Erlend Kristiansen
Norwegian University of Science and Technology
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Featured researches published by Erlend Kristiansen.
IFAC Proceedings Volumes | 2003
Erlend Kristiansen; Olav Egeland
Abstract The paper presents a method for generating a time domain formulation of the equations of motion for a ship with frequency-dependent hydrodynamic coefficients. Previous work on this topic has relied on the use of convolution terms, whereas in this work state-space models are used. This leads to a model formulation that is well suited for controller design and simulation.
Cryobiology | 2008
Erlend Kristiansen; Sindre Andre Pedersen; Karl Erik Zachariassen
Antifreeze proteins are a structurally diverse group of proteins characterized by their unique ability to cause a separation of the melting- and growth-temperatures of ice. These proteins have evolved independently in different kinds of cold-adapted ectothermic animals, including insects and fish, where they protect against lethal freezing of the body fluids. There is a great variability in the capacity of different kinds of antifreeze proteins to evoke the antifreeze effect, but the basis of these differences is not well understood. This study reports on salt-induced enhancement of the antifreeze activity of an antifreeze protein from the longhorn beetle Rhagium inquisitor (L.). The results imply that antifreeze activity is predetermined by a steady-state distribution of the antifreeze protein between the solution and the ice surface region. The observed salt-induced enhancement of the antifreeze activity compares qualitatively and quantitatively with salt-induced lowering of protein solubility. Thus, salts apparently enhance antifreeze activity by evoking a solubility-induced shift in the distribution pattern of the antifreeze proteins in favour of the ice. These results indicate that the solubility of antifreeze proteins in the solution surrounding the ice crystal is a fundamental physiochemical property in relation to their antifreeze potency.
Journal of Insect Physiology | 2001
Erlend Kristiansen; Karl Erik Zachariassen
The present study shows that freezing of freeze-tolerant larvae of the wood fly Xylophagus cinctus caused Na(+), K(+) and Mg(++) to move to electrochemical equilibrium across the cell membranes. Na(+) and Mg(++) moved from the haemolymph into the cells, while K(+) moved the opposite way. The original distribution of ions was restored after the larvae were thawed. The transmembrane fluxes of ions were of the same magnitude in the frozen and thawed larvae. The redistribution of ions in the frozen larvae did not give rise to any apparent change in the volume of cells and haemolymph upon thawing, i.e. the redistribution of solutes appeared to be osmotically neutral.
Insect Biochemistry and Molecular Biology | 2011
Erlend Kristiansen; Hans Ramløv; Peter Højrup; Sindre Andre Pedersen; Lars Hagen; Karl Erik Zachariassen
Antifreeze proteins (AFPs) are characterized by their capacity to inhibit the growth of ice and are produced by a variety of polar fish, terrestrial arthropods and other organisms inhabiting cold environments. This capacity reflects their role as stabilizers of supercooled body fluids. The longhorn beetle Rhagium inquisitor is known to express AFPs in its body fluids. In this work we report on the primary structure and structural characteristics of a 12.8 kDa AFP from this beetle (RiAFP). It has a high capacity to evoke antifreeze activity as compared to other known insect AFPs and it is structurally unique in several aspects. In contrast to the high content of disulfide bond-formation observed in other coleopteran AFPs, RiAFP contains only a single such bond. Six internal repeat segments of a thirteen residue repeat pattern is irregularly spaced apart throughout its sequence. The central part of these repeat segments is preserved as TxTxTxT, which is effectively an expansion of the TxT ice-binding motif found in the AFPs of several known insect AFPs.
Journal of Comparative Physiology B-biochemical Systemic and Environmental Physiology | 1999
Erlend Kristiansen; Sindre Andre Pedersen; Hans Ramløv; Karl Erik Zachariassen
Abstract The present study revealed that hibernating freeze-avoiding Rhagium inquisitor beetles have thermal hysteresis antifreeze agents in the intracellular fluid as well as in the intestinal fluid and the haemolymph. The antifreeze activity in all three compartments increased with diminishing size of the seeding ice crystal, suggesting that all three compartments are well protected against spontaneous ice nucleation at low sub-zero temperatures.
Journal of Comparative Physiology B-biochemical Systemic and Environmental Physiology | 2008
Karl Erik Zachariassen; N. G. Li; A. E. Laugsand; Erlend Kristiansen; Sindre Andre Pedersen
The strategy for cold-hardiness and water balance features of two closely related families of Coleoptera, Cerambycidae and Chrysomelidae, were investigated. Cerambycids were freeze-avoiding with low supercooling points, whereas chrysomelids froze at high temperatures and were tolerant to freezing. Hence, the two families have adopted different strategies for cold-hardiness. Due to their low trans-cuticular water permeability, the cerambycids have low rates of evaporative water loss. Chrysomelids have much higher trans-cuticular water permeability, but freezing brings their body fluids in vapour pressure equilibrium with ice and prevents evaporative water loss. The differences in cold-hardiness strategies and rates of water loss are likely to reflect the water content of the diets of the two families. Cerambycids feed on dry wood with low water content, causing a restrictive water balance. Chrysomelids feed on leaves with high water content and may use evaporation through the cuticle as a route of water excretion. Haemolymph ice nucleators help chrysomelids to freeze at a high temperature and thus to maximize the period they spend in the water saving frozen state. The diet-related differences in water balance may be the reason why the two families have developed different strategies for cold-hardiness.
Cryobiology | 2002
Karl Erik Zachariassen; Arthur L. DeVries; Ben Hunt; Erlend Kristiansen
The freezing-melting hysteresis in a given volume of hemolymph from the cerambycid beetle Rhagium inquisitor was linearly and negatively related to the logarithm of the mass fraction of ice in the sample. When the ice fraction dropped by a factor of 10, the hysteresis activity increased by about 2 degrees C. When the hemolymph was diluted, the hysteresis activity was linearly and negatively related to the logarithm of the dilution factor. Dilution of the hemolymph by a factor of 2 led to a 1 degree C reduction in hysteresis activity. In the diluted samples, the ice growth took place along the a-axes, implying that the antifreeze peptides of insects block ice growth along the c-axis, in addition to the a-axis.
Journal of Insect Physiology | 2012
Erlend Kristiansen; Casper Wilkens; Bjarne Vincents; Dennis Steven Friis; Anders Blomkild Lorentzen; Håvard Jenssen; Anders Løbner-Olesen; Hans Ramløv
This study reports on structural characteristics of hyperactive antifreeze proteins (AFPs) from two species of longhorn beetles. In Rhagium mordax, eight unique mRNAs coding for five different mature AFPs were identified from cold-hardy individuals. These AFPs are apparently homologues to a previously characterized AFP from the closely related species Rhagium inquisitor, and consist of six identifiable repeats of a putative ice binding motif TxTxTxT spaced irregularly apart by segments varying in length from 13 to 20 residues. Circular dichroism spectra show that the AFPs from both species have a high content of β-sheet and low levels of α-helix and random coil. Theoretical predictions of residue-specific secondary structure locate these β-sheets within the putative ice-binding motifs and the central parts of the segments separating them, consistent with an overall β-helical structure with the ice-binding motifs stacked in a β-sheet on one side of the coil. Molecular dynamics models based on these findings show that these AFPs would be energetically stable in a β-helical conformation.
Comparative Biochemistry and Physiology C-toxicology & Pharmacology | 2008
Sindre Andre Pedersen; Erlend Kristiansen; Rolf A. Andersen; Karl Erik Zachariassen
Binding of cadmium (Cd) to metallothionein (MT) and non-MT proteins with low contents of cysteine has been observed in terrestrial arthropods. We recently isolated a Cd-binding protein with no cysteine that was induced in Cd-exposed larvae of the beetle Tenebrio molitor. In this study we have examined the molecular distribution of Cd within extracts of different tissues and compartments of Cd-exposed T. molitor larvae. A Cd-peak consistent with the low cysteine Cd-binding protein was induced within the gut content where it could be detected after 4-8 days of exposure. Examination of gut wall tissue revealed no increase in Cd-binding capacity, indicating that no accumulation of MTs was taking place in this tissue. Incorporation of Cd in the gut wall tissue stabilized after 8 days of Cd-exposure at a rather low level compared to the other organs. There was a statistical trend towards Cd being incorporated in the gut content in a manner that was disproportionally high compared to the amount of Cd in the gut wall tissue. The possible role of the low cysteine Cd-binding protein in reducing the uptake of Cd in the tissues is discussed.
Marine Environmental Research | 2011
Karen Marie Hammer; Erlend Kristiansen; Karl Erik Zachariassen
The option of storing CO(2) in subsea rock formations to mitigate future increases in atmospheric CO(2) may induce problems for animals in the deep sea. In the present study the deep-sea bivalve Acesta excavata was subjected to environmental hypercapnia (pHSW 6.35, P(CO₂) =33,000 μatm) corresponding to conditions reported from natural CO(2) seeps. Effects on acid-base status and metabolic rate were related to time of exposure and subsequent recovery. During exposure there was an uncompensated drop in both hemolymph and intracellular pH. Intracellular pH returned to control values, while extracellular pH remained significantly lower during recovery. Intracellular non-bicarbonate buffering capacity of the posterior adductor muscle of hypercapnic animals was significantly lower than control values, but this was not the case for the remaining tissues analyzed. Oxygen consumption initially dropped by 60%, but then increased during the final stages of exposure, which may suggest a higher tolerance to hypercapnia than expected for a deep-living species.