ASN's Mission

To create a world without kidney diseases, the ASN Alliance for Kidney Health elevates care by educating and informing, driving breakthroughs and innovation, and advocating for policies that create transformative changes in kidney medicine throughout the world.

learn more

Contact ASN

1401 H St, NW, Ste 900, Washington, DC 20005

email@asn-online.org

202-640-4660

The Latest on X

Kidney Week

Abstract: TH-PO1024

Expression of Phosphate-Dependent Glutaminase (PDG) in Normal and Neoplastic Human Kidney

Session Information

  • Acid Base: Basic
    November 02, 2017 | Location: Hall H, Morial Convention Center
    Abstract Time: 10:00 AM - 10:00 AM

Category: Fluid, Electrolytes, and Acid-Base

  • 701 Acid-Base: Basic

Authors

  • Lee, Hyun-Wook, University of Florida, Gainesville, Florida, United States
  • Clapp, William L., University of Florida, Gainesville, Florida, United States
  • Wakefield, Dara N., University of Florida, Gainesville, Florida, United States
  • Verlander, Jill W., University of Florida, Gainesville, Florida, United States
  • Weiner, I. David, University of Florida, Gainesville, Florida, United States
Background

Phosphate-dependent glutaminase (PDG) is a mitochondrial protein that has a critical role in renal ammonia metabolism, catalyzing the initial step in ammoniagenesis, and may have a role in glutamine-derived ATP generation. The cellular distribution of PDG in the human kidney is currently unknown. This study’s purpose was to determine PDG's cellular expression in normal and neoplastic human kidney.

Methods

We used human kidney tissues from unused portions of nephrectomy specimens removed during routine treatment of renal cell carcinoma for immunohistochemistry studies. Three separate PDG antibodies were used; all gave similar results. Normal human kidney protein lysates were obtained from commercial sources.

Results

Immunoblot analysis of both human whole kidney and cortical protein revealed an ~63 kDa protein. Immunohistochemistry showed PDG immunolabel throughout the nephron and in arterial walls in a granular pattern consistent with mitochondrial expression. Glomerular label was punctate and weak compared to tubules. Tubule distribution of PDG was verified using H+-ATPase and NKCC2 as markers. Strong PDG expression was present in proximal tubule, descending and ascending thin limb, thick ascending limb, distal convoluted tubule, connecting segment (CNT), and throughout the collecting duct (CD). Cellular heterogeneity in label intensity was evident in CNT and CD profiles. PDG expression in kidney neoplasms varied among tumor types. In tumors of presumed proximal tubule origin, clear cell and papillary renal cell carcinoma (RCC), weak, 1+, PDG immunolabel was present. In tumors of presumed intercalated cell tubule origin, oncocytoma and chromophobe RCC, PDG immunolabel was substantially more intense, 2-3+, and immunolabel intensity was greater in oncocytoma than in chromophobe RCC.

Conclusion

1) PDG is widely expressed in epithelial and non-epithelial cells in the human kidney. 2) PDG expression in RCC varies with tumor type; it is weakly expressed in clear cell and papillary RCC, whereas in oncocytoma and chromophobe RCC it is expressed more strongly. 3) This wide-spread expression suggests PDG may have critical roles both in ammoniagenesis and glutamine-derived ATP generation.

Funding

  • NIDDK Support