title: Endothelial distribution of the membrane water channel molecule aquaporin-1: implications for tissue and lymph fluid physiology?
abstract: BACKGROUND
  Aquaporin-1 (AQ-1) is a transmembrane water channel protein reportedly expressed in continuous capillary endothelium and intestinal lacteals. We investigated endothelial AQ-1 expression in rat intestine and mesentery, and also in lymph nodes.
  
  
  RESULTS
  Rat intestine, mesentery, and lymph nodes were immunolabeled for AQ-1, revealing membrane expression in endothelial cells of vascular continuous capillaries and venules, and of initial and conducting lymphatics. Blood vessel profiles were identified with RECA-1 and circulating FITC-albumin. In nodes, capillaries and high endothelium venules (HEVs) showed AQ-1 labeling, as did intranodal lymphatic sinusoidal endothelium and reticular cells.
  
  
  CONCLUSIONS
  The labeling pattern of vessels with RECA-1, AQ-1, circulated FITC albumin, plus elastin autofluorescence permitted identification of arteriolar, continuous, and fenestrated capillaries and lymphatic vessels in tissue sections. Strong AQ-1 expression in continuous microvascular and initial lymphatic endothelium suggests its possible involvement in tissue fluid exchange between plasma and interstitial fluid, and perhaps between interstitial fluid and initial lymph. Endothelial AQ-1 expression was strong in lymphatic sinusoidal endothelium and intense in HEVs. This described endothelial AQ-1 expression has potential implications for tissue fluid physiology. Lymph protein is known to concentrate in lymph nodes by fluid loss, so AQ-1 may facilitate lymph to plasma water flux. Starling forces may not drive this flux, and we discuss a possible osmotic mechanism; consequently we hypothesize a suite of ion pumps/channels/exchangers/cotransporters in nodal vascular (probably HEV) endothelium, acting as a net ion pump from lymph to plasma, with water following osmotically.
authors.affiliation: Microcirculation and Lymphology Laboratory, Department of Anatomy, School of Medicine, & Center for Heart, Lung & Circulation Research, Flinders University, Adelaide, South Australia. bren.gannon@flinders.edu.au
authors.forename: Bren J
authors.initials: BJ
authors.lastname: Gannon
authors.forename: C J
authors.initials: CJ
authors.lastname: Carati
mesh_terms: D000818:Animals; D051398:Aquaporin 1; D020346:Aquaporins / Q000502:physiology*; D002196:Capillaries; D004729:Endothelium, Lymphatic / Q000473:pathology*; D004730:Endothelium, Vascular / Q000473:pathology; D005260:Female; D007413:Intestinal Mucosa / Q000378:metabolism; D007422:Intestines / Q000473:pathology; D007477:Ions; D008196:Lymph / Q000378:metabolism; D008198:Lymph Nodes / Q000473:pathology; D008208:Lymphatic System / Q000502:physiology*; D042601:Lymphatic Vessels / Q000473:pathology; D008297:Male; D008643:Mesentery / Q000378:metabolism; D008856:Microscopy, Fluorescence; D018715:Microscopy, Video; D008954:Models, Biological; D009995:Osmosis; D011312:Pressure; D017434:Protein Structure, Tertiary; D051381:Rats; D017207:Rats, Sprague-Dawley; D014867:Water / Q000378:metabolism
chemical_list: C496022:Aqp1 protein, rat; D020346:Aquaporins; D007477:Ions; D014867:Water; D051398:Aquaporin 1