ADAM28

  • Anne M. Fourie
Part of the Proteases in Biology and Disease book series (PBAD, volume 4)

Abstract

The ADAM family of disintegrin metalloproteases plays important roles in proteolytic “ectodomain shedding” and adhesion functions. Currently, this family has 34 members, approximately half of which are predicted to be active proteases, including ADAM28. ADAM28 is expressed in human lymphocytes, murine thymic epithelial cells, the epididymis in multiple species, and is upregulated in certain cancer cells. Both membrane-bound and secreted isoforms of ADAM28 have been identified. ADAM28 is activated by autocatalytic removal of the pro-domain and the mature transmembrane protein is expressed on the cell surface. The active form of ADAM28 cleaves specific sites in numerous peptides and protein substrates, including the low affinity IgE receptor, CD23, and IGFBP-3. The substrate selectivity of ADAM28 is very similar to that of the closely-related ADAMs, −8 and −15, but distinct from that of the more distantly-related ADAM17. An extended region of the disintegrin domain of ADAM28 specifically recognizes the leukocyte integrin, α4β1, in an activation-dependent conformation. The physiological functions of ADAM28 are not known, but its expression pattern, together with its substrate and integrin binding selectivity, suggest potential roles in spermatogenesis, lymphocyte maturation and function, inflammation and cancer.

Key words

metalloprotease lymphocyte thymic epithelium epididymis MDC-L eMDC II autocatalytic CD23 IGFBP-3 disintegrin α4β1 

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Copyright information

© Springer 2005

Authors and Affiliations

  • Anne M. Fourie
    • 1
  1. 1.Johnson & Johnson Pharmaceutical Research and DevelopmentSan DiegoUSA

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