Receptor-specific induction of insulin-like growth factor I in human monocytes by advanced glycosylation end product-modified proteins. (original) (raw)
- Journal List
- J Clin Invest
- v.90(2); 1992 Aug
- PMC443119
J Clin Invest. 1992 Aug; 90(2): 439–446.
Laboratory of Medical Biochemistry, Rockefeller University, New York 10021.
Abstract
Normal tissue homeostasis requires a finely balanced interaction between phagocytic scavenger cells (such as monocytes and macrophages) that degrade senescent material and mesenchymal cells (such as fibroblasts and smooth muscle cells), which proliferate and lay down new extracellular matrix. Macrophages and monocytes express specific surface receptors for advanced glycosylation end products (AGEs), which are covalently attached adducts resulting from a series of spontaneous nonenzymatic reactions of glucose with tissue proteins. Receptor-mediated uptake of AGE-modified proteins induces human monocytes to synthesize and release cytokines (TNF and IL-1), which are thought to contribute to normal tissue remodeling by mechanisms not entirely understood. We now report that AGEs also induce human monocytes to generate the potent progression growth factor insulin-like growth factor I (IGF-I), known to stimulate proliferation of mesenchymal cells. After in vitro stimulation with AGE-modified proteins, normal human blood monocytes express IGF-IA mRNA leading to the secretion of IGF-IA prohormone. The signal for IGF-IA mRNA induction seems to be initiated via the monocyte AGE-receptor, and to be propagated in an autocrine fashion via either IL-1 beta or PDGF. These data introduce a novel regulatory system for IGF-I, with broad in vivo relevance, and provide an essential link to the chain of events leading from the spontaneously formed tissue AGEs, hypothesized to act as markers of protein senescence, to their replacement and to tissue remodeling by the locally controlled induction of growth factors.
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- Rappolee DA, Mark D, Banda MJ, Werb Z. Wound macrophages express TGF-alpha and other growth factors in vivo: analysis by mRNA phenotyping. Science. 1988 Aug 5;241(4866):708–712. [PubMed] [Google Scholar]
- Leibovich SJ, Ross R. The role of the macrophage in wound repair. A study with hydrocortisone and antimacrophage serum. Am J Pathol. 1975 Jan;78(1):71–100. [PMC free article] [PubMed] [Google Scholar]
- Vlassara H, Brownlee M, Manogue KR, Dinarello CA, Pasagian A. Cachectin/TNF and IL-1 induced by glucose-modified proteins: role in normal tissue remodeling. Science. 1988 Jun 10;240(4858):1546–1548. [PubMed] [Google Scholar]
- Kirstein M, Brett J, Radoff S, Ogawa S, Stern D, Vlassara H. Advanced protein glycosylation induces transendothelial human monocyte chemotaxis and secretion of platelet-derived growth factor: role in vascular disease of diabetes and aging. Proc Natl Acad Sci U S A. 1990 Nov;87(22):9010–9014. [PMC free article] [PubMed] [Google Scholar]
- Brownlee M, Cerami A, Vlassara H. Advanced glycosylation end products in tissue and the biochemical basis of diabetic complications. N Engl J Med. 1988 May 19;318(20):1315–1321. [PubMed] [Google Scholar]
- Monnier VM, Kohn RR, Cerami A. Accelerated age-related browning of human collagen in diabetes mellitus. Proc Natl Acad Sci U S A. 1984 Jan;81(2):583–587. [PMC free article] [PubMed] [Google Scholar]
- Radoff S, Cerami A, Vlassara H. Isolation of surface binding protein specific for advanced glycosylation end products from mouse macrophage-derived cell line RAW 264.7. Diabetes. 1990 Dec;39(12):1510–1518. [PubMed] [Google Scholar]
- Yang Z, Makita Z, Horii Y, Brunelle S, Cerami A, Sehajpal P, Suthanthiran M, Vlassara H. Two novel rat liver membrane proteins that bind advanced glycosylation endproducts: relationship to macrophage receptor for glucose-modified proteins. J Exp Med. 1991 Sep 1;174(3):515–524. [PMC free article] [PubMed] [Google Scholar]
- Stiles CD, Capone GT, Scher CD, Antoniades HN, Van Wyk JJ, Pledger WJ. Dual control of cell growth by somatomedins and platelet-derived growth factor. Proc Natl Acad Sci U S A. 1979 Mar;76(3):1279–1283. [PMC free article] [PubMed] [Google Scholar]
- Froesch ER, Schmid C, Schwander J, Zapf J. Actions of insulin-like growth factors. Annu Rev Physiol. 1985;47:443–467. [PubMed] [Google Scholar]
- Baxter RC, Martin JL. Binding proteins for the insulin-like growth factors: structure, regulation and function. Prog Growth Factor Res. 1989;1(1):49–68. [PubMed] [Google Scholar]
- Clemmons DR, Shaw DS. Purification and biologic properties of fibroblast somatomedin. J Biol Chem. 1986 Aug 5;261(22):10293–10298. [PubMed] [Google Scholar]
- Clemmons DR, Van Wyk JJ. Evidence for a functional role of endogenously produced somatomedinlike peptides in the regulation of DNA synthesis in cultured human fibroblasts and porcine smooth muscle cells. J Clin Invest. 1985 Jun;75(6):1914–1918. [PMC free article] [PubMed] [Google Scholar]
- Rom WN, Basset P, Fells GA, Nukiwa T, Trapnell BC, Crysal RG. Alveolar macrophages release an insulin-like growth factor I-type molecule. J Clin Invest. 1988 Nov;82(5):1685–1693. [PMC free article] [PubMed] [Google Scholar]
- Timonen T, Saksela E. Isolation of human NK cells by density gradient centrifugation. J Immunol Methods. 1980;36(3-4):285–291. [PubMed] [Google Scholar]
- Vlassara H, Brownlee M, Cerami A. High-affinity-receptor-mediated uptake and degradation of glucose-modified proteins: a potential mechanism for the removal of senescent macromolecules. Proc Natl Acad Sci U S A. 1985 Sep;82(17):5588–5592. [PMC free article] [PubMed] [Google Scholar]
- Radoff S, Makita Z, Vlassara H. Radioreceptor assay for advanced glycosylation end products. Diabetes. 1991 Dec;40(12):1731–1738. [PubMed] [Google Scholar]
- Jones PA, Scott-Burden T, Gevers W. Glycoprotein, elastin, and collagen secretion by rat smooth muscle cells. Proc Natl Acad Sci U S A. 1979 Jan;76(1):353–357. [PMC free article] [PubMed] [Google Scholar]
- LOWRY OH, ROSEBROUGH NJ, FARR AL, RANDALL RJ. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
- Rotwein P, Pollock KM, Didier DK, Krivi GG. Organization and sequence of the human insulin-like growth factor I gene. Alternative RNA processing produces two insulin-like growth factor I precursor peptides. J Biol Chem. 1986 Apr 15;261(11):4828–4832. [PubMed] [Google Scholar]
- Hanukoglu I, Tanese N, Fuchs E. Complementary DNA sequence of a human cytoplasmic actin. Interspecies divergence of 3' non-coding regions. J Mol Biol. 1983 Feb 5;163(4):673–678. [PubMed] [Google Scholar]
- March CJ, Mosley B, Larsen A, Cerretti DP, Braedt G, Price V, Gillis S, Henney CS, Kronheim SR, Grabstein K, et al. Cloning, sequence and expression of two distinct human interleukin-1 complementary DNAs. Nature. 1985 Jun 20;315(6021):641–647. [PubMed] [Google Scholar]
- Wang AM, Creasey AA, Ladner MB, Lin LS, Strickler J, Van Arsdell JN, Yamamoto R, Mark DF. Molecular cloning of the complementary DNA for human tumor necrosis factor. Science. 1985 Apr 12;228(4696):149–154. [PubMed] [Google Scholar]
- Furlanetto RW, Underwood LE, Van Wyk JJ, D'Ercole AJ. Estimation of somatomedin-C levels in normals and patients with pituitary disease by radioimmunoassay. J Clin Invest. 1977 Sep;60(3):648–657. [PMC free article] [PubMed] [Google Scholar]
- Conover CA, Baker BK, Hintz RL. Cultured human fibroblasts secrete insulin-like growth factor IA prohormone. J Clin Endocrinol Metab. 1989 Jul;69(1):25–30. [PubMed] [Google Scholar]
- Hossenlopp P, Seurin D, Segovia-Quinson B, Hardouin S, Binoux M. Analysis of serum insulin-like growth factor binding proteins using western blotting: use of the method for titration of the binding proteins and competitive binding studies. Anal Biochem. 1986 Apr;154(1):138–143. [PubMed] [Google Scholar]
- Vlassara H, Brownlee M, Cerami A. Novel macrophage receptor for glucose-modified proteins is distinct from previously described scavenger receptors. J Exp Med. 1986 Oct 1;164(4):1301–1309. [PMC free article] [PubMed] [Google Scholar]
- Vlassara H, Moldawer L, Chan B. Macrophage/monocyte receptor for nonenzymatically glycosylated protein is upregulated by cachectin/tumor necrosis factor. J Clin Invest. 1989 Dec;84(6):1813–1820. [PMC free article] [PubMed] [Google Scholar]
- Tode B, Serio M, Rotella CM, Galli G, Franceschelli F, Tanini A, Toccafondi R. Insulin-like growth factor-I: autocrine secretion by human thyroid follicular cells in primary culture. J Clin Endocrinol Metab. 1989 Sep;69(3):639–647. [PubMed] [Google Scholar]
- Ross R. The pathogenesis of atherosclerosis--an update. N Engl J Med. 1986 Feb 20;314(8):488–500. [PubMed] [Google Scholar]
- Ross R, Masuda J, Raines EW, Gown AM, Katsuda S, Sasahara M, Malden LT, Masuko H, Sato H. Localization of PDGF-B protein in macrophages in all phases of atherogenesis. Science. 1990 May 25;248(4958):1009–1012. [PubMed] [Google Scholar]
- Greenberg ME, Ziff EB. Stimulation of 3T3 cells induces transcription of the c-fos proto-oncogene. Nature. 1984 Oct 4;311(5985):433–438. [PubMed] [Google Scholar]
- Smith EP, Svoboda ME, Van Wyk JJ, Kierszenbaum AL, Tres LL. Partial characterization of a somatomedin-like peptide from the medium of cultured rat Sertoli cells. Endocrinology. 1987 Jan;120(1):186–193. [PubMed] [Google Scholar]
- Esposito C, Gerlach H, Brett J, Stern D, Vlassara H. Endothelial receptor-mediated binding of glucose-modified albumin is associated with increased monolayer permeability and modulation of cell surface coagulant properties. J Exp Med. 1989 Oct 1;170(4):1387–1407. [PMC free article] [PubMed] [Google Scholar]
- Skolnik EY, Yang Z, Makita Z, Radoff S, Kirstein M, Vlassara H. Human and rat mesangial cell receptors for glucose-modified proteins: potential role in kidney tissue remodelling and diabetic nephropathy. J Exp Med. 1991 Oct 1;174(4):931–939. [PMC free article] [PubMed] [Google Scholar]
- Sherry B, Cerami A. Cachectin/tumor necrosis factor exerts endocrine, paracrine, and autocrine control of inflammatory responses. J Cell Biol. 1988 Oct;107(4):1269–1277. [PMC free article] [PubMed] [Google Scholar]
- Monnier VM, Vishwanath V, Frank KE, Elmets CA, Dauchot P, Kohn RR. Relation between complications of type I diabetes mellitus and collagen-linked fluorescence. N Engl J Med. 1986 Feb 13;314(7):403–408. [PubMed] [Google Scholar]
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