To evaluate the polymerogenic properties of serpina2 and a1 variants, we analyzed the insoluble fractions by western blot.
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Abnormal alpha-1 antitrypsin proteins may bind together to form a large moleculeor polymerthat cannot leave the liverThe accumulation of these polymers results in liver damageIn additionlung tissue is destroyed because not enough alpha-1 antitrypsin is available to protect against neutrophil elastasePolymers of alpha-1 antitrypsin may also contribute to excessive inflammationwhich may explain some of the other features of alpha-1 antitrypsin deficiencysuch as a skin condition called panniculitis.
(aallergologyccardiologyccclinical chemistryeepidemiologyexpexposureggenetic and molecular biologymmeteorologynnutritionooccupational healthppneumologypaphysical activitypdpediatricssstatistics.
This section provides information about the protein and gene name(sand synonym(sand about the organism that is the source of the protein sequence.
AffiliationInterfaculty Institute for Genetics and Functional GenomicsUniversity Medicine GreifswaldGreifswaldGermany.
AffiliationDepartment of Public HealthFaculty of MedicineUniversity of SplitSplitCroatia.
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