Disease relevance of SERPINB13

• Headpin is a novel serine proteinase inhibitor (serpin) that is down-regulated in squamous cell carcinoma of the oral cavity and in squamous cell carcinoma cell lines of the head and neck [1].
• Genomic cloning, mapping, structure and promoter analysis of HEADPIN, a serpin which is down-regulated in head and neck cancer cells [1].
• Maspin, SCCA1/2 and hurpin were identified by cDNA microarray analyses as dramatically differentially expressed transcripts in primary non-small cell lung cancer (NSCLC) [2].
• Moreover, in psoriasis, a skin disease characterized by hyperproliferation of keratinocytes and responsive to therapeutic UV irradiation, overexpression of hurpin is noted in psoriatic skin lesions compared to non-lesional skin [3].
• The localization of hurpin in dermatoses and neoplasias differed from that in normal skin in that the highest expression was found in the outermost layers of the granular and upper spinous layers [4].

Psychiatry related information on SERPINB13

• Individual differences in hurpin expression between patients were observed [5].

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

• Headpin (SERPINB13) is a novel member of the serine proteinase inhibitor (Serpin) gene family that was originally cloned from a keratinocyte cDNA library [7].
• Finally, it was found that the majority of hurpin is cytosolic and that its overexpression in human keratinocytes confers resistance to UV-induced apoptosis [8].
• The activity of the promoter/enhancer was not observed in head and neck cancer cell lines TU167 and UMSCC1 which lack headpin expression [1].
• The amino acid sequence of the hinge region in the reactive site loop suggests that hurpin has the potential for protease inhibition [3].
• Hinge region homology at the reactive site loop suggests that headpin belongs to the inhibitory class of serine protease inhibitors [9].

Anatomical context of SERPINB13

• Given that lysosomal disruption, release of catL, and catL-mediated caspase activation are known to occur in response to cellular stress, we propose that a physiological role of hurpin is to protect epithelial cells from ectopic catL [8].
• Headpin is a novel serine proteinase inhibitor (serpin) with constitutive mRNA expression in histologically normal oral mucosa but with lost or down-regulated expression in head and neck squamous cell carcinoma [6].
• Differential display was used to identify a novel serpin (headpin) underexpressed in squamous cell cancers of the oral cavity [9].
• Within the dermis of normal and diseased skin, hurpin was detected in sebaceous and sweat glands, hair follicles, and endothelial cells of blood vessels [5].
• Headpin is a novel serine proteinase inhibitor (serpin) that is downregulated in many established HNSCC tumor cell lines and human oral SCC specimens [10].

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

• Hurpin is a selective inhibitor of lysosomal cathepsin L and protects keratinocytes from ultraviolet-induced apoptosis [8].
• Although it has all of the features of an inhibitory serpin, a productive interaction between hurpin and a proteinase has not yet been reported [8].
• Similarly to Cat L, the highest expression for hurpin was found in psoriasis and SCC [4].
• Hurpin (serpinB13) is a cross-class specific serine protease inhibitor of Cat L [4].
• Using Northern analysis and relative reverse-transcription polymerase chain reaction (relative RT-PCR), downregulation of headpin mRNA expression was demonstrated in oral cavity squamous carcinomas [9].

Analytical, diagnostic and therapeutic context of SERPINB13

• We have analysed the expression and localization of Cat L and hurpin in various inflammatory and neoplastic diseases by immunohistochemistry [4].
• Western blot analysis using a headpin-specific antiserum recognized a protein with the predicted M(r) of 44kDa in lysates derived from a transformed keratinocyte cell line known to express headpin mRNA [7].
• A metal affinity column followed by a gel-filtration chromatography provides a rapid and efficient method for large quantity preparation of headpin [10].

References