Effects of starvation and time of day on crayfish foraging behaviors

Crayfish foraging behaviors can alter aquatic ecosystems. Starvation and time of day are two potential factors that can influence those foraging behaviors, but the interaction between the two variables has not been studied. In this study, we observed the movement of fed and starved crayfish during the day and at night in the presence of both water and food odor. We calculated both total movement and change in movement and predicted more activity when starved and at night. Crayfish did not show a preference for day or night, nor did they display significantly more movement when fed or starved. These results do not match previous literature, meaning that further research on these factors is necessary, especially in Cambarus acuminatus

Relocation of active acetylcholinesterase to liposome-gel conjugate

ArticleJOURNAL OF COLLOID AND INTERFACE SCIENCE. 307(1): 296-299 (2007)journal articl

Structure and thermal history dependant phase behavior of hydrated synthetic sphingomyelin analogue: 1,2-dimyristamido-1,2-deoxyphosphatidylcholine

The physical properties of hydrated multilamellar sample of 1,2-dimyristamido-1,2-deoxyphosphatidylcholine (DDPC) were investigated by means of differential scanning calorimetry (DSC), static X-ray diffraction, and simultaneous DSC and X-ray diffraction. The DDPC is a synthetic sphingomyelin analogue and has two amide bonds in its hydrophobic parts. This paper reports on metastable phase behavior of the hydrated DDPC sample. By cooling from a chain-melted state at the rates of greater than 4 oC min-1, hydrated DDPC bilayers form a metastable gel phase. In the gel phase, the hydrophobic chains are tilted with respect to the bilayer normal, as like the gel phase of glycero-phosphatidylcholines. By heating, the metastable gel phase is transformed in to a stable phase associated with an exothermic heat event at 18.3 oC (DH = 14.6 kJ mol-1) and then the stable phase is transformed into a liquid-crystalline phase at 25.6 oC (DH = 42 kJ mol-1). The incubation at 17 oC for more than 1 hour also induces the formation of the stable phase. In the stable phase, the hydrophobic chains are packed into highly ordered crystal-like structure. However, the X-ray diffraction pattern of the stable phase suggested that the entire DDPC molecules do not form a two-dimensional molecular ordered lattice, differing from normal subgel phase of glycero-phosphatidylcholines. The structure and phase behavior of DDPC revealed by the present study are discussed from the viewpoint of hydrogen bonds

Configuration of the active Mg-ATP complex in protein kinase C reaction

AbstractTo probe the active site structure of protein kinase C stereochemical studies were carried out by using ATPβs. The enzyme utilizes either one of the diastereomers (Sp and Rp) of ATPβs almost equally well as a substrate. This result contrasts with that for cyclic AMP-dependent protein kinase, suggesting that the topography of the nucleotide-binding site is significantly different between the two kinases

Immobilization of liposomes on hydrophobically modified polymer gel particles in batch mode interaction

ArticleCOLLOIDS AND SURFACES B-BIOINTERFACES. 55(2): 235-240 (2007)journal articl

HIV-1 expression induces cyclin D(1) expression and pRb phosphorylation in infected podocytes: cell-cycle mechanisms contributing to the proliferative phenotype in HIV-associated nephropathy

BACKGROUND: The aberrant cell-cycle progression of HIV-1-infected kidney cells plays a major role in the pathogenesis of HIV-associated nephropathy, however the mechanisms whereby HIV-1 induces infected glomerular podocytes or infected tubular epithelium to exit quiescence are largely unknown. Here, we ask whether the expression of HIV-1 genes in infected podocytes induces cyclin D(1) and phospho-pRb (Ser780) expression, hallmarks of cyclin D1-mediated G(1) → S phase progression. RESULTS: We assessed cyclin D(1) and phospho-pRb (Ser780) expression in two well-characterized models of HIV-associated nephropathy pathogenesis: HIV-1 infection of cultured podocytes and HIV-1 transgenic mice (Tg26). Compared to controls, cultured podocytes expressing HIV-1 genes, and podocytes and tubular epithelium from hyperplastic nephrons in Tg26 kidneys, had increased levels of phospho-pRb (Ser780), a target of active cyclin D(1)/cyclin-dependent kinase-4/6 known to promote G(1) → S phase progression. HIV-1-infected podocytes showed markedly elevated cyclin D(1) mRNA and cyclin D(1) protein, the latter of which did not down-regulate during cell-cell contact or differentiation, suggesting post-transcriptional stabilization of cyclin D(1) protein levels by HIV-1. The selective suppression of HIV-1 transcription by the cyclin-dependent kinase inhibitor, flavopiridol, abrogated cyclin D(1) expression, underlying the requirement for HIV-1 encoded products to induce cyclin D(1). Indeed, HIV-1 virus deleted of nef failed to induce cyclin D(1) mRNA to the level of other single gene mutant viruses. CONCLUSIONS: HIV-1 expression induces cyclin D(1) and phospho-pRb (Ser780) expression in infected podocytes, suggesting that HIV-1 activates cyclin D1-dependent cell-cycle mechanisms to promote proliferation of infected renal epithelium

Catalytic Efficiency of [20]Paracyclophane Oxime and Cycloheptaamylose in the Decomposition of Carboxylate and Carbonate Esters

The hydrolytic decomposition of dodecyl ρ-nitrophenyl carbonate (LPNC) and ρ-nitrophenyl dodecanoate (PNPL) as mediated by 10-hydroxy-ll-hydroxyimino[20]-paracyclophane (Oxime-I) and cycloheptaamylose (β-CD) has been investigated in aqueous media containing 9.9% (v/v) ethanol and 1.0% (v/v) acetonitrile to gain an insight into the reaction and/or substrate specificity. Both LPNC and PNPL were decomposed effectively by an equimolar amount of Oxime-I. It turned out from the analysis of kinetic data that the binding of LPNC to Oxime-I is 2.5 times tighter than that of PNPL, but the subsequent catalysis is 3.3 times more favorable for PNPL than for LPNC. Hence, the overall efficiency of Oxime-I is 1.3 times greater for PNPL, as changed from a 13-fold difference between both substrates in the simple alkaline hydrolysis. β-CD was found to be effective also in the decomposition of LPNC when added in large excess over substrate. Comparison of kinetic parameters between the two systems, Oxime-I and β-CD, indicated that the former is better in both binding and catalytic effects toward the extremely hydrophobic substrates

Antisense oligonucleotide inhibition of Heat Shock Protein (HSP) 47 improves bleomycin-induced pulmonary fibrosis in rats

<p>Abstract</p> <p>Background</p> <p>The most common pathologic form of pulmonary fibrosis arises from excessive deposition of extracellular matrix proteins such as collagen. The 47 kDa heat shock protein 47 (HSP47) is a collagen-specific molecular chaperone that has been shown to play a major role during the processing and/or secretion of procollagen.</p> <p>Objectives</p> <p>To determine whether inhibition of HSP47 could have beneficial effects in mitigating bleomycin-induced pulmonary fibrosis in rats.</p> <p>Methods</p> <p>All experiments were performed with 250–300 g male Wistar rats. Animals were randomly divided into five experimental groups that were administered: 1) saline alone, 2) bleomycin alone, 3) antisense HSP47 oligonucleotides alone, 4) bleomycin + antisense HSP47 oligonucleotides, and 5) bleomycin + sense control oligonucleotides. We investigated lung histopathology and performed immunoblot and immunohistochemistry analyses.</p> <p>Results</p> <p>In rats treated with HSP47 antisense oligonucleotides, pulmonary fibrosis was significantly reduced. In addition, treatment with HSP47 antisense oligonucleotides significantly improved bleomycin-induced morphological changes. Treatment with HSP47 antisense oligonucleotides alone did not produce any significant changes to lung morphology. Immunoblot analyses of lung homogenates confirmed the inhibition of HSP47 protein by antisense oligonucleotides. The bleo + sense group, however, did not exhibit any improvement in lung pathology compared to bleomycin alone groups, and also had no effect on HSP47 expression.</p> <p>Conclusion</p> <p>These findings suggest that HSP47 antisense oligonucleotide inhibition of HSP47 improves bleomycin-induced pulmonary fibrosis pathology in rats.</p