The cytoplasmic domain of the cellulose-synthesizing complex in vascular plants.

The cytoplasmic domain of the rosette terminal complex has been imaged in situ in patches of plasma membrane isolated from tobacco BY-2 protoplasts. By partially extracting the plasma membrane lipids, cellulose microfibrils were observed through the plasma membrane. Rosette terminal complexes were identified on the basis of their association with the ends of these cellulose microfibrils. The cytoplasmic domain of the rosette terminal complex has been shown to be hexagonal in shape and has been measured to be 45-50 nm in diameter and 30-35 nm tall. These findings demonstrate that the terminal complex does indeed have a substantial cytoplasmic component, and that the hexagonal array observed in the lipid bilayer by freeze fracture is actually only a small part of the overall complex. These findings will allow better modeling of the terminal complex and may facilitate predictions of how many proteins are associated with the rosette terminal complex in vivo.

A simple technique to minimize heat damage to specimens during thermal polymerization of LR White in plastic and gelatin capsules.

London Resin (LR) White is a commonly used resin for embedding specimens to be used for immuno- and/or cytochemical studies. In some instances, due to either the properties of the specimen or the availability of various reagents and equipment, it becomes necessary and/or more convenient to polymerize LR White using heat rather than chemical accelerators or UV light. It is known, however, that heat can reduce or even eliminate the anti genicity of the tissue being embedded. It is therefore desirable to polymerize specimens at the lowest temperature possible and to remove the specimens from the oven as soon as polymerization is complete. We have developed a technique that provides a visual marker that allows the exothermic polymerization of LR White to be monitored, thus minimizing the amount of time a specimen must stay in the oven while excluding oxygen from capsules of polymerizing LR White.

Structural and immunocytochemical characterization of the adhesive tendril of Virginia creeper (Parthenocissus quinquefolia [L.] Planch.).

The tendrils of Virginia creeper (Parthenocissus quinquefolia) do not coil around their supports. Rather, they adhere to supporting objects by flattening against the support surface and secreting an adhesive compound which firmly glues the tendril to the support. In this study, microscopic and immunocytochemical techniques were utilized to determine the nature of this adhesive. Following touch stimulation, epidermal cells of the tendril elongate toward the support substrate, becoming papillate in morphology. Following contact with the support surface, an adhesive is produced at the base of the papillate cells. The adhesive appears as a highly heterogeneous, raftlike structure and consists of pectinaceous, rhamnogalacturonan (RG) I-reactive components surrounding a callosic core. In addition, more mobile components, composed of arabinogalactans and mucilaginous pectins, intercalate both the support and the tendril, penetrating the tendril to the proximal ends of the papillate cells. Following adherence to the support, the anticlinal walls of the papillate cells are devoid of RG I side-chain reactivity, indicating that extensive debranching of RG I molecules has taken place. Furthermore, a large amount of RG I backbone reactivity was observed in the contact area. These results may indicate that the debranched RG I molecules diffuse into and permeate the contact region, forming an integral part of the adhesive compound. These results indicate that Virginia creeper adheres to objects by a composite adhesive structure consisting of debranched RG I, callose, and other, less-well characterized mucilaginous pectins and that this structure subsequently becomes lignified and very weather-resistant upon the ultimate senescence of the tendril.