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Gene Review

NAPSB  -  napsin B aspartic peptidase, pseudogene

Homo sapiens

Synonyms: NAP1L, NAP2, NAPB, NAPSBP
 
 
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Disease relevance of NAPSB

  • Several chemokines that are produced in the ground state, including MCP-1, NAP 2 and RANTES, are upregulated significantly by KSHV infection [1].
 

High impact information on NAPSB

  • This suggests that NAP-2 interacts with the neutrophil NAP-1 receptor [2].
  • Neutrophil attractant/activation protein-1 (NAP-1) has sequence similarity to platelet factor-4 (PF-4) and to NAP-2 (a truncated from of connective tissue activating protein-III [CTAP-III(des 1-15)] [2].
  • Synthetic NAP-2 was equivalent to purified natural NAP-2 in the elastase release and calcium mobilization assays, but it was consistently less potent (3-5-fold) as a stimulus of chemotaxis, perhaps indicative of additional chemotactic components in the natural preparation [3].
  • Other differences arise from single nucleotide changes in protease genes, such as NAPSB and CASP12, resulting in the presence of functional genes in chimpanzee and pseudogenes in human [4].
  • Its predicted amino acid sequence showed 46% identity and 65% similarity with NAP1L [5].
 

Biological context of NAPSB

 

Anatomical context of NAPSB

  • Similarly, comparable levels of expression were quantified in monocytes from healthy individuals and from a patient with acute myeloid leukaemia, whereas in alveolar macrophages, which are terminally differentiated myeloid cells, transcription of the pronapsin B gene was down-regulated by approximately one order of magnitude [6].
 

Analytical, diagnostic and therapeutic context of NAPSB

  • Deprotection resulted in crude products, which were allowed to fold by air oxidation, and were purified by two cycles of reverse-phase high-pressure liquid chromatography, yielding 27 mg of NAP-1/IL-8 and 22 mg of NAP-2 [3].

References

  1. Induction of chemokine production by latent Kaposi's sarcoma-associated herpesvirus infection of endothelial cells. Xu, Y., Ganem, D. J. Gen. Virol. (2007) [Pubmed]
  2. Chemotactic activity and receptor binding of neutrophil attractant/activation protein-1 (NAP-1) and structurally related host defense cytokines: interaction of NAP-2 with the NAP-1 receptor. Leonard, E.J., Yoshimura, T., Rot, A., Noer, K., Walz, A., Baggiolini, M., Walz, D.A., Goetzl, E.J., Castor, C.W. J. Leukoc. Biol. (1991) [Pubmed]
  3. Chemical synthesis, purification, and characterization of two inflammatory proteins, neutrophil activating peptide 1 (interleukin-8) and neutrophil activating peptide. Clark-Lewis, I., Moser, B., Walz, A., Baggiolini, M., Scott, G.J., Aebersold, R. Biochemistry (1991) [Pubmed]
  4. Comparative genomic analysis of human and chimpanzee proteases. Puente, X.S., Gutiérrez-Fernández, A., Ordóñez, G.R., Hillier, L.W., López-Otín, C. Genomics (2005) [Pubmed]
  5. Cloning, expression pattern and mapping to Xq of NAP1L3, a gene encoding a peptide homologous to human and yeast nucleosome assembly proteins. Watanabe, T.K., Fujiwara, T., Nakamura, Y., Hirai, Y., Maekawa, H., Takahashi, E. Cytogenet. Cell Genet. (1996) [Pubmed]
  6. Pronapsin A and B gene expression in normal and malignant human lung and mononuclear blood cells. Cook, M., Bühling, F., Ansorge, S., Tatnell, P.J., Kay, J. Biochim. Biophys. Acta (2002) [Pubmed]
 
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