Please use this identifier to cite or link to this item: https://ahro.austin.org.au/austinjspui/handle/1/11756
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
Antigens, CD36.biosynthesis
Arterioles.metabolism
Female
Humans
Kidney.blood supply
Lysosomal-Associated Membrane Protein 2
Lysosome-Associated Membrane Glycoproteins.biosynthesis
Lysosomes.metabolism
Male
Mice
Rats
Receptors, Scavenger.biosynthesis
Renin.secretion
Secretory Vesicles.metabolism
Appears in Collections:Journal articles

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