Population genetics information for the regional conservation of a tropical seagrass, <Emphasis Type="Italic">Enhalus acoroides</Emphasis>, around the Guimaras Strait,Philippines

Seagrasses are marine angiosperms and play an essential ecological role in coastal ecosystems; however, seagrass meadows are threatened locally by anthropogenic disturbances. Understanding the dispersal patterns of seagrasses is essential for appropriate ecosystem management and establishment of marine protected areas (MPAs) in coastal ecosystems. In the Guimaras Strait in the Philippines, Banate (BAN) has been established as an MPA. However, there is a lack of information on the genetic diversity of seagrasses in BAN and the surrounding areas. In the present study, population genetics analysis of Enhalus acoroides was performed by using polymorphic microsatellite markers, for the estimation of genetic diversity, differentiation, and migration patterns of seagrasses within the regional geographical scale (~200 km) around the Guimaras Strait. The results showed that the genetic diversity of BAN is extremely low, although the Guimaras Strait is located in the tropical central habitat. Guimaras Island geographically divides the populations of E. acoroides into south and north. However, the genetic structure did not show any relationship between the geographical location and distance. The floating, buoyant fruits of E. acoroides may play a role in their long-distance dispersal; however, such dispersal is not frequent. Almost all of the seeds and fruits are derived from self-recruitment in the natal meadow. This study suggests that E. acoroides populations possess a weak genetic connectivity, and that the persistence of the meadow is threatened due to the low genetic diversity and high degree of population isolation in BAN. To maintain and enhance the genetic diversity of seagrasses within the MPA, the seagrass meadows in the surrounding areas should also be conserved.     

Comparing the effects of rapid evolution and phenotypic plasticity on predator-prey dynamics

Ecologists have increasingly focused on how rapid adaptive trait changes can affect population dynamics. Rapid adaptation can result from either rapid evolution or phenotypic plasticity, but their effects on population dynamics are seldom compared directly. Here we examine theoretically the effects of rapid evolution and phenotypic plasticity of antipredatory defense on predator-prey dynamics. Our analyses reveal that phenotypic plasticity tends to stabilize population dynamics more strongly than rapid evolution. It is therefore important to know the mechanism by which phenotypic variation is generated for predicting the dynamics of rapidly adapting populations. We next examine an advantage of a phenotypically plastic prey genotype over the polymorphism of specialist prey genotypes. Numerical analyses reveal that the plastic genotype, if there is a small cost for maintaining it, cannot coexist with the pairs of specialist counterparts unless the system has a limit cycle. Furthermore, for the plastic genotype to replace specialist genotypes, a forced environmental fluctuation is critical in a broad parameter range. When these results are combined, the plastic genotype enjoys an advantage with population oscillations, but plasticity tends to lose its advantage by stabilizing the oscillations. This dilemma leads to an interesting intermittent limit cycle with the changing frequency of phenotypic plasticity.     

Vertical distribution of female adults and larval offspring of the white grub <Emphasis Type="Italic">Dasylepida ishigakiensis</Emphasis> (Coleoptera: Scarabaeidae) in the soil of a sugarcane field on Miyako Island,Okinawa

To determine the depth of soil at which mated females of the white grub beetle Dasylepida ishigakiensis Niijima et Kinoshita oviposited and their larval offspring stayed in the soil in different seasons, 847 mated female and male adults were released into a caged sugarcane field on Miyako Island. We then excavated this field systematically to collect adults and their larval offspring in the soil once or twice per month from 24 April 2002 to 31 March 2003. Dead females were found between 10 and 50 cm deep in the soil (N = 91), but most frequently in the layer 30–40 cm deep (N = 42; 46.2%). They were recovered more frequently in the soil at the plant foot (N = 73; 80.2%) than in the furrows (N = 18; 19.8%). On the other hand, no male carcass was discovered either in the soil or on the ground surface. The number of larvae discovered in the soil per row was large on 30 April (N = 52.5) and on 5 June (N = 58.3), when they were at the first instar. It decreased rapidly thereafter until 21 August (N = 9.5), when they molted to the second instar, and remained at similar levels through to the following 31 March (N = 8.0), during which they were mostly at the third instar. The larvae were found at various soil depths ranging from 0 to 70 cm, but the majority were found between 10 and 30 cm deep. The last sampling on 31 March indicated that mature larvae moved to a deeper layer for estivation. These results suggested that physical control through rotary tillage before they move to the deeper layer may be effective.     

Cholestatic liver fibrosis and toxin-induced fibrosis are exacerbated in matrix metalloproteinase-2 deficient mice

Matrix metalloproteinase (MMP) plays an important role in homeostatic regulation of the extracellular environment and degradation of matrix. During liver fibrosis, several MMPs, including MMP-2, are up-regulated in activated hepatic stellate cells, which are responsible for exacerbation of liver cirrhosis. However, it remains unclear how loss of MMP-2 influences molecular dynamics associated with fibrogenesis in the liver. To explore the role of MMP-2 in hepatic fibrogenesis, we employed two fibrosis models in mice; toxin (carbon tetrachloride, CCl4)-induced and cholestasis-induced fibrosis. In the chronic CCl4 administration model, MMP-2 deficient mice exhibited extensive liver fibrosis as compared with wild-type mice. Several molecules related to activation of hepatic stellate cells were up-regulated in MMP-2 deficient liver, suggesting that myofibroblastic change of hepatic stellate cells was promoted in MMP-2 deficient liver. In the cholestasis model, fibrosis in MMP-2 deficient liver was also accelerated as compared with wild type liver. Production of tissue inhibitor of metalloproteinase 1 increased in MMP-2 deficient liver in both models, while transforming growth factor β, platelet-derived growth factor receptor and MMP-14 were up-regulated only in the CCl4 model. Our study demonstrated, using 2 experimental murine models, that loss of MMP-2 exacerbates liver fibrosis, and suggested that MMP-2 suppresses tissue inhibitor of metalloproteinase 1 up-regulation during liver fibrosis.     

Ca-dependent binding of calcium-binding protein 1 to presynaptic group III metabotropic glutamate receptors and blockage by phosphorylation of the receptors

Presynaptic group III metabotropic glutamate receptors (mGluRs) and Ca²⁺ channels are the main neuronal activity-dependent regulators of synaptic vesicle release, and they use common molecules in their signaling cascades. Among these, calmodulin (CaM) and the related EF-hand Ca²⁺-binding proteins are of particular importance as sensors of presynaptic Ca²⁺, and a multiple of them are indeed utilized in the signaling of Ca²⁺ channels. However, despite its conserved structure, CaM is the only known EF-hand Ca²⁺-binding protein for signaling by presynaptic group III mGluRs. Because the mGluRs and Ca²⁺ channels reciprocally regulate each other and functionally converge on the regulation of synaptic vesicle release, the mGluRs would be expected to utilize more EF-hand Ca²⁺-binding proteins in their signaling. Here I show that calcium-binding protein 1 (CaBP1) bound to presynaptic group III mGluRs competitively with CaM in a Ca²⁺-dependent manner and that this binding was blocked by protein kinase C (PKC)-mediated phosphorylation of these receptors. As previously shown for CaM, these results indicate the importance of CaBP1 in signal cross talk at presynaptic group III mGluRs, which includes many molecules such as cAMP, Ca²⁺, PKC, G protein, and Munc18-1. However, because the functional diversity of EF-hand calcium-binding proteins is extraordinary, as exemplified by the regulation of Ca²⁺ channels, CaBP1 would provide a distinct way by which presynaptic group III mGluRs fine-tune synaptic transmission.     

Bis-THF motif of acetogenin binds to the third matrix-side loop of ND1 subunit in mitochondrial NADH-ubiquinone oxidoreductase

Natural acetogenins are among the most potent inhibitors of bovine heart mitochondrial NADH-ubiquinone oxidoreductase (complex I). Our photoaffinity labeling study suggested that the hydroxylated bis-THF ring moiety of acetogenins binds at "site A" in the third matrix-side loop connecting the fifth and sixth transmembrane helices in the ND1 subunit [Kakutani et al. (2010) Biochemistry 49, 4794-4803]. Nevertheless, since this proposition was led using a photoreactive Δlac-acetogenin derivative, it needs to be directly verified using a natural acetogenin-type probe. We therefore conducted photoaffinity labeling using a photoreactive natural acetogenin mimic ([(125)I]diazinylated natural acetogenin, [(125)I]DANA), which has a small photolabile diazirine group, in place of a hydroxy group, attached to the bis-THF ring moiety. Analysis of the photocross-linked protein in bovine heart submitochondrial particles unambiguously revealed that [(125)I]DANA binds to the membrane subunit ND1 with high specificity. The photocross-linking was completely blocked in the presence of just a 5-fold excess of bullatacin, indicating that [(125)I]DANA is an excellent mimic of natural acetogenins and hence binds to the site that accommodates natural products. Careful examination of the fragmentation patterns of the cross-linked ND1 generated by different proteases and their combinations indicated that the cross-linked residue is predominantly located at the supposed site A in the third matrix-side loop.     

The reconstituted 'humanized liver' in TK-NOG mice is mature and functional

The Marasmius oreades mushroom lectin (MOA) is well known for its exquisite binding specificity for blood group B antigens. In addition to its N-terminal carbohydrate-binding domain, MOA possesses a C-terminal domain with unknown function, which structurally resembles hydrolytic enzymes. Here we show that MOA indeed has catalytic activity. It is a calcium-dependent cysteine protease resembling papain-like cysteine proteases, with Cys215 being the catalytic nucleophile. The possible importance of MOA’s proteolytic activity for mushroom defense against pathogens is discussed.     

Distinct fucosylation of M cells and epithelial cells by Fut1 and Fut2, respectively, in response to intestinal environmental stress

The intestinal epithelium contains columnar epithelial cells (ECs) and M cells, and fucosylation of the apical surface of ECs and M cells is involved in distinguishing the two populations and in their response to commensal flora and environmental stress. Here, we show that fucosylated ECs (F-ECs) were induced in the mouse small intestine by the pro-inflammatory agents dextran sodium sulfate and indomethacin, in addition to an enteropathogen derived cholera toxin. Although F-ECs showed specificity for the M cell-markers, lectin Ulex europaeus agglutinin-1 and our monoclonal antibody NKM 16-2-4, these cells also retained EC-phenotypes including an affinity for the EC-marker lectin wheat germ agglutinin. Interestingly, fucosylation of Peyer’s patch M cells and F-ECs was distinctly regulated by α(1,2)fucosyltransferase Fut1 and Fut2, respectively. These results indicate that Fut2-mediated F-ECs share M cell-related fucosylated molecules but maintain distinctive EC characteristics, Fut1 is, therefore, a reliable marker for M cells.