In-situ particle segmentation approach based on average background modeling and graph-cut for the monitoring of l -glutamic acid crystallization

2018 ◽  
Vol 178 ◽  
pp. 11-23 ◽  
Author(s):  
Zhi M. Lu ◽  
Fan C. Zhu ◽  
Xue Y. Gao ◽  
Bing C. Chen ◽  
Zhen G. Gao
Keyword(s):  
Glutamic Acid ◽  
Graph Cut ◽  
Background Modeling ◽  
Segmentation Approach ◽  
Particle Segmentation

scholarly journals Fabrication of injectable hydrogels based on poly(l-glutamic acid) and chitosan

RSC Advances ◽  
2017 ◽  
Vol 7 (28) ◽  
pp. 17005-17019 ◽  
Author(s):  
Shifeng Yan ◽  
Taotao Wang ◽  
Xing Li ◽  
Yuhang Jian ◽  
Kunxi Zhang ◽  
...  
Keyword(s):  
Schiff Base ◽  
Glutamic Acid ◽  
Crosslinking Reaction ◽  
Injectable Hydrogels ◽  
Oppositely Charged

The in situ forming hydrogels based on oppositely charged poly(l-glutamic acid) (PLGA) and chitosan (CS) were prepared via a Schiff base crosslinking reaction.

A highly sensitive glutamic acid biosensor based on the determination of NADH enzymically generated by l-glutamic dehydrogenase

RSC Advances ◽  
2016 ◽  
Vol 6 (51) ◽  
pp. 45829-45834 ◽  
Author(s):  
Xia Lin ◽  
Qinghong Wang ◽  
Shu Zhu ◽  
Juanjuan Xu ◽  
Qiao Xia ◽  
...  
Keyword(s):  
Glutamic Acid ◽  
Highly Sensitive ◽  
Glutamic Dehydrogenase

In this article, a sensitive and stereo-selective biosensor for l-glutamic acid (l-Glu) based on the electrochemiluminescence (ECL) of Ru(bpy)32+ has been designed by applying l-glutamic dehydrogenase (GLDH) for enzymatic generation of NADH in situ.

Injectable In Situ Self-Cross-Linking Hydrogels Based on Poly(l-glutamic acid) and Alginate for Cartilage Tissue Engineering

2014 ◽  
Vol 15 (12) ◽  
pp. 4495-4508 ◽  
Author(s):  
Shifeng Yan ◽  
Taotao Wang ◽  
Long Feng ◽  
Jie Zhu ◽  
Kunxi Zhang ◽  
...  
Keyword(s):  
Tissue Engineering ◽  
Glutamic Acid ◽  
Cartilage Tissue Engineering ◽  
Cartilage Tissue ◽  
Cross Linking

Poly (γ-glutamic acid)/beta-TCP nanocomposites via in situ copolymerization: Preparation and characterization

2016 ◽  
Vol 31 (1) ◽  
pp. 102-111 ◽  
Author(s):  
Xiu-lin Shu ◽  
Qing-shan Shi ◽  
Jin Feng ◽  
Yun-hua Yang ◽  
Gang Zhou ◽  
...  
Keyword(s):  
Glutamic Acid ◽  
In Situ Copolymerization

scholarly journals Modulation of in Situ Estrogen Synthesis by Proline-, Glutamic Acid-, and Leucine-Rich Protein-1: Potential Estrogen Receptor Autocrine Signaling Loop in Breast Cancer Cells

2008 ◽  
Vol 22 (3) ◽  
pp. 649-664 ◽  
Author(s):  
Rajib Rajhans ◽  
Hareesh B. Nair ◽  
Sujit S. Nair ◽  
Valerie Cortez ◽  
Kijima Ikuko ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Estrogen Receptor ◽  
Glutamic Acid ◽  
Cancer Cells ◽  
Breast Cancer Cells ◽  
Breast Tumors ◽  
Aromatase Activity ◽  
Aromatase Expression ◽  
Estrogen Synthesis

Abstract In situ estrogen synthesis is implicated in tumor cell proliferation through autocrine or paracrine mechanisms especially in postmenopausal women. Several recent studies demonstrated activity of aromatase, an enzyme that plays a critical role in estrogen synthesis in breast tumors. Proline-, glutamic acid-, and leucine-rich protein-1 (PELP1/MNAR) is an estrogen receptor (ER) coregulator, and its expression is deregulated in breast tumors. In this study, we examined whether PELP1 promotes tumor growth by promoting local estrogen synthesis using breast cancer cells (MCF7) that stably overexpress PELP1. Immunohistochemistry revealed increased aromatase expression in MCF7-PELP1-induced xenograft tumors. Real-time PCR analysis showed enhanced activation of the aromatase promoter in MCF7-PELP1 clones compared with MCF7 cells. Using a tritiated-water release assay, we demonstrated that MCF7-PELP1 clones exhibit increased aromatase activity compared with control MCF-7 cells. PELP1 deregulation uniquely up-regulated aromatase expression via activation of aromatase promoter I.3/II, and growth factor signaling enhanced PELP1 activation of aromatase. PELP1-mediated induction of aromatase requires functional Src and phosphatidylinositol-3-kinase pathways. Mechanistic studies revealed that PELP1 interactions with ER-related receptor-α and proline-rich nuclear receptor coregulatory protein 2 lead to activation of aromatase. Immunohistochemistry analysis of breast tumor array showed increased expression of aromatase in ductal carcinoma in situ and node-positive tumors compared with no or weak expression in normal breast tissue. Fifty-four percent (n = 79) of PELP1-overexpressing tumors also overexpressed aromatase compared with 36% (n = 47) in PELP1 low-expressing tumors. Our results suggest that PELP1 regulation of aromatase represents a novel mechanism for in situ estrogen synthesis leading to tumor proliferation by autocrine loop and open a new avenue for ablating local aromatase activity in breast tumors.

scholarly journals Chromosomal organization and expression analysis of two distinct genes encoding glutamine/glutamic acid-rich proteins

1997 ◽  
Vol 324 (1) ◽  
pp. 177-184 ◽  
Author(s):  
Kelly G. TEN HAGEN ◽  
Thomas M. BERES ◽  
Josiane SZPIRER ◽  
Claude SZPIRER ◽  
Lawrence A. TABAK
Keyword(s):  
Glutamic Acid ◽  
Submandibular Gland ◽  
Fluorescent In Situ Hybridization ◽  
Tandem Repeats ◽  
Pcr Analysis ◽  
Chromosome 4 ◽  
Hybrid Analysis ◽  
Adrenergic Agonist ◽  
Genes Encoding

GRP-Ca and GRP-Cb are two genes that encode glutamine/glutamic acid-rich proteins of the rat. These genes are very similar in structure and sequence, differing only within an approx. 90 bp segment of exon 3. We have used distinct oligonucleotide probes to unambiguously distinguish GRP-Ca and GRP-Cb gene expression. The two genes are expressed to relatively equivalent levels only in the submandibular gland. Chronic daily exposure to the β-adrenergic agonist, isoprenaline, resulted in a statistically significant decrease in GRP-Ca expression, with no effect on GRP-Cb, in contrast with previous reports. Furthermore it was determined by PCR analysis of both submandibular-gland cDNA and genomic DNA that the GRP-Cb gene shows interanimal variability in the number of 69 bp tandem repeats found within exon 3; GRP-Cb genes were shown to contain four, five or six repeats. GRP-Ca shows no such variability, containing only five tandem repeats in all animals examined. The two genes were localized to within 450 kb of one another at q43-q44 of rat chromosome 4 using somatic cell hybrid analysis, pulsed-field gel analysis and fluorescent in situ hybridization.

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