Abstract
The Drosophila position-specific (PS) antigens are a family of cell surface glycoprotein complexes thought to be involved in morphogenesis. Their overall structures and biochemical properties are similar to those of a group of vertebrate receptors, including those for fibronectin, fibrinogen and vitronectin, and also the leukocyte antigens Mac-1, LFA-1 and p150,95 and the VLA family of cell surface antigens. The N-terminal sequences of the alpha subunits of some of these molecules are homologous to the N-terminus of a PS antigen component. The Drosophila PS antigens thus appear to be homologous to these vertebrate receptors.
Full text
PDF![1037](https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fc35/553500/2cf6f7808cce/emboj00244-0201.png)
![1038](https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fc35/553500/8d44a7500ac2/emboj00244-0202.png)
![1039](https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fc35/553500/e79e93cd9a94/emboj00244-0203.png)
![1040](https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fc35/553500/903732bee4b7/emboj00244-0204.png)
![1041](https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fc35/553500/873e20e86686/emboj00244-0205.png)
![1042](https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fc35/553500/4fc34d21da4a/emboj00244-0206.png)
![1043](https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fc35/553500/1e76c7b52a5b/emboj00244-0207.png)
Images in this article
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Aebersold R. H., Teplow D. B., Hood L. E., Kent S. B. Electroblotting onto activated glass. High efficiency preparation of proteins from analytical sodium dodecyl sulfate-polyacrylamide gels for direct sequence analysis. J Biol Chem. 1986 Mar 25;261(9):4229–4238. [PubMed] [Google Scholar]
- Akiyama S. K., Yamada S. S., Yamada K. M. Characterization of a 140-kD avian cell surface antigen as a fibronectin-binding molecule. J Cell Biol. 1986 Feb;102(2):442–448. doi: 10.1083/jcb.102.2.442. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Barclay A. N., Letarte-Muirhead M., Williams A. F., Faulkes R. A. Chemical characterisation of the Thy-1 glycoproteins from the membranes of rat thymocytes and brain. Nature. 1976 Oct 14;263(5578):563–567. doi: 10.1038/263563a0. [DOI] [PubMed] [Google Scholar]
- Bordier C., Crettol-Järvinen A. Peptide mapping of heterogeneous protein samples. J Biol Chem. 1979 Apr 25;254(8):2565–2567. [PubMed] [Google Scholar]
- Bordier C. Phase separation of integral membrane proteins in Triton X-114 solution. J Biol Chem. 1981 Feb 25;256(4):1604–1607. [PubMed] [Google Scholar]
- Boucaut J. C., Darribère T., Poole T. J., Aoyama H., Yamada K. M., Thiery J. P. Biologically active synthetic peptides as probes of embryonic development: a competitive peptide inhibitor of fibronectin function inhibits gastrulation in amphibian embryos and neural crest cell migration in avian embryos. J Cell Biol. 1984 Nov;99(5):1822–1830. doi: 10.1083/jcb.99.5.1822. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Brower D. L., Lawrence P. A., Wilcox M. Clonal analysis of the undifferentiated wing disk of Drosophila. Dev Biol. 1981 Sep;86(2):448–455. doi: 10.1016/0012-1606(81)90203-7. [DOI] [PubMed] [Google Scholar]
- Brower D. L., Piovant M., Reger L. A. Developmental analysis of Drosophila position-specific antigens. Dev Biol. 1985 Mar;108(1):120–130. doi: 10.1016/0012-1606(85)90014-4. [DOI] [PubMed] [Google Scholar]
- Brower D. L. Posterior-to-anterior transformation in engrailed wing imaginal disks of Drosophila. Nature. 1984 Aug 9;310(5977):496–497. doi: 10.1038/310496a0. [DOI] [PubMed] [Google Scholar]
- Brower D. L., Wilcox M., Piovant M., Smith R. J., Reger L. A. Related cell-surface antigens expressed with positional specificity in Drosophila imaginal discs. Proc Natl Acad Sci U S A. 1984 Dec;81(23):7485–7489. doi: 10.1073/pnas.81.23.7485. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Brown P. J., Juliano R. L. Selective inhibition of fibronectin-mediated cell adhesion by monoclonal antibodies to a cell-surface glycoprotein. Science. 1985 Jun 21;228(4706):1448–1451. doi: 10.1126/science.4012302. [DOI] [PubMed] [Google Scholar]
- Chan L. N., Gehring W. Determination of blastoderm cells in Drosophila melanogaster. Proc Natl Acad Sci U S A. 1971 Sep;68(9):2217–2221. doi: 10.1073/pnas.68.9.2217. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Cullen S. E., Kindle C. S., Shreffler D. C., Cowing C. Differential glycosylation of murine B cell and spleen adherent cell Ia antigens. J Immunol. 1981 Oct;127(4):1478–1484. [PubMed] [Google Scholar]
- Elder J. H., Alexander S. endo-beta-N-acetylglucosaminidase F: endoglycosidase from Flavobacterium meningosepticum that cleaves both high-mannose and complex glycoproteins. Proc Natl Acad Sci U S A. 1982 Aug;79(15):4540–4544. doi: 10.1073/pnas.79.15.4540. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Garcia-Bellido A., Ripoll P., Morata G. Developmental compartmentalization in the dorsal mesothoracic disc of Drosophila. Dev Biol. 1976 Jan;48(1):132–147. doi: 10.1016/0012-1606(76)90052-x. [DOI] [PubMed] [Google Scholar]
- Gardner J. M., Hynes R. O. Interaction of fibronectin with its receptor on platelets. Cell. 1985 Sep;42(2):439–448. doi: 10.1016/0092-8674(85)90101-1. [DOI] [PubMed] [Google Scholar]
- Geisow M. J. Cell-surface receptors: puzzles and paradigms. Bioessays. 1986 Apr;4(4):149–151. doi: 10.1002/bies.950040403. [DOI] [PubMed] [Google Scholar]
- Giancotti F. G., Tarone G., Knudsen K., Damsky C., Comoglio P. M. Cleavage of a 135 kD cell surface glycoprotein correlates with loss of fibroblast adhesion to fibronectin. Exp Cell Res. 1985 Jan;156(1):182–190. doi: 10.1016/0014-4827(85)90272-1. [DOI] [PubMed] [Google Scholar]
- Hasegawa T., Hasegawa E., Chen W. T., Yamada K. M. Characterization of a membrane-associated glycoprotein complex implicated in cell adhesion to fibronectin. J Cell Biochem. 1985;28(4):307–318. doi: 10.1002/jcb.240280409. [DOI] [PubMed] [Google Scholar]
- Hawkes R. Identification of concanavalin A-binding proteins after sodium dodecyl sulfate--gel electrophoresis and protein blotting. Anal Biochem. 1982 Jun;123(1):143–146. doi: 10.1016/0003-2697(82)90634-0. [DOI] [PubMed] [Google Scholar]
- Hewick R. M., Hunkapiller M. W., Hood L. E., Dreyer W. J. A gas-liquid solid phase peptide and protein sequenator. J Biol Chem. 1981 Aug 10;256(15):7990–7997. [PubMed] [Google Scholar]
- Hunkapiller M. W., Hood L. E. Analysis of phenylthiohydantoins by ultrasensitive gradient high-performance liquid chromatography. Methods Enzymol. 1983;91:486–493. doi: 10.1016/s0076-6879(83)91045-5. [DOI] [PubMed] [Google Scholar]
- Hunkapiller T., Hood L. The growing immunoglobulin gene superfamily. Nature. 1986 Sep 4;323(6083):15–16. doi: 10.1038/323015a0. [DOI] [PubMed] [Google Scholar]
- Keizer G. D., Borst J., Figdor C. G., Spits H., Miedema F., Terhorst C., De Vries J. E. Biochemical and functional characteristics of the human leukocyte membrane antigen family LFA-1, Mo-1 and p150,95. Eur J Immunol. 1985 Nov;15(11):1142–1148. doi: 10.1002/eji.1830151114. [DOI] [PubMed] [Google Scholar]
- Knudsen K. A., Horwitz A. F., Buck C. A. A monoclonal antibody identifies a glycoprotein complex involved in cell-substratum adhesion. Exp Cell Res. 1985 Mar;157(1):218–226. doi: 10.1016/0014-4827(85)90164-8. [DOI] [PubMed] [Google Scholar]
- Le Douarin N. M. Cell migrations in embryos. Cell. 1984 Sep;38(2):353–360. doi: 10.1016/0092-8674(84)90490-2. [DOI] [PubMed] [Google Scholar]
- McGregor J. L., Clemetson K. J., James E., Capitanio A., Greenland T., Lüscher E. F., Dechavanne M. Glycoproteins of platelet membranes from Glanzmann's thrombasthenia. A comparison with normal using carbohydrate-specific or protein-specific labelling techniques and high-resolution two-dimensional gel electrophoresis. Eur J Biochem. 1981 May 15;116(2):379–388. doi: 10.1111/j.1432-1033.1981.tb05346.x. [DOI] [PubMed] [Google Scholar]
- Morata G., Lawrence P. A. Control of compartment development by the engrailed gene in Drosophila. Nature. 1975 Jun 19;255(5510):614–617. doi: 10.1038/255614a0. [DOI] [PubMed] [Google Scholar]
- Naidet C., Sémériva M., Yamada K. M., Thiery J. P. Peptides containing the cell-attachment recognition signal Arg-Gly-Asp prevent gastrulation in Drosophila embryos. Nature. 1987 Jan 22;325(6102):348–350. doi: 10.1038/325348a0. [DOI] [PubMed] [Google Scholar]
- O'Farrell P. H. High resolution two-dimensional electrophoresis of proteins. J Biol Chem. 1975 May 25;250(10):4007–4021. [PMC free article] [PubMed] [Google Scholar]
- Patel V. P., Lodish H. F. The fibronectin receptor on mammalian erythroid precursor cells: characterization and developmental regulation. J Cell Biol. 1986 Feb;102(2):449–456. doi: 10.1083/jcb.102.2.449. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Plow E. F., Pierschbacher M. D., Ruoslahti E., Marguerie G. A., Ginsberg M. H. The effect of Arg-Gly-Asp-containing peptides on fibrinogen and von Willebrand factor binding to platelets. Proc Natl Acad Sci U S A. 1985 Dec;82(23):8057–8061. doi: 10.1073/pnas.82.23.8057. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Pytela R., Pierschbacher M. D., Ruoslahti E. A 125/115-kDa cell surface receptor specific for vitronectin interacts with the arginine-glycine-aspartic acid adhesion sequence derived from fibronectin. Proc Natl Acad Sci U S A. 1985 Sep;82(17):5766–5770. doi: 10.1073/pnas.82.17.5766. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Rothbard J. B., Brackenbury R., Cunningham B. A., Edelman G. M. Differences in the carbohydrate structures of neural cell-adhesion molecules from adult and embryonic chicken brains. J Biol Chem. 1982 Sep 25;257(18):11064–11069. [PubMed] [Google Scholar]
- Ruoslahti E., Pierschbacher M. D. Arg-Gly-Asp: a versatile cell recognition signal. Cell. 1986 Feb 28;44(4):517–518. doi: 10.1016/0092-8674(86)90259-x. [DOI] [PubMed] [Google Scholar]
- Sanchez-Madrid F., Nagy J. A., Robbins E., Simon P., Springer T. A. A human leukocyte differentiation antigen family with distinct alpha-subunits and a common beta-subunit: the lymphocyte function-associated antigen (LFA-1), the C3bi complement receptor (OKM1/Mac-1), and the p150,95 molecule. J Exp Med. 1983 Dec 1;158(6):1785–1803. doi: 10.1084/jem.158.6.1785. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Spits H., Yssel H., Takebe Y., Arai N., Yokota T., Lee F., Arai K., Banchereau J., de Vries J. E. Recombinant interleukin 4 promotes the growth of human T cells. J Immunol. 1987 Aug 15;139(4):1142–1147. [PubMed] [Google Scholar]
- Springer T. A., Teplow D. B., Dreyer W. J. Sequence homology of the LFA-1 and Mac-1 leukocyte adhesion glycoproteins and unexpected relation to leukocyte interferon. Nature. 1985 Apr 11;314(6011):540–542. doi: 10.1038/314540a0. [DOI] [PubMed] [Google Scholar]
- Suzuki S., Argraves W. S., Pytela R., Arai H., Krusius T., Pierschbacher M. D., Ruoslahti E. cDNA and amino acid sequences of the cell adhesion protein receptor recognizing vitronectin reveal a transmembrane domain and homologies with other adhesion protein receptors. Proc Natl Acad Sci U S A. 1986 Nov;83(22):8614–8618. doi: 10.1073/pnas.83.22.8614. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Tamkun J. W., DeSimone D. W., Fonda D., Patel R. S., Buck C., Horwitz A. F., Hynes R. O. Structure of integrin, a glycoprotein involved in the transmembrane linkage between fibronectin and actin. Cell. 1986 Jul 18;46(2):271–282. doi: 10.1016/0092-8674(86)90744-0. [DOI] [PubMed] [Google Scholar]
- Tarone G., Galetto G., Prat M., Comoglio P. M. Cell surface molecules and fibronectin-mediated cell adhesion: effect of proteolytic digestion of membrane proteins. J Cell Biol. 1982 Jul;94(1):179–186. doi: 10.1083/jcb.94.1.179. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci U S A. 1979 Sep;76(9):4350–4354. doi: 10.1073/pnas.76.9.4350. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Wilcox M., Brower D. L., Smith R. J. A position-specific cell surface antigen in the drosophila wing imaginal disc. Cell. 1981 Jul;25(1):159–164. doi: 10.1016/0092-8674(81)90240-3. [DOI] [PubMed] [Google Scholar]
- Wilcox M., Brown N., Piovant M., Smith R. J., White R. A. The Drosophila position-specific antigens are a family of cell surface glycoprotein complexes. EMBO J. 1984 Oct;3(10):2307–2313. doi: 10.1002/j.1460-2075.1984.tb02131.x. [DOI] [PMC free article] [PubMed] [Google Scholar]