Keywords
metastasis
benign neoplasms
alpha-smooth muscle actin
How to Cite
Abstract
Alpha-smooth muscle actin (α-SMA) is an isoform of the actin protein essential for cell motility, maintenance of
cytoskeletal structure, and muscle contraction. Numerous studies indicate that α-SMA is involved in carcinogenesis, epithelialmesenchymal
transition (EMT), metastasis (Mts) formation, and tumor drug resistance. Its expression serves as a marker of
cancer-associated fibroblasts (CAFs), which promote tumor growth, invasion, and Mts through interactions with cancer cells.
The aim of this study was to compare α-SMA levels in tissue samples of follicular adenoma (FA), goiter, papillary thyroid carcinoma
(PTC), metastases (Mts), conditionally normal thyroid tissue, as well as in blood plasma and peripheral blood mononuclear cells
(PBMC). Material and methods. Postoperative samples of tissue, blood plasma, and cells were obtained from the surgical
department of the clinic. The amount of α-SMA was determined using enzyme immunoassay kits. Results. α-SMA levels in
FA and goiter tissues did not differ from those in conditionally normal tissue. A significant difference was observed between
normal and PTC tissues with and without metastases. α-SMA levels in PTC tissue without Mts were nearly four times lower
than in PTC tissue with Mts. α-SMA expression in metastatic tissue was higher than in normal tissue. Additionally, significant
differences in α-SMA levels were detected between normal tissue samples from patients with and without Mts. In blood plasma
and PBMC of PTC patients, α-SMA concentration significantly exceeded control levels. Conclusions. α-SMA levels in benign
thyroid neoplasms did not differ from those in conditionally normal tissue. In the blood plasma and PBMC of PTC patients,
α-SMA concentrations were elevated compared to controls; however, no differences were observed between PTC cases with
and without Mts. Our findings reveal significant differences in α-SMA concentrations between PTC tumor tissues with and
without Mts, which may be useful for predicting metastatic potential.
References
Shinde AV, Humeres C, Frangogiannis NG. The role of α-smooth muscle actin in fibroblast-mediated matrix contraction and remodeling. Biochim Biophys Acta Mol Basis Dis. 2017 Jan;1863(1):298-309. doi: 10.1016/j.bbadis.2016.11.006.
Anggorowati N, Ratna Kurniasari Ch, Damayanti K, Cahyanti T, Widodo I, Ghozali A, et al. Histochemical and immunohistochemical study of α-SMA, Collagen, and PCNA in epithelial ovarian neoplasm. Asian Pac J Cancer Prev. 2017 Mar 1;18(3):667-71. doi: 10.22034/APJCP.2017.18.3.667.
Ping Q, Yan R, Cheng X, Wang W, Zhong Y, Hou Z, et al. Cancer-associated fibroblasts: overview, progress, challenges, and directions. Cancer Gene Ther. 2021 Sep;28(9):984-99. doi: 10.1038/s41417-021-00318-4. Erratum in: Cancer Gene Ther. 2021 Sep;28(9):1074. doi: 10.1038/s41417-021-00343-3.
Jia H, Chen X, Zhang L, Chen M. Cancer associated fibroblasts in cancer development and therapy. J Hematol Oncol. 2025 Mar 28;18(1):36. doi: 10.1186/s13045-025-01688-0.
Sun KH, Chang Y, Reed NI, Sheppard D. α-Smooth muscle actin is an inconsistent marker of fibroblasts responsible for forcedependent TGFβ activation or collagen production across multiple models of organ fibrosis. Am J Physiol Lung Cell Mol Physiol. 2016 May 1;310(9):L824-36. doi: 10.1152/ajplung.00350.2015.
Rao KB, Malathi N, Narashiman S, Rajan ST. Evaluation of myofibroblasts by expression of alpha smooth muscle actin: a marker in fibrosis, dysplasia and carcinoma. J Clin Diagn Res. 2014 Apr;8(4):ZC14-7. doi: 10.7860/JCDR/2014/7820.4231.
Enescu A, Enescu AŞ, Florou C, Petrescu F. E-cadherin and α-SMA expression in the epithelial-mesenchymal transition of salivary glands pleomorphic adenomas. Rom J Morphol Embryol. 2014;55(4):1383-7.
Vatseba TS, Sokolova LK, Pushkarev VV, Kovzun OI, Guda BB, Pushkarev VM, et al. Activation of the PI3K/Akt/mTOR/ p70S6K1 signaling cascade in the mononuclear cells of peripheral blood: association with insulin and insulin-like growth factor levels in the blood of patients with cancer and diabetes. Cytol Genet. 2019;53(6):489-93. doi: 10.3103/S0095452719060112.
Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of proteindye binding. Anal Biochem. 1976;72(1):248-54.
Ungefroren H, Sebens S, Seidl D, Lehnert H, Hass R. Interaction of tumor cells with the microenvironment. Cell Commun Signal. 2011 Sep 13;9:18. doi: 10.1186/1478-811X-9-18.