Skip to main content
NCBI home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1986 Oct;83(20):7603–7607. doi: 10.1073/pnas.83.20.7603

Evidence that a human soluble beta-galactoside-binding lectin is encoded by a family of genes.

M A Gitt, S H Barondes
PMCID: PMC386769  PMID: 3020551

Abstract

Two cDNA clones were isolated by immunoscreening a human hepatoma cDNA library with an antiserum that bound specifically to a human soluble beta-galactoside-binding lectin with Mr of approximately 14,000. The deduced amino acid sequences of the inserts of these two clones show considerable homology with each other, the sequence of chicken skin beta-galactoside-binding lectin, and eight peptides derived from purified human lung lectin of Mr approximately 14,000. However, the sequence differences between the two hepatoma clones as well as among each clone and the lung peptides suggest that at least three variants of the gene encoding this lectin are expressed in human tissue.

Full text

PDF
7603

Images in this article

7604Image
on p.7604
7605Image
on p.7605
7605Image
on p.7605

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Barondes S. H. Soluble lectins: a new class of extracellular proteins. Science. 1984 Mar 23;223(4642):1259–1264. doi: 10.1126/science.6367039. [DOI] [PubMed] [Google Scholar]
  2. Beyer E. C., Barondes S. H. Quantitation of two endogenous lactose-inhibitable lectins in embryonic and adult chicken tissues. J Cell Biol. 1982 Jan;92(1):23–27. doi: 10.1083/jcb.92.1.23. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Beyer E. C., Zweig S. E., Barondes S. H. Two lactose binding lectins from chicken tissues. Purified lectin from intestine is different from those in liver and muscle. J Biol Chem. 1980 May 10;255(9):4236–4239. [PubMed] [Google Scholar]
  4. Cerra R. F., Gitt M. A., Barondes S. H. Three soluble rat beta-galactoside-binding lectins. J Biol Chem. 1985 Sep 5;260(19):10474–10477. [PubMed] [Google Scholar]
  5. Close T. J., Rodriguez R. L. Construction and characterization of the chloramphenicol-resistance gene cartridge: a new approach to the transcriptional mapping of extrachromosomal elements. Gene. 1982 Dec;20(2):305–316. doi: 10.1016/0378-1119(82)90048-8. [DOI] [PubMed] [Google Scholar]
  6. Cohen S. N., Chang A. C., Hsu L. Nonchromosomal antibiotic resistance in bacteria: genetic transformation of Escherichia coli by R-factor DNA. Proc Natl Acad Sci U S A. 1972 Aug;69(8):2110–2114. doi: 10.1073/pnas.69.8.2110. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Edelman G. M., Wang J. L. Binding and functional properties of concanavalin A and its derivatives. III. Interactions with indoleacetic acid and other hydrophobic ligands. J Biol Chem. 1978 May 10;253(9):3016–3022. [PubMed] [Google Scholar]
  8. Feng D. F., Johnson M. S., Doolittle R. F. Aligning amino acid sequences: comparison of commonly used methods. J Mol Evol. 1984;21(2):112–125. doi: 10.1007/BF02100085. [DOI] [PubMed] [Google Scholar]
  9. Gabius H. J., Springer W. R., Barondes S. H. Receptor for the cell binding site of discoidin I. Cell. 1985 Sep;42(2):449–456. doi: 10.1016/0092-8674(85)90102-3. [DOI] [PubMed] [Google Scholar]
  10. Gitt M. A., Wang L. F., Doi R. H. A strong sequence homology exists between the major RNA polymerase sigma factors of Bacillus subtilis and Escherichia coli. J Biol Chem. 1985 Jun 25;260(12):7178–7185. [PubMed] [Google Scholar]
  11. Heidecker G., Messing J., Gronenborn B. A versatile primer for DNA sequencing in the M13mp2 cloning system. Gene. 1980 Jun;10(1):69–73. doi: 10.1016/0378-1119(80)90145-6. [DOI] [PubMed] [Google Scholar]
  12. Hoffman L. M., Donaldson D. D. Characterization of two Phaseolus vulgaris phytohemagglutinin genes closely linked on the chromosome. EMBO J. 1985 Apr;4(4):883–889. doi: 10.1002/j.1460-2075.1985.tb03714.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. King E. B., Vanderlaan M., Jensen R. H., Kromhout L. K., Hoffman J. W. Morphologic changes in rat urothelial cells during carcinogenesis: I. Histologic and cytologic changes. Cytometry. 1984 Sep;5(5):447–453. doi: 10.1002/cyto.990050503. [DOI] [PubMed] [Google Scholar]
  14. Leffler H., Barondes S. H. Specificity of binding of three soluble rat lung lectins to substituted and unsubstituted mammalian beta-galactosides. J Biol Chem. 1986 Aug 5;261(22):10119–10126. [PubMed] [Google Scholar]
  15. Messing J., Crea R., Seeburg P. H. A system for shotgun DNA sequencing. Nucleic Acids Res. 1981 Jan 24;9(2):309–321. doi: 10.1093/nar/9.2.309. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Messing J. New M13 vectors for cloning. Methods Enzymol. 1983;101:20–78. doi: 10.1016/0076-6879(83)01005-8. [DOI] [PubMed] [Google Scholar]
  17. Norrander J., Kempe T., Messing J. Construction of improved M13 vectors using oligodeoxynucleotide-directed mutagenesis. Gene. 1983 Dec;26(1):101–106. doi: 10.1016/0378-1119(83)90040-9. [DOI] [PubMed] [Google Scholar]
  18. Ohyama Y., Hirabayashi J., Oda Y., Ohno S., Kawasaki H., Suzuki K., Kasai K. Nucleotide sequence of chick 14K beta-galactoside-binding lectin mRNA. Biochem Biophys Res Commun. 1986 Jan 14;134(1):51–56. doi: 10.1016/0006-291x(86)90525-5. [DOI] [PubMed] [Google Scholar]
  19. Powell J. T. Purification and properties of lung lectin. Rat lung and human lung beta-galactoside-binding proteins. Biochem J. 1980 Apr 1;187(1):123–129. doi: 10.1042/bj1870123. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Roberts D. D., Goldstein I. J. Hydrophobic binding properties of the lectin from lima beans (Phaseolus lunatus). J Biol Chem. 1982 Oct 10;257(19):11274–11277. [PubMed] [Google Scholar]
  21. Roff C. F., Rosevear P. R., Wang J. L., Barker R. Identification of carbohydrate-binding proteins from mouse and human fibroblasts. Biochem J. 1983 Jun 1;211(3):625–629. doi: 10.1042/bj2110625. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Sanger F., Nicklen S., Coulson A. R. DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci U S A. 1977 Dec;74(12):5463–5467. doi: 10.1073/pnas.74.12.5463. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Whitney P., Maxwell S., Ryan U., Massaro D. Synthesis and binding of lactose-specific lectin by isolated lung cells. Am J Physiol. 1985 Mar;248(3 Pt 1):C258–C264. doi: 10.1152/ajpcell.1985.248.3.C258. [DOI] [PubMed] [Google Scholar]
  24. Young R. A., Davis R. W. Efficient isolation of genes by using antibody probes. Proc Natl Acad Sci U S A. 1983 Mar;80(5):1194–1198. doi: 10.1073/pnas.80.5.1194. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Young R. A., Davis R. W. Yeast RNA polymerase II genes: isolation with antibody probes. Science. 1983 Nov 18;222(4625):778–782. doi: 10.1126/science.6356359. [DOI] [PubMed] [Google Scholar]
  26. de Wet J. R., Fukushima H., Dewji N. N., Wilcox E., O'Brien J. S., Helinski D. R. Chromogenic immunodetection of human serum albumin and alpha-L-fucosidase clones in a human hepatoma cDNA expression library. DNA. 1984 Dec;3(6):437–447. doi: 10.1089/dna.1.1984.3.437. [DOI] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES