Recombinant Human AQP5 Protein (His Tag)

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

The protein known as Aquaporin 5 often abbreviated as AQP5 is a member of the aquaporin family which are integral membrane proteins that function as channels for water. This particular protein facilitates water transport across cell membranes an action critical in maintaining fluid balance. Aquaporin 5 has a molecular mass of approximately 29 kDa. It is largely expressed in epithelial cells in various tissues including the salivary glands lacrimal glands and respiratory tissues. It is recognized by different names such as Aquaporin-5 and sometimes referenced in studies as Aquazol 5.

Biological function summary

Water transport and secretion processes heavily rely on the presence of Aquaporin 5. It is integral in the formation of tight junctions in epithelial cells enhancing cell permeability to water. Unlike some other aquaporins Aquaporin 5 operates independently and is not known to be part of a larger protein complex. Its presence influences the efficiency of fluid secretion affecting activities such as salivation and tear secretion. The capacity of AQP5 to control water movement tightly connects it to cellular hydration homeostasis.

Pathways

Aquaporin 5 is significantly involved in the regulation of water balance and osmotic equilibrium in epithelial tissues. Its role in fluid secretion pathways is interconnected with other proteins like Aquaporin 4 which share similar duties in the osmotic control of water. In the water transport pathways AQP5 coordinates with proteins like CFTR (Cystic Fibrosis Transmembrane Conductance Regulator) to manage fluid movement particularly in the respiratory passages and glands. The precise regulation of water flow by these pathways ensures that overall tissue hydration remains constant.

Aquaporin 5 is directly associated with conditions such as Sjögren's syndrome and xerostomia (dry mouth syndrome). During Sjögren's syndrome malfunction of AQP5 can lead to impaired salivary and tear secretion contributing to the symptoms of dryness. Furthermore defects or polymorphisms in AQP5 have implications in respiratory diseases potentially affecting proteins like Aquaporin 3 which shares functional similarities. Understanding the role of AQP5 in these conditions enables further exploration into therapeutic targets and treatment methods.