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	Aquaporins Essay
		Aquaporins, a large family of integral membrane proteins that share a common and novel fold, transport water across cell membranes at a rate so fast that it is effectively limited only by the rate of diffusion.
		AQP1, the first aquaporin to be identified, has been found to be constitutively present in apical and basolateral membranes in kidney nephrons, at levels sufficient to account for the observed level of water reabsorption by that tissue; in a variety of eye tissues; and in a variety of capillary endothelia.
		The sunflower aquaporins SunTIP17 and SunTIP20 are markedly upregulated in stomatal closure.
	urchin.earth.li /~sax/biochem/essays/aquaporins.html (2915 words)

	Aquaporins
		Functional characterization of the first aquaporin was reported in 1992, but water channels were suspected to exist well before that time, because the osmotic permeability of some types of epithelial cells was much too large to be accounted for by simple diffusion through the plasma membrane.
		Most aquaporins have a protein kinase A phosphorylation motif in one of the cytoplasmic loops, and differential phosphorylation is suspected empart a regulatory function to the molecule.
		Considering the importance of water transport in a myriad of physiologic processes, it is to be expected that lesions in aquaporin genes or acquired dysfunction in aquaporins may cause or contribute to several disease states.
	arbl.cvmbs.colostate.edu /hbooks/molecules/aquaporins.html (814 words)

	Aquaporin - Wikipedia, the free encyclopedia
		Aquaporins are a class of integral membrane proteins or more commonly refered as a class of major intrinsic proteins (MIP) that form pores in the membrane of biological cells.
		Aquaporins are made up of six transmembrane α-helices arranged in a right-handed bundle, with the amino and the carboxyl termini located on the cytoplasmic surface of the membrane.
		Aquaporins form tetramers in the cell membrane, and facilitate the transport of water and, in some cases, other small uncharged solutes, such as glycerol, CO, ammonia and urea across the membrane depending on the size of the pore.
	en.wikipedia.org /wiki/Aquaporin (1977 words)

	Structure, Dynamics, and Function of Aquaporins
		Aquaporins are a very lucky family of membrane proteins, which are notoriously resistant against structure determination.
		Although many aquaporins function as always-open channels, a subgroup of aquaporins, particularly in plants have evolved a sophisticated molecular mechanism through which the channel can be closed in response to harsh conditions of the environment, under which exchange of water can be harmful for the organism.
		It was found that an elongated cytoplasmic loop in gating-competent aquaporins physically occludes the entrance of the water pore in the closed channel and blocks the access of water molecules to the pore.
	www.ks.uiuc.edu /Research/aquaporins (1584 words)

	The Physics of the Kidney," Physics Research Highlights, University of Illinois at Urbana-Champaign
		Aquaporins are membrane water channels that play critical roles in controlling the water contents of cells.
		More than ten different aquaporins have been found in the human body, and several diseases, such as congenital cataracts and nephrogenic diabetes insipidus, are associated with the impaired function of these channels.
		Aquaporins form tetramers in the cell membrane and facilitate the transport of water and, in some cases, other small solutes across the membrane.
	www.physics.uiuc.edu /Research/Highlights/aquaporins.htm (516 words)

	Finding how water channels - aquaporins - open and close may lead to new drugs (Site not responding. Last check: 2007-10-13)
		Peter Agre discovered the first aquaporin in 1992 in red blood cells and was awarded the 2003 Nobel Prize.
		Even though there are different variants of aquaporin, they are all similar and work in largely the same way.
		Open aquaporins are necessary for cells to be able to move and form new blood vessels, which tumors are very dependent on to grow.
	www.news-medical.net /?id=14941 (719 words)

	RedOrbit - Science - A Brief Survey of Aquaporins and Their Implications for Renal Physiology
		Aquaporins (AQPs) are an important family of proteins that efficiently channel water through the cell membranes.
		Aquaporins are a family of channel proteins that facilitate osmosis, or the rapid movement of water, across virtually every cell membrane in our bodies.
		Aquaporins are implicated, either as the primary lesion or sec\ondarily, in numerous diseases.
	www.redorbit.com /news/science/519677/a_brief_survey_of_aquaporins_and_their_implications_for_renal/?source=r_science (4092 words)

	Interactive Fly, Drosophila
		The archetypal aquaporin AQP1 is a partly glycosylated water-selective channel that is widely expressed in the plasma membranes of several water-permeable epithelial and endothelial cells.
		Individual residues in MIP were replaced by residues conserved among the aquaporins, and introduction of a proline in the 5th transmembrane domain of MIP raises the Pf by 50%.
		Most of the aquaporins are delivered to the plasma membrane in a non-regulated (constitutive) fashion, but AQP2 enters the regulated exocytotic pathway and its membrane expression is controlled by the action of the antidiuretic hormone, vasopressin.
	www.sdbonline.org /fly/neural/bigbrn2.htm (2300 words)

	Aquaporins. A Molecular Entry into Plant Water Relations -- Maurel and Chrispeels 125 (1): 135 -- PLANT PHYSIOLOGY
		The capacity of some aquaporins to transport solutes was demonstrated using test molecules such as glycerol and urea, and the physiological significance of this property is not yet clearly understood (see text).
		Plant aquaporins similar to their animal counterparts are thought to form tetramers, each monomer being functionally independent.
		Aquaporins may be involved in a large number of physiological functions in plants.
	www.plantphysiol.org /cgi/content/full/125/1/135 (2752 words)

	Aquaporins (AQP0-10, AQPAP) And Urea Transporter (UT2) Antibodies
		Over the last decade, genes for several members of aquaporin family have been cloned, expressed, and their distribution studied in many tissues.
		The individual members of aquaporin family have identical predicted secondary structures with up to 6 highly conserved hydrophobic membrane spanning domains (about 18-25 AA each) and two conserved NPA motifs.
		Physiol 282, G324-G331, Aquaporins in rat pancreatic interlobular ducts IHC, aqp5 perosnal 4% PF rat pancreas.
	www.vincibiochem.it /ADI/aquaporin.html (1776 words)

	Aquaporins of the PIP2 Class Are Required for Efficient Anther Dehiscence in Tobacco -- Bots et al. 137 (3): 1049 -- ...
		Aquaporins of the PIP2 Class Are Required for Efficient Anther Dehiscence in Tobacco -- Bots et al.
		Aquaporins are membrane proteins that mediate the movement of
		O'Brien M, Bertrand C, Matton DP (2002) Characterization of a fertilization-induced and developmentally regulated plasma-membrane aquaporin expressed in reproductive tissues, in the wild potato Solanum chacoense Bitt.
	www.plantphysiol.org /cgi/content/full/137/3/1049 (4768 words)

	Cells direct membrane traffic by channel width, scientists say
		The roadway is in aquaporins, a class of proteins that form trans-membrane channels in cell walls in all forms of life.
		In humans, 11 aquaporins have been identified, mostly in the kidney, brain and lens of the eye.
		Aquaporins are a target of scrutiny for the Theoretical and Computational Biophysics Group at the Beckman Institute for Advanced Science and Technology.
	www.news.uiuc.edu /news/05/0810channels.html (685 words)

	Long-term regulation of aquaporins in the kidney -- Marples et al. 276 (3): 331 -- AJP - Renal Physiology
		Immunocytochemical localization of aquaporin water channels in semithin cryosections of rat kidney using affinity-purified antibodies and peroxidase-conjugated secondary antibodies.
		Impaired aquaporin and urea transporter expression in rats with adriamycin-induced nephrotic syndrome.
		Expression and distribution of aquaporin of collecting duct are regulated by vasopressin V2 receptor in rat kidney.
	ajprenal.physiology.org /cgi/content/full/276/3/F331 (5188 words)

	Altered expression of renal aquaporins and Na+ transporters in rats treated with L-type calcium blocker -- Wang et al. ...
		The aquaporins are a family of membrane proteins that function as water channels (37).
		Role of renal aquaporins in escape from vasopressin-induced antidiuresis in rat.
		Figueiredo, JF, and Falkenstein D. Effect of propranolol and nifedipine on in vitro fluid absorption by the isolated perfused proximal convoluted tubule of the rabbit.
	ajpregu.physiology.org /cgi/content/full/280/6/R1632 (5918 words)

	Plasma Membrane Aquaporins in the Motor Cells of Samanea saman: Diurnal and Circadian Regulation -- Moshelion et al. 14 ...
		aquaporins in the context of the rhythmic and reversible cell
		the reversal by DTT of the aquaporin inhibition, because the
		Yang, B.X., and Verkman, A.S. Water and glycerol permeabilities of aquaporins 1–5 and MIP determined quantitatively by expression of epitope-tagged constructs in Xenopus oocytes.
	www.plantcell.org /cgi/content/full/14/3/727 (6926 words)

	PIP1 and PIP2 aquaporins are differentially expressed during tobacco anther and stigma development -- Bots et al. 56 ...
		Marin-Olivier M, Chevalier T, Fobis-Loisy I, Dumas C, Gaude T. Aquaporin PIP genes are not expressed in the stigma papillae in Brassica oleracea.
		Characterization of a fertilization-induced and developmentally regulated plasma-membrane aquaporin expressed in reproductive tissues, in the wild potato Solanum chacoense Bitt.
		Uehlein N, Lovisolo C, Siefritz F, Kaldenhoff R. The tobacco aquaporin NtAQP1 is a membrane CO pore with physiological functions.
	jxb.oxfordjournals.org /cgi/content/full/56/409/113 (4586 words)

	Osmotic shrinkage of cells of Synechocystis sp. PCC 6803 by water efflux via aquaporins regulates osmostress-inducible ...
		Aquaporins are responsible for rapid efflux of water in a hyperosmotic
		Heymann, J. and Engel, A. Aquaporins: phylogeny, structure, and physiology of water channels.
		Heymann, J. and Engel, A. Structural clues in the sequences of the aquaporins.
	mic.sgmjournals.org /cgi/content/full/151/2/447 (2825 words)

	Chrispeels Laboratory
		Aquaporins are water channel proteins that permit faster transport of water through cellular membranes.
		Aquaporins form a large gene family of about 35 genes.
		Phylogenetic tree showing the four subfamilies of Aquaporins.
	www-biology.ucsd.edu /labs/chrispeels/researchAQP1.htm (42 words)

	Aquaporins in complex tissues. I. Developmental patterns in respiratory and glandular tissues of rat -- King et al. ...
		Distribution of aquaporins in lung, upper airway, and salivary gland of adult rat.
		All four aquaporins are strongly expressed in the nasopharynx of postnatal rats.
		Ontogeny of the aquaporins is known to be complex.
	ajpcell.physiology.org /cgi/content/full/273/5/C1541 (3777 words)

	One protein, two channels Scientists explain mechanism in aquaporins
		Using computer simulations and experimental results, researchers at the University of Illinois at Urbana-Champaign and the University of Arizona have identified a key component of the gating mechanism in aquaporins that controls both the passage of water and the conduction of ions.
		Aquaporins are a class of proteins that form membrane channels in cell walls and allow for water movement between a cell and its surroundings.
		Gating of the central pore is controlled by cyclic guanosine monophosphate, a signaling nucleotide inside the cell, which induces a conformational change in one of the aquaporin loops (loop D).
	www.physorg.com /news78071321.html (691 words)

	Gene Information
		Aquaporins are water channels that are usually found in tissues where water movements are abundant and/or physiologically important.
		Aquaporins were expressed in both oocytes and embryos, but the types were different among the developmental stages: aquaporins 3 and 7 were expressed in oocytes and embryos at all stages examined, but aquaporins 8 and 9 were expressed only in blastocysts.
		On the other hand, aquaporins 1, 2, 4, 5, and 6 were not detected in any of the stages examined.
	ovary.stanford.edu /4_display.html?rec=955 (438 words)

	Nobelist Agre To Give NIH Director's Lecture, February 15, 2005 NIH Record - National Institutes of Health (NIH)
		More than 10 aquaporins have now been identified in humans and the clinical implications are enormous, Agre said.
		Several labs are using the newfound information on aquaporins to try to develop treatments for various diseases and conditions.
		Or, conversely, an overabundance of aquaporins may lead to fluid retention in congestive heart failure and in pregnancy.
	www.nih.gov /nihrecord/02_15_2005/story03.htm (651 words)

	Scientists document water molecule movement across cell walls
		Aquaporins, a class of proteins, form transmembrane channels found in cell walls.
		The structure of aquaporins was determined two years ago by Robert M. Stroud and colleagues at UCSF, who determined the geometry of the protein in the bacterium E. coli (GlpF).
		However, Shulten said, that work "still could not resolve exactly how water is conducted in the channel, and how it prevents the conduction of ions." Crystallographic methods available today cannot capture such minute detail, he said.
	www.news.uiuc.edu /scitips/02/0418aquaporins.html (624 words)

	Key Roles of Renal Aquaporins in Water Balance and Water-Balance Disorders -- Nielsen et al. 15 (3): 136 -- Physiology
		At least three aquaporins are known to be expressed in the kidney
		Aquaporins are water channels allowing passive flux of water
		Knepper, M. Molecular physiology of urinary concentrating mechanism: regulation of aquaporin water channels by vasopressin.
	physiologyonline.physiology.org /cgi/content/full/15/3/136 (3226 words)

	Understanding aquaporins may lead to new drugs - SWEDEN.SE (Site not responding. Last check: 2007-10-13)
		It may also pave the way for a new type of drug and for new cosmetic products.
		Aquaporins contain a conduit that is so tiny that only a single water molecule at a time can pass through it.
		Previously it had only been possible to produce open aquaporins.
	www.sweden.se /templates/cs/Print_News____14157.aspx (541 words)

	Reconstitution of water channel function of aquaporins 1 and 2 by expression in yeast secretory vesicles -- Coury et ...
		Aquaporins 1 (AQP1) and 2 (AQP2) were expressed in the yeast secretory mutant sec6-4.
		Aquaporins are members of the larger MIP family of proteins based on sequence homology (33).
		Molecular cloning and expression of a member of the aquaporin family with permeability to glycerol and urea in addition to water expressed at the basolateral membrane of kidney collecting duct cells.
	ajprenal.physiology.org /cgi/content/full/274/1/F34 (4111 words)

	The Role of Aquaporins in Root Water Uptake -- JAVOT and MAUREL 90 (3): 301 -- Annals of Botany
		Aquaporins are membrane proteins that belong to the major intrinsic
		aquaporin gene expression that occurs in response to salinity
		Characterization of a maize tonoplast aquaporin expressed in zones of cell division and elongation.
	aob.oxfordjournals.org /cgi/content/full/90/3/301 (7838 words)

	Highly selective water channel activity measured by voltage clamp: Analysis of planar lipid bilayers reconstituted with ...
		Aquaporins are membrane channels selectively permeated by water or water plus glycerol.
		Several studies have suggested that some aquaporins may be permeated by ions, raising the question of whether this is a general
		Unlike most aquaporins, AqpZ is not sensitive to mercurial compounds (5), so the presence of an aqueous pore was established
	www.pnas.org /cgi/content/full/98/17/9624 (3432 words)

	The Distribution of Aquaporin Subtypes (PIP1, PIP2 and {gamma}-TIP) is Tissue Dependent in Soybean (Glycine max) Root ...
		The Distribution of Aquaporin Subtypes (PIP1, PIP2 and {gamma}-TIP) is Tissue Dependent in Soybean (Glycine max) Root Nodules -- FLEURAT-LESSARD et al.
		High expression of the tonoplast aquaporin ZmTIP1 in epidermal and conducting tissues of maize.
		Chrispeels MJ, Maurel C. Aquaporins: the molecular basis of the facilitated water movement through living plant cells.
	aob.oxfordjournals.org /cgi/content/full/96/3/457 (1943 words)

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