RESUMEN
Background: The aim of this study was to identify factors associated with high Framingham Risk Score (FRS) in medicated patients with major depressive disorder (MDD). Methods: We examined 61 medicated patients with MDD (mean age 37.77 ± 7.67, 90.2% women) and 43 non-depressed controls (mean age 38.26 ± 9.20, 90.7% women). We administered the Hamilton Depression Rating Scale (HAM-D) and measured systolic blood pressure (SBP), diastolic BP (DBP), mean arterial BP (MAP), pulse wave velocity (PWV), intima-media thickness (IMT), interleukin-6 (IL-6) and triglycerides. Results: We found that medicated patients with MDD had significantly higher levels of HAM-D score (p < 0.01), SBP (p = 0.015), MAP (p = 0.037), IL-6 level (p = 0.007), as compared with controls. Medicated patients who remained moderately to severely depressed showed significantly higher SBP (p = 0.049), DBP (p = 0.009), MAP (p = 0.024), IL-6 level (p = 0.019), left PWV (p = 0.004) and average PWV (p = 0.026) than those with mild depression. Multivariate regression showed that the interaction effect between HAM-D score and triglyceride level (p = 0.018) was significantly associated with FRS in medicated patients with MDD. Conclusions: This study highlights that the interaction effect of the severity of depression and the triglyceride level, was a modifiable factor positively associated with high FRS.
Asunto(s)
Enfermedad de la Arteria Coronaria/etiología , Trastorno Depresivo Mayor/complicaciones , Adulto , Antidepresivos/uso terapéutico , Estudios de Casos y Controles , Enfermedad de la Arteria Coronaria/diagnóstico , Estudios Transversales , Trastorno Depresivo Mayor/diagnóstico , Trastorno Depresivo Mayor/tratamiento farmacológico , Trastorno Depresivo Mayor/fisiopatología , Femenino , Humanos , Masculino , Persona de Mediana Edad , Escalas de Valoración Psiquiátrica , Factores de Riesgo , Índice de Severidad de la EnfermedadRESUMEN
A cDNA fragment (FaPR4) encoding a class I pathogenesis-related protein 4 (PR-4) from Ficus awkeotsang was obtained by PCR cloning. Plant PR-4s were grouped into class I and II, differing by the presence of ChtBD and hinge. The predicted mature FaPR4 comprises N-terminal chitin-binding domain (ChtBD), hinge, Barwin domain and C-terminal extension. FaPR4-C, an N-terminal truncated form of FaPR4, was designed to mimic the structural feature of class II PR-4s. FaPR4 and FaPR4-C were over-expressed in yeast Pichia pastoris, and both recombinants exhibited RNase and anti-fungal activities. To our knowledge, it is the first report that FaPR4, a member of class I PR-4s has RNase activity as class II. FaPR4 possesses better anti-fungal activities toward Fusarium oxysporum and Sclerotium rolfsii than FaPR4-C. Heat-treated FaPR4 remained RNase and anti-fungal activities; while heat-treated FaPR4-C lost those activities. Therefore, ChtBD of FaPR4 may not only contribute to its anti-fungal but also improve the thermal stability of protein. It also implied the correlation of RNase activity with anti-fungal activity of FaPR4-C. Furthermore, FaPR4 was detected to have weak but significant chitinase activity, and its chitinase activity was reduced after heat treatment. The chitinase activity by FaPR4-C was much lower than FaPR4.
Asunto(s)
Antifúngicos/farmacología , Quitina/metabolismo , Ficus/química , Hongos/efectos de los fármacos , Expresión Génica , Proteínas de Plantas/farmacología , Ribonucleasas/farmacología , Secuencia de Aminoácidos , Antifúngicos/metabolismo , Quitinasas/metabolismo , Clonación Molecular , ADN Complementario , Fusarium/efectos de los fármacos , Calor , Datos de Secuencia Molecular , Pichia/metabolismo , Proteínas de Plantas/genética , Proteínas de Plantas/metabolismo , ARN/metabolismo , Ribonucleasas/genética , Ribonucleasas/metabolismo , Semillas/químicaRESUMEN
Adlay (Coix lachryma-jobi L. var. ma-yuen Stapf) is regarded as a nutritive food source as well as herbal medicine. The food nutrition is a consequence of its high protein content and superior amino acid composition. From ca. 200 expressed sequence tag (EST) sequences in maturing adlay grains, clones encoding precursor polypeptides of 10 seed storage proteins in the prolamin family, including 8 alpha-coixin isoforms, 1 delta-coixin, and 1 gamma-coixin, were identified. Full-length cDNA fragments encoding these 10 coixins were obtained by PCR cloning. Mass spectrometric analyses confirmed the presence of these 10 coixins in the extract of adlay grain. Calculated amino acid compositions indicate that all 10 coixins are rich in glutamine (>20% in alpha-coixin isoforms, 13.3% in delta-coixin, and 31.2% in gamma-coixin). The 8 alpha-coixin isoforms are low in methionine, cysteine, and lysine (on average, 0.8, 0.6, and 0.1%, respectively). However, the delta-coixin is a sulfur-rich protein (18.2% methionine and 9.1% cysteine), and the gamma-coixin is a nutritive protein composed of 2.0% methionine, 6.6% cysteine, 2.6% lysine, and 8.9% histidine. The company of delta-coixin and gamma-coixin with alpha-coixin isoforms enhances the nutritional value of alday grain for human consumption.
Asunto(s)
Clonación Molecular , Coix/química , Espectrometría de Masas , Valor Nutritivo , Proteínas de Plantas/química , Proteínas de Plantas/genética , Secuencia de Aminoácidos , Aminoácidos/análisis , ADN Complementario/genética , ADN de Plantas/análisis , ADN de Plantas/genética , Datos de Secuencia Molecular , Reacción en Cadena de la Polimerasa , Semillas/química , Alineación de SecuenciaRESUMEN
Thin-layer chromatography analysis revealed that the contents stored in oil bodies isolated from jelly fig (Ficus awkeotsang Makino) achenes were mainly neutral lipids (>90% triacylglycerols and approximately 5% diacylglycerols). Fatty acids released from the neutral lipids of achene oil bodies were highly unsaturated (62.65% alpha-linolenic acid, 18.24% linoleic acid, and 10.62% oleic acid). The integrity of isolated oil bodies was presumably maintained via electronegative repulsion and steric hindrance provided by their surface proteins. Immunological cross-recognition using antibodies against sesame oil-body proteins indicated that two oleosin isoforms and one caleosin were present in these oil bodies. MALDI-MS analyses confirmed that the three full-length cDNA fragments obtained by PCR cloning from maturing achenes encoded the two jelly fig oleosin isoforms and one caleosin identified by immunological screening.
Asunto(s)
Ficus/metabolismo , Cuerpos de Inclusión/metabolismo , Aceites de Plantas/metabolismo , Semillas/metabolismo , Secuencia de Aminoácidos , Western Blotting , Cromatografía en Capa Delgada , Diglicéridos/química , Diglicéridos/metabolismo , Electroforesis en Gel de Poliacrilamida , Ácidos Grasos/química , Ácidos Grasos/metabolismo , Ficus/genética , Cuerpos de Inclusión/química , Ácido Linoleico/química , Ácido Linoleico/metabolismo , Datos de Secuencia Molecular , Ácido Oléico/química , Ácido Oléico/metabolismo , Aceites de Plantas/química , Proteínas de Plantas/química , Proteínas de Plantas/genética , Proteínas de Plantas/metabolismo , Reacción en Cadena de la Polimerasa , Isoformas de Proteínas/química , Isoformas de Proteínas/genética , Isoformas de Proteínas/metabolismo , Semillas/genética , Homología de Secuencia de Aminoácido , Espectrometría de Masa por Láser de Matriz Asistida de Ionización Desorción , Triglicéridos/química , Triglicéridos/metabolismo , Ácido alfa-Linolénico/química , Ácido alfa-Linolénico/metabolismoRESUMEN
Seed storage proteins of plants commonly comprise several groups of multiple isoforms encoded by gene families. From about 300 expressed sequence tag (EST) clones in maturing jelly fig (Ficus awkeotsang Makino) achenes, gene families encoding precursor polypeptides of two storage protein classes, including six 11S globulin isoforms and two 2S albumin isoforms, were identified. Complete sequences encoding the precursor polypeptides of these eight storage proteins were obtained by sequencing the pertinent EST clones that contained full-length cDNA fragments. Matrix-assisted laser desorption/ionization mass spectrometry analysis confirmed the presence of these storage protein isoforms in the extract of jelly fig achenes resolved in SDS-PAGE. The amino acid compositions of the deduced storage proteins indicated that achene proteins in jelly fig are nutritive, for both isoforms of 2S albumin are sulfur-rich, and one of them is also rich in tryptophan.
Asunto(s)
Albúminas/genética , Ficus/genética , Globulinas/genética , Familia de Multigenes , Albúminas/química , Secuencia de Aminoácidos , ADN Complementario , Electroforesis en Gel de Poliacrilamida , Etiquetas de Secuencia Expresada , Genes de Plantas , Globulinas/química , Datos de Secuencia Molecular , Homología de Secuencia de Aminoácido , Espectrometría de Masa por Láser de Matriz Asistida de Ionización DesorciónRESUMEN
Jelly curd used for a popular summer drink in Taiwan is prepared by extracting the pericarpial portion of jelly fig (Ficus awkeotsang Makino) achenes. The two most abundant proteins found in jelly curd have been identified as a pectin methylesterase and a chitinase. A method was developed to purify the next abundant protein by 40% ammonium sulfate precipitation and flowing through Mono Q chromatography. In sodium dodecyl sulfate-polyacrylamide gel electrophoresis analyses, the purified protein migrated as a polypeptide of 20 kDa in the absence of beta-mercaptoethanol but split into a minor polypeptide of 20 kDa and a major polypeptide of 27 kDa in the presence of this reducing agent. Two cDNA fragments encoding precursor polypeptides of two putative thaumatin-like protein isoforms were obtained by polymerase chain reaction cloning and subsequently overexpressed in Escherichia coli to generate recombinant proteins for antibody preparations. Immunological detection and mass spectrometric analyses indicated that the two split polypeptides were thaumatin-like protein isoforms encoded by the two cloned cDNA fragments.