scholarly journals The lungfish cocoon is a living tissue with antimicrobial functions

2021 ◽  
Vol 7 (47) ◽  
Author(s):  
Ryan Darby Heimroth ◽  
Elisa Casadei ◽  
Ottavia Benedicenti ◽  
Chris Tsuyoshi Amemiya ◽  
Pilar Muñoz ◽  
...  
Keyword(s):  
Nature ◽  
2002 ◽  
Author(s):  
Philip Ball
Keyword(s):  

2021 ◽  
Vol 22 (3) ◽  
pp. 1085
Author(s):  
Aneeqa Noor ◽  
Saima Zafar ◽  
Inga Zerr

Proteinopathy refers to a group of disorders defined by depositions of amyloids within living tissue. Neurodegenerative proteinopathies, including Alzheimer’s disease, Parkinson’s disease, Creutzfeldt–Jakob disease, and others, constitute a large fraction of these disorders. Amyloids are highly insoluble, ordered, stable, beta-sheet rich proteins. The emerging theory about the pathophysiology of neurodegenerative proteinopathies suggests that the primary amyloid-forming proteins, also known as the prion-like proteins, may exist as multiple proteoforms that contribute differentially towards the disease prognosis. It is therefore necessary to resolve these disorders on the level of proteoforms rather than the proteome. The transient and hydrophobic nature of amyloid-forming proteins and the minor post-translational alterations that lead to the formation of proteoforms require the use of highly sensitive and specialized techniques. Several conventional techniques, like gel electrophoresis and conventional mass spectrometry, have been modified to accommodate the proteoform theory and prion-like proteins. Several new ones, like imaging mass spectrometry, have also emerged. This review aims to discuss the proteoform theory of neurodegenerative disorders along with the utility of these proteomic techniques for the study of highly insoluble proteins and their associated proteoforms.


NeuroImage ◽  
2002 ◽  
Vol 17 (3) ◽  
pp. 1649-1657 ◽  
Author(s):  
Lee J. Johnson ◽  
William Chung ◽  
Daniel F. Hanley ◽  
Nitish V. Thakor

Author(s):  
John Dougherty ◽  
Emily Schaefer ◽  
Kalyani Nair ◽  
Joseph Kelly ◽  
Alfonse Masi

The MyotonPro® (Myoton AS, Tallinn, Estonia) is commonly used to quantify stiffness properties of living tissues in situ. Current studies quantify the dynamic stiffness properties of living tissues, but do not validate or compare these measurements to a standardized method. Additionally, living tissue, being dynamic in nature, presents much variability in data collection. To address these issues this study focuses on the repeatability and reproducibility of the MyotonPro® on polymeric gel-based tissue phantoms. In addition, a correlation study is also performed to translate dynamic stiffness to a more standardized property, Young’s modulus. Such studies help to confirm the reliability of the measurements obtained in situ.


2012 ◽  
Vol 44 (12) ◽  
pp. 651-656 ◽  
Author(s):  
S. Ellefsen ◽  
M. Bliksøen ◽  
A. Rutkovskiy ◽  
I. B. Johansen ◽  
M.-L. Kaljusto ◽  
...  

In studies of gene expression in acute ischemic heart tissue, internal reference genes need to show stable expression per-unit-living tissue to hinder dead cells from biasing real-time RT-PCR data. Until now, this important issue has not been appropriately investigated. We hypothesized that the expression of seven internal reference genes would show stable per-unit-living tissue expression in Langendorff-perfused rat hearts subjected to ischemia-reperfusion. This was found for cyclophilin A, GAPDH, RPL-32, and PolR2A mRNA, with GAPDH showing the highest degree of stability ( R = 0.11), suggesting unchanged rates of mRNA transcription in live cells and complete degradation of mRNA from dead cells. The infarct size-dependent degradation of GAPDH was further supported by a close correlation between changes in GAPDH mRNA and changes in RNA quality measured as RNA integrity number (R = 0.90, P < 0.05). In contrast, β-actin and 18S rRNA showed stable expression per-unit-weight tissue and a positive correlation with infarct size (R = 0.61 and R = 0.77, P < 0.05 for both analyses). The amount of total RNA extracted per-unit-weight tissue did not differ between groups despite wide variation in infarct size (7.1–50.1%). When β-actin expression was assessed using four different normalization strategies, GAPDH and geNorm provided appropriate per-unit-living expression, while 18S and total RNA resulted in marked underestimations. In studies of ischemic tissues, we recommend using geometric averaging of carefully selected reference genes for normalization of real-time RT-PCR data. A marked shift in the mRNA/rRNA ratio renders rRNA as useless for normalization purposes.


Author(s):  
Danil Dobrynin ◽  
Sameer Kalghatgi ◽  
Gregory Fridman ◽  
Andrew Wu ◽  
Erica Podolsky ◽  
...  

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