Abstract
The physiologic effect of a hormone is governed by its bioavailability to receptors on the target organ. Chertow (1) has suggested that proteases can potentially regulate hormone availability by 1) intracellular conversion of precursor hormones to active hormones, 2) degradation of hormone in the cell prior to secretion, 3) facilitation of release of hormone from the cell, 4) activation or inactivation of the hormone in the circulation, and 5) degradation of hormone in target tissue. These regulatory mechanisms particularly apply to polypeptide hormones and enzymes, which are produced as larger molecular weight precursors and subsequently converted by limited proteolysis to their secreted forms.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
B.S. Chertow, The role of lysosomes and proteases in hormone secretion and degradation, Endo Rev., 2: 137 (1981).
G. Palade, Intracelluiar aspects of the process of protein synthesis, Science, 189: 347 (1975).
V.R. Lingappa and G. Blobel, Early events in the biosynthesis of secretory and membrane proteins: the signal hypothesis, Rec. Prog. Horm. Res. 36: 451 1980.
E. Barat, A. Patthy, and L. Graf, Action of cathepsin D on human β-lipotropin: a possible source of 3-melanotropin, Proc. Nati. Acad. Sci. USA 76: 6120 (1980).
R.V. Lewis, A.S. Stern, S. Kimura, J. Rossier, S. Stein, and S. Undenfriend, An about 50, 000-Dalton protein in adrenal medulla: a common precursor of [Met]-and [Leu], Enkephalin. Sci. 208: 1459 1980.
R.B. Puri, K. Anjaneyulu, J.R. Kidwai, and V.K.M. Rao, In vitro conversion of proinsul in to insulin by cathepsin B and role of C-peptide, Acta Diabetol. Lat. 15: 243 (1978).
J. Fischer, Precursor processing and metabolism of parathyroid hormone (PTH), this symposium.
J.A. Luetscher, J.W. Bialek, and G. Grislis, Human kidney cathepsins B and H activate and lower the molecular weight of human inactive renin, Clin. Expt. Hypertension (in press, 1982).
B.S. Chertow, D.J. Manke, G.A. Williams, G.R. Baker, G.K. Hargis, and R.J. Buschmann, Secretory and ultrastructural responses of hyperfunctioning human parathyroid tissues to varying calcium concentration and vinblastine, Lab. Invest. 36: 193 1977.
D.F. Sterner and H.S. Tager, Biosynthesis of insulin and glucagon, in: “Endocrinology,”, L.J. DeGroot, Grune and Stratton, New York (1979).
D.F. Steiner, W. Kemmler, H.S. Tager, A.H. Rubenstein, A. Lernmark, and A. Zuhlke, Mechanisms in the biosynthesis of polypeptide hormones, in “Proteases and Biological Control,” E. Reich, D.B. Rifkin, and E. Shaw, Cold Spring Harbor Laboratory, Col Spring Harbor (1975).
H.A. Virji, J.D. Vassalli, R.D. Estensen, and E. Reich, Plasminogen activator of islets of Langerhans: modulation by glucose and correlation with insul in production, Proc. Natl. Acad. Sci. USA 77: 875 (1980).
C.C. Yip, A bovine pancreatic enzyme catalyzing the conversion of proinsulin to insulin, Proc. Natl. Acad. Sci. USA 68: 1312 1971.
O. Ole-Moiyoi, G.S. Pinkus, J. Spragg, and K.F. Austen, Identification of human glandular kallikrein in the β cells of the pancreas, N Eng. J. Med. 200: 1289 1979.
G. Bommer, H-J. Schafer, and G. Koppel, Morphological effects of diazoxide and dephenylhydanto in on insulin secretion and biosynthesis in B cells of mice, Virchows. Arch. [Pathol. Anat.] 371: 227 1976.
W. Creutzfeldt, C. Cruetzfeldt, H. Frerichs, E. Perings, and R. Sickinger, The morphological substrate of the inhibition of insulin secretion by diazoxide, Horm. Metab. Res. 1: 53 (1969).
C.L.G. Dumm, O.R. Rebolledo, and J.J. Gargliardino, Ultrastructural responses of pancreatic β cells to metabolic alkalosis, Cell Tissue Res. 201: 159 1979.
G.A. Burghen, R.A. McKenzie, and T.M. Howarth, Evidence that C-peptide inhibits and divalent cations stimulate degradation of insulin by insulin protease, Diabetes 20: 46A (1981).
W.C. Duckworth, F.B. Stentz, M. Heinemann, and A.E. Kitabchi, Initial site of insulin cleavage by insulin protease, Proc. Natl. Acad. Sci. USA 76: 635 1979.
P.T. Varandi, Insulin degradation. V. Unmasking of glutathione-insulin transhydrogenase in rat liver microsomal membrane. Biochim. Biophys. Acta 304: 1973 1973.
H. Keilova, On the specificity and inhibition of cathepsins D and B, in: “Tissue Proteinases,” A.J. Barett and J.T. Dingle, North Holland Publishing Co., Amsterdam (1971).
A.H. Rubenstein, Insulin, proinsulin and C-peptide: Secretion, metabolism, regulation in health and disease, in: “Endocrinology,” L.J. DeGroot, Grune and Stratton, New York (1979).
D.H. Gabbay, K. DeLuca, J.N. Fisher, Jr., M.E. Mako, and A.H. Rubenstein, Familial hyperproinsulinemia: An autosomal dominant defect, N. Engl. J. Med. 294: 911 1976.
A.S. Kitabchi, Proinsulin and C-peptide: A review, Metabolism 26: 547 1977.
J.E. Sealey, S.A. Atlas, and J.H. Laragh, Prorenin and other large molecular weight forms of renin, Endocrine Rev. 1: 365 1980.
W.A. Hsueh, Inactive renin in human plasma—is it prorenin?, Min. Elect. Metab. 7: 169 1982.
W. Carlson, V. Dzau, S. Quay, J. Kreisberg, and E. Haber, Biosynthesis of renin in the dog kidney: Evidence for the presence of prorenin, Circulation 62: 111 1980.
K. Poulsen, J. Vuust, and T. Lund, Renin precursor from mouse kidney identified by cell-free translation of messenger RNA, Clin. Sci. 59: 297 1980.
V.J. Dzau, O. Lanaka, and R.E. Pratt, The nature of inactive renin and renin precursor and inactive renin, Clin. Exp. Hypertension, A4: 1973 (1982).
R.M. Cooper, G.E. Murray, and D.H. Osmond, Tryps in-induced activation or renin precursor in plasma of normal and anephric man, Circ. Res. 40: 171 1976.
B.J. Morris, Activation of human inactive (“pro-”) renin by cathepsin D and pepsin, J. Clin. Endocrinol. Metab. 46: 153 1978.
D.H. Osmond, E.K. Lo, A.Y. Loh, E.A. Zingg, and A.H. Hedlin, Kallikrein and plasmin as activators of inactive renin, Lancet 2: 1375 1978.
J.E. Sealey, S.A. Atlas, J.H. Laragh, N.B. Oza, and J.W. Ryan, Activation of prorenin-like substance in human plasma by trypsin and by urinary kallikrein, Hypertension 1: 179 1979.
J.E. Sealey, S.A. Atlas, J.H. Laragh, M. Silverberg, and A.P. Kaplan, Initiation of plasma prorenin activation by Hageman factor-dependent conversion of plasma prekallikrein to kallikrein, Proc. Natl. Acad. Sci. USA 76: 5914 1979.
W.A. Hsueh, E.J. Carlson, and M. Israel-Hagman, Mechanism of acid-activation of renin: Role of kallikrein in renin activation, Hypertension 3: 1–22 1981.
W.A. Hsueh, J.A. Luetscher, E.J. Carlson, and G. Grislis, Inactive renin of high molecular weight (big renin) in normal human plasma, Hypertension 2: 750 1980.
S.A. Atlas, J.E. Sealey, B. Dharmgrongartama, T.E. Hesson, and J.H. Laragh, Detection and isolation of inactive, large molecular weight renin in human kidney and plasma, Hypertension 3: 1–30 (1981).
J.J. Chang, M. Kisarag, H. Okamoto, and T. Inagami, Isolation and activation of inactive renin from human kidney and plasma: Plasma and renal inactive renin have different molecular weights, Hypertension 3: 509 1981.
W.A. Hsueh, E.J. Carlson, and V.J. Dzau, Characterization of renal and plasma inactive renin: Evidence for a renal source of circulating inactive renin, J Clin. Invest. (in press, 1983).
S.A. Atlas, J.E. Sealey, T.E. Hesson, A.P. Kaplan, J. Ménard, P. Corvol, and J.H. Laragh, Biochemical similarity of partially purified inactive renins from human plasma and kidney, Hypertension 4: II–86 (1982).
R.P. Day and J.A. Luetscher, Big renin: A possible prohormone in kidney and plasma of a patient with Wilms 1 tumor, J. Clin. Endocrinol. Metab. 38: 923 (1974).
A. Mimran, B.J. Leckie, J.C. Fourcade, P. Beldet, A. Davratil, and P. Barjon, Blood pressure, renin-angiotensin system and urinary kallikrein in a case of juxtaglomerular cell tumor, Am. J. Med. 65: 527 1978.
M.C. Ruddy, S. A. Atlas, and F.G. Salerno, Hypertension associated with a renin-secreting adenocarcinoma of the pancreas, N. Engl. J. Med. 307: 993 1982.
A. Deleiva, A. R. Christlieb, J. C. Melby, C. A. Graham, R. P. Day, J. A. Luetscher, and P.G. Zager, Big renin and biosynthetic defect of aldosterone in diabetes mellitus, N. Engl. J. Med. 295: 639 1976.
W.A. Hsueh, E. J. Carlson, J. A. Luetscher, and G. Grislis, Activation and characterization of inactive big renin in plasma of patients with diabetic nephropathy and unusual active renin, J. Clin. Endocrinol. Metab. 51: 535 1980.
R. Goldstone, E.J. Carlson, and W.A. Hsueh, Evidence for two independent mechanisms of juxtaglomerular (JG) cell impairment in hyporeninemic hypoaldosteronism, Endocrine Society Program (1982).
J.A. Hahn, R.D. Zipser, A. Burg, R.A. Stone, P.R. Zia, W.A. Hsueh, and R. Horton, Studies of the renal vasoactive systems in hyporeninemic hypoaldosteronism, Prost. and Med. 6: 549 1981.
J.A. Mitas, S.B. Levy, R. Holle, R. Frigon, and R.A. Stone, Urinary kallikrein activity in the hypertension of renal parenchymal disease, N. Engl. J. Med. 299: 162 1978.
J. Oates, R. Whorton, J. Gerkins, R. Banch, J. Hollified, and J. Frolich, The participation of prostaglandins in control of renin release, Fed. Proc. 38: 72 1979.
S.Y. Tan, I. Antonipillai, and P.J. Mulrow, Inactive renin and prostaglandin E2 production in hyporeninemic hypoaldosteronism, J. Clin. Endocrinol. Metab. 51: 849 1980.
S.Y. Tan, R. Shapiro, R. Franco, H. Stockard, and P.J. Mulrow, Indomethacin-induced prostaglandin inhibition with hyperkalemia. A reversible cause of hyporeninemic hypoaldosteronism, Ann. Intern. Med. 90: 783 1979.
H.P. Rodemann, L. Waxman, and A.L. Goldberg, The stimulation of protein degradation in muscle by Ca 2+ is mediated by prostaglandin E2 and does not require the calcium-activated protease, J. Biol. Chem. 257: 8716 1982.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1984 Plenum Press, New York
About this chapter
Cite this chapter
Hsueh, W.A. (1984). Proteases in Hormone Production and Metabolism. In: Hörl, W.H., Heidland, A. (eds) Proteases. Advances in Experimental Medicine and Biology, vol 167. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-9355-3_11
Download citation
DOI: https://doi.org/10.1007/978-1-4615-9355-3_11
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4615-9357-7
Online ISBN: 978-1-4615-9355-3
eBook Packages: Springer Book Archive