There were indications that c-Abl activity leads to Parkinson’s disease, and our experiments show there is indeed a connection,” says Ted Dawson, M.D., Ph.D., professor of neurology and director of the Institute for Cell Engineering at the Johns Hopkins University School of Medicine. “There is already a Food and Drug Administration-approved c-Abl inhibiting drug in use for leukemia,” he adds, “so we’re interested in whether it could be used safely against Parkinson’s disease or as a starting point to develop other treatments.”
Autopsies have revealed that c-Abl is especially active in the brains of people with Parkinson’s disease, a progressive disorder of the nervous system that affects movement. Additionally, studies in mice bred to be prone to the disease found drugs that block c-Abl may prevent or slow it. But, says Han Seok Ko, Ph.D., assistant professor of neurology at Johns Hopkins, “the drugs used in those studies could also have been blocking similar proteins, so it wasn’t clear that blocking c-Abl was what benefited the animals by either preventing symptoms or influencing disease progression.”
Non-receptor tyrosine kinases Arg and c-abl is differently modulated in B lymphoid cells at different stages of differentiation
“Glutathione peroxidase 1 is regulated by the c–Abl and Arg tyrosine kinases”. Glutathione peroxidase 1 is characterized in a polyalanine sequence polymorphism in the N-terminal region, which includes three alleles with five, six or seven alanine (Ala) repeats in this sequence. The allele with five Ala repeats is significantly associated with breast cancer risk
The tyrosine kinase ABL1 (acronym for As elson murine l eukemia viral oncogene homolog 1, also c-Abl, p150) is in various body cells occurring protein from the family of tyrosine kinases .
This protein is available in many cellular processes such as cell migration , cell adhesion , cell differentiation , and apoptosis involved and is an important element for the signal transduction via the T cell receptor . c-Abl is the gene product of the same proto-oncogene c-abl, a precursor of a potentially cancer-causing gene. Through exchange (translocation) of chromosome fragments between the c-abl harboring chromosome 9 and the bcr gene harboring chromosome 22 to the so-called Philadelphia chromosome may result, creates a new bcr-abl gene, which is the by clicking the link found chromosomal abnormalities resulting oncogene was and among others in 95% of chronic myelogenous leukemia (CML) can be detected. Therefore Abl proteins are popular targets for drug development .
c-Abl is a protein with a molecular mass of about 145 kDa, which by a gene on the chromosome 9 locus is encoded q34. It consists of a respective SH2 and SH3 domain that are responsible for the regulation of c-Abl, and the enzyme function bearing kinase domain . The C-terminus carrying a binding domain for interaction with the DNA and actin . Through different splicing two different N-terminal protein sequences can be formed. The N-terminus of c-Abl, the addition in the case of a splice variant 1B myristylation bears, is responsible for the autoinhibition. A binding site for Myristinsäurereste could be identified in the C-lobe of the kinase function. 
Comparison of the structural organization of c-Abl (splice variants 1a and 1b) with BCR / Abl. (BD: binding domain, NLS: nuclear localization signal , NES: nuclear export signal )
Activation and regulation
c-Abl is present in a basal inactive state. For the inactivity of the N-terminal part of the protein and myristyl is made responsible, although the splice variant 1A does not have such myristylation. But can to stabilize the inactive state also with fatty acids , modified proteins, such as Fus1 be involved.  A complete absence of the term, such as in the case of oncogenic viral offspring v-Abl and the oncogenic mutant BCR-Abl, is associated with the constitutive activity of the kinase function and a cancer-causing potential.
c-Abl, by receptor Tyrosikinasen such as the EGF receptor , and by non-receptor tyrosine kinases such as c-Src are activated. [
Lin J., Arlinghaus R. (2008). . Activated c-Abl tyrosine kinase in malignant solid tumors Oncogene 27: 4385-4391.
- Hochspringen ↑ Nagar B. et al. (2003). Structural basis for the Autoinhibition of c-Abl tyrosine kinase. Cell 112: 859-871.
- Hochspringen ↑ Lin J. et al. (2007). Oncogenic activation of c-Abl in non-small cell lung cancer cells lacking expression FUS1. Inhibition of c-Abl by the tumor suppressor gene product Fus1 Oncogene 26: 6989-6996.
- Hochspringen ↑ Srinivasan D. Plattner R. (2006). Activation of Abl tyrosine kinases Promotes invasion of aggressive breast cancer cells. Cancer Res . 66: 5648-5655.