Volume 5, Issue 3(Suppl)
Biochem Anal Biochem 2016
ISSN: 2161-1009, Biochem an open access journal
Page 59
Biochemistry 2016
October 10-12, 2016
conferenceseries
.com
Biochemistry
October 10-12, 2016 Kuala Lumpur, Malaysia
International Conference on
Sialic acid profile and sialidase activity in HIV infected individuals
Hadiza Abdullahi
Northwest University Kano, Nigeria
S
ialic Acids and sialidases have been implicated in many disease states particularly bacterial and viral infections which are common
opportunist infections of HIV disease. A study was carried out to determine sialic acid profile and sialidase activity in HIV infected
and apparently healthy individuals. Blood samples were collected from 200 subjects (150 HIV infected individuals and 50 apparently
healthy individuals, divided into four groups: HIV ART naive, HIV stable (on ART but have been stable with no clinical episodes),
HIV-OI (on ART with opportunistic infections), and apparently healthy). Complete blood count, erythrocyte surface sialic acid
(ESSA), free serum sialic acid (FSSA) concentrations and sialidase activity were determined for all 200 subjects. Analysis of variance
was used to compare the results of the different groups of HIV infected individuals as well as controls. Anemia and neutropenia were
the most common hematological abnormalities observed in this study with highest prevalence of anemia found in the ART naive
group. There was significant difference (p≤0.05) between groups in FSSA level. The highest levels of FSSA were observed in the HIV
ART naive (0.65±0.5 mg/ml). The mean ESSA value for the study population was 0.54±0.35 mg/ml with no significant difference
(p≤0.05) between groups. No significant difference (p≤0.05) was found between groups and also in gender and age. The findings in
this study of higher mean sialidase activity and FSSA levels in the ART naive HIV group compared with other groups indicate that
the virus and other opportunistic pathogens may be sialidase producers in vivo which cleave off sialic acids from erythrocytes surface,
leading to high levels of FSSA, anemia and neutropenia seen in this group. The higher ESSA concentration found in the HIV stable
group along with lowest FSSA concentration in the group suggests the presence of sialyltransferases.
khadeejahay@yahoo.comTo study allelic variants of
PON1
gene in ischemic stroke patients with high LDL/HDL ratios
Sushree S Rautaray
Army College of Medical Sciences, India
S
troke continues to be the leading cause of morbidity and mortality worldwide. Oxidative stress is a characteristic of ischemic
stroke. Elevated LDL/HDL ratio is an important factor for predicting arteriosclerosis. Paraoxonase 1(
PON1
) protects LDL from
oxidative modifications and has a protective effect against arteriosclerosis. Two common polymorphisms,
Q192R
and
L55M
, in
PON1
gene can affect PON1 levels and function. The aim of this study was to evaluate
Q192R
and
L55M
polymorphisms in ischemic stroke
patients with high LDL/HDL ratios and to investigate ox-LDL levels as a marker of oxidative stress. The study included 100 patients of
ischemic stroke admitted in ICU of Base Hospital, Army College of Medical Sciences, Delhi and 100 controls. Patients were in the age
group of 55-85 years.
PON1 Q192R
and
L55M
were determined by PCR-RFLP method, ox-LDL by ELISA kit method.
PON1 L55M
was associated with high LDL/HDL ratios in ischemic stroke patients. So, the L55M polymorphism can contribute in decreasing the
antioxidant function and decreasing HDL particles. Plasma levels of ox-LDL were increased in stroke patients (P<0.001) compared to
controls. In conclusion, it is important to explore the effects of
PON1 L55M
genetic polymorphisms and the inflammatory response
associated with stroke. We hypothesized that elevated ox-LDL levels and lower
PON1
activity may contribute for the development of
oxidative stress. The present study was carried out to emphasize the importance of these markers for early diagnosis and therapeutic
interventions in ischemic stroke patients.
sambit.nayak77@gmail.comBiochem Anal Biochem 2016, 5:3(Suppl)
http://dx.doi.org/10.4172/2161-1009.S1.006