PRSS8 Membrane Protein Introduction

Introduction of PRSS8

Protease serine 8 (PRSS8), a trypsin-like serine peptidase (40 kDa), is also known as Prostasin. PRSS8 is encoded by the gene PRSS8 in humans, which is located on chromosome 16p11.2. It is a glycophosphatidylinositol-anchored protein that is widely found in the prostate gland, kidney, bronchi, colon, liver, lung, pancreas, and salivary glands, with the highest expression in prostate epithelia. Since the first isolation from seminal fluid, PRSS8 has shown important physiological and pathological functions.

Function of PRSS8 Membrane Protein

The widespread localization of PRSS8 indicates that it may have different roles in multiple biological processes. One of the well-known functions of PRSS8 is to act as a proteolytic activator of the epithelial sodium channel (ENaC) in vitro and play a major role in regulating sodium balance. In addition, PRSS8 is reported to play important roles in maintaining the epidermal permeability barrier, regulating the inducible nitric oxide synthase gene expression during lipopolysaccharide-induced bladder inflammation, and regulating transepithelial resistance and current. Recently, PRSS8 deficiency has been detected in various human cancers, including prostate cancer, breast cancer, bladder cancer, gastric cancer, colorectal cancer as well as esophageal squamous cell carcinomas. Moreover, PRSS8 overexpression can inhibit tumor cell growth and metastasis and block cancer cell migration, invasion, colony formation and tumor sphere formation in vitro, but decreased PRSS8 expression facilitates malignancies in vivo and in vitro.

Fig.1 Proposed mechanism of the physiological functions of the matriptase/prostasin proteolytic pathway during development. (Szabo, 2016)

Application of PRSS8 Membrane Protein in Literature

1. Szabo R. and Bugge T.H. Loss of HAI-2 in mice with decreased prostasin activity leads to an early-onset intestinal failure resembling congenital tufting enteropathy. PLoS One. 2018, 13: e0194660. PubMed ID: 29617460
   
   

   This article indicates that the loss of HAI-2 in Prss8R44Q/R44Q mice leads to the development of progressive intestinal failure that bears a striking resemblance to human congenital tufting enteropathy, providing important clues for understanding and treating this debilitating human disease.

2. Lee S.P., et al. Tissue distribution and subcellular localizations determine in vivo functional relationship among prostasin, matriptase, HAI-1, and HAI-2 in human skin. PLoS One. 2018, 13, e0192632. PubMed ID: 29438412
   
   

   This study suggests the importance of tissue distribution and subcellular localization in the functional relationship between prostasin, matriptase, HAI-1, and HAI-2.

3. Oxlund C., et al. Albuminuria is associated with an increased prostasin in urine while aldosterone has no direct effect on urine and kidney tissue abundance of prostasin. Pflugers Arch. 2017, 469: 655-667. PubMed ID: 28233126
   
   

   This study suggests the reduction of urinary prostasin in spironolactone-treated patients is most likely the result of an improved glomerular filtration barrier function and generally reduced proteinuria.

4. Shiao F., et al. Selective Inhibition of Prostasin in Human Enterocytes by the Integral Membrane Kunitz-Type Serine Protease Inhibitor HAI-2. PLoS One. 2017, 12: e0170944. PubMed ID: 28125689
   
   

   This article studies the functional linkage of HAI-2 with two membrane-associated serine proteases, matriptase and prostasin in Caco-2 cells and the human GI tract, suggesting that dysregulated prostasin proteolysis may be particularly important in the GI tract when HAI-2 function is lost and/or dysregulated.

5. Bastani A., et al. Evaluation of the sensitivity and specificity of serum level of prostasin, CA125, LDH, AFP, and hCG+beta in epithelial ovarian cancer patients. Eur J Gynaecol Oncol. 2017, 38: 418-424. PubMed ID: 29693884
   
   

   The authors in this article describe a multimarker approach, consisting of cancer antigen 125 (CA125), lactate dehydrogenase (LDH), alpha-fetoprotein (AFP), human chorionic gonadotropin (hCG+β), and prostasin, that could provide a more accurate tool for a differential diagnosis of patients with epithelial ovarian cancer (EOC).

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Reference

1. Szabo R, et al. (2016). Delineation of proteolytic and non-proteolytic functions of the membrane-anchored serine protease prostasin. Development. 143: 2818-2828.

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