SLC12A7 Membrane Protein Introduction

Introduction of SLC12A7

SLC12A7, a member of the SLC12 family, is a 1083 amino acid long, transmembrane protein. Its primary physiologic function is to regulate cell volume via trans-membrane potassium and chloride transport. However, recently it has been implicated that SLC12A7 plays a significant role in the development and malignant behavior of several different cancer types. SLC12A7 is found to be overexpressed in cervical, ovarian and breast cancer tissues. It is also shown to promote tumor cell growth in vitro and in vivo. It is also demonstrated that SLC12A7 colocalizes to the lamellipodia of tumor cells with ezrin, a membrane cytoskeleton linker and promotes cell migration and invasion. Overexpression of SLC12A7 has been associated with local tumor invasion, lymph node metastases, and poor clinical outcomes in cervical, ovarian, and breast cancers.

Function of SLC12A7 Membrane Protein

SLC12A7 is a protein that can regulate cell volume via trans-membrane potassium and chloride transport; it has also been reported to have other functions, including electroneutral potassium-chloride cotransport when activated by cell swelling, K⁺ uptake into Deiters' cells in the cochlea and K⁺ recycling in the inner ear. Moreover, it is also important for the survival of cochlear outer/inner hair cells and the maintenance of the organ of Corti. Recent research shows that it may also be required for basolateral Cl⁻ extrusion in the kidney and contribute to renal acidification. SLC12A7 can be activated by N-ethylmaleimide (NEM). Common inhibitors for this protein contain furosemide, DIDS and bumetanide. The inhibition is much stronger with the presence of 50 mM K⁺ in the uptake medium. It affects chloride symporter activity and protein kinase binding, and also regulates biological process like cell volume homeostasis, chemical synaptic transmission and ion transport.

Fig.1 Chloride transport is carried out by the chloride channel ClC-Kb and potassium chloride cotransporter 4 in DCT.

Application of SLC12A7 Membrane Protein in Literature

1. Brown T.C., et al. DNA copy amplification and overexpression of SLC12A7 in adrenocortical carcinoma. Surgery. 2016, 159(1):250-7. PubMed ID: 26454676
   
   

   This article shows that SLC12A7 gene amplification and overexpression occurs frequently in ACC and may represent a novel molecular event associated with ACC.

2. Brown T.C., et al. SLC12A7 alters adrenocortical carcinoma cell adhesion properties to promote an aggressive invasive behavior. Cell Commun Signal. 2018, 16(1):27. PubMed ID: 29884238
   
   

   This article shows the amplification of SLC12A7 observed in ACCs, in vitro, to exacerbate the malignant behavior of ACC cells by promoting invasive capacities. It is possibly mediated by alterations in multiple signaling pathways, including the osmotic stress pathway.

3. Boettger T., et al. Deafness and renal tubular acidosis in mice lacking the K-Cl co-transporter Kcc4. Nature. 2002, 416(6883):874-8. PubMed ID: 11976689
   
   

   In this article, authors find that deafness in Kcc4-deficient mice is associated with renal tubular acidosis. It is probably brought by an impairment of Cl(-) recycling across the basolateral membrane of acid-secreting alpha-intercalated cells of the distal nephron.

4. Karadsheh M.F., et al. Localization of the KCC4 potassium-chloride cotransporter in the nervous system. Neuroscience. 2004, 123(2):381-91. PubMed ID: 14698746
   
   

   Their results show that KCC4 is expressed on the apical membrane of the choroid plexus, where it likely participates in K(+) reabsorption. KCC4 is also expressed in peripheral neurons, where its function remains to be determined.

5. Velázquez H. and Silva T. Cloning and localization of KCC4 in rabbit kidney: expression in distal convoluted tubule. Am J Physiol Renal Physiol. 2003, 285(1):F49-58. PubMed ID: 12709395
   
   

   This article postulates that KCC4 mediates potassium and chloride exit from the cell and may play an important role in salt absorption by the distal convoluted tubule.

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