The primary structure of NG2, a novel membrane-spanning proteoglycan

Journal of Cell Biology

Volumn 114, Issue 2, 1991, Pages 359-371

  Nishiyama, Akiko ^a   Dahlin, Kimberlee J ^a   Prince, John T ^a   Johnstone, Stephen R ^a   Stallcup, William B ^a  

^a BURNHAM INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEMENTARY DNA; MEMBRANE PROTEIN; PROTEOGLYCAN;

AMINO ACID SEQUENCE; ANIMAL CELL; ARTICLE; NONHUMAN; PRIORITY JOURNAL; RAT; SEQUENCE HOMOLOGY;

AMINO ACID SEQUENCE; ANIMAL; ANTIGENS; BASE SEQUENCE; BLOTTING, NORTHERN; BLOTTING, SOUTHERN; CELL LINE; CHONDROITIN SULFATES; DNA; IMMUNOHISTOCHEMISTRY; MEMBRANE GLYCOPROTEINS; MEMBRANE PROTEINS; MOLECULAR SEQUENCE DATA; NEURONS; PRECIPITIN TESTS; PROTEOGLYCANS; RATS; RNA, MESSENGER; SUPPORT, U.S. GOV'T, P.H.S.;

ANIMALIA;

EID: 0025743827     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.114.2.359     Document Type: Article

References (70)

1. Aviv, H., and P. Leder. 1972. Purification of biologically active globin messenger RNA by chromatography on oligo-thymidylic acid-cellulose. Proc. Natl. Acad. Sci. USA. 60:1408-1412.
2. + RNA. BioTechniques. 6:114-116.
3. Blin, N., and D. W. Stafford. 1976. A general method for isolation of high molecular weight DNA from eukaryotes. Nucleic Acids Res. 3:2303-2308.
4. Bourdon, M. A., T. Krusius, S. Campbell, N. B. Schwartz, and E. Ruoslahti. 1987. Identification and synthesis of a recognition signal for the attachment of glycosaminoglycans to proteins. Proc. Natl. Acad. Sci. USA. 84:3194-3198.
5. Carroll, S. B., and A. Laughon. 1987. Production and purification of polyclonal antibodies to the foreign segment of β-galactosidase fusion proteins. In DNA Cloning. Vol. III. D. M. Glover, editor. IRL Press, Oxford. 89-111.
6. Caterson, B., T. Calabro, P. J. Donohue, and M. R. Jahnke. 1986. Monoclonal antibodies against cartilage proteoglycan and link protein. In Articular Cartilage Biochemistry. K. Kuettner, editor. Raven Press, New York. 59-73.
7. Chirgwin, J. M., A. E. Przybyla, R. J. MacDonald, and W. J. Rutter. 1979. Isolation of biologically active ribonucleic acid from sources enriched in ribonucleases. Biochemistry. 18:5294-5299.
8. Doege, K., M. Sasaki, E. Horigan, J. R. Hassell, and Y. Yamada. 1987. Complete primary structure of the rat cartilage proteoglycan core protein deduced from cDNA clones. J. Biol. Chem. 262:17757-17767.
9. Doolittle, R. F., D. F. Feng, and M. S. Johnson. 1984. Computer-based characterization of epidermal growth factor precursor. Nature (Lond.). 307:558-560.
10. Feinberg, A. P., and B. Fogelstein. 1983. A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity. Anal. Biochem. 132:6-13.
11. Fransson, L.-A. 1987. Structure and function of cell-associated proteoglycans. TIBS (Trends Biochem. Sci.) 12:406-411.
12. Gallagher, J. T. 1989. The extended family of proteoglycans: social residents of pericellular zone. Curr. Opin. Cell Biol. 1:1201-1218.
13. Garnier, J., D. J. Osguthorpe, and B. Robson. 1978. Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins. J. Mol. Biol. 120:97-120.
14. Gascuel, O., and J. L. Golmard. 1988. A simple method for predicting the secondary structure of globular proteins. Comput. Appl. Biosci. 4:357-365.
15. Goldstein, L. A., D. F. Zhou, L. J. Picker, C. N. Minty, R. F. Bargatze, J. F. Ding, and E. C. Butcher. 1989. A human lymphocyte homing receptor, the hermes antigen, is related to cartilage link proteoglycan core and link proteins. Cell. 56:1063-1072.
16. Greene, L., and A. Tischler. 1976. Establishment of a noradrenergic clonal line of rat adrenal pheochromocytoma cells which respond to nerve growth factor. Proc. Natl. Acad. Sci. USA. 73:2424-2428.
17. Gubler, U., and B. J. Hoffman. 1983. A simple and very efficient method for generating cDNA libraries. Gene. 25:263-269.
18. Harper, J. R., and R. A. Reisfeld. 1987. Cell-associated proteoglycans in human malignant melanoma. In Biology of Proteoglycans. T. N. Wight and R. P. Mecham, editors. Academic Press, Inc. Orlando, FL. 345-366.
19. Hatta, K., A. Nose, A. Nagafuchi, and M. Takeichi. 1988. Cloning and expression of cDNA encoding a neural calcium-dependent cell adhesion molecule: its identity in the cadherin gene family. J. Cell Biol. 106:873-881.
20. Henikoff, S. 1984. Unidirectional digestion with exonuclease III creates targeted breakpoints for DNA sequencing. Gene. 28:351-359.
21. Hiss, D., T. Scott-Burden, and W. Gevers. 1987. Disulfide-bonded heparan sulfate proteoglycans associated with the surfaces of cultured bovine vascular endothelial cells. Eur. J. Biochem. 162:89-94.
22. Hubbard, A., and Z. Cohn. 1972. The enzymatic iodination of the red cell membrane. J. Cell Biol. 55:390-405.
23. Hubbard, S. C., and R. J. Ivatt. 1981. Synthesis and processing of asparagine-linked oligosaccharides. Annu. Rev. Biochem. 50:555-583.
24. Hunyh, T. V., R. A. Young, and R. W. Davis. 1985. Constructing and screening cDNA libraries in λgt10 and λgt11. In DNA Cloning. Vol 1. D. M. Glover, editor. IRL Press, Oxford. 49-78.
25. Jackman, R. W., D. L. Beeler, L. VanDeWater, and R. D. Rosenberg. 1986. Characterization of a thrombomodulin cDNA reveals structural similarity to the low density lipoprotein receptor. Proc. Natl. Acad. Sci. USA. 83:8834-8838.
26. Kaufman, J. F., M. S. Krangel, and J. L. Strominger. 1984. Cysteines in the transmembrane region of major histocompatibility complex antigens are fatty acylated via thioester bonds. J. Biol. Chem. 259:7230-7238.
27. Kemp, B. E., and R. B. Pearson. 1990. Protein kinase recognition sequence motifs. TIBS (Trends Biochem. Sci.) 15:342-346.
28. Kidd, S., M. K. Baylies, G. P. Gasic, and M. W. Young. 1989. Structure and distribution of the Notch protein in the developing Drosophila. Genes Dev. 3:1113-1129.
29. Kiefer, M. C., J. C. Stephans, K. Crawford, K. Okino, and P. J. Barr. 1990. Ligand-affinity cloning and structure of a cell surface heparan sulfate proteoglycan that binds basic fibroblast growth factor. Proc. Natl. Acad. Sci. USA. 87:6985-6989.
30. Kozak, M. 1984. Compilation and analysis of sequences upstream of the translational start site in eukaryotic mRNAs. Nucleic Acids Res. 12:857-872.
31. Kretsinger, R. H. 1980. Crystallographic studies of calmodulin and homologs. Ann. NY Acad. Sci. 356:14-19.
32. Krueger, R. J. Jr., T. A. Fields, J. Hidreth IV, and N. Schwartz. 1990. Chick cartilage chondroitin sulfate proteoglycan core protein. I. Generation and characterization of peptides and specificity for glycosaminoglycan attachment. J. Biol. Chem. 265:12075-12089.
33. Kyte, J., and R. F. Doolittle. 1982. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157:105-132.
34. Laemmli, U. 1970. Cleavage of structural proteins during the assembly of the head of the bacteriophage T4. Nature (Lond.). 227:680-685.
35. Lee, P. L., D. E. Johnson, L. S. Cousens, V. A. Fried, and L. T. Williams. 1989. Purification and complementary DNA cloning of a receptor for basic fibroblast growth factor. Science (Wash. DC). 245:57-60.
36. Levine, J. M., and J. P. Card. 1987. Light and electron microscopic localization of a cell surface antigen (NG2) in the rat cerebellum: association with smooth protoplasmic astrocytes. J. Neurosci. 7:2711-2720.
37. Levine, J. M., and W. B. Stallcup. 1987. Plasticity of developing cerebellar cells in vitro studied with antibodies against the NG2 antigen. J. Neurosci. 7:2721-2731.
38. Marynen, P., J. Zhang, J.-J. Cassiman, H. Van den Berghe, and G. David. 1989. Partial primary structure of the 48- and 90-kilodalton core proteins of cell surface-associated heparan sulfate proteoglycans of lung fibroblasts. J. Biol. Chem. 264:7017-7024.
39. Neame, P. J., J. E. Christner, and J. R. Baker. 1986. The primary structure of link protein from rat chondrosarcoma proteoglycan aggregate. J. Biol. Chem. 261:3519-3535.
40. Nishiyama, A., K. J. Dahlin, and W. B. Stallcup. 1991. The expression of NG2 proteoglycan in the developing rat limb. Development (Camb.). 111:933-944.
41. Pearson, W. R., and D. J. Lipman. 1988. Improved tools for biological sequence comparison. Proc. Natl. Acad. Sci. USA. 85:2444-2448.
42. Pedraza, L., G. C. Owens, L. A. David Green, and J. L. Salzer. 1990. The myelin-associated glycoproteins: membrane disposition, evidence of a novel disulfide linkage between immunoglobulin-like domains, and posttranslational palmitylation. J. Cell Biol. 111:2651-2661.
43. Perides, G., W. S. Lane, D. Andrews, D. Dahl, and A. Bignami. 1989. Isolation and partial characterization of a glial hyaluronate-binding protein. J. Biol. Chem. 264:5981-5987.
44. Perris, R., and S. Johansson. 1987. Amphibian neural crest cell migration on purified extracellular matrix components: a chondroitin sulfate proteoglycan inhibits locomotion on fibronectin substrates. J. Cell Biol. 105:2511-2521.
45. Raff, M., R. Miller, and M. Noble. 1983. A glial progenitor cell that develops in vitro into an astrocyte or an oligodendrocyte depending on culture medium. Nature (Lond.). 303:390-396.
46. Rapraeger, A., M. Jalkanen, and M. Bernfield. 1986. Cell surface proteoglycan associates with the cytoskeleton at the basolateral cell surface of mouse mammary epithelial cells. J. Cell Biol. 103:2683-2696.
47. 2+-dependent cell adhesion. EMBO (Eur. Mol. Biol. Organ.) J. 6:3647-3653.
48. Ripellino, J. A., R. U. Margolis, and R. K. Margolis. 1989. Immunoelectron microscopic localization of hyaluronic acid-binding region and link protein epitopes in the brain. J. Cell Biol. 108:1899-1907.
49. Ruoslahti, E. 1989. Proteoglycans in cell regulation. J. Biol. Chem. 264: 13369-13372.
50. Sabatini, D. D., G. Kreibich, T. Morimoto, and M. Adesnik. 1982. Mechanisms for the incorporation of proteins in membranes and organelles. J. Cell Biol. 92:1-22.
51. Saiki, R. K., S. Scharf, F. Faloona, K. B. Mullis, G. I. Horn, H. A. Erlich, and N. Arnheim. 1985. Enzymatic amplification of β-globin genomic sequences and restriction site analysis for diagnosis of sickle cell anemia. Science (Wash. DC). 230:1350-1354.
52. Sanger, F., S. Nicklen, and A. R. Coulson. 1977. DNA sequencing with chain-terminating inhibitors. Proc. Natl. Acad. Sci. USA. 74:5463-5467.
53. Saunders, S., M. Jalkanen, S. O'Farrell, and M. Berafield. 1989. Molecular cloning of syndecan, an integral membrane proteoglycan. J. Cell Biol. 108.1547-1556.
54. Schubert, D., S. Heinemann, W. Carlisle, H. Tarikas, B. Kimes, J. Patrick, J. Steinbach, W. Culp, and E. Brandt. 1974. Clonal cell lines from the rat central nervous system. Nature (Lond.). 249:224-227.
55. Shier, P., and V. M. Watt. 1989. Primary structure of a putative receptor for a ligand of the insulin family. J. Biol. Chem. 264:14605-14608.
56. Southern, E. M. 1975. Detection of specific sequences among DNA fragments separated by gel electrophoresis. J. Mol. Biol. 98:503-517.
57. Stallcup, W. B. 1981. The NG2 antigen, a putative lineage marker: immunofluorescent localization in primary cultures of rat brain. Dev. Biol. 83:154-165.
58. Stallcup, W. B., and L. Beasley. 1987. Bipotential glial precursor cells of the optic nerve express the NG2 proteoglycan. J. Neurosci. 7:2737-2744.
59. Stallcup, W. B., L. Beasley, and J. Levine. 1983. Cell-surface molecules that characterize different stages in the development of cerebellar interneurons. Cold Spring Harbor Symp. Quant. Biol. 48:761-774.
60. Stallcup, W. B., K. Dahlin, and P. Healy. 1990. Interaction of the NG2 chondroitin sulfate proteoglycan with type VI collagen. J. Cell Biol. 111:3177-3188.
61. Stamenovic, I., M. Amiot, J. M. Pesando, and B. Seed. 1989. A lymphocyte molecule implicated in lymph node homing as a member of the cartilage link protein family. Cell. 56:1057-1062.
62. Strubin, M., B. Mack, and E. O. Long. 1984. The complete sequence of the mRNA for the HLA-DR-associated invariant chain reveals a polypeptide with an unusual membrane polarity. EMBO (Eur. Mol. Biol. Organ.) J. 3:869-872.
63. Tan, S.-S., K. L. Crossin, S. Hoffman, and G. M. Edelman. 1987. Asymmetric expression in somites of cytotactin and its proteoglycan ligand is correlated with neural crest distribution. Proc. Natl. Acad. Sci. USA. 84:7977-7981.
64. Thomas, P. S. 1980. Hybridization of denatured RNA and small DNA fragments transferred to nitrocellulose. Proc. Natl. Acad. Sci. USA. 77:5201-5205.
65. Williams, A. F., and A. N. Barclay. 1988. The immunoglobulin superfamily - domains for cell recognition. Annu. Rev. Immunol. 6:381-405.
66. Wilson, S.-S., E. E. Baetge, and W. B. Stallcup. 1981. Antisera specific for cell lines with mixed neuronal and glial properties. Dev. Biol. 83:146-153.
67. Yamagata, M., S. Suzuki, S. K. Akiyama, K. M. Yamada, and K. Kimata. 1989. Regulation of cell-substrate adhesion by proteoglycans immobilized on extracellular substrates. J. Biol Chem. 264:8012-8018.
68. Yamaguchi, Y., and E. Ruoslahti. 1988. Expression of human proteoglycan in Chinese hamster ovary cells inhibits cell proliferation. Nature (Lond.). 336: 244-246.
69. Yamaguchi, Y., D. M. Mann, and E. Ruoslahti. 1990. Negative regulation of transforming growth factor-β by the proteoglycan decorin. Nature (Lond.). 346:281-284.
70. Zimmermann, D. R., and E. Ruoslahti. 1989. Multiple domains of the large fibroblast proteoglycan, versican. EMBO (Eur. Mol. Biol. Organ.) J. 8: 2975-2981.