A survey of deep-water coral and sponge habitats along the west coast of the US using a remotely operated vehicle: NOAA Fisheries Survey Vessel (FSV)'Bell M. Shimada', November 1-5, 2010

Remotely operated vehicle (ROV) surveys were conducted from NOAA’s state-of-the-art Fisheries Survey Vessel (FSV) Bell M. Shimada during a six-day transit November 1-5, 2010 between San Diego, CA and Seattle, WA. The objective of this survey was to locate and characterize deep-sea coral and sponge ecosystems at several recommended sites in support of NOAA’s Coral Reef Conservation Program. Deep-sea corals and sponges were photographed and collected whenever possible using the Southwest Fisheries Science Center’s (SWFSC) Phantom ROV ‘Sebastes’ (Fig. 1). The surveyed sites were recommended by National Marine Sanctuary (NMS) scientists at Monterey Bay NMS, Gulf of the Farallones NMS, and Olympic Coast NMS (Fig. 2). The specific sites were: Sur Canyon, The Football, Coquille Bank, and Olympic Coast NMS. During each dive, the ROV collected digital still images, video, navigation, and along-track conductivity-temperature-depth (CTD), and optode data. Video and high-resolution photographs were used to quantify abundance of corals, sponges, and associated fishes and invertebrates to the lowest practicable taxonomic level, and also to classify the seabed by substrate type. A reference laser system was used to quantify area searched and estimate the density of benthic fauna.

Differences in diet of Atlantic bluefin tuna (Thunnus thynnus) at five seasonal feeding grounds on the New England continental shelf

The stomachs of 819 Atlantic bluefin tuna (Thunnus thynnus) sampled from 1988 to 1992 were analyzed to compare dietary differences among five feeding grounds on the New England continental shelf (Jeffreys Ledge, Stellwagen Bank, Cape Cod Bay, Great South Channel, and South of Martha’s Vineyard) where a majority of the U.S. Atlantic commercial catch occurs. Spatial variation in prey was expected to be a primary influence on bluefin tuna distribution during seasonal feeding migrations. Sand lance (Ammodytes spp.), Atlantic herring (Clupea harengus), Atlantic mackerel (Scomber scombrus), squid (Cephalopoda), and bluefish (Pomatomus saltatrix) were the top prey in terms of frequency of occurrence and percent prey weight for all areas combined. Prey composition was uncorrelated between study areas, with the exception of a significant association between Stellwagen Bank and Great South Channel, where sand lance and Atlantic herring occurred most frequently. Mean stomach-contents biomass varied significantly for all study areas, except for Great South Channel and Cape Cod Bay. Jeffreys Ledge had the highest mean stomach-contents biomass (2.0 kg) among the four Gulf of Maine areas and Cape Cod Bay had the lowest (0.4 kg). Diet at four of the five areas was dominated by one or two small pelagic prey and several other pelagic prey made minor contributions. In contrast, half of the prey species found in the Cape Cod Bay diet were demersal species, including the frequent occurrence of the sessile fig sponge (Suberites ficus). Prey size selection was consistent over a wide range of bluefin length. Age 2–4 sand lance and Atlantic herring and age 0–1 squid and Atlantic mackerel were common prey for all sizes of bluefin tuna. This is the first study to compare diet composition of western Atlantic bluefin tuna among discrete feeding grounds during their seasonal migration to the New England continental shelf and to evaluate predator-prey size relationships. Previous studies have not found a common occurrence of demersal species or a pre-dominance of Atlantic herring in the diet of bluefin tuna.

Molecular cloning, characterization and localization of chicken type II procollagen gene

Chicken type II procollagen (ccol2a1) has become as an important oral tolerance protein for effective treatment of rheumatoid arthritis. However, its molecular identity remains unclear. Here, we reported the full-length cDNA and nearly complete genomic DN

A NOVEL PLASMINOGEN-ACTIVATOR FROM SNAKE-VENOM - PURIFICATION, CHARACTERIZATION, AND MOLECULAR-CLONING

A novel plasminogen activator from Trimeresurus stejnegeri venom (TSV-PA) has been identified and purified to homogeneity. It is a single chain glycoprotein with an apparent molecular weight of 33,000 and an isoelectric point of pH 5.2. It specifically activates plasminogen through an enzymatic reaction. The activation of human native GIu-plasminogen by TSV-PA is due to a single cleavage of the molecule at the peptide bond Arg(561)-Val-(562). Purified TSV-PA, which catalyzes the hydrolysis of several tripeptide p-nitroanilide substrates, does not activate nor degrade prothrombin, factor X, or protein C and does not clot fibrinogen nor show fibrino(geno)lytic activity in the absence of plasminogen. The activity of TSV-PA was readily inhibited by phenylmethanesulfonyl fluoride and by p-nitrophenyl-p-guanidinobenzoate. Oligonucleotide primers designed on the basis of the N-terminal and the internal peptide sequences of TSV-PA were used for the amplification of cDNA fragments by polymerase chain reaction. This allowed the cloning of a full-length cDNA encoding TSV-PA from a cDNA library prepared from the venom glands. The deduced complete amino acid sequence of TSV-PA indicates that the mature TSV-PA protein is composed of 234 amino acids and contains a single potential N-gIycosylation site at Asn(1G1). The sequence of TSV-PA exhibits a high degree of sequence identity with other snake venom proteases: 66% with the protein C activator from Aghistrodon contortrix contortrix venom, 63% with batroxobin, and 60% with the factor V activator from Russell's viper venom. On the other hand, TSV-PA shows only 21-23% sequence similarity with the catalytic domains of u-PA and t-PA. Furthermore, TSV-PA lacks the sequence site that has been demonstrated to be responsible for the interaction of t-PA (KHRR) and u-PA (RRHR) with plasminogen activator inhibitor type 1.

Identification and cloning of a trypsin inhibitor from skin secretions of Chinese red-belly toad Bombina maxima

A novel trypsin inhibitor was identified and purified from skin secretions of Chinese red-belly toad Bombina maxima. The partial N-terminal 29 amino acid residues of the peptide, named BMTI, were determined by automated Edman degradation. This allowed the cloning of a full-length cDNA encoding BMTI from a cDNA library prepared from the toad skin. The deduced complete amino acid sequence of BMTI indicates that mature BMTI is composed of 60 amino acids. A FASTA search in the databanks revealed that BMTI exhibits 81.7% sequence identity with BSTI, a trypsin/thrombin inhibitor from European toad Bombina bombina skin secretions. Sequence differences between BMTI and BSTI were due to 11 substitutions at positions 2, 9, 25, 27, 36-37, 39, 41-42, 50 and 56. BMTI potently inhibited trypsin with a K-i value of 0.06 muM, similar to that of BSTI. However, unlike BSTI, which also inhibited thrombin with a K-i value of 1 muM, no inhibitory effect of BMTI on thrombin was observed under the assay conditions. (C) 2002 Elsevier Science Inc. All rights reserved.