Skip to main content

New member of the trefoil factor family of proteins is an alpha-macroglobulin protease inhibitor.

Publication ,  Journal Article
Thøgersen, IB; Hammes, SR; Rubenstein, DS; Pizzo, SV; Valnickova, Z; Enghild, JJ
Published in: Biochim Biophys Acta
July 29, 2002

The amino acid sequence of the monomeric alpha-macroglobulin (alphaM) from the American bullfrog, Rana catesbiana, was determined. The mature protein consisted of 1469 amino acid residues and shared sequence identity with other members of the alphaM family of protein. The central portion of the frog monomeric alphaM contained Cys residues positioned analogously to the Cys residues in human alpha(2)-macroglobulin (alpha(2)M), known to be involved in disulfide bridges. Additionally, the frog monomeric alphaM contained six Cys residues in a approximately 60 residue COOH-terminal extension not present in previously characterized alphaMs. The spacing of the Cys residues and the overall sequence identity of this COOH-terminal extension were consistent with a trefoil motif. This is the first time a member of the trefoil factor family has been identified in the circulatory system. The "bait region" was located between Arg(675)-Lys(685) and contained mainly basic amino acid residues. The COOH-terminal receptor-binding domain was not exposed prior to proteolysis of this highly susceptible region. The proximity of the receptor-binding and trefoil domains implied that the trefoil domain is similarly concealed before bait region cleavage.

Duke Scholars

Published In

Biochim Biophys Acta

DOI

ISSN

0006-3002

Publication Date

July 29, 2002

Volume

1598

Issue

1-2

Start / End Page

131 / 139

Location

Netherlands

Related Subject Headings

  • alpha-Macroglobulins
  • Trefoil Factor-3
  • Trefoil Factor-2
  • Sequence Homology, Amino Acid
  • Sequence Alignment
  • Rana catesbeiana
  • Protease Inhibitors
  • Peptides
  • Peptide Fragments
  • Neuropeptides
 

Citation

APA
Chicago
ICMJE
MLA
NLM
Thøgersen, I. B., Hammes, S. R., Rubenstein, D. S., Pizzo, S. V., Valnickova, Z., & Enghild, J. J. (2002). New member of the trefoil factor family of proteins is an alpha-macroglobulin protease inhibitor. Biochim Biophys Acta, 1598(1–2), 131–139. https://doi.org/10.1016/s0167-4838(02)00360-6
Thøgersen, Ida B., Stephen R. Hammes, David S. Rubenstein, Salvatore V. Pizzo, Zuzana Valnickova, and Jan J. Enghild. “New member of the trefoil factor family of proteins is an alpha-macroglobulin protease inhibitor.Biochim Biophys Acta 1598, no. 1–2 (July 29, 2002): 131–39. https://doi.org/10.1016/s0167-4838(02)00360-6.
Thøgersen IB, Hammes SR, Rubenstein DS, Pizzo SV, Valnickova Z, Enghild JJ. New member of the trefoil factor family of proteins is an alpha-macroglobulin protease inhibitor. Biochim Biophys Acta. 2002 Jul 29;1598(1–2):131–9.
Thøgersen, Ida B., et al. “New member of the trefoil factor family of proteins is an alpha-macroglobulin protease inhibitor.Biochim Biophys Acta, vol. 1598, no. 1–2, July 2002, pp. 131–39. Pubmed, doi:10.1016/s0167-4838(02)00360-6.
Thøgersen IB, Hammes SR, Rubenstein DS, Pizzo SV, Valnickova Z, Enghild JJ. New member of the trefoil factor family of proteins is an alpha-macroglobulin protease inhibitor. Biochim Biophys Acta. 2002 Jul 29;1598(1–2):131–139.

Published In

Biochim Biophys Acta

DOI

ISSN

0006-3002

Publication Date

July 29, 2002

Volume

1598

Issue

1-2

Start / End Page

131 / 139

Location

Netherlands

Related Subject Headings

  • alpha-Macroglobulins
  • Trefoil Factor-3
  • Trefoil Factor-2
  • Sequence Homology, Amino Acid
  • Sequence Alignment
  • Rana catesbeiana
  • Protease Inhibitors
  • Peptides
  • Peptide Fragments
  • Neuropeptides