Disease relevance of AAMP

• The cDNA for AAMP (angio-associated, migratory cell protein) was first isolated from a human melanoma cell line during a search for motility-associated cell surface proteins [1].
• Upon analysis of the tissue distribution of AAMP, it was found to be expressed strongly in endothelial cells, cytotrophoblasts, and poorly differentiated colon adenocarcinoma cells found in lymphatics [1].
• Further study of angio-associated migratory cell protein by quantitative reverse transcriptase-PCR and in situ hybridization analysis of 37 cases of DCIS confirmed higher mRNA expression in DCIS(necrosis+) (P = 0.0095) [2].
• Among this set, the mRNA for angio-associated migratory cell protein and a serine threonine protein kinase, nuclear Dbf2 related, were consistently higher in DCIS(necrosis+) and were also found to be overexpressed in the T47D breast cancer cell line subjected to hypoxia [2].

High impact information on AAMP

• The shared expression of AAMP in endothelial cells, trophoblasts, and tumor cells implies a common function in migrating cells [1].
• A 1.6-kilobase mRNA transcript of AAMP is detected in tissue culture cell lines and tissues [1].
• The AAMP-derived peptide, P189, contains a heparin-binding domain (dissociation constant, 14 pmol) and mediates heparin-sensitive cell adhesion [1].
• Limited digestion of the reactive proteins with thermolysin destroys anti-P189's reactivity for alpha-actinin while reactivity for recombinant AAMP is retained [3].
• AAMP, a newly identified protein, shares a common epitope with alpha-actinin and a fast skeletal muscle fiber protein [3].

Biological context of AAMP

• Both the human and yeast proteins show an unusual and almost identical arrangement of immunoglobulin type domains, WD40 repeats, a protein kinase C phosphorylation consensus site in the carboxyl region, and a positively charged amino-terminal region that in AAMP has heparin binding potential [4].

Anatomical context of AAMP

• Polyclonal antibodies generated to P189 readily react with AAMP (52 kDa) in brain and activated T lymphocyte lysates, alpha-actinin (100 kDa) in all tissues tested, and a 23-kDa protein in skeletal muscle lysates [3].
• Therefore, regulation of extracellular AAMP by astrocytes is hypothesized to aid in angiogenesis of the nervous system [5].

Analytical, diagnostic and therapeutic context of AAMP

• The results of one such experimental measurement and analysis are here reported for a new design of 103palladium source, model MED3633 (North American Scientific, Inc.). By AAMP Task Group #43 recommendations, the reference material for brachytherapy dosimetry is liquid water [6].
• Transwell cocultures of human astrocytes and BAECs increase (53%) the amount of extracellular AAMP found associated with endothelial cells [5].

References