Linked Life Data

16749244

Source:http://linkedlifedata.com/resource/pubmed/id/16749244

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2006-6-5
pubmed:abstractText
Virtually all human cells incorporate aquaporins, or water channel proteins, into their cell membrane. Indeed, many cells produce several aquaporins, each adapted for a specific physiologic function. Thus, it is not surprising that aquaporin malfunctions are associated with numerous important clinical conditions. This article describes the clinical aspects of malfunctions in aquaporins or their regulation. Although water can diffuse across biological membranes (osmosis) without the aid of a transport system, researchers had predicted for decades that rapid reabsorption by renal tubule cells must be aided by a channel or pore. Yet, not until the 1990s were the first members of the aquaporin (AQP) family identified. Led by Dr. Peter Agre, recipient of the 2003 Nobel Prize in Chemistry, researchers have since amassed an astounding amount of information about AQPs and their function. For example, the flow rate of water through AQP1 is an extraordinary three billion water molecules per second per aquaporin channel, while a relative trickle of water crosses the hydrophobic lipid bilayer of cell membranes devoid of AQPs. Our understanding of renal physiology and pathophysiology has advanced greatly as we account for the subtle implications of various AQP systems. For example, nephrogenic diabetes insipidus (NDI), the inability to produce concentrated urine, can result from several different malfunctions in the hormonally controlled AQP2 system. The list of diseases known to involve AQPs now includes: early onset of cataracts, Sjogren's syndrome, cerebral and pulmonary edemas, cirrhotic liver development of ascites, and congestive heart failure (CHF).
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
T
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0894-959X
pubmed:author
pubmed:issnType
Print
pubmed:volume
19
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
80-9
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
CLS meets the aquaporin family: clinical cases involving aquaporin systems.
pubmed:affiliation
Department of Clinical Laboratory Science, University of Illinois at Springfield, IL 62703, USA. gade.wayne@uis.edu
pubmed:publicationType
Journal Article, Review