Lysosomes, growth factor activity, and carcinogenic implications.

The aim of this paper is to point out a body of literature which up to now has been largely ignored by investigators in the area of growth factors This paper will offer a response to the questions: Why is it that inhibition of endolysosomal proteases (by agents such as leupeptin, methylamine, etc.) or inhibition of endocytosis block the activities of all growth factors and carcinogens so far studied? What role therefore can endocytosis and endolysosomes (E/L) play in the signal transduction process? As will be detailed below, in many cases involving growth factors, inhibition of E/L proteases results in complete or very significant loss of growth factor activity. That is, treatment with inhibitors of E/L proteases (i.

Amino acid-anticodon binding specificity: rationale for a new class of therapeutic agent.

In this article a new class of anticancer and antiviral drugs is discussed. These new drugs consist of small di- and tri-peptides, designed to bind to single-stranded (ss) regions that are crucial for the expression of genes such as the c-myc oncogene in cancers and start sites (and other ss regions) of viral pathogenic genes. The components (i.

Role of the endocytic pathway in carcinogenesis.

This commentary was prompted by many reports that carcinogenesis involving various carcinogens and various types of systems is blocked by inhibitors of endolysosomal proteases (i.e. leupeptin, antipain).