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These modifications are caused by inflammation, hyperhomocysteinemia, oxidative stress, decreased angiogenic factors, and cellular senescence

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Gliotoxin can target integrins to modify their cysteines by a disulfide bond, thus blocking the binding of arginine-glysine-aspartic acid (RGD)-containing extracellular matrix, leading to the inhibition of focal adhesion kinase and the dephosphorylation of p190RhoGAP, which allows for the activation of RhoA and, subsequently, the activation of ROCK, MKK47/MKK7, and JNK and the induction of Bim phosphorylation, which is a proapoptotic factor