Pregnancy-associated plasma protein-A (PAPP-A): A local regulator of IGF bioavailability through cleavage of IGFBPs

Henning B. Boldt, Cheryl A. Conover

Research output: Contribution to journalReview articlepeer-review

142 Scopus citations


Pregnancy-associated plasma protein-A (PAPP-A) was originally isolated in 1974, as one of four proteins of placental origin found in high concentrations in the blood of pregnant women. In the early 1990s several laboratories reported novel protease activity against insulin-like growth factor binding protein-4 (IGFBP-4) in media conditioned by several cell types. This activity was unique, as it appeared to require the presence of IGF to cleave IGFBP-4. In 1999, this IGF-dependent IGFBP-4 protease activity was isolated from human fibroblast conditioned media and identified as PAPP-A. Subsequently, PAPP-A was shown to be expressed by a variety of cell types, and thus no longer could be considered to be just "pregnancy-associated". This review will describe what is currently known about the structure of PAPP-A and about its function as an IGFBP protease, with a focus on new insights obtained through study of a PAPP-A knock-out mouse model and on potential clinical applications.

Original languageEnglish (US)
Pages (from-to)10-18
Number of pages9
JournalGrowth Hormone and IGF Research
Issue number1
StatePublished - Feb 2007


  • IGF binding protein
  • Insulin-like growth factor
  • Pappalysin
  • Pregnancy associated plasma protein-A
  • Protease

ASJC Scopus subject areas

  • Endocrinology, Diabetes and Metabolism
  • Endocrinology


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