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Gene Review

NAP1L4  -  nucleosome assembly protein 1-like 4

Homo sapiens

Synonyms: NAP-2, NAP1L4b, NAP2, NAP2L, Nucleosome assembly protein 1-like 4, ...
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Disease relevance of NAP1L4


High impact information on NAP1L4

  • One of the truncated products of LDGF, NAP-2, is a potent neutrophil chemoattractant [6].
  • Sequence analysis of the LDGF peptide revealed that it is a precursor of other known peptides including platelet basic protein (PBP), connective tissue activating peptide III (CTAP-III), and neutrophil activating peptide 2 (NAP-2) [6].
  • Platelet-derived CTAP-III and a cleavage isoform with the electrophoretic mobility of CTAP-III-des 1-15/neutrophil-activating peptide-2 (NAP-2) and PGE2 were found in biologically active extracts of synovial samples from patients with RA and OA [7].
  • Here, we demonstrate that casein kinase 2 (CKII) from HeLa cell nuclear extracts interacts with immobilized NAP-II, and phosphorylates both NAP-2 and nucleosome assembly protein 1 (NAP-1) in vitro [8].
  • NAP-2: histone chaperone function and phosphorylation state through the cell cycle [8].

Biological context of NAP1L4

  • Phosphorylated NAP-2 remains in the cytoplasm in a complex with histones during the G0/G1 transition, whereas its dephosphorylation triggers its transport into the nucleus, at the G1/S-boundary, with the histone cargo, suggesting that binding to histones does not depend on phosphorylation status [8].
  • Finally, indirect immunofluorescence shows that NAP-2 is present during metaphase of HeLa and COS cells, and its localization is distinct from metaphase chromosomes [8].
  • The deduced amino acid sequence of NAP-2 indicates that it encodes a protein with a potential nuclear localization motif and two clusters of highly acidic residues [2].
  • Deletion mutagenesis of NAP-2 demonstrates that both NH3- and COOH-terminal domains are required for histone transfer activity [2].
  • During early inflammation, the chemoattractants neutrophil-activating peptide-2 (NAP-2), platelet-activating factor (PAF), and complement component C5a are rapidly generated within the vasculature and potently induce effector functions in neutrophils, such as chemotaxis and degranulation [9].

Anatomical context of NAP1L4

  • NAP-2 (0.1-1.5 microns) caused the release of human granulocyte elastase from cytochalasin B-treated neutrophils in a dose-dependent manner [10].
  • RESULTS: Crude (24.2 micrograms/mL-2.42 mg/mL), void (5.4 micrograms/mL-0.54 mg/mL), peak 2 (3.5 micrograms/mL-0.35 mg/mL), and NAP-2 (1-20 micrograms/mL) failed to release histamine from lung mast cells [11].
  • Radial nerve was first stimulated with a single shock and then with double shocks at intervals of 2, 3, 4, 5, 6, 7, and 8 ms; NAP amplitudes and NAP1/NAP2 ratios were calculated in normals and diabetics [12].
  • Chemotactically active NAP-2 was also demonstrated in PEFs but not in plasmas from patients with CHF and ARDS [5].

Associations of NAP1L4 with chemical compounds

  • Second, a negatively charged resin (heparin) was used, which retained small amounts of NAP-2 (a very acidic polypeptide) and topoisomerase I. This fraction, although able to supercoil relaxed DNA, did so to a lesser extent than the Q-Sepharose fraction [13].
  • Here, using HeLa cell nuclear extracts, we found NAP-2 migrates in a blue-native polyacrylamide gel with an apparent molecular weight of 300 kDa [13].
  • HeLa cell NAP-2, labeled in vivo with radioactive orthophosphate, co-precipitated with at least two phosphoproteins, with an apparent mass of 100 and 175 kDa, respectively, as determined by SDS-PAGE [13].

Other interactions of NAP1L4


Analytical, diagnostic and therapeutic context of NAP1L4

  • NAP-2, the shortest form of CXCL7 detected in the coculture media, was confirmed to decrease the size and number of CFU-Meg colonies [15].
  • Sensitive immunological identification of NAP-2 based on nonequilibrium isoelectric focusing and immunoblotting is described [10].
  • Neutrophil-activating peptide 2 (NAP-2), corresponding to platelet basic protein fragment 25-94, was prepared by chymotryptic digestion of its precursors, low affinity platelet factor 4 or beta-thromboglobulin, followed by purification by high performance liquid chromatography [10].


  1. Mutation analysis of H19 and NAP1L4 (hNAP2) candidate genes and IGF2 DMR2 in Beckwith-Wiedemann syndrome. Catchpoole, D., Smallwood, A.V., Joyce, J.A., Murrell, A., Lam, W., Tang, T., Munroe, D., Reik, W., Schofield, P.N., Maher, E.R. J. Med. Genet. (2000) [Pubmed]
  2. Functional characterization of human nucleosome assembly protein-2 (NAP1L4) suggests a role as a histone chaperone. Rodriguez, P., Munroe, D., Prawitt, D., Chu, L.L., Bric, E., Kim, J., Reid, L.H., Davies, C., Nakagama, H., Loebbert, R., Winterpacht, A., Petruzzi, M.J., Higgins, M.J., Nowak, N., Evans, G., Shows, T., Weissman, B.E., Zabel, B., Housman, D.E., Pelletier, J. Genomics (1997) [Pubmed]
  3. Connective tissue activation. XXXVI. The origin, variety, distribution, and biologic fate of connective tissue activating peptide-III isoforms: characteristics in patients with rheumatic, renal, and arterial disease. Castor, C.W., Andrews, P.C., Swartz, R.D., Ellis, S.G., Hossler, P.A., Clark, M.R., Matteson, E.L., Sachter, E.F. Arthritis Rheum. (1993) [Pubmed]
  4. Induction of chemokine production by latent Kaposi's sarcoma-associated herpesvirus infection of endothelial cells. Xu, Y., Ganem, D. J. Gen. Virol. (2007) [Pubmed]
  5. Neutrophil-activating peptide-2 in patients with pulmonary edema from congestive heart failure or ARDS. Cohen, A.B., Stevens, M.D., Miller, E.J., Atkinson, M.A., Mullenbach, G., Maunder, R.J., Martin, T.R., Wiener-Kronish, J.P., Matthay, M.A. Am. J. Physiol. (1993) [Pubmed]
  6. Leukocyte-derived growth factor links the PDGF and CXC chemokine families of peptides. Iida, N., Haisa, M., Igarashi, A., Pencev, D., Grotendorst, G.R. FASEB J. (1996) [Pubmed]
  7. Connective tissue activation. XXXV. Detection of connective tissue activating peptide-III isoforms in synovium from osteoarthritis and rheumatoid arthritis patients: patterns of interaction with other synovial cytokines in cell culture. Castor, C.W., Smith, E.M., Hossler, P.A., Bignall, M.C., Aaron, B.P. Arthritis Rheum. (1992) [Pubmed]
  8. NAP-2: histone chaperone function and phosphorylation state through the cell cycle. Rodriguez, P., Pelletier, J., Price, G.B., Zannis-Hadjopoulos, M. J. Mol. Biol. (2000) [Pubmed]
  9. The CXC chemokine NAP-2 mediates differential heterologous desensitization of neutrophil effector functions elicited by platelet-activating factor. Schwartzkopff, F., Brandt, E., Petersen, F., Flad, H.D., Bock, L., Ludwig, A. J. Interferon Cytokine Res. (2002) [Pubmed]
  10. Isolation, characterization, and immunological detection of neutrophil-activating peptide 2: a proteolytic degradation product of platelet basic protein. Holt, J.C., Yan, Z.Q., Lu, W.Q., Stewart, G.J., Niewiarowski, S. Proc. Soc. Exp. Biol. Med. (1992) [Pubmed]
  11. Effects of PBMC-derived histamine-releasing factors on histamine release from human skin and lung mast cells. Okayama, Y., Brzezińska-Błaszczyk, E., Kuna, P., Kaplan, A.P., Church, M.K. Clin. Exp. Allergy (1995) [Pubmed]
  12. Early diagnosis of diabetic neuropathy using double-shock stimulation of peripheral nerves. Tan, M., Tan, U. Clinical neurophysiology : official journal of the International Federation of Clinical Neurophysiology. (2003) [Pubmed]
  13. NAP-2 is part of multi-protein complexes in HeLa cells. Rodriguez, P., Ruiz, M.T., Price, G.B., Zannis-Hadjopoulos, M. J. Cell. Biochem. (2004) [Pubmed]
  14. Novel transcribed sequences within the BWS/WT2 region in 11p15.5: tissue-specific expression correlates with cancer type. Crider-Miller, S.J., Reid, L.H., Higgins, M.J., Nowak, N.J., Shows, T.B., Futreal, P.A., Weissman, B.E. Genomics (1997) [Pubmed]
  15. Monocyte-derived CXCL7 peptides in the marrow microenvironment. Pillai, M.M., Iwata, M., Awaya, N., Graf, L., Torok-Storb, B. Blood (2006) [Pubmed]
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