5 - CMB2015v5n1页

Computational Molecular Biology 2015, Vol. 5, No. 1, 1-13
http://cmb.biopublisher.ca
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Formation of GHB is irreversible and its level in the
erythrocytes depends on the blood glucose
concentration. Measurement of GHB, which was first
introduced in the 1970's, provides an index of long
term glycemic control, which has been proven to
evoke changes in diabetes treatment resulting in
improved metabolic control. An HbA1c extent directly
relates to the blood glucose levels in human, and
maybe so in other animals (Nathan et al., 2008;
Shahbazkia et al., 2010; Bazzi et al., 2013) Based on
the correlation between the AA and glucose, the
process of glycosylation in eukaryotes could be
categorized into five types: N-linked, O-linked,
C-linked, P-linked and G-linked which N- and
O-linked are most common glycosylation forms
(Chauhan et al., 2013).
Blood glucose concentration ratio in camel and cow is
about (9.7±2.8 mM) (at high level) and (5.7±0.73 mM)
(in lowest level). High level of blood glucose in
camels may be caused by their strong capacity for
insulin resistance (Jirimutu et al., 2012; Bazzi et al.,
2013). Level of glycosylated hemoglobin (GHB) is
3.4± 0.23% and 3.2± 0.11% in camel and cattle,
respectively. The low glycation of camel Hb at higher
glucose concentrations suggests that certain factors
protect the Hb from glycation at high glucose
concentrations (Bazzi et al., 2013). According to
Oyewale et al. (2011) Camelus dromedarius
hemoglobin provides an interesting case study of
adaptation to life in deserts at extremely high
temperatures. As well as camel Hb also exhibited
higher electrophoretic mobility than normal
hemoglobin in human or cow (Oyewale et al., 2011).
Lot numbers of researches have been carried out on
the erythrocytes and hemoglobin of camel species
(Lin et al., 1976; Braunitzer et al., 1980; Farooq et al.,
2011; Oyewale et al., 2011). Oyewale et al (2011) had
compared erythrocytes fragility between camel
(Camelus dromedarius ) and donkey (Equus asinus) in
different environmental situation. They had suggested
that variation in the temperature and pI of the
erythrocyte environment beside duration of blood
storage may each play a significant role in the osmotic
behavior of camel and donkey erythrocytes (Oyewale
et al., 2011). Bazzi et al (2013) had revealed high
blood glucose concentration (9.7±2.8 mM) and low
level of glycated-Hb (3.4±0.23%) in camel but cow
blood samples did not show sufficient variations in
glucose concentrations (5.7±0.73 mM) or glycated-Hb
levels (3.2± 0.11%) (Bazzi et al., 2013). They had
declared low glycation of camel Hb at higher glucose
concentrations revealed certain factors which protect
the Hb from glycation at high glucose concentrations.
Level of glycated-Hb may not only just reflect
dependence on blood glucose level, erythrocyte life
span and permeability of erythrocyte membrane, but
also shows on food regime (Ardia, 2006) Borai et al.
(2011) had suggested HbA1c can be used as a simple
and reliable marker of insulin resistance in normal
adult’s glucose tolerance with relatively high insulin
sensitivity (Borai et al., 2011). According to previous
researches on the role of hemoglobin in diabetes, we
decided to study on structure, chemical features and
compositions of hemoglobin in the Camelus
dromedaries, Camelus bactrianus ,Camelus ferus , Bos
taurus, Homo sapiens and Equus caballus. Despite the
fact that camels have higher blood glucose levels than
human, the extent of glycosylation is extremely less in
camel’s blood than in ours. Therefore, DNA and
protein sequences of HB subunits were compared
between mentioned species to study on resistivity of
glycosylation and to diabetes subsequently.
1 Material and methods
1.1 Data collection
The AA and nucleic acid (NA) sequences of HB (alpha
and beta subunits) were obtained for Camelus
dromedaries, Camelus bactrianus, Camelus ferus, Bos
taurus, Homo sapiens and Equus caballus from biological
database such as Uniprot and KEGG (Table 1).
1.2 In silico analysis
Sequences had converted to amino acid (*.pro) by
complex of Lasergene softwares. As well as mentioned
files were altered to FASTA form (*.fas), for which
this form is common for analysis of genomic data’s.
We used ClustalW to perform multiple alignments for
proteins in each species by MEGA 5.01 (Tamura et al.,
2011) and CLC Genomics Workbench 7.5. The
evolutionary history was inferred by using the
UPGMA based on Kimura protein distance measure.
UPGMA assumes a constant rate of evolution.