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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Gene Review: 

ASB2  -  ankyrin repeat and SOCS box containing 2

Homo sapiens

Synonyms: ASB-2, Ankyrin repeat and SOCS box protein 2
 
 
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Disease relevance of ASB2

  • Expression of ASB2 in myeloid leukemia cells inhibits growth and promotes commitment, recapitulating an early step known to be critical for differentiation [1].
 

High impact information on ASB2

  • Reverse transcription of brain mRNA followed by PCR with degenerate oligonucleotides for ASB2 and ASAL yielded a 338-bp fragment of the allatostatin gene that encoded six allatostatins [2].
  • The ASB2-(11-18)-octapeptide amide gives a full response at high concentrations at day 10 (IC50 = 48 nM), but the C-truncated (1-9)-, (1-11)-, and (1-17)-amide fragments of ASB2 are inactive [3].
  • The primary structure of this allatostatin has been elucidated by tandem mass spectrometry: Ala-Tyr-Ser-Tyr-Val-Ser-Glu-Tyr-Lys-Arg-Leu-Pro-Val-Tyr-Asn-Phe-Gly-Leu- NH2 (ASB2) [3].
  • PML-RARalpha strongly enhanced RA-induced ASB-2 mRNA expression [4].
  • Here we have identified the human ankyrin repeat-containing protein with a suppressor of cytokine signaling box-2 (ASB-2) cDNA, as a novel RA-induced gene in APL cells [4].
 

Chemical compound and disease context of ASB2

  • In myeloid leukemia cells, ASB-2 expression induced growth inhibition and chromatin condensation recapitulating early events critical to RA-induced differentiation of APL cells [4].
 

Biological context of ASB2

  • These findings indicate that ASB-2 is directly induced by ATRA and may act as a significant regulator, underlying such physiological processes as cell differentiation [5].
 

Anatomical context of ASB2

  • In this study, we screened the specific genes expressed in the course of differentiation of HL-60 cells, and demonstrated that ASB-2, one of the ASB proteins, was rapidly induced by all-trans retinoic acid (ATRA) [5].
 

Analytical, diagnostic and therapeutic context of ASB2

  • Midgut extracts were shown to be biologically active in an allatostatin bioassay and to contain several allatostatin-like peptides, including the octadecapeptide ASB2, which was identified by mass spectrometry following HPLC purification [2].
  • Enzyme-linked immunoassay and immunocytochemistry with antisera to two allatostatins, ASB2 (AYSYVSEYKRLPVYNFGL-NH2) and ASAL (APSGAQRLYGFGL-NH2), revealed that allatostatins were located not only in the insect brain but also in several peripheral tissues including the cockroach midgut and hindgut [2].

References

  1. ASB2 is an Elongin BC-interacting protein that can assemble with Cullin 5 and Rbx1 to reconstitute an E3 ubiquitin ligase complex. Heuzé, M.L., Guibal, F.C., Banks, C.A., Conaway, J.W., Conaway, R.C., Cayre, Y.E., Benecke, A., Lutz, P.G. J. Biol. Chem. (2005) [Pubmed]
  2. Expression of the allatostatin gene in endocrine cells of the cockroach midgut. Reichwald, K., Unnithan, G.C., Davis, N.T., Agricola, H., Feyereisen, R. Proc. Natl. Acad. Sci. U.S.A. (1994) [Pubmed]
  3. Identity of a second type of allatostatin from cockroach brains: an octadecapeptide amide with a tyrosine-rich address sequence. Pratt, G.E., Farnsworth, D.E., Fok, K.F., Siegel, N.R., McCormack, A.L., Shabanowitz, J., Hunt, D.F., Feyereisen, R. Proc. Natl. Acad. Sci. U.S.A. (1991) [Pubmed]
  4. ASB-2 inhibits growth and promotes commitment in myeloid leukemia cells. Guibal, F.C., Moog-Lutz, C., Smolewski, P., Di Gioia, Y., Darzynkiewicz, Z., Lutz, P.G., Cayre, Y.E. J. Biol. Chem. (2002) [Pubmed]
  5. ATRA-regulated Asb-2 gene induced in differentiation of HL-60 leukemia cells. Kohroki, J., Fujita, S., Itoh, N., Yamada, Y., Imai, H., Yumoto, N., Nakanishi, T., Tanaka, K. FEBS Lett. (2001) [Pubmed]
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