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A 25 kDa alpha 2-microglobulin-related protein is a component of the 125 kDa form of human gelatinase

S Triebel1, J Bläser, H Reinke

  • 1Department of Biochemistry, Faculty of Chemistry, University of Bielefeld, Germany.

FEBS Letters
|December 21, 1992
PubMed

Insights

Researchers identified novel forms of progelatinase in human leukocytes, including a 125 kDa form. This form is a heterodimer linked to a previously unknown human protein homologous to rat alpha 2-microglobulin.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Progelatinase, a key enzyme in extracellular matrix degradation, exists in various forms.
  • Human polymorphonuclear (PMN) leukocytes are a source of matrix metalloproteinases, including gelatinases.

Purpose of the Study:

  • To characterize novel forms of progelatinase isolated from human PMN leukocytes.
  • To identify the protein component of a newly discovered 125 kDa progelatinase complex.

Main Methods:

  • Isolation and purification of progelatinase forms from human PMN leukocytes.
  • Affinity chromatography using gelatin-Sepharose.
  • Peptide sequencing and homology analysis.

Main Results:

  • Three progelatinase forms were isolated: 95 kDa monomer, 220 kDa dimer, and 125 kDa form.
  • The 125 kDa form is a disulfide-bridged heterodimer of monomeric progelatinase and a 25 kDa protein.
  • The 25 kDa protein showed homology to rat alpha 2-microglobulin, a protein previously unknown in humans.

Conclusions:

  • Human PMN leukocytes contain complex forms of progelatinase.
  • A novel 25 kDa protein, homologous to rat alpha 2-microglobulin, is associated with human progelatinase.
  • This discovery expands the known repertoire of proteins interacting with gelatinase in humans.

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