A down regulated event with possible diverse function PIP2;1.

Expression of human AQP8-aquaporin and plant Arabidopsis TIP1;1 and TIP1;2[1] produces reactive oxygen species potentially toxic compounds, that function in signaling to cross membranes. At present, 13 human AQPs are known (Colton blood group) permeable to the osmotic water permeability and ammonia relevant to the regulation of mitochondria metabolisms in non-apoptotic thymocytes possible functional role not associated with osmotic and ischemic stresses. This event is driven by a loss of intracellular K(+), drawing water out of the cell through AQPs (aquaporins) coupled with continued K(+) efflux allowing the completion of the apoptotic cascade. These proteins are members of the larger family of major intrinsic proteins (MIPs) tentatively identified as intravacuolar invaginations the Na(+)/H(+) antiporter that cross reacted with PIP2;1 aquaporin AT5G10420 antiporter/ drug transporter . All PIP and TIP aquaporin transcripts in close proximity to the vascular tissue[1]. A clone (AQP10) in human with other aquaporins represents a new member of aquaglyceroporins [3H] and Na(+)/K(+)-ATPase [AQP8] was determined indicate that the physiological importance of each AQP may be different in various tissues of animals.

Wellner, R.B., Redman, R.S., Swaim, W.D., Baum, B.J. (2006). Further evidence for AQP8 expression in the myoepithelium of rat submandibular and parotid glands. Pflügers Archiv - European Journal of Physiology, 451(5), 642-645. DOI: 10.1007/s00424-005-1489-0; [§§]