Summary
Mature juxtaglomerular epithelioid cell secretory granules of the rat exhibit both renin-and cathepsin D-like immunoreactivity. On the basis of the coexistence with renin at a pH which, according to previous experiments, is probably in the range of that in lysosomes, cathepsin D is suggested to be involved in the regulation of the granular renin stores available for secretion.
Similar content being viewed by others
References
Farquhar MG (1977) Secretion and crinophagy in prolactin cells. Adv Exp Med Biol 80:37–94
Fisher, ER (1966) Lysosomal nature of juxtaglomerular granules. Science 152:1752–1753
Gomba Sz, Soltesz MB (1969) Histochemistry of lysosomal enzymes in juxtaglomerular cells. Experientia 25:513
Hopkins CR (1969) The fine structural localization of acid phosphatase in the prolactin cell of the teleost pituitary following the stimulation and inhibition of secretory activity. Tissue Cell 1:653–671
Lee JC, Hurley S, Hopper J Jr (1966) Secretory activity of the juxtaglomerular granular cells of the mouse. Morphologic and enzyme histochemical observations. Lab Invest 15:1459–1476
Katunuma N, Kominami E (1983) Structures and functions of lysosomal thiol proteinases and their endogenous inhibitor. Curr Top Cell Regul 22:71–101
Newman GR, Jasani B (1984) Post-embedding immunoenzyme techniques. In: Polak JM, Varndell IM (eds) Immunolabelling for electron microscopy. Elsevier, Amsterdam New York Oxford, pp 53–70
Newman GR, Jasani B, Williams ED (1983) A simple post-embedding system for the rapid demonstration of tissue antigens under electron microscope. Histochem J 15:543–555
Ogunro EA, Lanman RB, Spencer JR, Ferguson, AG, Lesch m (1979) Degradation of canine cardia myosin and actin by cathepsin D isolated from homologous tissue. Cardiovasc Res 13:621–629
Schwartz WN, Bird JWC (1977) Degradation of myofibrillar proteins by cathepsins B and D. Biochem J 167:811–820
Smith RE, Farquhar MG (1966) Lysosome function in the regulation of the secretory process in cells of the anterior pituitary gland. J Cell Biol 31:319–347
Steiner DG, Docherty K, Chan SJ, San Segundo B, Carroll B (1983) Intracellular propeolytic mechanisms in the biosynthesis of hormones and peptide neurotransmitters. In: Koch G, Richter D (eds) Biochemical and clinical aspects of neuropeptides: Synthesis, processing, and gene structure. Academic Press, London New York, pp 3–13
Takahashi S, Murakami K, Miyake Y (1982) Activation of kidney prorenin by kidney cathepsin B isozymes. J Biochem 91:419–422
Taugner R, Bührle Ch Ph, Nobiling R (1984a) Ultrastructural changes associated with renin secretion from the juxtaglomerular apparatus of mice. Cell Tissue Res 237:459–472
Taugner R, Bührle CP, Hackenthal E, Mannek E, Nobiling R (1984b) Morphology of the juxtaglomerular apparatus and secretory mechanisms. Contr Nephrol 43:76–101
Taugner R, Whalley A, Angermüller S, Bührle CP, Hackenthal E (1985a) Are the renin-containing granules of juxtaglomerular epithelioid cells modified lysosomes? Cell Tissue Res 239:575–587
Taugner R, Bührle CP, Nobiling R, Kirschke H (1985b) Coexistence of renin and cathepsin B in epithelioid cell secretory granules. Histochemistry 83:103–108
Yokota S, Tsuji H, Kato K (1985) Immunocytochemical localization of cathepsin D in lysosomes of cortical collecting tubule cells of the rat kidney. J Histochem Cytochem 33:191–200
Author information
Authors and Affiliations
Additional information
These studies were supported by the German Research Foundation within the SFB 90 “Cardiovasculäres System”
Rights and permissions
About this article
Cite this article
Taugner, R., Yokota, S., Bührle, C.P. et al. Cathepsin D coexists with renin in the secretory granules of juxtaglomerular epithelioid cells. Histochemistry 84, 19–22 (1986). https://doi.org/10.1007/BF00493415
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1007/BF00493415