Abstract

Thirteen members of aquaporin (AQP), a water channel, are expressed in mammals. In this review, we briefly overview these mammalian AQPs, then focus on AQP5, an exocrine gland-type AQP. Namely, we discuss: (1) the mechanism for coupling of AQP5 dynamics with the secretion and restoration cycle of amylase after isoproterenol (IPR) in the parotid gland (PG); (2) roles of parasympathetic nerve for maintaining AQP5 level in the submandibular gland (SMG), and; (3) AQP5 down-regulation in an experimental pathological model by LPS administration in the PG. We then move to the effects of single nucleotide mutation (SNP) found in rats and humans and its affected phenotypes. That is, G308A point mutation found in rat AQP5 cDNA resulted in amino acid substitutions of Gly103 for Asp103, and causes diminished expression of its protein product. In humans, several SNPs in AQP5 are found in European and Chinese families and cause autosomal-dominant diffuse nonepidermolytic palmoplantar keratoderma.

Highlights

  • One of the characteristics of cell membranes is their semi-permeability

  • These results suggest the aquaporin 5 (AQP5) levels in the submandibular gland (SMG) is maintained by the parasympathetic nerve, and that this water channel in the parotid gland (PG) is translocated to the apical membrane in conjunction with trafficking/docking of secretory granules containing amylase upon stimulation with β-adrenergic agents (Hosoi et al, 2020)

  • AQP5 is involved in water secretion from the salivary gland acinar cells via a transcellular route

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Summary

Introduction

One of the characteristics of cell membranes is their semi-permeability. This feature allows water to enter and exit cells. Aquaporin (AQP) is a membrane protein with a serpentine-type structure which functions as a water channel. CDNA for AQP5 was first cloned from the salivary gland; it is known as an exocrine-type water channel with a unique tissue expression (Raina et al, 1995).

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