Scribd
Upload
154 views2 pages

Cystic Fibrosis

Cystic fibrosis is caused by a genetic mutation that results in the misfolding of the CFTR protein. Specifically, the deletion of a single amino acid, phenylalanine 508, prevents the CFTR protein from properly folding into its normal spiral shape. As a result, the misfolded protein cannot travel to the cell membrane where it is needed to fight bacterial infections in the lungs. This misfolding impairs the protein's function and leads to the chronic lung infections and early death that are hallmarks of cystic fibrosis. Pharmacological treatments aim to target this ΔF508 mutation directly by binding to the mutant protein or indirectly altering cellular processes to promote the targeting and stability of the ΔF508 CFTR protein at

Uploaded by

オオカミ白
Copyright
© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
Available Formats
Download as DOCX, PDF, TXT or read online on Scribd
154 views2 pages

Cystic Fibrosis

Cystic fibrosis is caused by a genetic mutation that results in the misfolding of the CFTR protein. Specifically, the deletion of a single amino acid, phenylalanine 508, prevents the CFTR protein from properly folding into its normal spiral shape. As a result, the misfolded protein cannot travel to the cell membrane where it is needed to fight bacterial infections in the lungs. This misfolding impairs the protein's function and leads to the chronic lung infections and early death that are hallmarks of cystic fibrosis. Pharmacological treatments aim to target this ΔF508 mutation directly by binding to the mutant protein or indirectly altering cellular processes to promote the targeting and stability of the ΔF508 CFTR protein at

Uploaded by

オオカミ白
Copyright
© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
Available Formats
Download as DOCX, PDF, TXT or read online on Scribd
You are on page 1/ 2

CYSTIC FIBROSIS (missfolded CFRT protein)

Introduction
Protein folding and misfolding:

Initially protein folding encounters in highly operative processes of a cell, however its
function is crucial for a certain molecule to engage into proper work. Protein folding creates
and hides structures of other proteins enbling them to cooperate in proper manner. Even
though, it may seem like a simplistic work, folding is quite complex and even a slight error
may lead to catastrophic results. Such errors are called PROTEIN MISFOLDING.
Protein misfolding, simplistically speaking may be thought off as an error in proper folding of
the protein. It happens that in just one enzyme fails to recognize its target for the whole
process to end in disease of an organism. The misfolded protein may be nonfunctional or
suboptimally functional, or it may be degraded by cellular machinery, or the misfolding may
expose epitopes which lead to dysfunctional interactions with other proteins.
Is scientific research of Biomedical students, the assembly of students and scientist have come
up to a simple explanation of errors of protein folding and to what extent can it cause a
damage. Thus meaning it is like folding a large bed sheet, if there is a single displacement of
a crease, the result it asymmetric, irregular shape. This explanation posed, it is quite easy to
understand how many diseases appear as a result of misfolded protein. Such diseases are CF,
Alzheimers disease, many other syndromes, etc.

Cystic Fibrosis
In this homework the protein folding, more precisely misfolding is encountered in CF
disease, that is when a genetic slip deletes a tiny but essential slice of CFTR.
This deletionof a single amino acid along a chain of nearly 1,500 of themoccurs at a
critical juncture in the twisting, turning protein. So instead of folding into an orderly,
spiral shape, the molecule unwinds, unravels or otherwise comes undone.
The deleted amino acid is like a passport, says Young-Hee Ko, Ph.D., who

initiated the project, supported by grants from the National Institutes of Health and
the American Lung Association. Without it, the protein cant travel to the cell
membrane, where it is critical for killing bacteria, especially in the lungs. The
result is that CF patients suffer a lifetime of chronic lung infections and an early
death. Quote from article: (http://www.hopkinsmedicine.org/hmn/F99/mu_8.html)
The process itself that occurs, as I have already mentioned previously, it the
deletion of Phenylalalnin (F508), the very slightest but crucial part of folding

protein. The misfold inables the protein to travel to the cell membrane, causing
impairment and resulting in disease of CF.
The most common mutation, deletion of phenylalanine 508 impairs CFTR folding
and, consequently, its biosynthetic and endocytic processing as well as chloride
channel function.

Pharmacological treatments
Pharamacological treatments of CF disease targets the already mentioned deleted F508.
Pharmacological treatments may target the CFTR structural defect directly by binding to the
mutant protein and/or indirectly by altering cellular protein homeostasis (proteostasis) to
promote F508 CFTR plasma membrane targeting and stability. This review discusses recent
basic research aimed at elucidating the structural and trafficking defects of F508 CFTR, a
prerequisite for the rational design of CF therapy to correct the loss-of-function phenotype.

You might also like

pFad - Phonifier reborn

Pfad - The Proxy pFad of © 2024 Garber Painting. All rights reserved.

Note: This service is not intended for secure transactions such as banking, social media, email, or purchasing. Use at your own risk. We assume no liability whatsoever for broken pages.


Alternative Proxies:

Alternative Proxy

pFad Proxy

pFad v3 Proxy

pFad v4 Proxy