Disease relevance of KRT81

• We concluded that, in breast carcinomas, expression of truncated hHb1 is related to epithelial cell transformation [1].

High impact information on KRT81

• Furthermore, ligand blotting studies showed that only 125I-labeled CF4.DMPC associated specifically with HB1 and HB2, two HDL binding proteins recently identified in rat liver plasma membranes [2].
• A comparison of clinical features and severity between cases with hHb1 and hHb6 mutations does not suggest distinct effects on phenotype, with the possible exception of nail dystrophy, commoner with hHb1 defects [3].
• We have cloned two complete type II hair-specific keratin genes (ghHb1 and ghHb6) [4].
• Comparison with the template structure (submitted to the same minimization procedure) indicates that, in T. newnesi Hb1 T-state model, the substitution of Ile for Thr in 41 C6, in central position of the switch region, induces at the alpha(1)beta(2) interface structural modifications able to hamper the protonation [5].
• Expression of a truncated form of hHb1 hair keratin in human breast carcinomas [1].

Biological context of KRT81

• Because the hHb1 gene maps to 12q11-q13, a chromosome region known to present several breakpoints in solid tumours, we propose that the hHb1 gene might represent a target for such alterations [1].
• In five patients no mutations were found, while in two patients we identified de novo germline missense mutations at the helix termination motif: E402K (hHb6) and E413K (hHb1) [6].
• Hemoglobin from the Antarctic fish Notothenia coriiceps neglecta. 2. Amino acid sequence of the alpha chain of Hb1 [7].
• As part of an effort to determine levels of fumonisins in human food, a liquid chromatographic (LC) method was devised for determining fumonisin B1 (FB1) and the total hydrolysis product of FB1 (HB1) in tortillas [8].

Anatomical context of KRT81

• HB1 antigen was found on almost all monolayer cell lines and not on most cultured suspension cells [9].

Analytical, diagnostic and therapeutic context of KRT81

• Immunoprecipitation experiments revealed that the HB1 antigen is a bimolecular complex with an Mr 170,000 alpha chain and Mr 130,000 beta chain under non-reducing conditions, and three subunits of Mr 140,000, Mr 30,000 and Mr 130,000 under reducing conditions [9].

References