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Gene Review

SERPINB13  -  serpin peptidase inhibitor, clade B...

Homo sapiens

Synonyms: HSHUR7SEQ, HUR7, HaCaT UV-repressible serpin, Headpin, Hurpin, ...
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Disease relevance of SERPINB13


Psychiatry related information on SERPINB13


High impact information on SERPINB13

  • In light of our findings of nuclear subcellular localization of headpin, we investigated the expression and secretion of angiogenic factors and found reduced mRNA, protein, and promoter activities of IL-8 and VEGF [6].
  • Using immunohistochemical analysis of invasive squamous cell carcinoma and matched normal squamous mucosa of patient specimens, headpin expression was lost or down-regulated in the vast majority of tumor specimens [6].
  • In assays of cellular events in angiogenesis, headpin blocked the invasion, migration, and tube formation of endothelial cells [6].
  • Furthermore, expression of hurpin appears to be related to the activation or proliferation state of keratinocytes, since hurpin transcripts are more abundant in immortalized keratinocytes (HaCaT) and in cultured normal human keratinocytes, compared to the expression in normal skin [3].
  • Among those UV-repressible genes, a novel serine proteinase inhibitor (serpin) termed hurpin (HaCaT UV-repressible serpin) has been identified [3].

Biological context of SERPINB13


Anatomical context of SERPINB13


Associations of SERPINB13 with chemical compounds

  • These results demonstrate that the serpin headpin possesses specificity for inhibiting lysosomal cysteine proteinases [7].

Other interactions of SERPINB13


Analytical, diagnostic and therapeutic context of SERPINB13


  1. Genomic cloning, mapping, structure and promoter analysis of HEADPIN, a serpin which is down-regulated in head and neck cancer cells. Nakashima, T., Pak, S.C., Silverman, G.A., Spring, P.M., Frederick, M.J., Clayman, G.L. Biochim. Biophys. Acta (2000) [Pubmed]
  2. Maspin - the most commonly-expressed gene of the 18q21.3 serpin cluster in lung cancer - is strongly expressed in preneoplastic bronchial lesions. Smith, S.L., Watson, S.G., Ratschiller, D., Gugger, M., Betticher, D.C., Heighway, J. Oncogene (2003) [Pubmed]
  3. Cloning and characterization of hurpin (protease inhibitor 13): A new skin-specific, UV-repressible serine proteinase inhibitor of the ovalbumin serpin family. Abts, H.F., Welss, T., Mirmohammadsadegh, A., Köhrer, K., Michel, G., Ruzicka, T. J. Mol. Biol. (1999) [Pubmed]
  4. Expression of cathepsin L and its inhibitor hurpin in inflammatory and neoplastic skin diseases. Bylaite, M., Moussali, H., Marciukaitiene, I., Ruzicka, T., Walz, M. Exp. Dermatol. (2006) [Pubmed]
  5. Expression of hurpin, a serine proteinase inhibitor, in normal and pathological skin: overexpression and redistribution in psoriasis and cutaneous carcinomas. Moussali, H., Bylaite, M., Welss, T., Abts, H.F., Ruzicka, T., Walz, M. Exp. Dermatol. (2005) [Pubmed]
  6. Headpin: a serpin with endogenous and exogenous suppression of angiogenesis. Shellenberger, T.D., Mazumdar, A., Henderson, Y., Briggs, K., Wang, M., Chattopadhyay, C., Jayakumar, A., Frederick, M., Clayman, G.L. Cancer Res. (2005) [Pubmed]
  7. Inhibition of the cysteine proteinases cathepsins K and L by the serpin headpin (SERPINB13): a kinetic analysis. Jayakumar, A., Kang, Y., Frederick, M.J., Pak, S.C., Henderson, Y., Holton, P.R., Mitsudo, K., Silverman, G.A., EL-Naggar, A.K., Brömme, D., Clayman, G.L. Arch. Biochem. Biophys. (2003) [Pubmed]
  8. Hurpin is a selective inhibitor of lysosomal cathepsin L and protects keratinocytes from ultraviolet-induced apoptosis. Welss, T., Sun, J., Irving, J.A., Blum, R., Smith, A.I., Whisstock, J.C., Pike, R.N., von Mikecz, A., Ruzicka, T., Bird, P.I., Abts, H.F. Biochemistry (2003) [Pubmed]
  9. Identification and cDNA cloning of headpin, a novel differentially expressed serpin that maps to chromosome 18q. Spring, P., Nakashima, T., Frederick, M., Henderson, Y., Clayman, G. Biochem. Biophys. Res. Commun. (1999) [Pubmed]
  10. Production of serpins using baculovirus expression systems. Jayakumar, A., Cataltepe, S., Kang, Y., Frederick, M.J., Mitsudo, K., Henderson, Y., Crawford, S.E., Silverman, G.A., Clayman, G.L. Methods (2004) [Pubmed]
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