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(NAS Colloquium) Proteolytic Processing and Physiological Regulation (1999) / Chapter Skim
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Reverse biochemistry: Use of macromolecular protease inhibitors to dissect complex biological processes and identify a membrane-type serine protease in epithelial cancer and normal tissue
Pages 11054-11061

The Chapter Skim interface presents what we've algorithmically identified as the most significant single chunk of text within every page in the chapter.
Select key terms on the right to highlight them within pages of the chapter.


From page 11054...
... Ecotin and variant ecotins are subnanomolar inhibitors of the MT SP1 activated protease domain, suggesting a possible role for MT-SP1 in prostate differentiation and the growth of pros tatic carcinomas. Serine proteases possessing a chymotrypsin fold are of great interest because they provide detailed understanding of their enzymatic properties and their proposed role in a number of physiological and pathological processes.
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From page 11055...
... In this report we have extended the strategy of using PCR with degenerate oligonucleotide primers that were designed by using conserved sequence homology (12-14) to identify additional serine proteases made by cancer cells.
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From page 11056...
... PCR amplification of serine protease cDNA was performed by using "consensus cloning", where the amplification was performed with degenerate primers designed to anneal to cDNA encoding the region about the conserved catalytic histidine (5' His-primer) and the conserved catalytic serine (3' Ser-primer)
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From page 11057...
... ; L, LDLR repeat (29~; SP, a chymotrypsin family serine protease domain (40~; MAM, a domain homologous to members of a family defined by meprin, protein AS, and the protein tyrosine phosphatase ~ (48~; MSCR, a macrophage scavenger receptor cysteine-rich motif (29~. The predicted disulfide linkages are shown labeled as C-C.
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From page 11058...
... (A) Multiple sequence alignment of the serine protease domain of MT-SP1 with human trypsinogen B (49)
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From page 11059...
... We propose that proteins that are localized to the membrane through a SA and that encode a chymotrypsin fold serine protease domain be categorized in the MT-SP family. The membrane localization of MT-SP1 is supported by immunofluorescence experiments that localize the protease domain to the extracellular cell surface (unpublished results)
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From page 11060...
... . Because wild-type ecotin is a poor, micromolar inhibitor of uPA, serine proteases other than uPA likely are involved in this primary tumor proliferation.
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From page 11061...
... Colloquium Paper: Takeuchi et al.
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Key Terms

  • serine protease
  • serine proteases
  • spectrozyme tpa
  • amino acid
  • cub domains

  • chymotrypsin fold
  • sequence tag
  • ventral prostate
  • expressed sequence
  • amino acids

  • embryonic growth
  • cell line
  • rat ventral
  • morphogenetic protein
  • substrate spectrozyme

  • tumor size
  • primary tumor
  • catalytic serine
  • signal anchor
  • acid sequence

  • proteolytic activity
  • dna sequencing
  • catalytic histidine
  • degenerate primers
  • ldlr repeats

  • northern blotting
  • ala protease
  • nucleotide sequence
  • prostate differentiation
  • activated protease


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