U Laforenza

U Laforenza

Group Members

U Laforenza
(Head of Laboratory)

G Gastaldi
(Associate Professor, Collaborator)

G Pellavio
(undergraduate project student)



Aquaporins (AQPs) are small transmembrane proteins (26–34 kDa) that were initially thought to function only as bidirectional water-selective channels, they have successively been found to play a role in important cellular functions, such as cell proliferation, cell differentiation, cell migration and cell adhesion.

Thirteen water channel proteins have been identified in mammals and they have been divided into three groups based on their structural and functional characteristics: (i) aquaporins (AQP1, 2, 4, 5, 6 and 8) selectively permeable to water; (ii) aquaglyceroporins (AQP3, 7, 9 and 10) permeable to glycerol, urea and other small solutes in addition to water; (iii) S-aquaporins (AQP11 and 12), with peculiar intracellular localization and functions. There are lines of evidence that modulation of AQP function or expression could have therapeutic potential in refractory glaucoma,  obesity, oedema, brain injury, and especially in cancer.

Current laboratory lines of investigation:
(i) aquaglyceroporins functions and regulation in human white adipose tissue: implication in obesity and type-2 diabetes.
(ii) Aquaporin-8 transport of  hydrogen peroxide regulation of  cell signaling, proliferation and survival.


Selected Papers


Mammalian aquaglyceroporin function in metabolism. Laforenza U, Bottino C, Gastaldi G.Biochim Biophys Acta. 2016 Jan;1858(1):1-11. doi: 10.1016/j.bbamem.2015.10.004.

Aquaporin-10 represents an alternative pathway for glycerol efflux from human adipocytes. Laforenza U, Scaffino MF, Gastaldi G. PLoS One. 2013;8(1):e54474. doi: 10.1371/journal.pone.0054474.

Water channel proteins in the gastrointestinal tract. Laforenza U. Mol Aspects Med. 2012 Oct-Dec;33(5-6):642-50. doi: 10.1016/j.mam.2012.03.001.

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