1022-7954/05/4107- © 2005 Pleiades Publishing, Inc.
Russian Journal of Genetics, Vol. 41, No. 7, 2005, pp. 805–807. From Genetika, Vol. 41, No. 7, 2005, pp. 986–989.
Original English Text Copyright © 2005 by Hakki Ta tan, Ozlem Osmanagaoglu, Ayla Tuzun.
The human SAA family consists of
) [1, 2]. They are bound to HDL in circula-
tion. SAA1 and SAA2 are acute phase reactants whose
synthesis are regulated by interleukin—1, interleukin—6
and tumor necrosis factor—
. The physiological
role of SAA remains unclear, although some have sug-
gested its role in cholesterol metabolism . In addi-
tion, others have proposed immuno-suppressive effects
expressed via platelets and neutrophils .
Serum amyloid A (SAA) is a serum precursor of
amyloid A (AA), the main fibrillar component in reac-
tive amyloid deposits . SAA is a polymorphic pro-
tein, for which there are at least for major loci present
) in humans [7–9].
pseudogene and has no product .
are acute phase reactants; their sythesis in the liver is
greatly induced by inflammatory cytokines. Both types
from amyloid fibrils, AA—derived from
, is pre-
dominant in human AA deposits . There are two
) which differ in a single
base pair substitution in exon 4 .
Although the frequencies at the
different populations were previously reported by Ya-
mada and Moriguchi [8, 12], very few data are available
from this particular area (middle Asia and Europe). So,
we have determined the frequencies of the genotypes
and alleles at the
locus in Turkish, Azerbaijani,
and Kazakh healthy populations.
MATERIALS AND METHODS
Blood samples were randomly taken from
200 Turkish (138 male, 62 female; aged 17–22 years),
65 Azerbaijan (50 male, 15 female; aged 18–22 years),
and 65 Kazakh (63 male, 2 female; aged 17–22 years)
healthy volunteers who are students at the Ankara Uni-
versity. A written consent was obtained from each indi-
PCR–RFLP for SAA2 alleles.
Genomic DNA was
isolated as previously described [12, 13]. The poly-
merase chain reaction (PCR) to amplify a segment of
gene including the polymorphic site was per-
formed with 0.5
M SAA2—forward (5'-AGA GAA
TAT CCA GAG ACT CAC AGG C-3') and 0.5
SAA2—reverse (5'-CAG GCC AGC AGG TCG GAA
GT-3') primers in a PCR mixture (50
0.2 mM dNTP, 10 mM Tris-HCl, pH 8.3, 1.5 mM MgCl
50 mM KCl, 2.5 U
DNA polymerase and approxi-
mately 300 ng genomic DNA. The mixture was heated
to 94°C for 5 min and then subjected to 35 cycles of
The Frequencies of the Serum Amyloid A2 Alleles
in Healthy (Turkish, Azerbaijani, and Kazakh) Populations*
, Ozlem Osmanagaoglu, and Ayla Tuzun
Ankara University, Department of Biology, Ankara, Turkey; e-mail: email@example.com
Received August 9, 2004
—The Amyloid A1 (
) and A2 (
) proteins, which result from proteolytic cleavage of the Serum
Amyloid A1 (
) and A2 (
) proteins, are major protein components of the Amyloid A deposits found
in secondary amyloidosis. This study determines frequency of serum amyloid A2 alleles (
) in healthy Turk-
ish, Azerbaijani, and Kazakh subjects. Two hundred Turkish, sixty-ﬁve Azerbaijani and sixty-ﬁve Kazakh
healthy individuals were studied by previously described the PCR–RFLP methods. Our data revealed that the
frequencies of the
alleles at the
locus in the Turkish healthy population were different when com-
pared to those in Azerbaijani and Kazakh healthy populations (
= 0.014 and 0.02), respectively. In contrast,
the difference between
alleles at the
locus was not different in both Kazakh and Azerbaijani
healthy populations (
* The text was submitted by the authors in English.
Intron 3 Genomic sequence
Exon 3 Exon 4
Schematic description of the positions of the primers
for the PCR ampliﬁcation.