Metabolic suppression in thecosomatous pteropods as an effect of low temperature and hypoxia in the eastern tropical North Pacific

Author Posting. © The Author(s), 2011. This is the author's version of the work. It is posted here by permission of Springer for personal use, not for redistribution. The definitive version was published in Marine Biology 159 (2012): 1955-1967, doi:10.1007/s00227-012-1982-x.Many pteropod species in the eastern tropical north Pacific Ocean migrate vertically each day, transporting organic matter and respiratory carbon below the thermocline. These migrations take species into cold (15-10ºC) hypoxic water (< 20 µmol O2 kg-1) at depth. We measured the vertical distribution, oxygen consumption and ammonia excretion for seven species of pteropod, some of which migrate and some which remain in oxygenated surface waters throughout the day. Within the upper 200 meters of the water column, changes in water temperature result in a ~60-75% reduction in respiration for most species. All three species tested under hypoxic conditions responded to low O2 with an additional ~35-50% reduction in respiratory rate. Combined, low temperature and hypoxia suppress the metabolic rate of pteropods by ~80-90%. These results shed light on the ways in which expanding regions of hypoxia and surface ocean warming may impact pelagic ecology.This work was funded by National Science Foundation grants to K. Wishner and B. Seibel (OCE – 0526502 and OCE – 0851043) and to K. Daly (OCE – 0526545), the University of Rhode Island, and the Rhode Island Experimental Program to Stimulate Competitive Research Fellowship program.2013-06-3

The genetic basis and evolution of red blood cell sickling in deer

Crescent-shaped red blood cells, the hallmark of sickle-cell disease, present a striking departure from the biconcave disc shape normally found in mammals. Characterized by increased mechanical fragility, sickled cells promote haemolytic anaemia and vaso-occlusions and contribute directly to disease in humans. Remarkably, a similar sickle-shaped morphology has been observed in erythrocytes from several deer species, without obvious pathological consequences. The genetic basis of erythrocyte sickling in deer, however, remains unknown. Here, we determine the sequences of human β-globin orthologues in 15 deer species and use protein structural modelling to identify a sickling mechanism distinct from the human disease, coordinated by a derived valine (E22V) that is unique to sickling deer. Evidence for long-term maintenance of a trans-species sickling/non-sickling polymorphism suggests that sickling in deer is adaptive. Our results have implications for understanding the ecological regimes and molecular architectures that have promoted convergent evolution of sickling erythrocytes across vertebrates

Familial hyperinsulinemia due to a structurally abnormal insulin: Definition of an emerging new clinical syndrome.

Massachusetts Medical Society, Haneda, M. ; Polonsky, KS. ; Bergenstal, RM. ; Jaspan, JB ; Shoelson, SE, ; Blix, PM ; Chan, SJ ; Kwok, SCM ; Wishner, WB ; Zeidler; A. ; Olefsky, JM ; Freidenberg, G,: Tager, HS. ; Steiner, DF : Rubenstein, AH, New England Journal of Medicine, 310(20), 1984, 1288-1294. publisherWe have identified a patient with mild diabetes, marked fasting hyperinsulinemia (89 to 130 microU of insulin per milliliter), and a reduced fasting C-peptide: insulin molar ratio of 1.11 to 1.50 (normal, greater than 4). The patient responded normally to exogenous insulin. However, her endogenous immunoreactive insulin showed reduced biologic activity during a glucose-clamp study with hyperglycemia and a reduced ability to bind to the insulin receptor and stimulate glucose transport in vitro. Family studies showed that five additional relatives in three generations had variable degrees of glucose intolerance, marked hyperinsulinemia, and a reduced peripheral C-peptide:insulin molar ratio. Restriction-endonuclease cleavage of DNA isolated from circulating leukocytes in the patient and in family members with hyperinsulinemia revealed loss of the MboII recognition site in one allele of the insulin gene--consistent with a point mutation at position 24 or 25 in the insulin B chain. Other studies using high-pressure liquid chromatography and detailed gene analysis have identified the defect as a serine for phenylalanine substitution at position 24 of the insulin B chain. The secretion of a structurally abnormal insulin should be considered in patients with hyperinsulinemia who respond normally to exogenous insulin and have a reduced C-peptide:insulin molar ratio. Glucose tolerance may range from relatively normal to overtly diabetic