Identification of actin-binding protein as the protein linking the membrane skeleton to glycoproteins on platelet plasma membranes

Platelets have previously been shown to contain a membrane skeleton that is composed of actin filaments, actin-binding protein, and three membrane glycoproteins (GP), GP Ib, GP Ia, and a minor glycoprotein of Mr = 250,000. The present study was designed to determine how the membrane glycoproteins were linked to actin filaments. Unstimulated platelets were lysed with Triton X-100, and the membrane skeleton was isolated on sucrose density gradients or by high-speed centrifugation. The association of the membrane glycoproteins with the actin filaments was disrupted when actin-binding protein was hydrolyzed by activity of the Ca2+-dependent protease, which was active in platelet lysates upon addition of Ca2+ in the absence of leupeptin. Similarly, activation of the Ca2+-dependent protease in intact platelets by the addition of a platelet agonist also caused the membrane glycoproteins to dissociate from the membrane skeleton. Affinity-purified actin-binding protein antibodies immunoprecipitated the membrane glycoproteins from platelet lysates in which actin filaments had been removed by DNase I-induced depolymerization and high-speed centrifugation. These results demonstrate that actin-binding protein links actin filaments of the platelet membrane skeleton to three plasma membrane glycoproteins and that filaments are released from their attachment site when actin-binding protein is hydrolyzed by the Ca2+-dependent protease within intact platelets during platelet activation.     

Some professional and scientific problems and opportunities for biofeedback

This paper will deal with a variety of topics such as dangers and opportunities from the developing crisis in health care costs, a cooperative study of the cost-effectiveness of treatments for headaches, the need for a federation of related societies, exploiting remarkable electronic advances, the wide range of adaptive functions of visceral learning (including its role in homeostasis), why maladjustments occur and their implications for biofeedback, and the need for analytic experiments involving adequate amounts of training.     

Escherichia coli CAN lacks a tRNA-processing nuclease.

Escherichia coli strain CAN is unable to support the growth of bacteriophage T4 strains requiring the suppressor function of T4 tRNASer. Biochemical analysis of the mutant strain revealed that it is deficient in a RNase which acts on the artificial tRNA precursor tRNA-C-U.     

Capillary transport of macromolecules: pores and other endothelial pathways

Can a pore or pore-equivalent model account for transport of macromolecules across microvascular endothelium, or are alternate nonpore pathways necessary? Pores may be defined as aqueous channels of any shape or configuration, including those through a fiber matrix. Such pathways exhibit selective restriction to passage of macromolecules depending on their size, shape, and electrical charge. At least two pore pathways (small and large), differing in both sieve-element spacing and in hydraulic conductivity by an order of magnitude, are required to account for observed size selectivity for plasma proteins of similar shapes and charges. For the two organs examined critically in this review (cat ileum and dog paw), transport of macromolecules through small and large pore pathways is predominately convective. Total transport through small and large pores (alternatively, narrow and wide slits or fine and coarse fiber matrices) is insufficient to account for observed transport rates at low-to-moderate levels of volume flow. Either the estimated pore sizes and hydraulic conductivities derived from measurements of high volume-flow sieving are incorrect or other nonconvective transport pathways contribute substantially to macromolecular transport at low (normal) volume flow.     

Teixeiria lusitanica, a new fossil flower from the Early Cretaceous of Portugal with affinities to Ranunculales

A charcoalified fossil flower bud of a new genus and species (Teixeiria lusitanica) is described from the Early Cretaceous of Portugal. The flower is actinomorphic and unisexually male. At the base of the bud there are several bracts of different sizes, which are followed by sepal-like and petal-like tepals. Bracts and perianth organs seem to be arranged spirally and to exhibit transitions between different organ categories. The androecium has numerous stamens in two sizes, but with unclear arrangement. Pollen is small and tricolpate with a perforate tectum and a densely columellate infratectal layer. No carpels or remains of carpels could be observed on the floral axis. Teixeiria lusitanica shows most affinities to members of Ranunculales. There are also some similarities with Berberidopsis (Berberidopsidaceae, Berberidopsidales) and members of the Saxifragales (Hamamelidaceae and Daphniphyllaceae).