Alpha 1-antitrypsin deficiency causes

Revision as of 16:35, 14 December 2017 by Mazia Fatima (talk | contribs) (→‎Causes)
Jump to navigation Jump to search

Alpha 1-antitrypsin deficiency Microchapters

Home

Patient Information

Overview

Historical Perspective

Classification

Pathophysiology

Causes

Differentiating Alpha 1-antitrypsin deficiency from other Diseases

Epidemiology and Demographics

Risk Factors

Screening

Natural History, Complications, and Prognosis

Diagnosis

History and Symptoms

Physical Examination

Laboratory Findings

Electrocardiogram

X Ray

CT

MRI

Ultrasound

Other Imaging Findings

Other Diagnostic Studies

Treatment

Medical Therapy

Surgery

Primary Prevention

Secondary Prevention

Cost-Effectiveness of Therapy

Future or Investigational Therapies

Case Studies

Case #1

Alpha 1-antitrypsin deficiency causes On the Web

Most recent articles

Most cited articles

Review articles

CME Programs

Powerpoint slides

Images

American Roentgen Ray Society Images of Alpha 1-antitrypsin deficiency causes

All Images
X-rays
Echo & Ultrasound
CT Images
MRI

Ongoing Trials at Clinical Trials.gov

US National Guidelines Clearinghouse

NICE Guidance

FDA on Alpha 1-antitrypsin deficiency causes

CDC on Alpha 1-antitrypsin deficiency causes

Alpha 1-antitrypsin deficiency causes in the news

Blogs on Alpha 1-antitrypsin deficiency causes

Directions to Hospitals Treating Alpha 1-antitrypsin deficiency

Risk calculators and risk factors for Alpha 1-antitrypsin deficiency causes

Editor-In-Chief: C. Michael Gibson, M.S., M.D. [1]; Associate Editor(s)-in-Chief:

Please help WikiDoc by adding content here. It's easy! Click here to learn about editing.

Overview

Alpha1-antitrypsin deficiency (AATD) is caused by a mutation in the SERPINA1 gene. SERPINA1 is located on chromosome 14.

Causes

  • Alpha1-antitrypsin deficiency (AATD) is caused by a mutation in the SERPINA1 gene.[1][2]
  • SERPINA1 is located on chromosome 14 and is highly pleomorphic, with more than 100 allelic variants.This gene instructs the body to make a protein called alpha-1 antitrypsin (AAT), which functions to protect the body from called neutrophil elastase enzyme.
  • Neutrophil elastase helps the body fight infections, but it can also attack healthy tissue in the lung if not inactivated by AAT.Alpha1-antiprotease functions to protect the lungs from unregulated protease activity.
  • Mutations associated with AAT can result in deficiency or complete absence of AAT, or a form of AAT that does not work effectively to protect healthy tissue. This allows neutrophil elastase to destroy lung tissue, causing lung disease.
  • In addition, the accumulation of intrahepatic alpha1-antitrypsin can build up in the liver and can result in apoptosis of hepatocytes.
  • The severity of AATD may also be worsened by environmental factors such as exposure to tobacco smoke, dust, and chemicals. This initially presents as laboratory abnormalities on liver function test, but can progress to hepatitis, followed by fibrosis and cirrhosis.

References

  1. Hazari YM, Bashir A, Habib M, Bashir S, Habib H, Qasim MA, Shah NN, Haq E, Teckman J, Fazili KM (2017). "Alpha-1-antitrypsin deficiency: Genetic variations, clinical manifestations and therapeutic interventions". Mutat. Res. 773: 14–25. doi:10.1016/j.mrrev.2017.03.001. PMID 28927525.
  2. Stoller JK (2016). "Alpha-1 antitrypsin deficiency: An underrecognized, treatable cause of COPD". Cleve Clin J Med. 83 (7): 507–14. doi:10.3949/ccjm.83a.16031. PMID 27399863.


Template:WikiDoc Sources