Skip to main content
SpringerLink
Log in

Isolation and partial sequence of goat spleen prothymosin α

  • Published:
Molecular and Cellular Biochemistry Aims and scope Submit manuscript

Abstract

Goat prothymosin α, a highly acidic polypeptide of pl 3.5, 109 amino acid residues, has been isolated from lymphoid and non-lymphoid tissues of young female goats. Unlike rat, murine and porcine prothymosins α, goat prothymosin α appears at a higher concentration in the spleen compared with the thymus. The sequence of segments of the polypeptide involving known mutations has been determined, by automatic sequencing of its tryptic peptide fragments. The acidic amino acid-rich segment in the middle of the molecule, including residues 49–83, has not been sequenced. Goat prothymosin α closely resembles bovine prothymosin α, with only one substitution, proline for alanine at position 85. It also resembles human prothymosin α, with only three substitutions. It differs more significantly from rat and murine prothymosins α, by two deletions and three substitutions. The results show the highly conserved nature of the molecule, with substitutions at given positions only.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

Abbreviations

ProTα:

Prothymosin α

Tα1 :

Thymosin α1

MLR:

Mixed Lymphocyte Response

HPLC:

High Performance Liquid Chromatography

RIA:

Radioimmunoassay

B:

Aspartic acid or Asparagine

Z:

Glutamic acid or Glutamine

References

  1. Haritos AA, Goodall GJ, Horecker BL: Prothymosin a: Isolation and properties of the major immunoreactive form of thymosin al in rat thymus. Proc Natl Acad Sci USA 81: 1008–1011, 1984

    Google Scholar 

  2. Haritos AA, Tsolas O, Horecker BL: Distribution of prothymosin a in rat tissues. Proc Natl Acad Sci USA 81: 1391–1393, 1984

    Google Scholar 

  3. Economou M, Seferiadis K, Frangou-Lazaridis M, Horecker BL, Tsolas O: Isolation and partial characterization of prothymosin a from porcine tissues. FEBS Lett 233: 342–346, 1988

    Google Scholar 

  4. Clinton M, Frangou-Lazaridis M, Panneerselvam C, Horecker BL: Prothymosin a and parathymosin: mRNA and polypeptide levels in rodent tissues. Arch Biochem Biophys 269:256–263, 1989

    Google Scholar 

  5. Haritos AA, Blacher R, Stein S, Caldarella J, Horecker BL: Primary structure of rat thymus prothymosin α. Proc Natl Acad Sci USA 82: 343–346, 1985

    Google Scholar 

  6. Frangou-Lazaridis M, Clinton M, Goodall GJ, Horecker BL: Prothymosin a and parathymosin: Amino acid sequences deduced from the cloned rat spleen cDNAs. Arch Biochem Biophys 263: 305–310, 1988

    Google Scholar 

  7. Low TLK, Pan T-L, Lin Y-S: Depression of prothymosin-α production in murine thymus correlates with staphylococcal enterotoxin-B-induced immunosuppression. FEBS Lett 273:1–5, 1990

    Google Scholar 

  8. Pan L-X, Haritos AA, Wideman J, Komiyama T, Chang M, Stein S, Salvin SB, Horecker BL: Human prothymosin α: Amino acid sequence and immunologic properties. Arch Biochem Biophys 250: 197–201, 1986

    Google Scholar 

  9. Goodall GJ, Dominquez F, Horecker BL: Molecular cloning of cDNA for human prothymosin α. Proc Natl Acad Sci USA 83: 8926–8928, 1986

    Google Scholar 

  10. Eschenfeldt WH, Berger SL: The human prothymosin a gene is polymorphic and induced upon growth stimulation: Evidence using a cloned cDNA. Proc Natl Acad Sci USA 83:9403–9407, 1986

    Google Scholar 

  11. Eschenfeldt WH, Manrow RE, Krug MS, Berger SL: Isolation and partial sequencing of the human prothymosin a gene family: Evidence against export of the gene products. J Biol Chem 264: 7546–7555, 1989

    Google Scholar 

  12. Panneerselvam C, Wellner D, Horecker BL: The amino acid sequence of bovine thymus prothymosin α. Arch Biochem Biophys 265: 454–457, 1988

    Google Scholar 

  13. Low TLK, Goldstein AL: The chemistry and biology of thymosin. 11. Amino acid sequence analysis of thymosin a, and polypeptide β1. J Biol Chem 254: 987–995, 1979

    Google Scholar 

  14. Haritos AA, Salvin S, Blacher R, Stein S, Horecker BL: Parathymosin a: A peptide from rat tissues with structural homology to prothymosin α. Proc Natl Acad Sci USA 82: 1050–1053, 1985

    Google Scholar 

  15. Baxevanis CN, Reclos GJ, Panneerselvam C, Papamichail M: Enhancement of human T-lymphocyte functions by prothymosin α. I. Augmentation of mixed lymphocyte culture reactions and soluble protein-induced proliferative responses. Immunopharmacology 15: 73–79, 1988

    Google Scholar 

  16. Baxevanis CN, Reclos GJ, Economou M, Arsenis P, Katsiyiannis A, Seferiadis K, Papadopoulos G, Tsolas O, Papamichail M: Mechanism of action of prothymosin a in the human autologous mixed lymphocyte response. Immunopharmacol Immunotoxicol 10: 443–461, 1988

    Google Scholar 

  17. Gómez-Marquez J, Segade F, Dosil M, Pichel JG, Bustelo XR, Freire M: The expression of prothymosin α gene in T lymphocytes and leukemic lymphoid cells is tied to lymphocyte proliferation. J Biol Chem 264: 8451–8454, 1989

    Google Scholar 

  18. Conteas CN, Mutchnick MG, Palmer KC, Weller FE, Luk GD, Naylor PH, Erdos MR, Goldstein AL, Panneerselvam C, Horecker BL: Cellular levels of thymosin immunoreactive peptides are linked to proliferative events: Evidence for a nuclear site of action. Proc Natl Acad Sci USA 87: 3269–3273,1990

    Google Scholar 

  19. Gómez-Marquez J, Segade F: Hypothesis: Prothymosin a is a nuclear protein. FEBS Lett 226: 217–219, 1988

    Google Scholar 

  20. Watts JD, Cary PD, Sautiere P, Crane-Robinson C: Thymosins: Both nuclear and cytoplasmic proteins. Eur J Biochem 192: 643–651, 1990

    Google Scholar 

  21. Palvimo J, Linnala-Kankkunen A: Identification of a low-M4 acidic nuclear protein as prothymosin α. FEBS Lett 277: 257–260, 1990

    Google Scholar 

  22. Eilers M, Schirm S, Bishop JM: The myc protein activates transcription of the α-prothymosin gene EMBO J 10: 133–141, 1991

    Google Scholar 

  23. Baxevanis CN, Frillingos S, Reclos GJ, Anastasopoulos E, Seferiadis K, Tsolas O, Papamichail M: Prothymosin a enhances interleukin-2 production by activated T lymphocytes. Immunopharmacol Immunotoxicol 12: 336–351, 1990

    Google Scholar 

  24. Vlachoyiannopoulos PG, Frillingos S, Tzioufas AG, Seferiadis K, Moutsopoulos HM, Tsolas O: Circulating antibodies to prothymosin a in systemic lupus erythematosus. Clin Immunol Immunopathol 53: 151–160, 1989

    Google Scholar 

  25. Wang S-S, Kulesha ID, Winter DP: Synthesis of thymosin α1. J Amer Chem Soc 101: 253–254, 1979

    Google Scholar 

  26. Komiyama T, Pan L-X, Haritos AA, Wideman JW, Pan Y-CE, Chang M, Rogers I, Horecker BL: The primary structure of rat parathymosin. Proc Natl Acad Sci USA 83: 1242–1245, 1986

    Google Scholar 

  27. Haritos AA, Horecker BL: A radioimmunoassay for thymosin α1 that detects the native polypeptide, prothymosin α. J Immunol Methods 81: 199–205, 1985

    Google Scholar 

  28. Margolis FL: Solid-phase radioimmune assay using 3H-la-beled antigen for the mouse olfactory bulb specific protein. Anal Biochem 50: 602–607, 1972

    Google Scholar 

  29. Lai C-Y: Detection of peptides by fluorescamine methods. Methods Enzymol 47: 236–243, 1977

    Google Scholar 

  30. Heinrikson RL, Meredith SC: Amino acid analysis by reverse-phase high-performance liquid chromatography: Precolumn derivatization with phenylisothiocyanate. Anal Biochem 136: 65–74, 1984

    Google Scholar 

  31. Erickson-Viitanen S, Ruggieri S, Natalini P, Horecker BL: Thymosin β10, a new analog of thymosin β4 in mammalian tissues. Arch Biochem Biophys 225: 407–413, 1983

    Google Scholar 

  32. Panneerselvam C, Clinton M, Wellner D, Horecker BL: Bovine parathymosin: Amino acid sequence and comparison with rat parathymosin. Biochem Biophys Res Commun 155: 439–545, 1988

    Google Scholar 

  33. Papadopoulos GK, Economou M, Seferiadis K, Tsolas O: Secondary structure of porcine prothymosin a and parathymosin. Eighth European Immunology Meeting, Zagreb. Period Biol 89 (suppl 1): 87 Abstr, 1987

    Google Scholar 

  34. Trompeter H-I, Brand IA, Soling H-D: The primary sequence of the PFK-1 inactivating zinc-binding protein as deduced from cDNA sequencing. Identity of the zinc-binding protein with rat parathymosin. FEBS Lett 253: 63–66, 1989

    Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Laboratory of Biological Chemistry, University of Ioannina Medical School, GR-451 10, Ioannina, Greece

    S. Frillingos, M. Frangou-Lazaridis, K. Seferiadis & O. Tsolas

  2. Department of Protein Biochemistry, Hoffmann-La Roche Inc., 07110, Nutley, NJ, USA

    J. D. Hulmes & Y. -C. E. Pan

Authors
  1. S. Frillingos
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. M. Frangou-Lazaridis
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. K. Seferiadis
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. J. D. Hulmes
    View author publications

    You can also search for this author in PubMed Google Scholar

  5. Y. -C. E. Pan
    View author publications

    You can also search for this author in PubMed Google Scholar

  6. O. Tsolas
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

About this article

Cite this article

Frillingos, S., Frangou-Lazaridis, M., Seferiadis, K. et al. Isolation and partial sequence of goat spleen prothymosin α. Mol Cell Biochem 108, 85–94 (1991). https://doi.org/10.1007/BF00239545

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00239545

Key words

Search

Navigation