The Role of Testin in Human Cancers

Abstract

Testin is a protein expressed in almost all normal human tissues. It locates in the cytoplasm along stress fibers being recruited to focal adhesions. Together with zyxin and vasodilator stimulated protein it forms complexes with various cytoskeleton proteins such as actin, talin and paxilin. They jointly play significant role in cell motility and adhesion. In addition, their involvement in the cell cycle has been demonstrated. Expression of testin protein level correlates positively with percentage of cells in G1 phase, while overexpression can induce apoptosis and decreased colony forming ability. Decreased testin expression associate with loss by cells epithelial morphology and gain migratory and invasive properties of mesenchymal cells. Latest reports indicate that TES is a tumor suppressor gene which can contribute to cancerogenesis but the mechanism of loss TES gene expression is still unknown. Some authors point out hypermethylation of the CpG island as a main factor, however loss of heterozygosity may also play an important role [4, 5]. The altered expression of testin was found in malignant neoplasm, i.a. ovarian, lung, head and neck squamous cell cancer, breast, endometrial, colorectal, prostate and gastric cancers [1–9]. Testin participate in the processes of tumor growth, angiogenesis, and metastasis [10]. Many researchers stated involvement of testin in tumor progression, what suggest its potential usage in immunotherapy [7, 11]. Understanding the molecular functions of testin may be crucial in development personalized treatment. In the present manuscript up-to-date review of literature can be found.

Preliminary Study on the Expression of Testin, p16 and Ki-67 in the Cervical Intraepithelial Neoplasia

“…Testin is localized along the actin stress fibers at the cell-cell junction and focal adhesion. Testin can interact with cytoskeletal proteins such as zyxin, talin, and VASP [9,37]. Together, they play a significant role in cell motility and adhesion.…”

Exploiting Interdata Relationships in Prostate Cancer Proteomes: Clinical Significance of HO-1 Interactors

“…The eluates were digested for analysis by LC ESI-MS/MS ( Figure 1 A). We identified 41 HO-1 interactor proteins, including GSN (Gelsolin), FLNB (filamin B), 14-3-3 family proteins, TES (testin), TRIM28 (tripartite motif-containing 28), and SRSF3 (splicing factor rich in serine and arginine 3), with clinical relevance in PCa [ 32 , 33 , 34 , 35 , 36 , 37 ]. Supplementary Table S2 shows the differential proteins identified (GST-HO-1 vs. GST) together with the number of unique peptides, the name of the encoding gene, the score, and the percentage of coverage with respect to the complete sequence.…”

Mass Spectrometry Proteomic Analysis of Four p53 Patterns in Differentiated Vulvar Intraepithelial Neoplasia

“…p53 overexpression showed increased myoglobin, an oxygen-binding protein associated with increased p53 signaling 21 . The cytoplasmic pattern showed altered expression of testin, a finding also seen in multiple gynecologic and bowel cancers 22 . Also abundant was SET-binding protein 1, identified as a promising oncogenic marker in myeloid malignancies and involved in chromatin remodeling and apoptosis 23 .…”

“…21 The cytoplasmic pattern showed altered expression of testin, a finding also seen in multiple gynecologic and bowel cancers. 22 Also abundant was SET-binding protein 1, identified as a promising oncogenic marker in myeloid malignancies and involved in chromatin remodeling and apoptosis. 23 In wild-type expression, excess tyrosine-protein kinase ABL1 relates to DNA repair, activation of apoptosis, and inhibition of cell growth, whereas KH homology domain-containing protein 4 is involved in pre-mRNA splicing.…”