Lipids of the tropical seagrass Thallassia hemprichii

The component sterols, alcohols, hydrocarbons, monocarboxylic, α,ω-dicarboxylic and α- and ω-hydroxy acids from the leaves and roots of the tropical seagrass Thallassia hemprichii are reported. The leaves contained significant concentrations of cholest-5-en-3β-ol, a sterol not normally detected in either higher plants or seagrasses. The lower abundance of polyunsaturated fatty acids found in both the leaves and roots compared to other seagrass species may be a result of the warmer waters from which this species was collected. Solvent-extractable, long-chain (> C₂₂)α,ω-diacids, α- and ω-hydroxy and monocarboxylic acids were also isolated from the leaves. The distribution pattern of these lipids should enable these components along with other distinctive components to be used as chemical markers for this seagrass.     

Immunohistochemical evidence for the NO cGMP signaling pathway in respiratory ciliated epithelia of rat.

Airway epithelia play a crucial role in protecting the lung from the external environment. Ciliated airway epithelial cells contribute to mucociliary transport systems via ciliary beating and electrolyte transport mechanisms to defend against respiratory tract infection. Both of these activities are regulated by nitric oxide (NO)-dependent mechanisms. To better understand the role of the NO-cGMP signal transduction cascade in these responses, we investigated the localization of endothelial nitric oxide synthase (eNOS), soluble guanylyl cyclase (sGC), cGMP-dependent protein kinase (PKG) I-alpha, and PKG I-beta in the tracheas and lungs of normal rats by immunohistochemistry. Mouse anti-eNOS, rabbit anti-sGC, PKG I-alpha, and PKG I-beta antibodies were used. Strong immunostaining for eNOS was detected in ciliated tracheal, bronchial, and bronchiolar epithelia, in Clara cells, and in Type II alveolar cells. The pattern of sGC and PKG I-beta immunostaining showed striking parallels with that of eNOS staining. No staining was detectable in ciliated epithelium with the anti-PKG I-alpha antibody. Taken together, these observations suggest that PKG I-beta might transduce NO-sGC signaling into biological responses in ciliated respiratory epithelia.(J Histochem Cytochem 47:1369-1374, 1999)     

Haplotype diversity of mt<Emphasis Type="Italic">COI</Emphasis> in the fall webworm <Emphasis Type="Italic">Hyphantria cunea</Emphasis> (Lepidoptera: Arctiidae) in introduced regions in China,Iran, Japan,Korea, and its homeland,the United States

Hyphantria cunea (Drury) has colonized many countries outside its native range of North America and has become a model species for studies of the colonization and subsequent adaptation of agricultural pests. Molecular genetic analyses can clarify the origin and subsequent adaptations to non-native habitats. Using the mitochondrial COI gene, we examined the genetic relationships between invasive populations (China, Iran, Japan, and Korea) and native populations (i.e., the United States). The Jilin (China) and Guilan (Iran) populations showed nine previously unknown haplotypes that differed from those found in the south–central United States, suggesting multiple colonization events and different regions of invasion. A dominant mtDNA haplotype in populations in the United States was shared by all of the populations investigated, suggesting that H. cunea with that haplotype have successfully colonized China, Iran, Japan, and Korea.     

Cloning and characterization of E-dlg, a novel splice variant of mouse homologue of the Drosophila discs large tumor suppressor binds preferentially to SAP102

Membrane-associated guanylate kinases (MAGUKs) act as scaffolds to coordinate signaling events through their multiple domains at the plasma membrane. The MAGUK SH3 domain is noncanonical and its function remains unclear. To identify potential binding partners of MAGUK SH3, the synapse-associated protein 102 (SAP102) SH3 domain was used as bait in a yeast two-hybrid screen of a mouse embryonic cDNA library. A mouse homologue of the Drosophila discs large tumor suppressor (Dlg, also known as SAP97) bound preferentially to SAP102 SH3. The 4347bp cDNA sequence encoded an 893 amino acid protein with 94% identity to mouse SAP97. A deleted region (33-aa) strongly suggests this is a novel splice variant, which we call Embryonic-dlg/SAP97 (E-dlg). The interaction of SAP102 and E-dlg was confirmed in mammalian cells. E-dlg can also bind to potassium channel Kv1.4 in a pull-down assay. E-dlg was highly expressed in embryonic and some adult mouse tissues, such as brain, kidney, and ovary. Furthermore, in situ hybridization showed that E-dlg was mostly expressed in olfactory bulb and cerebellum.     

Towards optimum permeability reduction in porous media using biofilm growth simulations

While biological clogging of porous systems can be problematic in numerous processes (e.g., microbial enhanced oil recovery—MEOR), it is targeted during bio‐barrier formation to control sub‐surface pollution plumes in ground water. In this simulation study, constant pressure drop (CPD) and constant volumetric flow rate (CVF) operational modes for nutrient provision for biofilm growth in a porous system are considered with respect to optimum (minimum energy requirement for nutrient provision) permeability reduction for bio‐barrier applications. Biofilm growth is simulated using a Lattice‐Boltzmann (LB) simulation platform complemented with an individual‐based biofilm model (IbM). A biomass detachment technique has been included using a fast marching level set (FMLS) method that models the propagation of the biofilm–liquid interface with a speed proportional to the adjacent velocity shear field. The porous medium permeability reduction is simulated for both operational modes using a range of biofilm strengths. For stronger biofilms, less biomass deposition and energy input are required to reduce the system permeability during CPD operation, whereas CVF is more efficient at reducing the permeability of systems containing weaker biofilms. Biotechnol. Bioeng. 2009;103: 767–779. © 2009 Wiley Periodicals, Inc.