Faculty Opinions recommendation of Structure of an ultraweak protein-protein complex and its crucial role in regulation of cell morphology and motility.

Excessive adipogenesis caused obesity, which was a serious risk of health and led to a series of diseases, including type II diabetes (T2D) for example. Adipocyte as the basic unit of adipose tissue has emerged as one of significant target of the treatment of obesity-related metabolic syndromes by revealed its adipogenic molecular mechanism. MicroRNAs (miRNAs) have been demonstrated involving adipogenesis, and played a crucial role in the competitive endogenous RNA (ceRNA) effect. Besides that, C/EBPα as a crucial adipogenic regulator still lacked epigenetic explanation during pre-adipocyte adipogenesis. In this study, we first verified FoxO1 was one of the ceRNA of C/EBPα. They co-regulated adipogenesis through formed a protein complex that directly bound to its promoter to activate AdipoQ, and AdipoQ (Adiponectin) was a negative adipocytokines that suppressed adipogenesis, which played an important role in retaining adipogensis balance. Moreover, an adipose tissue specific enriched miRNA, miR-144 was the key regulator of the ceRNA effect between C/EBPα and FoxO1, which mediated the C/EBPα-FoxO1 complex formation, thus altered AdipoQ, furthermore regulated pre-adipocyte adipogenesis. This research will provide a new supplementary idea of the C/EBPα epigenetic role in pre-adipocyte adipogenesis.

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Functions of Plexins/Neuropilins and Their Ligands during Hippocampal Development and Neurodegeneration

Cells ◽

10.3390/cells8030206 ◽

2019 ◽

Vol 8 (3) ◽

pp. 206 ◽

Cited By ~ 4

Author(s):

Vanessa Gil ◽

José del Río

Keyword(s):

Nervous System ◽

Cell Migration ◽

Cell Morphology ◽

Crucial Role ◽

Hippocampal Formation ◽

Vascular Development ◽

Memory And Learning ◽

Signaling Mechanisms ◽

Cellular Cytoskeleton ◽

Prime Target

There is emerging evidence that molecules, receptors, and signaling mechanisms involved in vascular development also play crucial roles during the development of the nervous system. Among others, specific semaphorins and their receptors (neuropilins and plexins) have, in recent years, attracted the attention of researchers due to their pleiotropy of functions. Their functions, mainly associated with control of the cellular cytoskeleton, include control of cell migration, cell morphology, and synapse remodeling. Here, we will focus on their roles in the hippocampal formation that plays a crucial role in memory and learning as it is a prime target during neurodegeneration.

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A Microtiter Assay for Quantifying Protein-Protein Interactions Associated with Cell-Cell Adhesion

CrossRef Listing of Deleted DOIs ◽

10.1177/1087057107301941 ◽

2007 ◽

Vol 12 (5) ◽

pp. 683-693 ◽

Cited By ~ 2

Author(s):

Nicholas A. Graham ◽

Melissa D. Pope ◽

Tharathorn Rimchala ◽

Beijing K. Huang ◽

Anand R. Asthagiri

Keyword(s):

Protein Complex ◽

Crucial Role ◽

Cell Biology ◽

Transmembrane Protein ◽

Critical Role ◽

Enzyme Linked Immunosorbent Assay ◽

Dramatic Improvement ◽

E Cadherin ◽

Cell Cell

Cell-cell adhesions are a hallmark of epithelial tissues, and the disruption of these contacts plays a critical role in both the early and late stages of oncogenesis. The interaction between the transmembrane protein E-cadherin and the intracellular protein β-catenin plays a crucial role in the formation and maintenance of epithelial cell-cell contacts and is known to be downregulated in many cancers. The authors have developed a protein complex enzyme-linked immunosorbent assay (ELISA) that can quantify the amount of β-catenin bound to E-cadherin in unpurified whole-cell lysates with a Z′ factor of 0.74. The quantitative nature of the E-cadherin:β-catenin ELISA represents a dramatic improvement over the low-throughput assays currently used to characterize endogenous E-cadherin:β-catenin complexes. In addition, the protein complex ELISA format is compatible with standard sandwich ELISAs for parallel measurements of total levels of endogenous E-cadherin and β-catenin. In 2 case studies closely related to cancer cell biology, the authors use the protein complex ELISA and traditional sandwich ELISAs to provide a detailed, quantitative picture of the molecular changes occurring within adherens junctions in vivo. Because the E-cadherin: β-catenin protein complex plays a crucial role in oncogenesis, this protein complex ELISA may prove to be a valuable quantitative prognostic marker of tumor progression. ( Journal of Biomolecular Screening 2007:683-693)

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Author response for "Differential temporal and spatial post‐injury alterations in cerebral cell morphology and viability"

10.1002/cne.24955/v3/response1 ◽

2020 ◽

Author(s):

Zareen Amtul ◽

Abdullah N. Najdat ◽

David J. Hill ◽

Edith J. Arany

Keyword(s):

Cell Morphology ◽

Author Response ◽

Post Injury ◽

Temporal And Spatial

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Cell morphology, volume, and surface area determinations from multilevel contouring within HVEM micrographs of serial sections and whole-cell mounts

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100127426 ◽

1987 ◽

Vol 45 ◽

pp. 588-589

Author(s):

M. Marko ◽

A. Leith ◽

D. Parsons

Keyword(s):

Surface Area ◽

Electron Micrographs ◽

Cell Morphology ◽

Individual Variation ◽

Serial Section ◽

Stereo Pair ◽

Complex Structures ◽

Serial Sections ◽

Surface Areas ◽

Computer Based

The use of serial sections and computer-based 3-D reconstruction techniques affords an opportunity not only to visualize the shape and distribution of the structures being studied, but also to determine their volumes and surface areas. Up until now, this has been done using serial ultrathin sections.The serial-section approach differs from the stereo logical methods of Weibel in that it is based on the Information from a set of single, complete cells (or organelles) rather than on a random 2-dimensional sampling of a population of cells. Because of this, it can more easily provide absolute values of volume and surface area, especially for highly-complex structures. It also allows study of individual variation among the cells, and study of structures which occur only infrequently.We have developed a system for 3-D reconstruction of objects from stereo-pair electron micrographs of thick specimens.

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High-Resolution electron crystallography of the light-harvesting chlorophyll-a/b protein complex from chloroplast membranes

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100181816 ◽

1990 ◽

Vol 48 (1) ◽

pp. 610-610

Author(s):

Werner Kühlbrandt ◽

Da Neng Wang ◽

K.H. Downing

Keyword(s):

High Resolution ◽

Electron Diffraction ◽

Chlorophyll A ◽

Protein Complex ◽

Structural Integrity ◽

Light Harvesting ◽

Lhc Ii ◽

Diffraction Patterns ◽

Difference Fourier ◽

2D Crystals

The light-harvesting chlorophyll-a/b protein complex (LHC-II) is the most abundant membrane protein in the chloroplasts of green plants where it functions as a molecular antenna of solar energy for photosynthesis. We have grown two-dimensional (2d) crystals of the purified, detergent-solubilized LHC-II . The crystals which measured 5 to 10 μm in diameter were stabilized for electron microscopy by washing with a 0.5% solution of tannin. Electron diffraction patterns of untilted 2d crystals cooled to 130 K showed sharp spots to 3.1 Å resolution. Spot-scan images of 2d crystals were recorded at 160 K with the Berkeley microscope . Images of untilted crystals were processed, using the unbending procedure by Henderson et al . A projection map of the complex at 3.7Å resolution was generated from electron diffraction amplitudes and high-resolution phases obtained by image processing .A difference Fourier analysis with the same image phases and electron diffraction amplitudes recorded of frozen, hydrated specimens showed no significant differences in the 3.7Å projection map. Our tannin treatment therefore does not affect the structural integrity of the complex.

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Use of Antibody to aid Visualization of Protein at the Termini of Bacteriophage Ø29 DNA

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s1431927600002385 ◽

1980 ◽

Vol 38 ◽

pp. 540-541

Author(s):

Dwight Anderson ◽

Charlene Peterson ◽

Gursaran Notani ◽

Bernard Reilly

Keyword(s):

Electron Microscopy ◽

Bacillus Subtilis ◽

Dna Synthesis ◽

Restriction Endonuclease ◽

Protein Complex ◽

Protein Product ◽

Viral Dna ◽

Small Proteins ◽

Antibody Labeling ◽

Subtilis Bacteriophage

The protein product of cistron 3 of Bacillus subtilis bacteriophage Ø29 is essential for viral DNA synthesis and is covalently bound to the 5’-termini of the Ø29 DNA. When the DNA-protein complex is cleaved with a restriction endonuclease, the protein is bound to the two terminal fragments. The 28,000 dalton protein can be visualized by electron microscopy as a small dot and often is seen only when two ends are in apposition as in multimers or in glutaraldehyde-fixed aggregates. We sought to improve the visibility of these small proteins by use of antibody labeling.

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