RESUMEN
Seed mucilage polysaccharide production, storage and release in Plantago ovata is strikingly different to that of the model plant Arabidopsis. We have used microscopy techniques to track the development of mucilage secretory cells and demonstrate that mature P. ovata seeds do not have an outer intact cell layer within which the polysaccharides surround internal columellae. Instead, dehydrated mucilage is spread in a thin homogenous layer over the entire seed surface and upon wetting expands directly outwards, away from the seed. Observing mucilage expansion in real time combined with compositional analysis allowed mucilage layer definition and the roles they play in mucilage release and architecture upon hydration to be explored. The first emergent layer of hydrated mucilage is rich in pectin, extremely hydrophilic, and forms an expansion front that functions to 'jumpstart' hydration and swelling of the second layer. This next layer, comprising the bulk of the expanded seed mucilage, is predominantly composed of heteroxylan and appears to provide much of the structural integrity. Our results indicate that the synthesis, deposition, desiccation, and final storage position of mucilage polysaccharides must be carefully orchestrated, although many of these processes are not yet fully defined and vary widely between myxospermous plant species.
Asunto(s)
Mucílago de Planta/metabolismo , Plantago/fisiología , Semillas/fisiología , Pared Celular/metabolismo , Técnica del Anticuerpo Fluorescente , Fenotipo , Desarrollo de la Planta , Plantago/ultraestructura , Semillas/ultraestructuraRESUMEN
Many plants translocate sugar alcohols in the phloem. However, the mechanism(s) of sugar alcohol loading in the minor veins of leaves are debated. We characterized the loading strategies of two species that transport sorbitol (Plantago major and apple [Malus domestica]), and one that transports mannitol (Asarina scandens). Plasmodesmata are abundant at all interfaces in the minor vein phloem of apple, and in one of two types of phloem in the minor veins of A. scandens. Few plasmodesmata are present in the minor veins of P. major. Apple differs from the other two species in that sugar alcohol and sucrose (Suc) are present in much higher concentrations in leaves. Apple leaf tissue exposed to exogenous [(14)C]sorbitol, [(14)C]Suc, or (14)CO(2) did not accumulate radiolabel in the minor veins, as determined by macroautoradiography. P. major minor veins accumulated radiolabel from [(14)C]Suc, [(14)C]sorbitol, and (14)CO(2). A. scandens minor veins accumulated (14)C from [(14)C]Suc and (14)CO(2), but not from [(14)C]mannitol. We conclude that the movement of sugar alcohol from the mesophyll into the phloem in apple and A. scandens is symplastic and passive, but in P. major it involves an apoplastic step and is energized. We also suggest that apple leaves transport sorbitol in high concentrations to avoid the feedback limitation of photosynthesis that would result from driving passive movement of solute into the phloem with high levels of Suc alone. The loading pathways and the mechanisms by which hydrostatic pressure is maintained in the minor vein phloem of these species are discussed.
Asunto(s)
Magnoliopsida/metabolismo , Malus/metabolismo , Floema/metabolismo , Plantago/metabolismo , Alcoholes del Azúcar/metabolismo , Autorradiografía , Transporte Biológico , Magnoliopsida/ultraestructura , Malus/ultraestructura , Modelos Biológicos , Floema/ultraestructura , Hojas de la Planta/citología , Hojas de la Planta/metabolismo , Plantago/ultraestructura , Plasmodesmos/ultraestructuraRESUMEN
Comestible fruit production from Musaceas plants is an important economical activity in developing countries like Colombia. However, it generates a large amount of agro-industrial residues. Some of them are a potential resource of natural fibres, which can be used as reinforcement for composite materials. In this work, a series of commercial plantain (Musa AAB, cv "Dominico Harton") fibre bundles extracted from pseudostem, leaf sheath and rachis agricultural wastes were analyzed. Mechanical decortication and biological retting processes were used during fiber extraction. No significant differences in composition of vascular bundles were observed for both extraction processes. Gross morphological characteristics and mechanical behavior have been evaluated. Conducting tissues with spiral-like arrangement are observed attached to fibre bundles. This fact suggests a big amount of these tissues in commercial plantain plants. Both used extraction methods are not enough to remove them. Pseudostem fibre bundles have higher specific strength and modulus and lower strain at break than leaf sheath and rachis fibre bundles, having values comparable to other lignocellulosic fibres bundles.
Asunto(s)
Productos Agrícolas/anatomía & histología , Residuos Industriales , Plantago/anatomía & histología , Colombia , Hojas de la Planta/citología , Hojas de la Planta/ultraestructura , Tallos de la Planta/citología , Tallos de la Planta/ultraestructura , Plantago/citología , Plantago/ultraestructura , Espectroscopía Infrarroja por Transformada de FourierRESUMEN
BACKGROUND: English plantain (Plantago lanceolata L.) and olive (Olea europaea L.) pollens are important causes of pollinosis in large areas of North America, Australia, and the Mediterranean basin. The major pollen allergens of both plants, Pla I 1 and Ole e 1, share 38.7% of their amino acid sequences. OBJECTIVE: To analyze putative cross-reactivity between these 2 proteins. METHODS: Several antibodies and patients' sera were used in immunoblot and immunocytochemistry experiments. RESULTS: Two anti-Pla I 1 antibodies were able to bind to 3 polypeptides from olive pollen protein extracts, which correspond to the 3 glycosylation isoforms of Ole e 1 (18-22 kDa) previously described. Moreover, Pla I 1 protein was found in the cytoplasm of both the vegetative and the generative cells of P lanceolata mature pollen. On olive pollen sections, these anti-Pla I 1 antibodies displayed significant labeling in the cytoplasm of the vegetative cell and in both the exine and the material adhering to this outer layer of the pollen wall. In addition, the anti-Ole e 1 antibody 10H1 was found to cross-react with proteins of similar masses (16-20 kDa) to Pla I 1 variants. In Plantago pollen sections, the 10H1 antibody recognized proteins located in the cytoplasm of both the vegetative and generative cells. Cross-reaction was confirmed using sera from patients allergic to either plant pollen. CONCLUSION: Both allergens share common epitopes, which can be cross-recognized by different antibodies and sera from different patients, although this antigenic similarity seems to have little clinical relevance.
Asunto(s)
Alérgenos/inmunología , Glicoproteínas/inmunología , Olea/inmunología , Proteínas de Plantas/inmunología , Plantago/inmunología , Polen/inmunología , Alérgenos/análisis , Antígenos de Plantas , Reacciones Cruzadas , Ensayo de Inmunoadsorción Enzimática , Epítopos , Glicoproteínas/análisis , Humanos , Microscopía Electrónica de Transmisión , Olea/ultraestructura , Proteínas de Plantas/análisis , Plantago/ultraestructura , Polen/ultraestructuraRESUMEN
A combined light- and electron-microscopic examination of chromosomes from two angiospermous plants, Plantago ovata and Lycopersicon esculentum, and a mammal, Mus musculus, was performed. From this investigation three observations have been made that may be relevant to the observed lack of crossing over in heterochromatin. (1) Differential staining indicates that heterochromatin represents a smaller fraction of the length of pachytene chromosomes than it represents in the length of mitotic metaphase chromosomes. Since the synaptonemal complex (SC) runs throughout the length of these pachytene chromosomes, it is under-represented in heterochromatin. Considering the evidence for a rough correlation between the length of SC and the amount of crossing over, this could result in less crossing over in heterochromatin than expected on the basis of its length in mitotic metaphase chromosomes. (2) Electron microscopy indicates that, unlike the SC in euchromatin, the SC in heterochromatin is densely ensheathed in highly compact chromatin. If crossing over occurs in the SC or even in the surrounding chromatin, the compaction of the chromatin may prevent the penetration of enzymes needed in recombination. (3) Finally, a difference in the structure of SCs in euchromatin versus heterochromatin was observed that could be associated with the lack of crossing over in heterochromatin.