Alpha-1-Antitrypsin Levels and Genetic Variation of the Alpha-1-Antitrypsin Gene in Peyronie’s Disease

Serum levels and genotype distribution of α1-antitrypsin in the general population

“…Some studies identified mean values or reference intervals of AAT serum concentration but they were limited to target groups, mostly COPD cases or populations in which the frequency of AATD is low, such as Japanese19 and Korean populations,20 or in patients with a peculiar clinical phenotype, such as Peyronie's disease,21 or characteristic cohorts, such as paediatric subjects7 and pregnant women 22. The use of advanced technologies makes this study innovative.…”

“…Other factors that impact AAT concentration variability include active smoking25 and age 21. An in-depth analysis of the same SAPALDIA population has shown that an inter-relationship among circulating AAT, smoke exposure, gender and systemic inflammatory status exists 13.…”

The Management of Peyronie’s Disease: Evidence-based 2010 Guidelines

“…A widely accepted hypothesis on the etiology of the PD plaque is that it originates from trauma or microtrauma to the erect penis [44][45][46][47][48][49][50][51][52][53][54][55] in patients with genetic predisposition to form localized fibrosis as a response to trauma. [56][57][58][59][60][61][62]. The main pathological process is tissue fibrosis with disorganization of elastic fibers, combined in most cases with fibrin accumulation and different degrees of inflammation [48,50,[63][64][65][66][67][68][69][70][71][72][73][74][75].…”

Tissue Taurine Depletion Induces Profibrotic Pattern of Gene Expression and Causes Aging-Related Cardiac Fibrosis in Heart in Mice

“…Serpina1 can inhibit several proteases, such as trypsin, chymotrypsin, thrombin, plasmin, cathepsin G, kallikrein, proteinase 3, renin, and pancreatic elastase. 22) Importantly, Serpina1 can cause a change in collagen metabolism. 23) While the role of Serpina1 in fibrosis has never been reported, other protease inhibitors, plasminogen activator inhibitor-1 (PAI-1) and tissue inhibitor of metalloproteinase-1 (TIMP-1) contribute to the reduction in collagen degradation by inhibiting matrix metalloproteinases.…”