Please use this identifier to cite or link to this item:
|Title:||Expression of the transmembrane lysosomal protein SCARB2/Limp-2 in renin secretory granules controls renin release.||Austin Authors:||Lee, D ;Desmond, Michael J;Fraser, S A;Katerelos, M ;Gleich, Kurt;Berkovic, Samuel F ;Power, David Anthony||Affiliation:||Department of Nephrology, Austin Health, Heidelberg, Victoria, Australia||Issue Date:||26-Apr-2013||Publication information:||Nephron. Experimental Nephrology 2013; 122(3-4): 103-13||Abstract:||Renin processing and storage is believed to occur in lysosome-like structures in the afferent arteriole. SCARB2/Limp-2 is a transmembrane lysosomal protein responsible for the intracellular trafficking of β-glucocerebrosidase. This study aimed to confirm the expression of SCARB2/Limp-2 in renin secretory granules, and explore its role in renin processing and secretion.Co-localisation studies of (pro)renin with lysosomal membrane proteins, SCARB2/Limp-2, LAMP-1 and LAMP-2, were performed in mouse and human kidney sections. Intrarenal expression and secretion of (pro)renin in wild-type (WT) and Limp-2(-/-) mice were compared with and without stimulation.SCARB2/Limp-2, LAMP-1 and LAMP-2 co-localised with (pro)- renin in mouse and human kidney. Plasma renin concentration was increased in Limp-2(-/-) mice when compared to WT littermates. No change in (pro)renin expression, however, was observed in Limp-2(-/-) mouse kidney cortex by immunofluorescence microscopy, Western blotting, quantitative RT-PCR or the ultrastructural appearance of renin secretory granules. Acute stimulation of renin release by isoprenaline or hydralazine was similar in WT and Limp-2(-/-) mice. Following chronic salt restriction, however, immunofluorescence microscopy showed less (pro)renin expressed in Limp-2(-/-) compared with WT mouse kidneys, and there was significantly less prorenin but not renin by Western blotting in Limp-2(-/-) mouse kidney cortex, despite no difference in circulating renin levels.Renin secretory granules possess integral lysosomal proteins, confirming that they are indeed modified lysosomes. Limp-2 deficiency leads to a minor increase in circulating renin. Limp-2, however, is not required for acute or chronic stimulation of renin release.||Gov't Doc #:||23635510||URI:||http://ahro.austin.org.au/austinjspui/handle/1/11756||DOI:||10.1159/000350737||URL:||https://pubmed.ncbi.nlm.nih.gov/23635510||Type:||Journal Article||Subjects:||Animals
Lysosomal-Associated Membrane Protein 2
Lysosome-Associated Membrane Glycoproteins.biosynthesis
|Appears in Collections:||Journal articles|
Show full item record
checked on Nov 30, 2022
Items in AHRO are protected by copyright, with all rights reserved, unless otherwise indicated.