117 results match your criteria: "Oregon Institute of Marine Biology[Affiliation]"
Integr Comp Biol
October 2007
*Department of Biology and Center for Molecular Phylogeny and Evolution, Ghent University, B-9000, Ghent, Belgium; Oregon Institute of Marine Biology and Department of Biology, University of Oregon, Charleston, OR 97420, USA; Department of Molecular and Cellular Pharmacology and the Vascular Biology Institute, University of Miami Medical Center, Miami, FL 33136, USA; Department of Genetics, Development, and Cell Biology, Iowa State University, Ames, IA 50011, USA; Environmental Science Division, School of Life Sciences, Tokyo University of Pharmacy and Life Sciences, Horinouchi, Hachioji, Tokyo 192-0392, Japan; Institute of Molecular Genetics, University of Mainz, D-55099 Mainz, Germany; Institute of Animal Physiology, University of Hamburg, D-20146 Hamburg, Germany; **Centre of Excellence in Evolutionary Genetics and Physiology, Department of Biology, University of Turku, FI-20014 Turku, Finland; Alfred-Wegener Institute for Polar and Marine Research, Physiology of Marine Animals, D-27570 Bremerhaven, Germany; Institut für Physiologie, Universität Duisburg-Essen, D-45122 Essen, Germany; Renal Section, Hammersmith Campus, Imperial College London, London W12 0NN, UK; Division of Molecular Medicine, Department of Laboratory Medicine, Lund University, University Hospital MAS, SE-205 02 Malmö, Sweden; Institute of Veterinary Physiology, Vetsuisse Faculty and Zurich Center for Integrative Human Physiology (ZIHP), University of Zurich, CH-8057 Zurich, Switzerland.
The objective of this symposium at the First International Congress of Respiratory Biology (ICRB) was to enhance communication between comparative biologists and cancer researchers working on O(2) sensing via the HIF pathway. Representatives from both camps came together on August 13-16, 2006, in Bonn, Germany, to discuss molecular adaptations that occur after cells have been challenged by a reduced (hypoxia) or completely absent (anoxia) supply of oxygen. This brief "critters-to-cancer" survey discusses current projects and new directions aimed at improving understanding of hypoxic signaling and developing therapeutic interventions.
View Article and Find Full Text PDFEcology
July 2007
University of Oregon, Oregon Institute of Marine Biology, P.O. Box 5389, Charleston, Oregon 97420, USA.
Ecologists have long debated the relative importance of biotic interactions vs. abiotic forces on the population dynamics of both marine and terrestrial organisms. Investigation of stock size in Dungeness crab (Cancer magister) is a classic example of this debate.
View Article and Find Full Text PDFBiol Bull
June 2007
Oregon Institute of Marine Biology, University of Oregon, Charleston, Oregon 97420, USA.
In the intertidal zone in the Pacific Northwest, body temperatures of sessile marine organisms can reach 35 degrees C for an extended time during low tide, resulting in potential physiological stress. We used immunochemical assays to examine the effects of thermal stress on endogenous Hsp70 levels in the intertidal barnacle Balanus glandula. After thermal stress, endogenous Hsp70 levels did not increase above control levels in B.
View Article and Find Full Text PDFIntegr Comp Biol
December 2006
Oregon Institute of Marine Biology, University of Oregon Charleston, OR 97420, USA.
Proteins in the arthropod hemocyanin gene family are involved in major physiological processes, including aerobic respiration, the innate immune response, and molting. Members of this family, hemocyanin, cryptocyanin, and phenoloxidase, are multisubunit molecules that assemble into hexamers and higher aggregates. The hemocyanin hexamers show species-specific subunit heterogeneity.
View Article and Find Full Text PDFIntegr Comp Biol
June 2006
Oregon Institute of Marine Biology and Department of Biology, University of Oregon PO Box 5389 Charleston, OR 97420, USA.
Many marine invertebrates with complex life cycles produce planktonic larvae that experience environmental conditions different from those encountered by adults. Factors such as temperature and food, known to impact the larval period, can also affect larval size and consequently the size of newly settled juveniles. After documenting natural variation in the size of cyprids (the final larval stage) of the barnacle Balanus glandula, we experimentally manipulated temperature and food given to larvae to produce cyprids of differing sizes but within the size range of cyprids found in the field.
View Article and Find Full Text PDFEcology
January 2006
University of Oregon, Oregon Institute of Marine Biology, Charleston 97420, USA.
Over the past 30 years, numerous attempts to understand the relationship between offspring size and fitness have been made, and it has become clear that this critical relationship is strongly affected by environmental heterogeneity. For marine invertebrates, there has been a long-standing interest in the evolution of offspring size, but there have been very few empirical and theoretical examinations of post-metamorphic offspring size effects, and almost none have considered the effect of environmental heterogeneity on the offspring size/fitness relationship. We investigated the post-metamorphic effects of offspring size in the field for the colonial marine invertebrate Botrylloides violaceus.
View Article and Find Full Text PDFBiol Bull
February 2006
Oregon Institute of Marine Biology, University of Oregon, PO Box 5389, Charleston, 97420, USA.
Arthropod phenoloxidases catalyze the melanization and sclerotization of the new postmolt exoskeleton, and they function in the immune response. Hemocyanin, phylogenetically related to phenoloxidase, can function as a phenoloxidase under certain conditions. We investigated the relative contributions of hemocyte phenoloxidase and hemocyanin in the brachyuran crab Cancer magister, using the physiological ratio at which they occur in the hemolymph, and found that hemocyte phenoloxidase has higher activity.
View Article and Find Full Text PDFJ Exp Biol
July 2005
Oregon Institute of Marine Biology, University of Oregon, Box 5389, Charleston, OR 97420, USA.
Hemocyanin, the blue blood protein of many arthropods and molluscs, reversibly binds oxygen at its highly conserved copper-oxygen-binding sites and supplies tissues with oxygen. Cryptocyanin, closely related structurally and phylogenetically to arthropod hemocyanin, lacks several of the six critical copper-binding histidines, however, and has lost the ability to bind oxygen. Despite this loss of function, cryptocyanin continues to be synthesized, an indication that it has been exploited to carry out new functions.
View Article and Find Full Text PDFEvolution
May 2003
Oregon Institute of Marine Biology, University of Oregon, P.O. Box 5389, Charleston, Oregon 97420, USA.
Taxonomic revision and cladistic analysis of a morphological dataset for Australian Tertiary temnopleurids resolve the phylogeny of the group and allow the testing of a series of hypotheses about the evolution of larval development and consequences of changes in development. Australian Tertiary temnopleurids encompass all three major developmental types found in marine invertebrates (planktotrophy, lecithotrophy, and brooding). Planktotrophy is plesiomorphic for this clade, and nonplanktotrophic larval development evolved independently at least three times during the Tertiary.
View Article and Find Full Text PDFMol Phylogenet Evol
July 2003
Oregon Institute of Marine Biology, University of Oregon, P.O. Box 5389, Charleston, OR 97420, USA.
The phylogenetic relationships of 24 nominal species of temnopleurid echinoid were established using molecular and morphological data sets. The analysis combined sequence data from mitochondrial 16S rRNA and cytochrome c oxidase subunit I genes and the nuclear 18S-like small subunit rRNA gene with morphological data concerning coronal, lantern, spine, and pedicellarial traits. All four data sets contain similar phylogenetic information, although each provides support at a different taxonomic level.
View Article and Find Full Text PDFJ Exp Biol
March 2001
Oregon Institute of Marine Biology, University of Oregon, Charleston, OR 97420, USA.
Hemocyanin is present throughout the decapod crustacean's life, usually as one-hexamer and two-hexamer oligomers. Hemocyanins of some decapod crustaceans undergo changes in subunit composition and oxygen affinity during development. Maternal hemocyanin is taken up from the hemolymph via endocytosis by the oocyte.
View Article and Find Full Text PDFJ Exp Biol
April 1999
Institute of Neuroscience and Oregon Institute of Marine Biology, University of Oregon, Eugene, OR 97403-1254, USA.
Most larval external muscles in Manduca sexta degenerate at pupation, with the exception of the accessory planta retractor muscles (APRMs) in proleg-bearing abdominal segment 3 and their homologs in non-proleg-bearing abdominal segment 2. In pupae, these APRMs exhibit a rhythmic 'pupal motor pattern' in which all four muscles contract synchronously at approximately 4 s intervals for long bouts, without externally visible movements. On the basis of indirect evidence, it was proposed previously that APRM contractions during the pupal motor pattern circulate hemolymph in the developing wings and legs.
View Article and Find Full Text PDFProc Natl Acad Sci U S A
March 1999
Oregon Institute of Marine Biology, University of Oregon, Charleston, OR 97420, USA.
Cryptocyanin, a copper-free hexameric protein in crab (Cancer magister) hemolymph, has been characterized and the amino acid sequence has been deduced from its cDNA. It is markedly similar in sequence, size, and structure to hemocyanin, the copper-containing oxygen-transport protein found in many arthropods. Cryptocyanin does not bind oxygen, however, and lacks three of the six highly conserved copper-binding histidine residues of hemocyanin.
View Article and Find Full Text PDFJ Exp Biol
April 1998
Oregon Institute of Marine Biology, University of Oregon, Charleston, OR 97420, USA.
Oxygen-transport proteins are multisubunit, circulating molecules that provide an efficient supply of oxygen to metabolically active metazoans. Hemoglobins, hemerythrins and hemocyanins have evolved in both structural and functional diversity and exhibit functional repertoires beyond that of simple, monomeric tissue myoglobins. Their phylogenetic distribution is intriguing, especially with respect to those organisms that express more than one type of oxygen-transport protein.
View Article and Find Full Text PDFMol Biol Evol
March 1997
Oregon Institute of Marine Biology, Charleston, Oregon 97420, USA.
The complete cDNA sequence and protein reading frame of a developmentally regulated hemocyanin subunit in the Dungeness crab (Cancer magister) is presented. The protein sequence is aligned with 18 potentially homologous hemocyanin-type proteins displaying apparent sequence similarities. Functional domains are identified, and a comparison of predicted hydrophilicities, surface probabilities, and regional backbone flexibilities provides evidence for a remarkable degree of structural conservation among the proteins surveyed.
View Article and Find Full Text PDFJ Biol Chem
February 1997
Oregon Institute of Marine Biology, University of Oregon, Charleston, Oregon 97420.
The copper-based respiratory protein hemocyanin undergoes a developmental shift in subunit composition and function analogous to that seen in many hemoglobins. We studied hemocyanin gene expression in the Dungeness crab (Cancer magister) by Northern blot analysis. Animals were raised under controlled conditions, and total RNA was isolated from 13 developmental stages as well as from six tissue types in the adult animal.
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