Respiration of the air breathing fishPiabucina festae

Summary Piabucina festae, a Central American stream fish, breathes air frequently, even in air saturated water, however, is not an obligate air breather. Without access to air, it can maintain routine by aquatic respiration down to aP _wO₂ of about 70 Torr which is its critical O₂ tension (P _cO₂, Fig. 5). Aerial respiration averages 10% of total in air saturated water and 70% in hypoxic water (Fig. 4). At lowP _wO₂ air breathing is more frequent (Fig. 1), and more O₂ is utilized from each air breath (Table 3), and tidal volume may increase (Fig. 7). Vascularized respiratory compartments or cells (Fig. 6), located in the second chamber of the physostomus gas bladder, function for aerial respiration. In ventilation air is gulped and forced through a large pneumatic duct into the gas bladder, excess gas is then released through opercula. Inspiration always precedes expiration and tidal volume is small, keeping gas bladderP _{O 2} low (Table 4). Major differences in the air breathing physiology ofP. festae and other species are its higherP _cO₂, a low aerial in normoxic water, even though air gulps are frequent, and its pattern of inhalation prior to expiration. The interrelationship and optimization of the three gas bladder functions (buoyancy, sound reception, and air breathing) inP. festae is discussed. Aerial respiration may have evolved secondarily to the gas bladder's function in buoyancy control.     

Sesquiterpenes of thalloid liverworts of the genera Conocephalum,Lunularia, Metzgeria and Riccardia

Thalloid liverworts of orders Metzgeriales and Marchantiales elaborate essential oils distinguishable from those of the Jungermanniales by the absence of β-barbatene and anastreptene. Riccardia sinuata elaborates a novel tricyclic exomethylene sesquiterpene of as yet undetermined structure. Conocephalum conicum elaborates cadinene-type sesquiterpenes. β-Cadinene from the latter species is clearly enantiomeric to the same product from vascular plants.     

Interaction of methotrexate with polycationic carriers

Binding parameters were measured for the $\text{in vitro}$ interaction of methotrexate with poly-L-lysine and diethylaminoethyl dextran. The complexes were found to have apparent affinity constants of 2590 and 440 M^?1 respectively at 37°, ionic strength 0.02. For hypotonic solutions containing therapeutic concentrations of methotrexate, this results in 87% binding of the drug to poly-L-lysine and 74% to diethylaminoethyl dextran. While the binding decreased to about 50% upon increasing ionic strength to physiologic levels, sufficient drug-carrying capacity was retained at isotonicity to support the potential utility of such complexes as tissue-specific drug carriers.     

The integrin complex alpha v beta 3 participates in the adhesion of microvascular endothelial cells to fibronectin.

Fibronectin is a major adhesive glycoprotein of the vascular basement membrane. Since fibronectin is also found in the interstitium, it may be important not only for attachment but also for endothelial cell migration during neovascularization. We have analyzed how human dermal microvascular endothelial cells use their diverse set of integrin receptors to interact with this ligand. Immunofluorescent staining with specific antibodies identified both beta 1 and beta 3 integrin receptor complexes in focal adhesion plaques on cells adhering to immobilized fibronectin. Adhesion assays with blocking monoclonal antibodies implicated both beta 1 and beta 3 complexes, specifically alpha 5 beta 1 and alpha v beta 3, in the initial adhesion of cells to fibronectin. Finally, ligand affinity chromatography of extracts of surface radiolabeled cells established that both alpha 5 beta 1 and alpha v beta 3 could bind to the 110-kDa cell-binding fragment of fibronectin. An additional receptor complex composed of an alpha v subunit and a beta 5-like subunit was also detected. These results provide evidence that microvascular endothelial cells use multiple integrin receptors, from several beta families, to attach to fibronectin surfaces.     

Mechanism of human keratinocyte migration on fibronectin: unique roles of RGD site and integrins.

The migration of human keratinocytes over the wound bed plays an important role in the re-epithelialization of cutaneous wounds. Fibronectin, a large glycoprotein matrix component that is abundant within cutaneous wound beds, promotes keratinocyte migration. However, the mechanisms by which keratinocytes migrate over fibronectin are unknown. In this study, we sought to identify specific sites within the fibronectin molecule that induce keratinocyte locomotion and to characterize the cell surface receptors involved. The data show that the domain within the fibronectin molecule that induces human keratinocyte migration is the 120 kD cell-binding domain close to the carboxyl terminus. The 40 kD heparin-binding domain near the carboxyl terminus and the 45 kD gelatin-binding domain near the amino terminus did not promote keratinocyte migration. In addition, keratinocyte migration on both fibronectin and the 120 kD cell-binding domain was completely inhibited by the presence of GRGDSP peptide, suggesting that keratinocyte migration on fibronectin is mediated by recognizing the RGD sequence located within the cell-binding domain of fibronectin. Furthermore, keratinocytes were able to migrate directly on immobilized RGD substratum. Cell migration on fibronectin is mediated by the alpha 5 beta 1 integrin since antibodies blocking the alpha 5 and the beta 1 subunits completely inhibited keratinocyte migration on fibronectin. In addition, we demonstrate that human keratinocytes express alpha 5 beta 1 integrin in culture by flow cytometry.