Psychiatry related information on NCKAP1

• We previously reported the isolation of a novel apoptosis-related gene, human Nap1 (HGMW-approved symbol NCKAP1), the expression of which was strongly down-regulated in sporadic Alzheimer's disease (AD) [1].

High impact information on NCKAP1

• 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].
• The centrosomal protein C-Nap1 is required for cell cycle-regulated centrosome cohesion [3].
• The present data suggest that T cell receptor engagement provokes a rapid, tyrosine kinase- and actin-dependent transport of Nck-associated FasL-carrying lysosomes to the contact area [4].
• The findings supporting a global conservation of molecular mechanisms for membrane protrusion have been further strengthened by the identification of plant homologs of upstream regulators of the complex such as PIR121, NAP125 and HSPC300 [5].

Biological context of NCKAP1

• The gene was thus designated human Nap1 (HGMW-approved symbol NCKAP1) and was mapped to human chromosome 2q32 by fluorescence in situ hybridization [6].
• Antisense oligo DNA of human Nap1 transcripts was found to induce apoptosis of neuronal cells [6].
• Human Nck-associated protein 1 and its binding protein affect the metabolism of beta-amyloid precursor protein with Swedish mutation [7].
• The deduced amino acid sequence of SNAP-1 shares sequence similarity with yeast NAP-1 (38%) and human hNRP (32%) [8].
• Histone exchange as well as nucleosome sliding is independent of ATP and relies on the presence of the C-terminal acidic domain of yeast NAP-1, even though this region is not required for histone binding and chromatin assembly [9].

Anatomical context of NCKAP1

• Neutrophil attractant protein-1-immunoglobulin G immune complexes and free anti-NAP-1 antibody in normal human serum [2].
• The purpose of this study was to determine if NAP-1 interacted with other types of blood leukocytes [10].
• Neutrophil attractant/activation protein-1 (NAP-1) was previously shown to attract human neutrophils, but not monocytes [10].
• Here it was examined how NAP1 interacts with chromatin fibers isolated from HeLa cells [11].
• Intradermal NAP-1 did not cause basophil or lymphocyte infiltration [12].

Associations of NCKAP1 with chemical compounds

• Neutrophil attractant/activation protein-1 (NAP-1) causes human basophil histamine release [13].

Physical interactions of NCKAP1

• Isolation of hNap1BP which interacts with human Nap1 (NCKAP1) whose expression is down-regulated in Alzheimer's disease [1].

Enzymatic interactions of NCKAP1

• In addition, Nck-associated proteins are highly tyrosine phosphorylated and JNK reaches a higher level of activation when FGF-2 triggers DNA synthesis [14].

Analytical, diagnostic and therapeutic context of NCKAP1

• The mobilities of the 125 kDa protein and Nap1 on SDS/PAGE were indistinguishable, and the 125 kDa protein was depleted from brain extract by preincubation with the Src homology 3 domain of Nck to which Nap1 binds [15].
• Molecular cloning and functional characterization of a cDNA encoding nucleosome assembly protein 1 (NAP-1) from soybean [8].
• 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 [11].
• NAP1 induced a reversible change toward an extended fiber conformation as demonstrated by sedimentation velocity ultracentrifugation experiments [11].

References