Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1974743 | Comparative Biochemistry and Physiology Part A: Molecular & Integrative Physiology | 2007 | 15 Pages |
Abstract
This review focuses on using the knowledge on volume-sensitive transport systems in Ehrlich ascites tumour cells and NIH-3T3 cells to elucidate osmotic regulation of salt transport in epithelia. Using the intestine of the European eel (Anguilla anguilla) (an absorptive epithelium of the type described in the renal cortex thick ascending limb (cTAL)) we have focused on the role of swelling-activated K+- and anion-conductive pathways in response to hypotonicity, and on the role of the apical (luminal) Na+-K+-2Clâ cotransporter (NKCC2) in the response to hypertonicity. The shrinkage-induced activation of NKCC2 involves an interaction between the cytoskeleton and protein phosphorylation events via PKC and myosin light chain kinase (MLCK). Killifish (Fundulus heteroclitus) opercular epithelium is a Clâ-secreting epithelium of the type described in exocrine glands, having a CFTR channel on the apical side and the Na+/K+ATPase, NKCC1 and a K+ channel on the basolateral side. Osmotic control of Clâ secretion across the operculum epithelium includes: (i) hyperosmotic shrinkage activation of NKCC1 via PKC, MLCK, p38, OSR1 and SPAK; (ii) deactivation of NKCC by hypotonic cell swelling and a protein phosphatase, and (iii) a protein tyrosine kinase acting on the focal adhesion kinase (FAK) to set levels of NKCC activity.
Keywords
OSR1NKCCRVDPKCCK2BAELTD4MLCKpKaRVIWNKste20PGE2Ehrlich ascites tumour cellsTASK-2EATCJnkc-Jun N-terminal kinaseAnguilla anguillaMAPKPTKsPTPsSeawaterfreshwaterUssing chamberBovine aortic endothelialSPAKELAOpercular epitheliumEETIntestinemyosin light chain kinaseVRACLeukotriene D4Fundulus heteroclitusprotein tyrosine phosphatasesProtein tyrosine kinasesProtein kinaseprotein kinase AProtein kinase Cmitogen-activated protein kinaseProstaglandin E2casein kinase
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Authors
E.K. Hoffmann, T. Schettino, W.S. Marshall,