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1.
Biochim Biophys Acta ; 1770(4): 617-29, 2007 Apr.
Artigo em Inglês | MEDLINE | ID: mdl-17184920

RESUMO

A rhamnose-binding glycoprotein (lectin), named SML, was isolated from the eggs of Spanish mackerel (Scomberomorous niphonius) by affinity and ion-exchange chromatographies. SML was composed of a non-covalently linked homodimer. The SML subunit was composed of 201 amino acid residues with two tandemly repeated domains, and contained 8 half-Cys residues in each domain, which is highly homologous to the N-terminal lectin domain of calcium-independent alpha-latrotoxin receptor in mammalian brains. Each domain has the same disulfide bonding pattern; Cys10-Cys40, Cys20-Cys99, Cys54-Cys86 and Cys67-Cys73 were located in the N-terminal domain, and Cys108-Cys138, Cys117-Cys195, Cys152-Cys182 and Cys163-Cys169 were in the C-terminal domain. SML was N-glycosylated at Asn168 in the C-terminal domain. The structure of the sugar chain was determined to be NeuAc-Galbeta1-4GlcNAcbeta1-2Manalpha1-6-(NeuAc-Galbeta1-4GlcNAcbeta1-2Manalpha1-3)Manbeta1-4GlcNAcbeta1-4GlcNAc-Asn.


Assuntos
Proteínas de Peixes/química , Glicoproteínas/química , Hemaglutininas/química , Lectinas/química , Óvulo/química , Perciformes/metabolismo , Processamento de Proteína Pós-Traducional , Sequência de Aminoácidos , Animais , Sequência de Carboidratos , Cromatografia de Afinidade , Cromatografia Líquida de Alta Pressão , Cromatografia por Troca Iônica , Dissulfetos/química , Dissulfetos/metabolismo , Proteínas do Ovo/química , Proteínas do Ovo/metabolismo , Proteínas de Peixes/isolamento & purificação , Proteínas de Peixes/metabolismo , Glicoproteínas/isolamento & purificação , Glicoproteínas/metabolismo , Glicosilação , Hemaglutininas/isolamento & purificação , Hemaglutininas/metabolismo , Lectinas/isolamento & purificação , Lectinas/metabolismo , Dados de Sequência Molecular , Conformação Proteica , Subunidades Proteicas , Alinhamento de Sequência , Análise de Sequência de Proteína , Espectrometria de Massas por Ionização e Dessorção a Laser Assistida por Matriz
2.
Biofactors ; 25(1-4): 175-8, 2005.
Artigo em Inglês | MEDLINE | ID: mdl-16873943

RESUMO

We have already shown that prolonged supplementation of CoQ(10) in humans reduces the wrinkle area rate and wrinkle volume per unit area in the corner of the eye. CoQ(10) supplementation is known to increase the CoQ(10) level in serum and in many organs; however, the level of CoQ(10) in skin has not yet been fully investigated yet. We examined whether CoQ(10) intake elevates the CoQ(10) and CoQ(9) levels in epidermis, dermis, serum and other organs (kidney, heart, brain, muscle and crystalline lens) in 43-week-old hairless male mice. We also established a method using a high performance liquid chromatograph equipped with an electrochemical detector (HPLC-ECD) to simultaneously quantify CoQ(9) and CoQ(10) in the tissues. CoQ(10) (0, 1, 100 mg/kg p.o.) was administered daily for 2 weeks. CoQ(10) supplementation of 100 mg/kg increased the serum and epidermal CoQ(10) levels significantly, but did not increase the CoQ(10) levels in either dermis or other organs. In conclusion, we showed that CoQ(10) intake elevates the epidermal CoQ(10) level, which may be a prerequisite to the reduction of wrinkles and other benefits related to the potent antioxidant and energizing effects of CoQ(10) in skin.


Assuntos
Epiderme/química , Ubiquinona/análogos & derivados , Administração Oral , Animais , Coenzimas , Epiderme/efeitos dos fármacos , Masculino , Camundongos , Camundongos Pelados , Distribuição Tecidual , Ubiquinona/administração & dosagem , Ubiquinona/metabolismo , Ubiquinona/farmacologia
3.
Biofactors ; 35(5): 435-41, 2009.
Artigo em Inglês | MEDLINE | ID: mdl-19753652

RESUMO

Coenzyme Q10 (CoQ10), which has both energizing and anti-oxidative effects, is also reported to have antiaging action, e.g., reducing the area of facial wrinkles. However, the mechanism of its anti-aging activity is not fully established. Here, we examined the effect of CoQ10 on human dermal and epidermal cells. CoQ10 promoted proliferation of fibroblasts but not keratinocytes. It also accelerated production of basement membrane components, i.e., laminin 332 and type IV and VII collagens, in keratinocytes and fibroblasts, respectively; however, it had no effect on type I collagen production in fibroblasts. CoQ10 also showed protective effects against cell death induced by several reactive oxygen species in keratinocytes, but only when its cellular absorption was enhanced by pretreatment of the cells with highly CoQ10-loaded serum. These results suggest that protection of epidermis against oxidative stress and enhancement of production of epidermal basement membrane components may be involved in the antiaging properties of CoQ10 in skin.


Assuntos
Membrana Basal/fisiologia , Morte Celular/efeitos dos fármacos , Derme/metabolismo , Epiderme/metabolismo , Estresse Oxidativo/efeitos dos fármacos , Ubiquinona/análogos & derivados , Amidinas/farmacologia , Moléculas de Adesão Celular/biossíntese , Proliferação de Células/efeitos dos fármacos , Colágeno Tipo IV/biossíntese , Colágeno Tipo VII/biossíntese , Derme/citologia , Células Epidérmicas , Fibroblastos/citologia , Fibroblastos/efeitos dos fármacos , Humanos , Peróxido de Hidrogênio/farmacologia , Queratinócitos/citologia , Queratinócitos/efeitos dos fármacos , Masculino , Ubiquinona/fisiologia , Calinina
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