Typing of genetic variants of alpha 1-antitrypsin by electrofocusing.

Jeppsson, Jan‐Olof; Franzen, B.

doi:10.1093/clinchem/28.1.219

Cited by 108 publications

(22 citation statements)

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“…The aj-AT phenotype was determined by isoelectric focusing [20]. Briefly, aliquots of frozen serum were thawed, 15/:xl electrophoresed in an acrylamide gel using ampholytes in the range 4-2-4-9 (Pharmacia, Uppsala, Sweden).…”

Section: A\-at Phenotypesmentioning

confidence: 99%

α1-Antitrypsin deficiency and anti-proteinase 3 antibodies in anti-neutrophil cytoplasmic antibody (ANCA)-associated systemic vasculitis

Savige

Chang

Cook

et al. 1995

Clinical and Experimental Immunology

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alpha 1-antitrypsin (alpha 1-AT) is a naturally occurring inhibitor of proteinase 3 (PR3) and elastase, two of the target antigens of anti-neutrophil cytoplasmic antibodies (ANCA). An increased incidence of alpha 1-AT phenotypes associated with dysfunctional alpha 1-AT or low serum levels has been reported in patients with anti-PR3 antibodies. We have studied the relationship between ANCA, and phenotypes and serum levels of alpha 1-AT. Phenotypes usually associated with a moderate or severe reduction in alpha 1-AT serum levels or in dysfunctional activity were found more often in individuals with anti-PR3 antibodies than in the general population: four of the 31 patients (13%) with anti-PR3 antibodies had phenotypes MZ (n = 2), S (n = 1) or Z (n = 1) (P < 0.05). However, the corresponding alpha 1-AT serum levels were normal (n = 3) or elevated (n = 1). None of the 31 sera with anti-PR3 antibodies had low levels of alpha 1-AT. No abnormal alpha 1-AT phenotype was demonstrated in seven patients with anti-elastase antibodies, despite a low level of alpha 1-AT in one serum. Anti-myeloperoxidase antibodies are common in patients with ANCA, but no abnormal phenotype or low serum alpha 1-AT level was demonstrated in any of 29 sera containing these antibodies. Finally anti-glomerular basement membrane (GBM) antibodies occur occasionally in patients with ANCA-associated diseases, but again none of 10 sera had an abnormal alpha 1-AT phenotype or low serum level. ANCA were not demonstrated by indirect immunofluorescence in any serum from 73 patients with abnormal alpha 1-AT phenotypes. These results confirm that patients with anti-PR3 antibodies often have alpha 1-AT phenotypes that are usually associated with low serum levels of alpha 1-AT or with dysfunctional protein. Nevertheless, the incidence of anti-PR3 antibodies in patients with abnormal alpha 1-AT phenotypes is very low. This probably reflects the rarity of Wegener's granulomatosis, the major disease associated with anti-PR3 antibodies, and the relative frequency of abnormal alpha 1-AT phenotypes. The mechanism for the development of anti-PR3 antibodies in patients with abnormal alpha 1-AT phenotypes is not clear, but may relate to the increased propensity of unbound and uninhibited PR3 to stimulate autoantibody production.

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Section: A\-at Phenotypesmentioning

confidence: 99%

α1-Antitrypsin deficiency and anti-proteinase 3 antibodies in anti-neutrophil cytoplasmic antibody (ANCA)-associated systemic vasculitis

Savige

Chang

Cook

et al. 1995

Clinical and Experimental Immunology

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“…In an electric field multiple isoforms of A1PI (M0/M1-M8) are separated mainly due to the different numbers of sialic acids residues on the N-glycans. 3,4 Two minor isoforms, M7 and M8, are truncated at the N-terminus lacking five amino acids (1)(2)(3)(4)(5) leading to an additional cathodal shift due to the loss of negatively charged glutamic and aspartic acid residues. 5 Correct glycosylation of a glycoprotein is important because a difference in N-glycosylation can influence, for example, correct protein folding, 6 biologic activity, 7 specific interactions with receptors, 8,9 and serum halflife.…”

mentioning

confidence: 99%

Biochemical, molecular characterization, and glycoproteomic analyses of α₁‐proteinase inhibitor products used for replacement therapy*

Kolarich¹,

Turecek²,

Weber

et al. 2006

Transfusion

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Protein chemical characterization of A1PI showed that all A1PI products to some extent differ from A1PI circulating in human plasma. Bioinformatic analysis indicated that removal of C-terminal Lys394 and cysteinylation of Cys232 are unlikely to affect structure and/or function of A1PI but cysteinylation may influence interaction between A1PI and its physiologic ligands. Aralast, Prolastin, and Zemaira contain the same set of N-glycans in the same ratios as those in normal human plasma A1PI. Tri- and tetraantennary structures are responsible for the partitioning into IEF isoforms, with the migration shift of Aralast not being due to any difference in the N-glycosylation, but to the partial loss of the C-terminal lysine.

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“…SDS-electrophoresis was performed in a IO-I5^( or 12-18% linear polyacryla-mide gradient slab gel essentially as described [5], with the buffer system of Maizel [18|. The electrofocusing systems have been described previously [1,11,15]. Serum concentrations of PA were determined by electroimmunoassay [17], using Seronorm protein® (Nyegaard, Oslo, Norway) as standard.…”

Section: Methodsmentioning

confidence: 99%

Prealbumin in Swedish Patients with Senile Systemic Amyloidosis and Familial Amyloidotic Polyneuropathy

et al. 1985

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A prealbumin (PA)-like protein was demonstrated in amyloid fibrils both from a patient with senile systemic amyloidosis (SSA) and from a patient in northern Sweden with familial amyloidotic polyneuropathy (FAP). The investigated properties of this protein were similar in the two types of fibrils. The protein had molecular weight, antigenic determinants, and at least one cysteinyl residue in common with the subunit of normal PA. In contrast to normal PA, it contained disulphide-linked subunits and was to some extent bound to the fibril via the cysteinyl residues. The noncovalent forces between its subunits were weaker than in normal PA. It constituted part of the previously described AScl protein of the SSA fibrils. Proteins with lower molecular weight than the PA monomer were major proteins in both SSA and FAP fibrils. These proteins had similar properties in the two kinds of fibril and may be derived from PA. PA in serum from Swedish patients with FAP and SSA was normal with regard to the isoelectric pH of the monomers and tetramers.

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Typing of genetic variants of alpha 1-antitrypsin by electrofocusing.

Cited by 108 publications

References 0 publications

α1-Antitrypsin deficiency and anti-proteinase 3 antibodies in anti-neutrophil cytoplasmic antibody (ANCA)-associated systemic vasculitis

α1-Antitrypsin deficiency and anti-proteinase 3 antibodies in anti-neutrophil cytoplasmic antibody (ANCA)-associated systemic vasculitis

Biochemical, molecular characterization, and glycoproteomic analyses of α₁‐proteinase inhibitor products used for replacement therapy*

Prealbumin in Swedish Patients with Senile Systemic Amyloidosis and Familial Amyloidotic Polyneuropathy

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Typing of genetic variants of alpha 1-antitrypsin by electrofocusing.

Cited by 108 publications

References 0 publications

α1-Antitrypsin deficiency and anti-proteinase 3 antibodies in anti-neutrophil cytoplasmic antibody (ANCA)-associated systemic vasculitis

α1-Antitrypsin deficiency and anti-proteinase 3 antibodies in anti-neutrophil cytoplasmic antibody (ANCA)-associated systemic vasculitis

Biochemical, molecular characterization, and glycoproteomic analyses of α1‐proteinase inhibitor products used for replacement therapy*

Prealbumin in Swedish Patients with Senile Systemic Amyloidosis and Familial Amyloidotic Polyneuropathy

Contact Info

Product

Resources

About

Biochemical, molecular characterization, and glycoproteomic analyses of α₁‐proteinase inhibitor products used for replacement therapy*