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1.
Microsurgery ; 43(4): 365-372, 2023 May.
Artigo em Inglês | MEDLINE | ID: mdl-36645336

RESUMO

BACKGROUND: The innervated vastus lateralis flap (IVLF) is a barely used possibility for facial palsy reconstruction because of its thickness compared to the gracilis, latissimus dorsi, and pectoralis minor flaps. The aim of this study is to perform a precise description of the intramuscular distribution of the nerve motor branches and its relationship with the vascular pedicle in order to harvest a segmental muscle flap with the best contractile strength to restore facial reanimation. METHODS: The study was performed on 16 adult cadaver thighs identifying the vastus lateralis muscle and the distribution and relationships of its neurovascular pedicle and branches. We evaluated where the nerve pierced the muscle and the course of the nerve within it. Transverse segments of the nerve were obtained from the proximal and distal ends of the nerve and stained using anti-ChAT (Choline acetyltransferase) antibodies which are specific of motor neurons. RESULTS: A nerve for the vastus lateralis from the posterior division of the femoral nerve divided into 2 branches in 56% of cases; the principal branch coursed along the vascular pedicle and pierced the muscle more proximally than the respective vessels, and a minor branch that pierced the muscle 25-60 mm proximally. There were 3 main intramuscular branches. The nerve length (mean 132.65 ± 22.89 mm) allowed to reach the contralateral side of the face in almost all cases (95%). The mean ChAT positive fibers was 351.0 ± 92.4/mm2 at the proximal end, and 270.3 ± 87.9/mm2 at the distal end (p = 0.49). The number of ChAT negative fibers was higher than ChAT positive in both proximal and distal ends of the nerve. CONCLUSION: We propose the IVLF as a one-step surgical flap for facial paralysis reanimation due to the constant neurovascular pattern and lengthy pedicle. The amount of motor fibers in several segments of the nerve is appropriate to produce a powerful contraction for dynamic reconstruction.


Assuntos
Paralisia Facial , Músculo Quadríceps , Adulto , Humanos , Músculo Quadríceps/inervação , Retalhos Cirúrgicos/irrigação sanguínea , Paralisia Facial/cirurgia , Paralisia Facial/etiologia , Nervo Femoral , Cadáver , Nervo Facial/cirurgia
2.
PLoS Genet ; 10(2): e1004175, 2014 Feb.
Artigo em Inglês | MEDLINE | ID: mdl-24586202

RESUMO

Loss-of-function mutations in the Caenorhabditis elegans gene sup-18 suppress the defects in muscle contraction conferred by a gain-of-function mutation in SUP-10, a presumptive regulatory subunit of the SUP-9 two-pore domain K(+) channel associated with muscle membranes. We cloned sup-18 and found that it encodes the C. elegans ortholog of mammalian iodotyrosine deiodinase (IYD), an NADH oxidase/flavin reductase that functions in iodine recycling and is important for the biosynthesis of thyroid hormones that regulate metabolism. The FMN-binding site of mammalian IYD is conserved in SUP-18, which appears to require catalytic activity to function. Genetic analyses suggest that SUP-10 can function with SUP-18 to activate SUP-9 through a pathway that is independent of the presumptive SUP-9 regulatory subunit UNC-93. We identified a novel evolutionarily conserved serine-cysteine-rich region in the C-terminal cytoplasmic domain of SUP-9 required for its specific activation by SUP-10 and SUP-18 but not by UNC-93. Since two-pore domain K(+) channels regulate the resting membrane potentials of numerous cell types, we suggest that the SUP-18 IYD regulates the activity of the SUP-9 channel using NADH as a coenzyme and thus couples the metabolic state of muscle cells to muscle membrane excitability.


Assuntos
Proteínas de Caenorhabditis elegans/genética , Caenorhabditis elegans/metabolismo , Iodeto Peroxidase/metabolismo , Proteínas de Membrana/genética , Canais de Potássio/genética , Animais , Caenorhabditis elegans/genética , Proteínas de Caenorhabditis elegans/metabolismo , Iodeto Peroxidase/genética , Proteínas de Membrana/metabolismo , Músculos/metabolismo , Mutação , Fenótipo , Canais de Potássio/metabolismo , Estrutura Terciária de Proteína
3.
J Health Care Poor Underserved ; 25(1): 383-95, 2014 Feb.
Artigo em Inglês | MEDLINE | ID: mdl-24509033

RESUMO

Patient navigation is increasingly being used to support vulnerable patients to receive timely and quality medical care. We sought to understand whether patients with depression utilize additional patient navigation services after abnormal cancer screening. We compared depressed and non-depressed women using three different measures of intensity of patient navigation: number of patient-navigator encounters, encounter time, and number of unique barriers to care. The study population consisted of 1,455 women who received navigation after abnormal screening for breast or cervical cancer at one of six community health centers in Boston. Navigators spent a median of 60-75 minutes over one or two encounters per participant, with 49% of participants having one or more documented barrier to care. Depressed women did not differ in total numbers of encounters, encounter time, or unique barriers compared with non-depressed women. Our findings suggest that pre-existing depression does not predict which women will utilize additional navigation services.


Assuntos
Neoplasias da Mama/diagnóstico , Depressão/epidemiologia , Navegação de Pacientes , Neoplasias do Colo do Útero/diagnóstico , Adulto , Idoso , Boston/epidemiologia , Centros Comunitários de Saúde , Feminino , Humanos , Pessoa de Meia-Idade
4.
J Neurosci ; 23(27): 9133-45, 2003 Oct 08.
Artigo em Inglês | MEDLINE | ID: mdl-14534247

RESUMO

Genetic studies of sup-9, unc-93, and sup-10 strongly suggest that these genes encode components of a multi-subunit protein complex that coordinates muscle contraction in Caenorhabditis elegans. We cloned sup-9 and sup-10 and found that they encode a two-pore K+ channel and a novel transmembrane protein, respectively. We also found that UNC-93 and SUP-10 colocalize with SUP-9 within muscle cells, and that UNC-93 is a member of a novel multigene family that is conserved among C. elegans, Drosophila, and humans. Our results indicate that SUP-9 and perhaps other two-pore K+ channels function as multiprotein complexes, and that UNC-93 and SUP-10 likely define new classes of ion channel regulatory proteins.


Assuntos
Proteínas de Caenorhabditis elegans/metabolismo , Caenorhabditis elegans/fisiologia , Proteínas de Membrana/metabolismo , Contração Muscular/fisiologia , Proteínas Musculares/metabolismo , Canais de Potássio de Domínios Poros em Tandem , Canais de Potássio/metabolismo , Sequência de Aminoácidos , Animais , Caenorhabditis elegans/efeitos dos fármacos , Proteínas de Caenorhabditis elegans/genética , Clonagem Molecular , Éxons , Agonistas GABAérgicos/farmacologia , Proteínas Ativadoras de GTPase/genética , Proteínas de Fluorescência Verde , Íntrons , Proteínas Luminescentes/biossíntese , Proteínas Luminescentes/genética , Proteínas de Membrana/genética , Dados de Sequência Molecular , Atividade Motora/efeitos dos fármacos , Atividade Motora/genética , Atividade Motora/fisiologia , Muscimol/farmacologia , Contração Muscular/efeitos dos fármacos , Proteínas do Tecido Nervoso/genética , Especificidade de Órgãos/genética , Fenótipo , Canais de Potássio/genética , Subunidades Proteicas/metabolismo , Proteínas de Saccharomyces cerevisiae/genética , Homologia de Sequência de Aminoácidos
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