Effects of Smoking

Smoking accelerates lung function decline

Smoking Accelerates Lung Function Decline in Alpha-11

FEV1 is a lung function measurement which measures how much air you can breathe out in one second. It is a measure of lung health.

When lungs are irritated by tobacco smoke, your body produces neutrophil elastase to eliminate it from your lungs. When the neutrophil elastase has finished breaking down the tobacco smoke, it continues to work, destroying your lung tissue and reducing its ability to expand and contract.7

Your body responds by producing AAT to neutralize excess neutrophil elastase. If there is a shortage of AAT, neutrophil elastase continues to break down your lung tissue, leaving you with less lung function.7

In 1 clinical study of 927 patients with Alpha-1, 78.7% of patients were either current smokers (8.1%) or ex-smokers (70.6%)1

Cigarette smoke destroys delicate lung tissue5,6

As shown above, normal lung tissue which has small, regular sized openings (left) is destroyed by smoking, causing large openings that interfere with lung function (right) because of cigarette smoke,2,3 which:

  • Contains oxidants capable of inactivating AAT2
  • Recruits inflammatory cells and increases neutrophil elastase concentration8
  • Can be detrimental to lung function,2,4 even as second-hand smoke

Learn how to quit smoking. Get information about quitting on the web site of the American Lung Association.

Help Alphas stay healthy. Download Managing Environmental Risk Factors, a brochure from AlphaNet that you can help you stay healthy.

A Guide for the Recently Diagnosed

PROLASTIN®-C (alpha1-proteinase inhibitor [human]) is indicated for chronic augmentation and maintenance therapy in adults with clinical evidence of emphysema due to severe hereditary deficiency of alpha1-PI (alpha1-antitrypsin deficiency).

The effect of augmentation therapy with any alpha1-proteinase inhibitor (alpha1-PI), including PROLASTIN-C, on pulmonary exacerbations and on the progression of emphysema in alpha1-antitrypsin deficiency has not been conclusively demonstrated in randomized, controlled clinical trials. Clinical data demonstrating the long-term effects of chronic augmentation or maintenance therapy with PROLASTIN-C are not available.

PROLASTIN-C is not indicated as therapy for lung disease in patients in whom severe alpha1-PI deficiency has not been established.

PROLASTIN-C is contraindicated in IgA-deficient patients with antibodies against IgA due to the risk of severe hypersensitivity and in patients with a history of anaphylaxis or other severe systemic reactions to alpha1-PI.

Hypersensitivity reactions, including anaphylaxis, may occur. Monitor vital signs and observe the patient carefully throughout the infusion. Should hypersensitivity symptoms be observed, promptly stop infusion and begin appropriate therapy. Have epinephrine and other appropriate therapy available for the treatment of any acute anaphylactic or anaphylactoid reaction.

PROLASTIN-C may contain trace amounts of IgA. Patients with known antibodies to IgA, which can be present in patients with selective or severe IgA deficiency, have a greater risk of developing potentially severe hypersensitivity and anaphylactic reactions.

The most common drug-related adverse reaction observed at a rate of >5% in subjects receiving PROLASTIN-C was upper respiratory tract infection. The most serious adverse reaction observed during clinical trials with PROLASTIN-C was an abdominal and extremity rash in 1 subject.

Because PROLASTIN-C is made from human plasma, it may carry a risk of transmitting infectious agents, eg, viruses, the variant Creutzfeldt-Jakob disease (vCJD) agent, and, theoretically, the Creutzfeldt-Jakob disease (CJD) agent. This also applies to unknown or emerging viruses and other pathogens.

Please click here for full Prescribing Information for PROLASTIN-C.


References

  1. Alpha-1-Antitrypsin Deficiency Registry Study Group. Survival and FEV1 decline in individuals with severe deficiency of alpha1-antitrypsin. The Alpha-1-Antitrypsin Deficiency Registry Study Group. Am J Respir Crit Care Med. 1998;158(1):49-59.
  2. American Thoracic Society/European Respiratory Society. American Thoracic Society/European Respiratory Society statement: standards for the diagnosis and management of individuals with alpha-1 antitrypsin deficiency. Am J Respir Crit Care Med. 2003;168(7):818-900.
  3. DeMeo DL, et al. Determinants of airflow obstruction in severe alpha-1-antitrypsin deficiency. Thorax. 2007;62(9):806-813.
  4. Mayer AS, Stoller JK, Vedal S, et al. Risk factors for symptom onset in PI*Z alpha-1 antitrypsin deficiency. Int J Chron Obstruct Pulmon Dis. 2007;1(4):485-492.
  5. Köhnlein T, Welte T. Alpha-1 Antitrypsin Deficiency: Clinical Aspects and Management. Bremen, Germany: UNI-MED Verlag AG; 2007.
  6. Snell GI. Airway bypass stenting for severe emphysema. CTSNet. April 16, 2006. www.ctsnet.org/portals/thoracic/newtechnology/article-4.html. Accessed April 23, 2008. Reproduced with permission of CTSNet, Inc.
  7. Alpha-1 Antitrypsin Deficiency: A Guide For The Recently Diagnosed Individual. Alpha-1 Foundation. Version 1.6, December 2006.
  8. MacNee W. Chest. 2000;117(5 suppl 1):303S-317S. Copyright 2000 by American College of Chest Physicians. Reproduced with permission of American College of Chest Physicians via Copyright Clearance Center.