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Anp32a  -  acidic (leucine-rich) nuclear...

Mus musculus

Synonyms: Acidic leucine-rich nuclear phosphoprotein 32 family member A, Acidic nuclear phosphoprotein pp32, Anp32, I1PP2A, LANP, ...
 
 
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Disease relevance of Anp32a

  • Alternative use of genes of the closely-related pp32 family is a common occurrence in human prostate cancer. pp32r1 and pp32r2, the oncogenic members of the pp32 family, are expressed in prostatic adenocarcinoma, while adjacent benign prostate continues to express pp32 [1].
 

Psychiatry related information on Anp32a

  • The suitability of this novel screening system was established by the selection of mAbs recognising Alzheimer's disease (AD)-neurofibrillary pathology in histological preparations and phosphoprotein pp32 in rat brain sections [2].
 

High impact information on Anp32a

  • In vivo colocalization and transfection studies show that pp32 INHAT domains are responsible for histone binding, HAT inhibitory activity, and repression of transcription [3].
  • Regulation of histone acetylation and transcription by nuclear protein pp32, a subunit of the INHAT complex [3].
  • The C-terminal third is exceptionally acidic, comprised of approximately 70% aspartic and glutamic acid residues; the predicted pI of human pp32 is 3.81 [4].
  • Upon B cell stimulation the associated proteins are phosphorylated, giving rise to pp32/33 (alpha), pp37 (beta), and pp34 (previously designated gamma) [5].
  • Both pp35 and pp32 appear to be associated with cell proliferation [6].
 

Biological context of Anp32a

  • We demonstrate that antisense inhibition of pp32 in NIH3T3 cells leads to a variety of phenotypic changes associated with transformation including reduced serum dependence and loss of contact inhibition [1].
  • Inhibition of T cell activation correlates with the ability of IgM and of cross-linked IgG anti-CD4 antibodies to induce tyrosine phosphorylation of the CD4-associated tyrosine kinase p56lck and an unknown substrate, pp32 [7].
 

Anatomical context of Anp32a

  • Quantitative immunoblotting showed that both pp35 and pp32 are, respectively, expressed at 5.9 x 10(4) and 7.0 x 10(4) copies/cell in small, dense resting B lymphocytes, increasing approximately 12- and 7-fold after polyclonal stimulation with lipopolysaccharide [6].
  • Two nuclear phosphoproteins, pp35 and pp32, were purified from A20 cells, a murine B-lymphoblastoid cell line [6].
  • Antibodies specific for pp35 and pp32 show prominent intranuclear staining in A20 cells but only focal staining in normal murine lymphoid tissues [6].
  • Overexpression of GFP-I1PP2A/lanp in PC12 cells leads to markedly reduced neurite length on laminin 5 after induction with nerve growth factor [8].
 

Associations of Anp32a with chemical compounds

  • The phosphatase binds to the cytoplasmic membrane-proximal conserved GFFKR motif of the alpha integrin subunit, whereas I1PP2A/lanp requires a longer sequence for binding [8].
  • The proteins pp32 and pp30 have apparent isoelectric points of 6.6 and 6.5 and molecular weights of approximately 32 30 kDa respectively, as determined by two-dimensional polyacrylamide gel electrophoresis [9].
 

Analytical, diagnostic and therapeutic context of Anp32a

  • By two-dimensional peptide mapping, pp35 and pp32 are related but do not appear to represent sequential proteolytic products [6].

References

  1. Tumor suppression and potentiation by manipulation of pp32 expression. Bai, J., Brody, J.R., Kadkol, S.S., Pasternack, G.R. Oncogene (2001) [Pubmed]
  2. A rapid immunohistochemical primary screening assay for hybridomas. Zilka, N., Vechterová, L., Kontseková, E., Novák, M. J. Immunol. Methods (2003) [Pubmed]
  3. Regulation of histone acetylation and transcription by nuclear protein pp32, a subunit of the INHAT complex. Seo, S.B., Macfarlan, T., McNamara, P., Hong, R., Mukai, Y., Heo, S., Chakravarti, D. J. Biol. Chem. (2002) [Pubmed]
  4. Structure of pp32, an acidic nuclear protein which inhibits oncogene-induced formation of transformed foci. Chen, T.H., Brody, J.R., Romantsev, F.E., Yu, J.G., Kayler, A.E., Voneiff, E., Kuhajda, F.P., Pasternack, G.R. Mol. Biol. Cell (1996) [Pubmed]
  5. The gamma subunit of the B cell antigen-receptor complex is a C-terminally truncated product of the B29 gene. Friedrich, R.J., Campbell, K.S., Cambier, J.C. J. Immunol. (1993) [Pubmed]
  6. Identification and preliminary characterization of two related proliferation-associated nuclear phosphoproteins. Malek, S.N., Katumuluwa, A.I., Pasternack, G.R. J. Biol. Chem. (1990) [Pubmed]
  7. Extensive CD4 cross-linking inhibits T cell activation by anti-receptor antibody but not by antigen. Dianzani, U., Shaw, A., Fernandez-Cabezudo, M., Janeway, C.A. Int. Immunol. (1992) [Pubmed]
  8. Integrin alpha3beta1 interacts with I1PP2A/lanp and phosphatase PP1. Mutz, D., Weise, C., Mechai, N., Hofmann, W., Horstkorte, R., Br??ning, G., Danker, K. J. Neurosci. Res. (2006) [Pubmed]
  9. Acute action of luteinizing hormone on mouse Leydig cells: accumulation of mitochondrial phosphoproteins and stimulation of testosterone synthesis. Epstein, L.F., Orme-Johnson, N.R. Mol. Cell. Endocrinol. (1991) [Pubmed]
 
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