factor (ADF)/cofilin microinjected into Listeria-infected cells. In Xenopus extracts, Listeria tail lengths are also calcium-sensitive, markedly shortening on addition of calcium. Immunodepletion of gelsolin, but not Xenopus ADF/cofilin, eliminates calcium-sensitive actin-filament shortening. Listeria tail length is also calcium-insensitive in gelsolin-null mouse embryo fibroblasts. We conclude that gelsolin is the primary Ca2+-sensitive actin filament recycling protein in the cell and is capable of enhancing Listeria actin tail disassembly at normal resting [Ca2+]i (145 nM). These experiments illustrate the unique and complementary functions of gelsolin and ADF/cofilin in the recycling of actin filaments.


Assuntos
Actinas/metabolismo , Cálcio/metabolismo , Ácido Egtázico/análogos & derivados , Gelsolina/metabolismo , Listeria monocytogenes/metabolismo , Fatores de Despolimerização de Actina , Actinas/genética , Animais , Células Cultivadas , Quelantes/metabolismo , Ácido Egtázico/metabolismo , Quinase 1 de Adesão Focal , Proteína-Tirosina Quinases de Adesão Focal , Listeria monocytogenes/citologia , Camundongos , Camundongos Knockout , Proteínas dos Microfilamentos/metabolismo , Proteínas Tirosina Quinases/genética , Proteínas Tirosina Quinases/metabolismo , Proteínas Recombinantes de Fusão/genética , Proteínas Recombinantes de Fusão/metabolismo , Xenopus laevis
3.
Semin Respir Infect ; 17(3): 189-94, 2002 Sep.
Artigo em Inglês | MEDLINE | ID: mdl-12226798

RESUMO

Extended-spectrum beta-lactamases (ESBLs) were discovered in Europe in the early 1980s after widespread use of broad-spectrum antibiotics. They are largely derivatives of 3 progenitor beta-lactamases that confer resistance to ampicillin in gram-negative bacteria and are now carried on plasmids. Substitutions at the active enzyme site of these progenitor enzymes at single or multiple amino sites have resulted in altered substrate affinities for ESBLs. Depending on the location of the substitution, susceptibility to broad-spectrum antibiotics is variably diminished. ESBLs are most commonly found in Klebsiella species and Escherichia coli, but also in other bacteria including Pseudomonas, Salmonella, Proteus, and Enterobacter species. The discovery of ESBLs in hospital and nursing-home outbreaks and their ability to be transferred to other bacterial species makes management and treatment of ESBLs of great medical concern.This article provides a review of ESBLs and their impact on patient care.


Assuntos
Infecções Bacterianas/etiologia , Infecções Bacterianas/fisiopatologia , Farmacorresistência Bacteriana/fisiologia , beta-Lactamases/efeitos adversos , beta-Lactamases/fisiologia , Infecções Bacterianas/tratamento farmacológico , Humanos , beta-Lactamases/isolamento & purificação
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