Author/Authors :
Tarighi، Parastoo نويسنده Department of Medical Biotechnology, School of Advanced Technologies in Medicine, Tehran University of Medical Sciences, Tehran, Iran Tarighi, Parastoo , Khorramizadeh، MohammadReza نويسنده Department of Medical Biotechnology, School of Advanced Technologies in Medicine, Tehran University of Medical Sciences, Tehran, Iran Khorramizadeh, MohammadReza , Madadkar-Sobhani، Armin نويسنده Department of Bioinformatics, Institute of Biochemistry and Biophysics, Tehran University, Tehran, Iran Madadkar-Sobhani, Armin , Ostad، SeyedNasser نويسنده Department of Toxicology and Pharmacology, Faculty of Pharmacy and Pharmaceutical Sciences
Research Center, Tehran University of Medical Sciences, Tehran, Iran. Ostad, SeyedNasser , Ghahremani، MohammadHossein نويسنده Department of Toxicology Pharmacology, School of Pharmacy, Tehran University of Medical Sciences, Tehran, Iran AND Department of Molecular Medicine, School of Advanced Technologies in Medicine, Tehran University of Medical Sciences, Tehran, Iran Ghahremani, MohammadHossein
Abstract :
Interaction between urokinase-type plasminogen activator (uPA) and its receptor (uPAR) plays an important role in the progression of numerous cancer types including breast cancer by promoting tumor initiating, proliferation, invasion and metastasis. Hence, disruption of this interaction inhibits their downstream cascades and subsequently tumor growth. For this, we created two series of 8 and 10 amino acids linear peptides, derived from uPA binding region to target uPAR and studied the inhibition of proliferation in MDA-MB-231 cell line. Results revealed that all of the 10-mer peptides inhibited breast cancer cell proliferation significantly with maximum 40% inhibition of 103 peptides. Meanwhile, none of the 8-mer peptides showed significant toxicity. Current results indicate that the linear 10-mer peptides which mimic a small part of a sequence of a binding domain of uPA to uPAR could be exploited to design a novel class of anti-cancer agents.
