Anti-Annexin IV polyclonal antibody

The aim of the present study was to elucidate differentially expressed proteins in lesional tissues of psoriasis vulgaris (PV) and normal tissues. Lesional skin tissues were collected from PV patients, along with normal skin tissues from healthy individuals. The protein content of the samples was extracted and then separated by two-dimensional gel electrophoresis (2-DGE). Any proteins that were differentially expressed in the lesional skin of PV patients compared with the healthy controls were analyzed by mass spectrometry and bioinformatics. In the stratum corneum and dermis of PV patients, the total number of proteins identified by 2-DGE was 1,969 +/- 21 and 1,928 +/- 49, respectively. Of these, 30 proteins were differentially expressed in the PV patients, of which 14 were identified as: Type 1 keratin cytoskeleton proteins (including K1C10, K1C14, K1C15 and K1C16); the type 2 keratin cytoskeleton protein, K2C1; actin-associated proteins (including ARP3, ACTA and ACTBM); prohibitin; heat shock proteins (HSPB1 and CH60); centrosome protein, CP135; and membrane associated proteins (including ANXA4 and ANXA5). The differential expression of protein between PV lesions and normal tissue can be considered as pathological biomarker. Elucidating the abnormal regulation of these proteins can provide mechanism of the development of PV and may contribute to significant approaches for PV treatments.

We recently reported that Fhit is in a molecular complex with annexin A4 (ANXA4); following to their binding, Fhit delocalizes ANXA4 from plasma membrane to cytosol in paclitaxel-resistant lung cancer cells, thus restoring their chemosensitivity to the drug. Here, we demonstrate that Fhit physically interacts with A4 through its N-terminus; molecular dynamics simulations were performed on a 3D Fhit model to rationalize its mechanism of action. This approach allowed for the identification of the QHLIKPS eptapeptide (position 7 to 13 of the wild-type Fhit protein) as the smallest Fhit sequence still able to preserve its ability to bind ANXA4. Interestingly, Fhit peptide also recapitulates the property of the native protein in inhinibiting Annexin A4 translocation from cytosol to plasma membrane in A549 and Calu-2 lung cancer cells treated with paclitaxel. Finally, the combination of Tat-Fhit peptide and paclitaxel synergistically increases the apoptotic rate of cultured lung cancer cells and blocks in vivo tumor formation. Our findings address to the identification of chemically simplified Fhit derivatives that mimic Fhit tumor suppressor functions; intriguingly, this approach might lead to the generation of novel anticancer drugs to be used in combination with conventional therapies in Fhit-negative tumors to prevent or delay chemoresistance.