Publications by authors named "Terwilliger N"

Infertility is an impactful late effect of cancer therapy. Options for fertility preservation exist, however, barriers remain. Within our division, we lacked a standard approach to discussing fertility preservation.

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The purpose of this systematic review is to (1) synthesize evidence facilitators and barriers affecting adolescent willingness to communicate symptoms to health care providers (HCPs) and (2) create practice recommendations. The PICOT (Population, Intervention, Comparison, Outcome, Time) question guiding the review was, among adolescents with cancer, what factors affect their willingness to communicate symptoms to HCPs? Three databases, PubMed, CINAHL, and PsychINFO, were searched using keywords from the PICOT question. Inclusion criteria included original research studies with samples of at least 51% adolescents aged 10-18 years who were receiving or had received cancer treatment.

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The interaction between environmental salinity and gene expression was studied in gills of the euryhaline green shore crab Carcinus maenas. A 4462-feature oligonucleotide microarray was used to analyze changes in transcript abundance in posterior ion-transporting gills at 8 time periods following transfer of animals from 32 to 10 or 15 ppt salinity. Transcripts encoding Na(+)/K(+)-ATPase α-subunit and cytoplasmic carbonic anhydrase were upregulated with significant changes between 6 and 24h post-transfer.

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Many invertebrates and ectothermic vertebrates successfully cope with a fluctuating supply of ambient oxygen-and consequently, a highly variable tissue oxygenation-through increasing their antioxidant barriers. During chronic deprivation of oxygen, however, the hypometabolic defense mode of the fruit fly Drosophila, the hypoxia-induced behavioral hypothermia of the crayfish Pacifastacus leniusculus, and the production of ethanol during anoxia by the crucian carp Carassius carassius all indicate that these animals are also capable of utilizing a suite of genetic and physiological defenses to survive otherwise lethal reductions in tissue oxygenation. Normally, much of an organism's gene response to hypoxia is orchestrated via the hypoxia-inducible transcription factor HIF.

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Crustaceans are a diverse and ancient group of arthropods that have long been studied as interesting model systems in biology, especially for understanding animal evolution and physiology and for environmentally relevant studies. Like many model systems, advances in DNA-sequencing methodologies have led to a large amount of genomics-related projects. The purpose of this article is to highlight the genome projects and functional genomics (transcriptomics) projects that are currently underway in crustacean biology.

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The innate immune response is a conserved trait shared by invertebrates and vertebrates. In crustaceans, circulating hemocytes play significant roles in the immune response, including the release of prophenoloxidases. Activated phenoloxidase (tyrosinase) participates in encapsulation and melanization of foreign organisms as well as sclerotization of the new exoskeleton after wound-repair or molting.

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This article summarizes the contributions given at the symposium "The Benefits of Gas-binding Proteins. Integrative and Evolutionary Physiology of Copper Proteins: Molecules to Organisms and their Environment," presented at the First International Congress of Respiratory Biology, August 14-16, at Bad Honnef/Bonn, Germany.

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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.

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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.

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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.

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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.

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Upon exposure to air (emersion), the purple sea urchin Strongylocentrotus purpuratus releases an "emersion fluid" from its esophagus. Release of this fluid causes air to appear within the test (or calcareous theca), most likely inside the intestine. The air space is large, occupying 33.

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Phenoloxidase, widely distributed among animals, plants, and fungi, is involved in many biologically essential functions including sclerotization and host defense. In chelicerates, the oxygen carrier hemocyanin seems to function as the phenoloxidase. Here, we show that hemocyanins from two ancient chelicerates, the horseshoe crab Limulus polyphemus and the tarantula Eurypelma californicum, exhibit O-diphenoloxidase activity induced by submicellar concentrations of SDS, a reagent frequently used to identify phenoloxidase activity.

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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.

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Two closely related copper proteins, phenoloxidase and haemocyanin, are known to be involved in different physiological functions such as the primary immune response and oxygen transport. Although the proteins differ structurally, they have the same active site by which dioxygen is bound. Recent results reveal that haemocyanin also exhibits phenoloxidase activity.

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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.

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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.

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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.

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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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The rat-tailed sea cucumber, Paracaudina chilensis, has abundant hemoglobin-filled hemocytes in its perivisceral coelom, water vascular system, and hemal system. The perivisceral oxyhemoglobin consisted of 34 kDa dimers and molecules with an apparent molecular weight of ca. 50 kDa.

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The ontogeny of osmoregulation and specific ion regulation was studied in the megalopa, 1st instar juvenile, 5th instar juvenile and adult of Cancer magister. Hemolymph Na+, Cl-, K+, Mg++, and Ca++ concentrations and osmolality were measured after 8-h exposure to 100%, 75%, and 50% seawater at 10°C and 20°C. The ability to hyperosmotically regulate is present in the megalopa, and ontogenic changes occur in both ionic and osmotic regulation.

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1. The hemocyanins of the protobranch bivalves Yoldia thraciaeformis, Yoldia limatula and Acila castrensis have absorption spectra similar to other hemocyanins. 2.

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1. The concentration of myoglobin (Mb) and the isozymic distribution and activity of lactate dehydrogenase (LDH) in heart and pectoralis muscle were investigated at three stages of maturation of the Pigeon Guillemot, Cepphus columba. 2.

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A heterodont bivalve mollusk Calyptogena magnifica, from the East Pacific Rise and the Galápagos Rift hydrothermal vent areas, contains abundant hemoglobin in circulating erythrocytes. No other known heterodont clam contains a circulating intracellular hemoglobin. The hemoglobin is tetrameric and has a relatively high oxygen affinity, which varies only slightly between 2 degrees and 10 degrees C.

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