Encyclopedia of Cancer

Living Edition
| Editors: Manfred Schwab

AAMP

Living reference work entry
DOI: https://doi.org/10.1007/978-3-642-27841-9_6-3

Definition

Angio-associated migratory cell protein; gene maps to chromosome 2q35. AAMP has been conserved in evolution, is distributed intracellularly in many cells and also extracellularly on vascular cells, shares an epitope with motility-related proteins (alpha-actinin and a fast twitch skeletal muscle protein), and contains potential heparin binding and thrombin cleavage sites. Antibody and antisense studies have indicated compartment (intracellular or extracellular) specific roles for AAMP in angiogenesis, cell-cell and cell-matrix interactions, and cell migration.

Characteristics

The cDNA derived from mRNA encoding AAMP was originally cloned from a human melanoma cell library (A2058) in a search for migration-related proteins. AAMP has been found in the cytoplasm of many nucleated cells, in an extracellular mesh-like network on monolayers of endothelial and vascular-associated smooth muscle cells, and on the apical membranes of endometrial glandular cells. AAMP expression when...

Keywords

Aspartic Acid Residue Heparin Binding Human Immunodeficiency Viral Protein Heparin Binding Site Endothelial Tube Formation 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
This is a preview of subscription content, log in to check access

References

  1. Adeyinka A, Emberley E, Niu Y et al (2002) Analysis of gene expression in ductal carcinoma in situ of the breast. Clin Cancer Res 8:3788–3795PubMedGoogle Scholar
  2. Allander SV, Nupponen NN, Ringner M et al (2001) Gastrointestinal stromal tumors with KIT mutations exhibit a remarkably homogeneous gene expression profile. Cancer Res 61:8624–8628PubMedGoogle Scholar
  3. Beckner ME, Krutzsch HC, Stracke ML et al (1995) Identification of a new immunoglobulin superfamily protein expressed in blood vessels with a heparin-binding consensus sequence. Cancer Res 55:2140–2149PubMedGoogle Scholar
  4. Beckner ME, Krutzsch HC, Klipstein S et al (1996) AAMP, a newly identified protein, shares a common epitope with alpha-actinin and a fast skeletal muscle fiber protein. Exp Cell Res 225:306–314CrossRefPubMedGoogle Scholar
  5. Beckner ME, Jagannathan S, Peterson VA (2002) Extracellular angio-associated migratory cell protein plays a positive role in angiogenesis and is regulated by astrocytes in coculture. Microvasc Res 63:259–269CrossRefPubMedGoogle Scholar

See Also

  1. (2012) Alpha-Actinin. In: Schwab M (ed) Encyclopedia of Cancer, 3rd edn. Springer Berlin Heidelberg, p 143. doi:10.1007/978-3-642-16483-5_203Google Scholar
  2. (2012) Amino Terminal End. In: Schwab M (ed) Encyclopedia of Cancer, 3rd edn. Springer Berlin Heidelberg, p 156. doi:10.1007/978-3-642-16483-5_224Google Scholar
  3. (2012) Domain. In: Schwab M (ed) Encyclopedia of Cancer, 3rd edn. Springer Berlin Heidelberg, p 1150. doi:10.1007/978-3-642-16483-5_1702Google Scholar
  4. (2012) Epitope. In: Schwab M (ed) Encyclopedia of Cancer, 3rd edn. Springer Berlin Heidelberg, p 1297. doi:10.1007/978-3-642-16483-5_1966Google Scholar
  5. (2012) Glycosaminoglycans. In: Schwab M (ed) Encyclopedia of Cancer, 3rd edn. Springer Berlin Heidelberg, p 1570. doi:10.1007/978-3-642-16483-5_2453Google Scholar
  6. (2012) Phorbol Ester. In: Schwab M (ed) Encyclopedia of Cancer, 3rd edn. Springer Berlin Heidelberg, p 2865. doi:10.1007/978-3-642-16483-5_4522Google Scholar
  7. (2012) Secondary Structure. In: Schwab M (ed) Encyclopedia of Cancer, 3rd edn. Springer Berlin Heidelberg, p 3348. doi: 10.1007/978-3-642-16483-5_5205Google Scholar
  8. (2012) WD Repeats. In: Schwab M (ed) Encyclopedia of Cancer, 3rd edn. Springer Berlin Heidelberg, p 3945. doi:10.1007/978-3-642-16483-5_6233Google Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 2014

Authors and Affiliations

  1. 1.Department of PathologyUniversity of Pittsburgh School of MedicinePittsburghUSA