Proteome differences in the first- and third-trimester human placentas. 2015

Behrouz Gharesi-Fard, and Jaleh Zolghadri, and Eskandar Kamali-Sarvestani
Department of Immunology, Shiraz University of Medical Sciences, Shiraz, Iran Infertility Research Center, Shiraz University of Medical Sciences, Shiraz, Iran Proteomics Laboratory, School of Advanced Medical Sciences and Technologies, Shiraz, Iran gharesifb@sums.ac.ir.

Placenta is a transient and unique pregnancy tissue that supports the fetus nutritionally and metabolically. Expression of the unique placental proteins in different stages may influence the development of the fetus as well as the pregnancy outcome. The present study aimed to compare the total placental proteome differences between the normal first- and third-trimester human placentas. In the current study, placental proteome was compared between normal first- and third-trimester placentas using 2-dimensional polyacrylamide gel electrophoresis method for separation and matrix-assisted laser desorption/ionization time-of flight mass spectrometry technique for identification of the proteins. Despite the overall similarities, comparison of the mean intensity of the protein spots between the first- and third-trimester placental proteomes revealed that 22 spots were differentially expressed (P < .05) among which 11 distinct spots were successfully identified. Of the 11 differentially expressed proteins, 4 were increased (protein disulfide isomerase, tropomyosin 4 isoform 2, enolase 1, and 78-kDa glucose-regulated protein), while the remaining 7 (actin γ1 propeptide, heat shock protein gp96, α1-antitrypsin, EF-hand domain family member D1, tubulin α1, glutathione S-transferase, and vitamin D binding protein) showed decreased expression in the placentas from the first-trimester compared to the full-term ones. In summary, the results of the present study as the first research on the comparison of the first- and third-trimester human placental proteomes introduced a group of 11 proteins with altered expression. Interestingly, some of these proteins are reported to be altered in pregnancy-related disorders.

UI MeSH Term Description Entries
D010920 Placenta A highly vascularized mammalian fetal-maternal organ and major site of transport of oxygen, nutrients, and fetal waste products. It includes a fetal portion (CHORIONIC VILLI) derived from TROPHOBLASTS and a maternal portion (DECIDUA) derived from the uterine ENDOMETRIUM. The placenta produces an array of steroid, protein and peptide hormones (PLACENTAL HORMONES). Placentoma, Normal,Placentome,Placentas,Placentomes
D011247 Pregnancy The status during which female mammals carry their developing young (EMBRYOS or FETUSES) in utero before birth, beginning from FERTILIZATION to BIRTH. Gestation,Pregnancies
D011261 Pregnancy Trimester, First The beginning third of a human PREGNANCY, from the first day of the last normal menstrual period (MENSTRUATION) through the completion of 14 weeks (98 days) of gestation. Early Placental Phase,Pregnancy, First Trimester,Trimester, First,Early Placental Phases,First Pregnancy Trimester,First Pregnancy Trimesters,First Trimester,First Trimester Pregnancies,First Trimester Pregnancy,First Trimesters,Phase, Early Placental,Phases, Early Placental,Placental Phase, Early,Placental Phases, Early,Pregnancies, First Trimester,Pregnancy Trimesters, First,Trimesters, First
D011263 Pregnancy Trimester, Third The last third of a human PREGNANCY, from the beginning of the 29th through the 42nd completed week (197 to 294 days) of gestation. Pregnancy, Third Trimester,Trimester, Third,Last Trimester,Last Trimesters,Pregnancies, Third Trimester,Pregnancy Trimesters, Third,Third Pregnancy Trimester,Third Pregnancy Trimesters,Third Trimester,Third Trimester Pregnancies,Third Trimester Pregnancy,Third Trimesters,Trimester, Last,Trimesters, Last,Trimesters, Third
D011506 Proteins Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein. Gene Products, Protein,Gene Proteins,Protein,Protein Gene Products,Proteins, Gene
D005260 Female Females
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000328 Adult A person having attained full growth or maturity. Adults are of 19 through 44 years of age. For a person between 19 and 24 years of age, YOUNG ADULT is available. Adults
D015153 Blotting, Western Identification of proteins or peptides that have been electrophoretically separated by blot transferring from the electrophoresis gel to strips of nitrocellulose paper, followed by labeling with antibody probes. Immunoblotting, Western,Western Blotting,Western Immunoblotting,Blot, Western,Immunoblot, Western,Western Blot,Western Immunoblot,Blots, Western,Blottings, Western,Immunoblots, Western,Immunoblottings, Western,Western Blots,Western Blottings,Western Immunoblots,Western Immunoblottings
D015180 Electrophoresis, Gel, Two-Dimensional Electrophoresis in which a second perpendicular electrophoretic transport is performed on the separate components resulting from the first electrophoresis. This technique is usually performed on polyacrylamide gels. Gel Electrophoresis, Two-Dimensional,Polyacrylamide Gel Electrophoresis, Two-Dimensional,2-D Gel Electrophoresis,2-D Polyacrylamide Gel Electrophoresis,2D Gel Electrophoresis,2D PAGE,2D Polyacrylamide Gel Electrophoresis,Electrophoresis, Gel, 2-D,Electrophoresis, Gel, 2D,Electrophoresis, Gel, Two Dimensional,Polyacrylamide Gel Electrophoresis, 2-D,Polyacrylamide Gel Electrophoresis, 2D,Two Dimensional Gel Electrophoresis,2 D Gel Electrophoresis,2 D Polyacrylamide Gel Electrophoresis,Electrophoresis, 2-D Gel,Electrophoresis, 2D Gel,Electrophoresis, Two-Dimensional Gel,Gel Electrophoresis, 2-D,Gel Electrophoresis, 2D,Gel Electrophoresis, Two Dimensional,PAGE, 2D,Polyacrylamide Gel Electrophoresis, 2 D,Polyacrylamide Gel Electrophoresis, Two Dimensional,Two-Dimensional Gel Electrophoresis

Related Publications

Behrouz Gharesi-Fard, and Jaleh Zolghadri, and Eskandar Kamali-Sarvestani
April 2013, American journal of physiology. Endocrinology and metabolism,
Behrouz Gharesi-Fard, and Jaleh Zolghadri, and Eskandar Kamali-Sarvestani
July 1994, The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society,
Behrouz Gharesi-Fard, and Jaleh Zolghadri, and Eskandar Kamali-Sarvestani
January 1990, Hormone research,
Behrouz Gharesi-Fard, and Jaleh Zolghadri, and Eskandar Kamali-Sarvestani
March 2022, Biology of reproduction,
Behrouz Gharesi-Fard, and Jaleh Zolghadri, and Eskandar Kamali-Sarvestani
September 2005, Cellular and molecular biology (Noisy-le-Grand, France),
Behrouz Gharesi-Fard, and Jaleh Zolghadri, and Eskandar Kamali-Sarvestani
February 1979, The Journal of biological chemistry,
Behrouz Gharesi-Fard, and Jaleh Zolghadri, and Eskandar Kamali-Sarvestani
January 2013, Pregnancy hypertension,
Behrouz Gharesi-Fard, and Jaleh Zolghadri, and Eskandar Kamali-Sarvestani
January 2012, PloS one,
Behrouz Gharesi-Fard, and Jaleh Zolghadri, and Eskandar Kamali-Sarvestani
January 2014, PloS one,
Behrouz Gharesi-Fard, and Jaleh Zolghadri, and Eskandar Kamali-Sarvestani
January 2012, PloS one,
Copied contents to your clipboard!