Characterisation of insulin-like growth factor receptors and insulin receptors in the human placenta using lectin affinity methods

Growth Hormone and IGF Research

Volumn 16, Issue 3, 2006, Pages 174-184

  Masnikosa, Romana ^a   Baričević, Ivona ^a   Jones, David R ^b   Nedić, Olgica ^a  

^a UNIVERSITY OF BELGRADE   (Serbia)

^b NETHERLANDS CANCER INSTITUTE   (Netherlands)

Author keywords

BanLec; Con A; IGF IIR; IGF IR; IR; Lectin chromatography; PHA; SNA; WGA

Indexed keywords

CONCANAVALIN A; INSULIN RECEPTOR; LECTIN; OLIGOSACCHARIDE; PHYTOHEMAGGLUTININ; PLANT LECTIN; SOMATOMEDIN B RECEPTOR; SOMATOMEDIN C RECEPTOR; WHEAT GERM AGGLUTININ;

ARTICLE; BINDING SITE; CARBOHYDRATE ANALYSIS; CELL MEMBRANE; CONTROLLED STUDY; FEMALE; HUMAN; HUMAN CELL; HUMAN TISSUE; PLACENTA; PRIORITY JOURNAL; PROTEIN GLYCOSYLATION; PROTEIN IMMOBILIZATION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; SIGNAL TRANSDUCTION;

EID: 33746304547     PISSN: 10966374     EISSN: 15322238     Source Type: Journal    
DOI: 10.1016/j.ghir.2006.04.001     Document Type: Article

References (45)

1. LeRoith D., Werner H., Beitner-Johnson D., and Roberts Jr. C.T. Molecular and cellular aspects of the insulin-like growth factor I receptor. Endocr. Rev. 16 (1995) 143-163
2. Adams T.E., Epa V.C., Garrett T.P.J., and Ward C.W. Structure and function of the type 1 insulin-like growth factor receptor. Cell. Mol. Life Sci. 57 (2000) 1050-1093
3. Chernausek S.D., Jacobs S., and Van Wyk J.J. Structural similarities between human receptors for somatomedin C and insulin: analysis by affinity labeling. Biochemistry 20 (1981) 7345-7350
4. Kim J.J., and Accili D. Signalling through IGF-I and insulin receptors: where is the specificity. Growth Horm. IGF Res. 12 (2002) 84-90
5. Liu J.P., Baker J., Perkins A.S., Robertson E.J., and Efstratiadis A. Mice carrying null mutations of the genes encoding insulin-like growth factor I (Igf-1) and type 1 IGF receptor (Igf1r). Cell 75 (1993) 59-72
6. Frasca F., Pandini G., Scalia P., Sciacca L., Mineo R., Costantino A., Goldfine I.D., Belfiore A., and Vigneri R. Insulin receptor isoform A, a newly recognized, high-affinity insulin-like growth factor II receptor in fetal and cancer cells. Mol. Cell. Biol. 195 (1999) 3278-3288
7. Moxham C.P., Duronio V., and Jacobs S. Insulin-like growth factor I receptor β-subunit heterogeneity. J. Biol. Chem. 264 (1989) 13238-13244
8. Garofalo R.S., and Barenton B. Functional and immunological distinction between insulin-like growth factor I receptor subtypes in KB cells. J. Biol. Chem. 267 (1992) 11470-11475
9. Tollefsen S.E., Thompson K., and Petersen D.J. Separation of the high affinity insulin-like growth factor I receptor from low affinity binding sites by affinity chromatography. J. Biol. Chem. 262 (1987) 16461-16469
10. Moss A.M., and Livingston J.N. Distinct beta-subunits are present in hybrid insulin-like-growth-factor-1 receptors in the central nervous system. Biochem. J. 294 (1993) 685-692
11. Germain-Lee L., Janicot M., Lammers R., Ullrich A., and Casella S.J. Expression of a type I insulin-like growth factor receptor with low affinity for insulin-like growth factor II. Biochem. J. 281 (1992) 413-417
12. Ota A., Wilson G.L., and LeRoith D. Insulin-like growth factor I receptors on mouse neuroblastoma cells. Two beta subunits are derived from differences in glycosylation. Eur. J. Biochem. 174 (1988) 521-530
13. Bailyes E.M., Navé B.T., Soos M.A., Orr S.R., Hayward A.C., and Siddle K. Insulin receptor/IGF-I receptor hybrids are widely distributed in mammalian tissues: quantification of individual receptor species by selective immunoprecipitation and immunoblotting. Biochem. J. 327 (1997) 209-215
14. Soos M.A., Field C.E., and Siddle K. Purified hybrid insulin/insulin-like growth factor-I receptors bind insulin-like growth factor-I, but not insulin, with high affinity. Biochem. J. 290 (1993) 419-425
15. Cosgrove L., Lovrecz G.O., Verkuylen A., Cavaleri L., Black L.A., Bentley J.D., Howlett G.J., Gray P.P., Ward C.W., and McKern N.M. Purification and properties of insulin receptor ectodomain from large-scale mammalian cell culture. Protein Exp. Purif. 6 (1995) 789-798
16. Hedo J.A., Kasuga M., Van Obberghen E., Roth J., and Kahn C.R. Direct demonstration of glycosylation of insulin receptor subunits by biosynthetic and external labeling: evidence for heterogeneity. Proc. Natl. Acad. Sci. USA 78 (1981) 4791-4795
17. Hedo J.A., Kahn C.R., Hayashi M., Yamada K.M., and Kasuga M. Biosynthesis and glycosylation of the insulin receptor. Evidence for a single polypeptide precursor of the two major subunits. J. Biol. Chem. 258 (1983) 10020-10026
18. Hedo J.A., and Gorden P. Biosynthesis of the insulin receptor. Horm. Metab. Res. 17 (1985) 487-490
19. Herzberg V.L., Grigorescu F., Edge A.S.B., Spiro R.G., and Kahn C.R. Characterization of insulin receptor carbohydrate by comparison of chemical and enzymatic deglycosylation. Biochem. Biophys. Res. Commun. 129 (1985) 789-796
20. LeConte I., Auzan C., Debant A., Rossi B., and Clausner E. N-linked oligosaccharide chains of the insulin receptor β subunit are essential for transmembrane signaling. J. Biol. Chem. 267 (1992) 17415-17423
21. Collier E., Carpentier J.L., Beitz L., Caro L.H.P., Taylor S.I., and Gorden P. Specific glycosylation site mutations of the insulin receptor alfa-subunit impair intracellular transport. Biochemistry 32 (1993) 7818-7823
22. Ullrich A., Gray A., Tam A.W., Yang-Feng T., Tsubokawa M., Collins C., Henzel W., LeBon T., Kathuria S., and Chen E. Insulin-like growth factor 1 receptor primary structure: comparison with insulin receptor suggests structural determinants that define functional specificity. EMBO J. 5 (1986) 2503-2512
23. Carlberg M., Dricu A., Blegen H., Wang M., Hjertman M., Zickert P., Hoog A., and Larsson O. Mevalonic acid is limiting for N-linked glycosylation and translocation of the insulin-like growth factor-1 receptor to the cell surface. Evidence for a new link between 3-hydroxy-3-methylglutaryl-coenzyme A reductase and cell growth. J. Biol. Chem. 271 (1996) 17453-17462
24. Dricu A., Wang M., Hjertman M., Malec M., Blegen H., Wejde J., Carlberg M., and Larsson O. Mevalonate-regulated mechanisms in cell growth control: role of dolichyl phosphate in expression of the insulin-like growth factor-1 receptor (IGF-1R) in comparison to Ras prenylation and expression of c-myc. Glycobiology 7 (1997) 625-633
25. Kornfeld S. Structure and function of the mannose 6-phosphate/insulin-like growth factor II receptors. Annu. Rev. Biochem. 61 (1992) 307-330
26. Hawkes C., and Kar S. The insulin-like growth factor-II/mannose-6-phosphate receptor: structure, distribution and function in the central nervous system. Brain. Res. Rev. 44 (2004) 117-140
27. Helenius A., and Aebi M. Intracellular functions of N-linked glycans. Science 291 (2001) 2364-2369
28. Yamashita K., Hara-Kuge S., and Ohkura T. Intracellular lectins associated with N-linked glycoprotein traffic. Biochim. Biophys. Acta 1473 (1999) 147-160
29. Hauri H.P., Appenzeller C., Kuhn F., and Nufer O. Lectins and traffic in the secretory pathway. FEBS Lett. 476 (2000) 32-37
30. Jankoviċ M., and Viċovac Lj. A specific wheat germ agglutinin-immunoreactive protein in human placenta. Comp. Biochem. Physiol. Part B 127 (2000) 135-146
31. Liener I.E., Sharon N., and Goldstein I.J. The Lectins, Properties, Functions, and Applications in Biology and Medicine (1986), Academic Press, Inc. p. 174
32. Hunter W.M., and Greenwood F.C. Preparation of iodine-131 labelled human growth hormone of high specific activity. Nature 194 (1962) 495-499
33. Masnikosa R., Nikolić J.A., and Nedić O. Membrane-associated insulin-like growth factor (IGF) binding structures in placental cells. J. Serb. Chem. Soc. 68 (2003) 811-818
34. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
35. Bhaumick B., Bala R.M., and Hollenberg M.T. Somatomedin receptor of human placenta: solubilization, photolabeling, partial purification, and comparison with insulin receptor. Proc. Natl. Acad. Sci. USA 78 (1981) 4279-4283
36. Fujita-Yamaguchi Y., LeBon T.R., Tsubokawa M., Henzel W., Kathuria S., Koyal D., and Ramachandran J. Comparison of insulin-like growth factor I receptor and insulin receptor purified from human placental membranes. J. Biol. Chem. 261 (1986) 16727-16731
37. Nagata Y., and Burger M.M. Wheat germ agglutinin. Molecular characteristics and specificity for sugar binding. J. Biol. Chem. 249 (1974) 3116-3122
38. Mo H., Winter H.C., Van Damme E.J.M., Peumans W.J., Misaki A., and Goldstein I.J. Carbohydrate binding properties of banana (Musa acuminata) lectin I. Novel recognition of internal α1,3-linked glucosyl residues. Eur. J. Biochem. 268 (2001) 2609-2615
39. Goldstein I.J., Winter H.C., Mo H., Misaki A., Van Damme E.J.M., and Peumans W.J. Carbohydrate binding properties of banana (Musa acuminata) lectin II. Binding of laminaribiose oligosaccharides and β-glucans containing β1,6-glucosyl end groups. Eur. J. Biochem. 268 (2001) 2616-2619
40. Liener I.E., Sharon N., and Goldstein I.J. The Lectins Properties Functions and Applications in Biology and Medicine (1986), Academic Press, Inc. p. 46
41. Rini J.M. Lectin structure. Annu. Rev. Biophys. Biomol. Struct. 24 (1995) 551-577
42. Shibuya N., Goldstein I.J., Broekaert W.F., Nsimba-Lubaki M., Peeters B., and Peumans W.J. The elderberry (Sambucus nigra L.) bark lectin recognizes the Neu5Ac(alpha 2-6)Gal/GalNAc sequence. J. Biol. Chem. 262 (1987) 1596-1601
43. Hernandez J.D., and Baum L.G. Ah, sweet mystery of death! Galectins and control of cell fate. Glycobiology 12 (2002) 127R-136R
44. Buxser S.E., Kelleher D.J., Watson L., Puma P., and Johnson G.L. Change in state of nerve growth factor receptor. Modulation of receptor affinity by wheat germ agglutinin. J. Biol. Chem. 258 (1983) 3741-3749
45. Sørensen H., Whittaker L., Hinrichsen J., Groth A., and Whittaker J. Mapping of the insulin-like growth factor II binding site of the Type I insulin-like growth factor receptor by alanine scanning mutagenesis. FEBS Lett. 565 (2004) 19-22