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Salisbury Cove, ME, United States

The MDI Biological Laboratory is an independent non-profit biomedical research institution founded in 1898 and located in Salisbury Cove, Maine, on Mount Desert Island. Its mission is to improve human health and well- being through basic research, education, and development ventures that transform discoveries into cures. In 2013, the Laboratory was designated a Center for Biomedical Research Excellence by the National Institutes of Health, which awarded the Laboratory a grant of $13 million over five years to expand the institution’s research program. The MDI Biological Laboratory has a full-time staff of 63, and will offer 23 research training courses in 2014. Wikipedia.


Strome S.,University of California at Santa Cruz | Updike D.,Mount Desert Island Biological Laboratory
Nature Reviews Molecular Cell Biology | Year: 2015

Germ cells are the special cells in the body that undergo meiosis to generate gametes and subsequently entire new organisms after fertilization, a process that continues generation after generation. Recent studies have expanded our understanding of the factors and mechanisms that specify germ cell fate, including the partitioning of maternally supplied 'germ plasm', inheritance of epigenetic memory and expression of transcription factors crucial for primordial germ cell (PGC) development. Even after PGCs are specified, germline fate is labile and thus requires protective mechanisms, such as global transcriptional repression, chromatin state alteration and translation of only germline-appropriate transcripts. Findings from diverse species continue to provide insights into the shared and divergent needs of these special reproductive cells. © 2015 Macmillan Publishers Limited. All rights reserved. Source


Christie A.E.,Mount Desert Island Biological Laboratory
Cell and Tissue Research | Year: 2011

Decapod crustaceans have long served as important models for the study of neuroendocrine signaling. For example, the process of neurosecretion was first formally demonstrated by using a member of this order. In this review, the major decapod neuroendocrine organs are described, as are their phylogenetic conservation and neurochemistry. In addition, recent advances in crustacean neurohormone discovery and tissue mapping are discussed, as are several recent advances in our understanding of hormonal control in this group of animals. © 2011 Springer-Verlag. Source


Monahan-Earley R.,Beth Israel Deaconess Medical Center | Dvorak A.M.,Beth Israel Deaconess Medical Center | Aird W.C.,Beth Israel Deaconess Medical Center | Aird W.C.,Mount Desert Island Biological Laboratory
Journal of Thrombosis and Haemostasis | Year: 2013

Every biological trait requires both a proximate and evolutionary explanation. The field of vascular biology is focused primarily on proximate mechanisms in health and disease. Comparatively little attention has been given to the evolutionary basis of the cardiovascular system. Here, we employ a comparative approach to review the phylogenetic history of the blood vascular system and endothelium. In addition to drawing on the published literature, we provide primary ultrastructural data related to the lobster, earthworm, amphioxus, and hagfish. Existing evidence suggests that the blood vascular system first appeared in an ancestor of the triploblasts over 600 million years ago, as a means to overcome the time-distance constraints of diffusion. The endothelium evolved in an ancestral vertebrate some 540-510 million years ago to optimize flow dynamics and barrier function, and/or to localize immune and coagulation functions. Finally, we emphasize that endothelial heterogeneity evolved as a core feature of the endothelium from the outset, reflecting its role in meeting the diverse needs of body tissues. © 2013 International Society on Thrombosis and Haemostasis. Source


All eukaryotic and some prokaryotic ClC anion transport proteins have extensive cytoplasmic C-termini containing two cystathionine-β-synthase (CBS) domains. CBS domain secondary structure is highly conserved and consists of two α-helices and three β-strands arranged as β1-α1-β2-β3-α2. ClC CBS domain mutations cause muscle and bone disease and alter ClC gating. However, the precise functional roles of CBS domains and the structural bases by which they regulate ClC function are poorly understood. CLH-3a and CLH-3b are C. elegans ClC anion channel splice variants with strikingly different biophysical properties. Splice variation occurs at cytoplasmic N- and C-termini and includes several amino acids that form α2 of the second CBS domain (CBS2). We demonstrate that interchanging α2 between CLH-3a and CLH-3b interchanges their gating properties. The "R-helix" of ClC proteins forms part of the ion-conducting pore and selectivity filter and is connected to the cytoplasmic C-terminus via a short stretch of cytoplasmic amino acids termed the "R-helix linker". C-terminus conformation changes could cause R-helix structural rearrangements via this linker. X-ray structures of three ClC protein cytoplasmic C-termini suggest that α2 of CBS2 and the R-helix linker could be closely apposed and may therefore interact. We found that mutating apposing amino acids in α2 and the R-helix linker of CLH-3b was sufficient to give rise to CLH-3a-like gating. We postulate that the R-helix linker interacts with CBS2 α2, and that this putative interaction provides a pathway by which cytoplasmic C-terminus conformational changes induce conformational changes in membrane domains that in turn modulate ClC function. Source


Strange K.,Mount Desert Island Biological Laboratory
Channels (Austin, Tex.) | Year: 2011

CLC anion transport proteins function as Cl (-) channels and Cl (-) /H (+) exchangers and are found in all major groups of life including archaebacteria. Early electrophysiological studies suggested that CLC anion channels have two pores that are opened and closed independently by a "fast" gating process operating on a millisecond timescale, and a "common" or "slow" gate that opens and closes both pores simultaneously with a timescale of seconds (Figure 1A). Subsequent biochemical and molecular experiments suggested that CLC channels/transporters are homodomeric proteins ( 1-3) . Source

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