Cyclophosphamide treatment modifies the thermal stability of profilin bound monomeric and leiomodin2 bound filamentous actin

Abstract The monomeric (G-actin) and polymer (F-actin) forms of actin play important role in muscle development contraction, cellular motility, division, transport processes. Leiomodins 1–3 (Lmod1–3) are crucial for the sarcomeres. Unlike tropomodulins that localize only at pointed ends, striated specific Lmod2 shows diffuse distribution along entire length thin filaments. G-actin-binding profilin (Pro) facilitates nucleotide exchange on inhibits polymerization barbed end, therefore contributes to maintenance intracellular pool competent ATP-G-actin. Cyclophosphamide (CP) is a cytostatic drug can have potential side effects filaments level myofilaments. Here, we aimed investigating influence CP its complexes with actin-binding proteins by using differential scanning calorimetry (DSC). We found upon treatment, denaturation Pro-G-actin Lmod2-F-actin was characterized an increased enthalpy change. However, after melting temperature F-actin same as presence Lmod2, seems like does not any effect structure alkylated F-actin. In case Pro bound G-actin did respond addition. function cells be modified within treatment.