Disease relevance of AZI2

• Synthetic peptide AZ2, amino acids 75-99 from V1 CD4, KIEDSDTYIC(Acm)-EVEDQKEEVQLLVFG, and dextran sulfate 500,000 (DS 500) were used as inhibitory agents of antibody binding in ELISA using: (1) anti-peptide rabbit antibodies; (2) sera from HIV infected persons [1].

High impact information on AZI2

• NAP-1-IgG did not compete with 125I-NAP-1 for binding to neutrophils, which suggests that IgG anti-NAP-1 is a molecular trap that prevents binding of NAP-1 to neutrophils after it diffuses from production sites into the circulation [2].
• However, at pH 2.0 in 9 M urea approximately 15% of the total NAP-1 could be dissociated from the complex [2].
• NAP1 activates NAK and facilitates its oligomerization [3].
• Depletion of NAP1 reduced NF-kappaB-dependent reporter gene expression and sensitized cells to TNF-alpha-induced apoptosis [3].
• The findings suggest a possible role of NAP1 in chromatin remodeling processes involved in transcription and replication by modulating the local linker histone content [4].

Biological context of AZI2

• We have isolated a novel cDNA clone, named AZ2, from a cDNA library of mRNA prepared from C3H10T1/2 cells that had been transiently exposed to 5-azacytidine, a potent inhibitor of DNA methyltransferase [5].
• The AZ2 cDNA contained a 1215-nucleotide open reading frame, and the expected amino acid sequence had a molecular mass of 46090 [5].

Anatomical context of AZI2

• Specific antibodies raised against a fusion protein including glutathione S-transferase revealed a band of an approximately 48kDa translation product for testis, brain, lung, and cultured cells that ectopically expressed the AZ2 protein [5].
• Neutrophil attractant protein-1-immunoglobulin G immune complexes and free anti-NAP-1 antibody in normal human serum [2].
• In addition to its chemotactic activity for neutrophils, NAP-1 induced chemotactic responses by T lymphocytes and basophils [6].
• The purpose of this study was to determine if NAP-1 interacted with other types of blood leukocytes [6].
• Neutrophil attractant/activation protein-1 (NAP-1) was previously shown to attract human neutrophils, but not monocytes [6].

Associations of AZI2 with chemical compounds

• Neutrophil attractant/activation protein-1 (NAP-1) causes human basophil histamine release [7].
• Chemical modification of lysine epsilon-amino groups of these peptides resulted in complete failure to bind either DS or AZ2 [1].

Analytical, diagnostic and therapeutic context of AZI2

• The ELISA for free NAP-1 used a monoclonal capture antibody that did not bind NAP-1-IgG [2].
• The effect of NAP1 on the chromatin fiber structure was examined by scanning/atomic force microscopy [4].
• NAP1 induced a reversible change toward an extended fiber conformation as demonstrated by sedimentation velocity ultracentrifugation experiments [4].
• The symmetrical histogram obtained by flow cytometry of neutrophils equilibrated at 0 degree C with fluoresceinated NAP-1 indicates that all neutrophils bound the ligand [6].
• Intradermal injection into normal human subjects of 40 microliters of NAP-1, over a concentration range of 4 x 10(-8) M to 10(-6) M, caused no symptoms or signs such as wheal-and-flare, itching, induration, or tenderness [8].

References