Characterization of two novel human small heat shock proteins: protein kinase-related HspB8 and testis-specific HspB9

Biochim Biophys Acta. 2001 Jul 30;1520(1):1-6. doi: 10.1016/s0167-4781(01)00237-8.

Abstract

Using search profiles based on the conserved alpha-crystallin domain that is characteristic for small heat shock proteins (sHsps), we traced two new human sHsps. One of these, being the eighth known human sHsp and thus named HspB8, was recently described as a serine-threonine protein kinase (H11), but not identified as an sHsp (C.C. Smith, Y.X. Yu, M. Kulka, L. Aurelian, J. Biol. Chem. 275 (2000)). Northern blotting showed that HspB8/H11 is predominantly transcribed in skeletal muscle and heart, like most other sHsps. The other, named HspB9, is specifically expressed in testis, notably in the spermatogenic cells from late pachytene spermatocyte stage till elongate spermatid stage. While mammalian sHsps are generally highly conserved, mouse HspB9 shows 38% sequence difference with human HspB9, which may confirm its sex-related role.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Animals
  • DNA, Complementary / isolation & purification
  • Heat-Shock Proteins / chemistry*
  • Humans
  • In Situ Hybridization
  • Male
  • Mice
  • Molecular Chaperones
  • Molecular Sequence Data
  • Protein Serine-Threonine Kinases / chemistry*
  • Protein Serine-Threonine Kinases / genetics
  • Protein Serine-Threonine Kinases / metabolism
  • RNA, Messenger / analysis
  • Sequence Alignment
  • Testis / metabolism

Substances

  • DNA, Complementary
  • HSPB8 protein, human
  • HSPB9 protein, human
  • Heat-Shock Proteins
  • Molecular Chaperones
  • RNA, Messenger
  • Protein Serine-Threonine Kinases