Concept explainers
To determine: The ways by which the potential to differentiate leukemic cells from healthy cells provides an opportunity to develop a therapy for CML treatment.
Introduction: In the case of CML (chronic myelogenous leukemia), leukemic cells can be distinguished from healthy body cells. This difference occurs due to the presence of functional BCR-ABL hybrid protein.
Explanation of Solution
One of the approaches that can be utilized to fight CML includes the use of tyrosine kinase inhibitor. This inhibitor binds to the ATP binding site of ABL kinase by inhibiting BCR-ABL phosphorylation and preventing the activation signaling pathways.
Moreover, real-time Q-RT-PCR (quantitative reverse transcription-polymerase chain reaction) allows an individual to monitor drug responses of cell populations in the patient. This approach is used to develop less toxic and effective treatments.
The potential to differentiate leukemic cells from normal cells allows an individual not to target therapy to specific cell populations but also to quantify responses to therapy. The leukemic cells produce an unusual hybrid protein known as BCR-ABL. Therefore, it may be possible to develop a therapy such as immunotherapy, based on the uniqueness of BCR-ABL protein.
Thus, the uniqueness of BCR-ABL protein may be used to develop immunotherapy for CML treatment.
Want to see more full solutions like this?
Chapter 24 Solutions
Concepts of Genetics (12th Edition)
- Given that a faulty ribosomal protein is the culprit and causes DBA, discuss the possible role of normal ribosomal proteins. Why might bone marrow cells be more susceptible to such a mutation than other cells?arrow_forwardTwo possible point mutations are the substitution of lysine for leucine or the substitution of serine for threonine. Which is likely to be more serious and why?arrow_forwardApproximately 1 in 100 West Africans suffer from sickle-cell anemia. Given the often devastating consequences of the disease, why is the HbS mutation so prevalent in Africa and in some other regions?arrow_forward
- The haemoglobin proteins of RNA polymerase ii sub units RPB1-P24928 RPB2-P30876 RPB3-P19387 RPB4-015514 are they similar? Explain?arrow_forwardTPA protein function. Use at least two sentences to describe the function of the TPA protein.arrow_forwardThe physical foundation of sickle cell disease is caused by a hemoglobin mutation that is prone to polymerization as a consequence of a surface-exposed valine residue on the hemoglobin molecule. if it is true or untruearrow_forward
- Sickle cell anemia is caused by a point mutation in the β-globin chain of hemoglobin. Glutamic acid is replaced by Valine. HBB sequence in normal adult hemoglobin (Hb A): Leu-Thr-Pro-Glu-Glu-Lys-Ser HBB sequence in mutant adult hemoglobin (Hb S): Leu-Thr-Pro-Val-Glu-Lys-Ser What effect does this mutation have on the structure and function of the protein? Predict what would happen to the RBC if the glutamic acid was replaced with asparagine instead of valine.arrow_forwardSickle cell anemia patients suffer from a distorted red blood cell shape and an anemic condition as a result of a genetic mutation in the HBB gene, which codes for the hemoglobin β subunits. This mutation changes a Glu to a Val at position 6 in the protein, and these patients express two alleles (one from each parent) with this mutation. When individuals inherit just one copy of this mutated gene, they are considered carriers, and have very few symptoms. Based on the quaternary structure of hemoglobin, what can you predict about the assembly of hemoglobin in sickle cell anemia patients versus carriers of the sickle cell trait? a. In sickle cell anemia patients, the α globin subunits have complementary mutations to ensure the quaternary structure of hemoglobin is attained. b. In sickle cell anemia patients, 100% of the hemoglobin is fully functional, whereas in those that carry the trait, there is no functional hemoglobin assembled. c. In individuals with the sickle cell…arrow_forwardMice and humans with inactivating mutations in the gene encoding activation-induced cytidine deaminase (AID) have an immunodeficiency disease known as ‘hyper IgM type 2’. Since AID is the enzyme that catalyzes the conversion of cytosines in the DNA to uracils, thereby initiating the process of somatic hypermutation, why do individuals with this deficiency only produce IgM antibodies?arrow_forward
- What is the Philadelphia chromosome? Briefly describe how it causes chronic myeloid leukemia.arrow_forwardBriefly describe the effects of colchicine treatment on cells. What are the genetic implications of such effects?arrow_forwardWhat percentage of cells in an organ or a tissue need toexpress a therapeutic gene to alleviate the effects of agenetic disorder?arrow_forward