a person wit sickle cell anemia ,the rbc's are sickle shaped!wat causes the changee?do they create new rbc's tat r sickle celled,wich wud lead to the destruction of the nomal ones,or do they change the shape of the existing rbc.s?can sumone actually explain wat exactly happens?
the gene involved in sickle cell anemia is the gene controlling haemoglobin production. the mutated gene produces haemoglobin S(hbS) which is eactly the same as normal haemoglobin A (HsA) except in one amino acid. this causes a change in the 3 dimensional shape that akes HbS less soluble. The HbS molecules tend to clump together causing the red blood cell to become sickle shaped. This interferes with oxgen carrying property of RBC and al;so makes them fragile, resulting in severe anaemia which is fatal
low oxygen tension causes sickling of RBC. the RBCs of a persion with sickle anemia carries the devestating potential to change their form in low oxygen tension. caused by intra RBC aggregation of hemoglobin (due to the mutation) at low oxygen tension - which alter the tertiary/quartenaty structure of hemoglobin
The Haemaglobin molecule that makes up the RBC has a single gene mutation which leads to a small patch on the molecule with a charge, this interacts with another mutated molecules and they bind/stick together, this forms to long chains on the hemoglobin with push and distort the overall shape of the RBC. I have more details if you want i, thats just an overview
sickle cell anaemia is an autosome linked recessive trait that can be transmitted from parents to offspring when both the parents are the carrier for the gene responsible for it.The disease is controlled by the single pair of allele, Hb^a and Hb^s. Out of the three possible genotypes only the homozygous individuals for Hb^s,i.e, (Hb^s Hb^s) show the diseased phenotype. Hetrozygous genotypes remain unaffected, but they behave as carriers of the disease. The defect is caused by the the substitution of glutamic acid by Valine at the sixth position of the beta globin chain of the haemoglobin molecule. Val-His-Leu-Thr-Pro-Glu-Glu ( Hb^a peptide or normal haemoglobin) Val-His-Leu-Thr-Pro-Val-Glu ( Hb^s peptide or affected haemoglobin) The mutant haemoglobin molecule undergoes polymerisation under low oxygen tension, thus producing the change in the shape of RBC from bi-concave to elongated sickle. It don't affect the shape of present haemoglobin molecules but it affects the shape of new haemoglobin molecules.
@biomed-well,if ya don't mind plz gimme othr details!thnx lottt
thnxx guyss!
Ill post it up tomorrow for ya
@biomed-thnxxx alotttttttttttttttt!:)
Realllllllly sorry, im in the airport waiting to go to Holland, the day caught up with me so i had no chance to get you a good answer, my bad and again, apologies :(
@biomed-chilll!relaxx!tats kkk!no worries!and hav a nice time in holland!:)
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