Publications by authors named "Ramin Raoufinia"

6 Publications

  • Page 1 of 1

Maternal exposure to ambient particulate matter and green spaces and fetal renal function.

Environ Res 2020 05 23;184:109285. Epub 2020 Feb 23.

ISGlobal, Barcelona, Spain; Universitat Pompeu Fabra (UPF), Barcelona, Spain; CIBER Epidemiología y Salud Pública (CIBERESP), Spain.

Exposure to air pollution has been associated with different harmful effects and exposure to greenspace has been related to improved human health. However, the available evidence on the impact of these exposures on renal function is still scarce. The aim of this study was to determine the relationship between exposure to ambient levels of PM, PM, PM and indicators of exposure to traffic as well as greenspace during pregnancy and fetal renal function based on the umbilical cord blood. This study was based on 150 pregnant women residing in Sabzevar, Iran (2018). Multiple linear regression models were developed to estimate the association of glomerular filtration rate (GFR), creatinine (Cr) and blood urea nitrogen (BUN) with exposure to air pollution, traffic, and greenspace (one at a time) controlled for relevant covariates. There was an inverse significant association between exposure to PM, PM PM and total street length in a 100 m buffer around the home and eGFR. Increase in distance to major road and residential surrounding greenness (100 m buffer) was associated with increase in eGFR. We observed a significant direct association between exposure to PMs as well as street length in 100 m buffer and serum level of Cr. There was also an inverse association between distance to major road and NDVI in 100 m buffer and Cr. The associations for blood urea nitrogen (BUN) were not statistically significant. Our results suggest that exposure to air pollution during pregnancy could have negative impact and exposure to greenspace could have positive impact on renal function of fetal.
View Article and Find Full Text PDF

Download full-text PDF

Source
http://dx.doi.org/10.1016/j.envres.2020.109285DOI Listing
May 2020

Exposure to air pollution during pregnancy and newborn liver function.

Chemosphere 2019 Jul 30;226:447-453. Epub 2019 Mar 30.

Cellular and Molecular Research Center, Department of Environmental Health, School of Health, Sabzevar University of Medical Sciences, Sabzevar, Iran. Electronic address:

Exposure to air pollution has been associated with a wide range of adverse health outcomes. However, the available evidence on the impact of air pollution exposures on liver enzymes is still scarce. The aim of the present study was to assess the relationship between exposure to ambient PM, PM and PM during pregnancy and serum level of aspartate aminotransferase (AST), alanine aminotransferase (ALT), alkaline phosphatase (ALP) and gamma-glutamyl transferase (GGT) in cord blood samples of newborns. Moreover, the association between total street length in different buffers and distance to major roads at the maternal residential address and liver enzymes were investigated. This cross-sectional study was based on data from a sample of 150 newborns, from Sabzevar, Iran. Land use regression models were used to estimate concentrations of air pollutants at home during pregnancy. Multiple linear regression was developed to estimate association of AST, ALT, ALP and GGT with air pollution controlled for relevant covariates. In fully adjusted models, increase in PM and PM as well as PM were associated with higher levels of AST, ALT and GGT. Moreover, there was a significant association between total street length in a 100 m buffer at residential address with AST, ALT and GGT. Each meter increase in distance to major roads was associated with -0.017 (95% confidence interval (CI): -0.028, -0.006) decrease in AST. Overall, our findings were supportive for association between PMs exposure during pregnancy and increase in liver enzymes in newborns. Further studies are needed to confirm these findings in other settings and populations.
View Article and Find Full Text PDF

Download full-text PDF

Source
http://dx.doi.org/10.1016/j.chemosphere.2019.03.185DOI Listing
July 2019

Human albumin purification: a modified and concise method.

J Immunoassay Immunochem 2018 12;39(6):687-695. Epub 2018 Oct 12.

c Drug Applied Research Center , Tabriz University of Medical Sciences , Tabriz , Iran.

Background: Among different proteins of blood, albumin is considered a unique protein due to having special properties. Now, various protocols are used for the albumin purification worldwide, each of them has its own advantages and disadvantages. Meanwhile, a common method which is often used for the production of albumin is a combination of Cohn along with different types of chromatography. The aim of the present study was to create a concise and cost-effective albumin purification method by employing a conventional method with some modifications.

Methods: In this research, the albumin was purified from human serum using chilled ethanol, followed by chromatographic methods. The purity of harvested albumin was evaluated by cellulose acetate membrane electrophoresis (CAME) and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Western blotting (WB) analysis and thermostability were used for functional and stability measurement assessment, respectively.

Results: SDS-PAGE and CAME showed that the purity of purified human albumin was about 99%. Purified human albumin showed a single band with a molecular weight of 66 kDa. The results were validated by WB analysis .Also, the thermostability of purified albumin was same as the commercial albumin.

Conclusion: This method can be a robust technique for purification of albumin in order to use clinical and research approaches.
View Article and Find Full Text PDF

Download full-text PDF

Source
http://dx.doi.org/10.1080/15321819.2018.1531884DOI Listing
November 2018

Purification and Characterization of Bovine Serum Albumin Using Chromatographic Method.

Adv Pharm Bull 2016 Dec 22;6(4):651-654. Epub 2016 Dec 22.

Paramedical faculty, Tabriz University of Medical Sciences, Tabriz, Iran. ; Immunology Research Center, Tabriz University of Medical Sciences, Tabriz, Iran.

Albumin is an abundant protein of blood and has many biopharmaceutical applications. The aim of this study was to purify bovine serum albumin (BSA) using produced rabbit anti-BSA antibody. The polyclonal antibody was produced against the BSA in rabbits. Then, the pure BSA was injected to three white New Zealand rabbits. ELISA test was done to evaluate antibody production. After antibody purification,the purified antibody was attached to CNBr-activated sepharose and finally it was used for purification of albumin from bovine serum. Western blotting analysis was used for functional assessment of immunoaffinity purified BSA. The titer of anti-bovine albumin determined by ELISA was obtained 1: 256000. The SDS-PAGE showed up to 98% purity of isolated BSA and western blotting confirmed the BSA functionality. Purified bovine serum albumin by affinity chromatography showed a single band with molecular weight of 66 KDa. Affinity chromatography using produced rabbit anti-BSA antibody would be an economical and safe method for purification of BSA.
View Article and Find Full Text PDF

Download full-text PDF

Source
http://dx.doi.org/10.15171/apb.2016.080DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5241424PMC
December 2016

Overview of Albumin and Its Purification Methods.

Adv Pharm Bull 2016 Dec 22;6(4):495-507. Epub 2016 Dec 22.

Immunology Research Center, Tabriz University of Medical Sciences, Tabriz, Iran.; Paramedical faculty, Tabriz University of Medical Sciences, Tabriz, Iran.

As the most frequent plasma protein, albumin constitutes more than 50% of the serum proteins in healthy individuals. It has a key role in oncotic pressure maintenance and it is known as a versatile protein carrier for transportation of various endogenous and exogenous ligands. Reduced amounts of albumin in the body will lead to different kinds of diseases such as hypovolemia and hypoproteinemia. It also has various indications in shocks, burns, cardiopulmonary bypass, acute liver failure and etc. Further applications in research consist of cell culture supplement, drug delivery carrier and protein/drug stabilizer. So, the demand for albumin increased annually worldwide. Due to different applications of albumin, many efforts have been accomplished to achieve albumin during a long period of time. In this review, an overview of serum albumin and different purification methods are summarized.
View Article and Find Full Text PDF

Download full-text PDF

Source
http://dx.doi.org/10.15171/apb.2016.063DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5241407PMC
December 2016

A methodological approach for purification and characterization of human serum albumin.

J Immunoassay Immunochem 2016 ;37(6):623-35

d Immunology Research Center , Tabriz University of Medical Sciences , Tabriz , Iran.

As the most predominant protein in plasma, albumin is synthesized in the liver. Given to various applications of albumin as biopharmaceutical agent, the annual demand for it is 500 tons in the world, which is the highest in the biomedical solutions demand ranking. There exist different procedures for production of albumin. The aim of this study was the purification of human serum albumin (HSA) using immunoaffinity chromatography. After immunization of rabbits, passive immunodiffusion and indirect ELISA tests were applied for assessment of polyclonal antibody production against HSA. Purification was performed by ion exchange chromatography (IEC) and protein G affinity chromatography. The produced anti-HSA IgG was attached to the CNBR-activated Sepharose and applied for albumin purification from human serum. Western blotting (WB) analysis and heat-induced insolubility were performed for functional and stability measurement assessment of immunoaffinity purified HSA, respectively. The optimum titer of anti-HSA determined by indirect ELISA was 256000. The SDS-PAGE showed that the purity rate of albumin was approximately 98% and WB confirmed the HSA functionality. Also, the heat-induced insolubility of immunoaffinity purified HSA was the same as the commercial HSA. Affinity chromatography using produced polyclonal antibody would be a robust method for purification of HSA.
View Article and Find Full Text PDF

Download full-text PDF

Source
http://dx.doi.org/10.1080/15321819.2016.1184163DOI Listing
May 2017
-->