Primary structure of a putative serine protease specific for IGF-binding proteins

FEBS Lett. 1996 Dec 2;398(2-3):187-92. doi: 10.1016/s0014-5793(96)01229-x.


From a subtracted cDNA library we have isolated a cDNA clone coding for a novel transformation-sensitive protein which is expressed by human fibroblasts, but not by their matched SV40 transformed counterparts. This protein has a molecular mass of 51 kDa and is highly related to the HtrA family of serine proteases from bacteria. At the N-terminal end, it contains an IGF-binding domain which may modulate the activity of the associated serine protease. Our data are consistent with the assumption that the novel protein represents one of the proteases that regulate the availability of IGFs by cleaving IGF-binding proteins.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / chemistry
  • Base Sequence
  • Binding Sites
  • Carrier Proteins / chemistry*
  • Carrier Proteins / genetics
  • Carrier Proteins / metabolism
  • Cell Line
  • Cell Line, Transformed
  • Cell Transformation, Viral
  • Cloning, Molecular
  • DNA, Complementary / genetics
  • Heat-Shock Proteins*
  • High-Temperature Requirement A Serine Peptidase 1
  • Humans
  • Insulin-Like Growth Factor Binding Proteins / metabolism*
  • Molecular Sequence Data
  • Molecular Weight
  • Periplasmic Proteins*
  • Sequence Alignment
  • Serine Endopeptidases / chemistry*
  • Serine Endopeptidases / genetics
  • Serine Endopeptidases / metabolism


  • Bacterial Proteins
  • Carrier Proteins
  • DNA, Complementary
  • Heat-Shock Proteins
  • Insulin-Like Growth Factor Binding Proteins
  • Periplasmic Proteins
  • DegP protease
  • High-Temperature Requirement A Serine Peptidase 1
  • HtrA1 protein, human
  • Serine Endopeptidases

Associated data

  • GENBANK/Y07921