Primary structure of a putative serine protease specific for IGF-binding proteins
J Zumbrunn, B Trueb - FEBS letters, 1996 - Elsevier
J Zumbrunn, B Trueb
FEBS letters, 1996•ElsevierFrom 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 …
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 …
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.
Elsevier