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...
References
Adeyinka A, Emberley E, Niu Y et al (2002) Analysis of gene expression in ductal carcinoma in situ of the breast. Clin Cancer Res 8:3788–3795
Allander SV, Nupponen NN, Ringner M et al (2001) Gastrointestinal stromal tumors with KIT mutations exhibit a remarkably homogeneous gene expression profile. Cancer Res 61:8624–8628
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 55:2140–2149
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 225:306–314
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 63:259–269
See Also
(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_203
(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_224
(2012) Domain. In: Schwab M (ed) Encyclopedia of Cancer, 3rd edn. Springer Berlin Heidelberg, p 1150. doi:10.1007/978-3-642-16483-5_1702
(2012) Epitope. In: Schwab M (ed) Encyclopedia of Cancer, 3rd edn. Springer Berlin Heidelberg, p 1297. doi:10.1007/978-3-642-16483-5_1966
(2012) Glycosaminoglycans. In: Schwab M (ed) Encyclopedia of Cancer, 3rd edn. Springer Berlin Heidelberg, p 1570. doi:10.1007/978-3-642-16483-5_2453
(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_4522
(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_5205
(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_6233
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Beckner, M.E. (2014). AAMP. In: Schwab, M. (eds) Encyclopedia of Cancer. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-27841-9_6-3
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DOI: https://doi.org/10.1007/978-3-642-27841-9_6-3
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Publisher Name: Springer, Berlin, Heidelberg
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