AATVar : a database of human alpha-1 antitrypsin variants
Mmineral springs
Mutation sequence analysis
Contributed by
CHU Lyon
HGVS nomenclature (NM_000295.4)
Usual nomenclature (Without signal peptide)
Nomenclarure including the signal peptide
c.272G>A
Type of variation
AAT variant
Mutation Location
Exon 2
Genetic background
M1 Val
ACMG classification
Pathogenic
Comments
rs28931568
This mutation creates a polymorphism for the restriction endonuclease AvaII.
AAT variant and Q0 alleles
Variant name
Mmineral springs
Also Known as
pathogenicity
Deficient Dysfunctional
HGVS nomenclature protéine
p.Gly91Glu
3D position of aa affecteded
Mobility on polyacrylamide gel
Mobility on agarose gel
AATserum level (g/L)
Heterozygous
0.5 à 0.8
Homozygous
Anti-elastolytic activity (IU/L)
Heterozygous
Homozygous
Comments
The alpha 1AT Mmineral springs migrates cathodal to the normal M2 allele.
Occurrence
Ethnic background without frequency range
Ethnic background and frequency
Frequency range
from (%)
To (%)
Group tested
Size
Description (who was tested)
Occurrence comments
The Mmineral springs allele was first observed in a black family.
Overall comments
Occurrence comments
- Cytoplasmic blot analysis of blood monocytes of the Mmineral springs homozygote demonstrated levels of alpha 1AT mRNA transcripts comparable to those in cells of a normal M1 control.
- Evaluation of in vitro translation of Mmineral springs alpha 1AT mRNA transcript demonstrated a normal capacity to direct the translation of alpha 1AT.
- However, a reduced alpha 1AT secretion on the basis of aberrant post-translational alpha 1AT biosynthesis was demonstrated for the Mmineral springs allele.
- Furthermore, for alpha 1AT protein that does reach the circulation, the causing mutation markedly affects the ability of the molecule to neutrophil elastase.
