bluuebunny/crossref_metadata_2025_split huggingface dataset:
A complex scalenus muscle variant: Case report
Authors: Miller Joseph M. A. , Trelease Robert B. 
Published: June 2021

During dissection in a first year dental gross anatomy laboratory, we identified an unusual, complex muscle variant in the left posterior triangle of an 87 year‐old, Caucasian female cadaver. This consisted of the left anterior scalene divided longitudinally into two approximately equal ‘heads', superficial and deep, with the fifth and sixth cervical nerve roots passing between them, along with a small but substantial muscle bundle passing between and attaching to portions of the anterior and middle scalene muscles. This extra muscle bundle passed antero‐medially from the middle of the anterior surface of the middle scalene, to attach inferiorly on the superficial aspect of the deep head of the anterior scalene. This ‘bridging’ muscle also passed anterior to and in contact with the middle trunk (C7) of the brachial plexus. The left subclavian artery was observed to pass as expected between the anterior scalene (both superficial and deep heads) and middle scalene insertions. Scalene muscle anatomy and neurovascular relationships on the right side were observed to be normal. Amidst the numerous reports of morphological variations in scalene muscles, particularly in association with the clinical anatomy of thoracic outlet syndrome, myofascial pain, and upper brachial plexopathies, we were unable to find any accounts of a similar complex scalene muscle variant. Most certainly, our specimen did not fit the accepted morphological descriptions of ‘scalenus anticus', scalenus minimus, or Sibson's muscle variants. Although we had no available clinical records, the muscular variations we described were arranged in configurations that other investigators have recognized as contributing to compression of brachial plexus roots associated with thoracic outlet syndrome.This abstract is from the Experimental Biology 2018 Meeting. There is no full text article associated with this abstract published in The FASEB Journal.
TOPOGRAPHICAL ANATOMY OF THE ULNAR NERVE AND ITS MUSCULAR BRANCHES RELATED TO SURFACE LANDMARK
Authors: Galdeano Denival Soares , Cricenti Vicente S. 
Published: June 2021

Understanding of the anatomy of the ulnar nerve and its branches is vital to the treatment of cubital tunnel syndrome, tennis elbow, ulnar neuropathy, nerve transfer in the surgical management of compression at the elbow, tennis elbow or the restoration of upper extremity function. In the search to add details and pertinent information and ulnar nerve in the region of the forearm, we carry out this work. We have dissected 30 upper extremities from adult cadavers to locate the course of the ulnar nerve and the origins and insertions of the branches of the ulnar nerve using elbow joint like surface landmark. In average, 2.7 (max. 4) branches left the ulnar nerve to Flexor Carpi Ulnaris. 60.24% arose the nerve above elbow joint (AEJ) (−59.21mm above), 30.12% origins in the Proximal Upper Third (PUT) of forearm, 4.82% origin in Distal Upper Third (DUT) and 4.82% in the Proximal Middle Third (PMT), being the most distal origin 100.90 mm below the elbow joint. These branches reach the muscle belly in average in 6 points (max 15). The most proximal penetrated AEJ in 8.29% (−15.31 mm above), 56.91% in PUT, 19.89 % in DUT, 12.7 % in PMT and 2.21% in DMT with the most distal to 132.25 mm below the elbow joint. To Flexor Digitorum Profundus, in average 1.17 (max. 2) branches left the ulnar nerve to muscle. 31.42% left the nerve AEJ (−18.31 mm above), 65.71% in the PUT and 2.87% in DUT, being the most distal origin in 39.13 mm below the elbow joint. These branches penetrated in the muscle belly in average in 3.1 points (max 5). The most proximal penetrated in 52.69% in PUT (4.86 mm), 45.16 % in DUT and 2.15 % in PMT with the most distal 84.09 mm below the elbow joint. In this study we found 5(five) Martin‐Gruber Anastomosis. Using these data, the course of the branches of the ulnar nerve can be estimated by observing the surface of the elbow joint.Support or Funding InformationnoneThis abstract is from the Experimental Biology 2018 Meeting. There is no full text article associated with this abstract published in The FASEB Journal.
Associations Between External Forearm Dimensions and Internal Ulnar Nerve Spaces at the Elbow
Authors: Kanwar Kiran , Khan Mustafa Tamim Alam , Khan Tasrif Alam , Khan Mahwish Iqbal , Lovely Rehana Sultana 
Published: June 2021

Ulnar nerve injury is frequently seen in athletes such as golfers, baseball pitchers, tennis players and weightlifters, typically in the epicondylar groove or cubital tunnel areas, where it may be subjected to compression, traction and friction during certain rapid sports movements. A relationship between the dimensions of some visually easy‐to‐discern external structures of the forearm, and selected internal elbow structures that the ulnar nerve passes through, might help to predict which sportspersons may be at greater risk for ulnar nerve entrapment, with smaller spaces expected to involve greater risk. Two conspicuous external features are the distance between the olecranon of the ulna (OL) and the medial epicondyle of the humerus (ME); and forearm length measured from the ME to the pisiform carpal bone (PI). It was hypothesized that a positive correlation would exist between either one, or both of, OL‐ME (medial forearm width) and ME‐PI (forearm length); and some or all of: ulnar nerve thickness, inner epicondylar space, OL‐ME line to Osborne ligament, and OL‐ME line to the point of entry of the ulnar nerve into the flexor carpi ulnaris muscle, between its humeral and ulnar heads. Twenty cadavers, ten male and ten female (40 forearms) were measured for the above dimensions, using digital calipers and tape. Forearms were maintained at 30° flexion (measured with a digital goniometer). The most prominent part of the crest of each of ME, OL and PI was used, and the average of three measurements was taken for each variable. A Spearman's correlation (SPSS ver. 24), used for non‐normally distributed data, showed that the inner width of the epicondylar groove was significantly related to the external OL to ME distance (r = .403, p = .01) and to the thickness of the ulnar nerve at the OL‐ME line (r = .32, p = .047). In addition, the distance between ME and PI was significantly correlated with the external OL to ME distance (r = .62, p < .001). It may be concluded that the distance between the OL and the ME, as well as the length of the forearm, might be good indicators of the likely internal space that the ulnar nerve is contained within at the OL‐ME line, as well as of the thickness of the ulnar nerve at that line.This abstract is from the Experimental Biology 2018 Meeting. There is no full text article associated with this abstract published in The FASEB Journal.
Enhancer epigenomic regulation in differentiation, development and cancer
Authors: Ge Kai 
Published: June 2021

Enhancers control cell type‐specific gene expression and are marked by H3K4me1. Active enhancers are further marked by H3K27ac. We previously identified CBP/p300 as major H3K27 acetyltransferases and MLL3/MLL4 as major enhancer H3K4me1 methyltransferases [1, 2]. We show that during differentiation of adipocytes, myocytes and ES cells, MLL3/MLL4 are required for enhancer activation, cell type‐specific gene expression, and cell differentiation [2, 3]. Further, we show that while enhancer‐priming by MLL3/MLL4 is dispensable for cell identity maintenance, it controls cell fate transition by orchestrating CBP/p300‐mediated enhancer activation. MLL4 protein, rather than MLL4‐mediated H3K4me1, controls p300 recruitment to enhancers [3, 4].Our data suggest a model of sequential actions of epigenomic regulators on enhancers: 1) pioneer TFs and lineage‐determining TFs recruit MLL3/MLL4 to prime enhancer regions and label them with H3K4me1; 2) MLL3/MLL4 facilitate the binding of CBP/p300, which activate enhancers and label them with H3K27ac; 3) H3K27ac and acetylated TFs are recognized by the epigenomic reader Brd4, which recruits Mediator and RNA Pol II to establish enhancer‐promoter interactions and activate cell type‐specific genes (Nat Comm, in press).MLL3/MLL4 are tumor suppressors frequently mutated in many types of cancers as well as developmental diseases. We show that MLL3/MLL4 are required for the development of adipose, muscle, mammary gland, B cells, T cells, and heart and that depletion of MLL3/MLL4 in mice promotes tumorigenesis [2, 5–9]. Our findings suggest that mutations in MLL3/MLL4 would lead to defects in enhancer activation, cell type‐specific gene expression and cell differentiation. Such a mechanism may contribute to the pathogenesis of these developmental diseases and cancers.Support or Funding InformationThis work was supported by the Intramural Research Program of the NIDDK, NIH.This abstract is from the Experimental Biology 2018 Meeting. There is no full text article associated with this abstract published in The FASEB Journal.
Exploring a transcriptional regulation model governing a cis‐antisense small RNA in Vibrio cholerae
Authors: Zhang Mark Guangde , Wang Jessica J. , Lang Theodore , Liu Jane M. 
Published: June 2021

Cholera disease, a gastrointestinal ailment caused by the Gram‐negative bacterium Vibrio cholerae, remains a global health burden affecting an estimated 3–5 million people annually. V. cholerae's capacity to persist in different environments stems from its adaptability to a variety of sugar sources, including the six‐carbon sugar alcohol mannitol. Produced by algae metabolism, mannitol is transported into V. cholerae through the mannitol transporter MtlA, whose production is downregulated at the post‐transcriptional level by the small RNA (sRNA) MtlS. Currently, little is known surrounding what governs the transcription of mtlS, other than that mtlS expression is equally robust in non‐mannitol sugars. We examined the hypothesis that mtlS expression is subject to transcriptional interference from the divergently transcribed mtlA. Because MtlS is a cis‐encoded sRNA transcribed directly antisense to mtlA, transcriptional activity from mtlA could pose a hindrance to mtlS transcription occurring in the opposite direction. To test this model, we grew V. cholerae in different sugar conditions and stimulated mtlA expression by knocking out mtlR (a transcriptional repressor of mtlA) or by adding exogenous mannitol. We then measured MtlS sRNA levels by northern blot analysis. Our results indicate a strict inverse relationship between mtlA expression and mtlS expression, whereby the degree to which mtlA expression increases correlates with the extent to which mtlS expression decreases. In glucose, knocking out mtlR restores MtlA levels to 30% of maximum expression (n=3, p<0.05) and decreases MtlS levels by 33% (n=2, p=0.1). In non‐mannitol, non‐glucose sugars such as mannose, knocking out mtlR restores MtlA levels to 50% of maximum expression (n=3, p<0.05) and decreases MtlS levels by nearly 95% (n=3, p<0.01). These findings support a transcriptional regulation model regarding cis‐antisense RNAs, known as the transcriptional interference model, for which there exist few characterized examples. Ultimately, this project has contributed to our understanding of how V. cholerae deploy sRNAs as an adaptive mechanism to buffer against environmental flux.Support or Funding InformationNIH R15 AI090606This abstract is from the Experimental Biology 2018 Meeting. There is no full text article associated with this abstract published in The FASEB Journal.
Determining the Effects of N‐Terminal Acetylation on the Microtubule‐associated Protein Tau
Authors: Lally Anna , Holmes William 
Published: June 2021

The microtubule‐associated protein tau is notably associated with neurodegenerative diseases such as Alzheimer's Disease and more recently the disease found in deceased NFL players, Chronic Traumatic Encephalopathy (CTE). Aggregation of the protein tau causes these diseases, which endogenously stabilizes microtubules in neurons. Tau is a target for the most common mammalian post‐translational modification (PTM), N‐terminal acetylation. This modification alters the structure of a protein by changing the positive N‐terminus to a neutral one by adding an acetyl functional group. Any alteration to the structure of a protein also affects the function, and the N‐terminus of tau has been implicated with aggregation rates. Since tau and N‐terminal acetylation have never been studied together before, the effects are unknown. Historically, tau has been efficiently expressed and purified out of Escherichia coli and studied in vitro, however, N‐terminal acetylation is a eukaryotic specific PTM, but occurs in a prokaryotic system when the catalytic acetyltransferase complex is co‐expressed with tau. This project determines the effects of N‐terminal acetylation on the microtubule‐associated protein tau by assessing the differences between acetylated and unacetylated tau. Expression, purification, and precipitation of tau with around 98% purity occurs by lysing and boiling samples. Various tests determine that tau is N‐terminally acetylated, estimated by SDS‐PAGE and Western blot, and confirmed by mass spectrometry and isoelectric gel electrophoresis. Furthermore, various environments can have an effect on aggregation, and exposing fibers made from the purified protein to different stressors can give insight into optimized aggregation conditions. Increased amounts of thioflavin T evaluates aggregation, an assay measured by florescent spectroscopy. Also, tubulin stability in the presence of acetylated and unacetylated tau can give insight into microtubule stability in the cell. The microtubule‐associated protein tau has been widely associated with neurodegenerative diseases because of its tendency to aggregate. Proteins aggregate because of their structure, so exploring structural and functional changes to tau is important to understanding why it aggregates. This system looks specifically at one post‐translational modification and how it affects the protein tau, and studying tau with the correct PTMs will give a more correct understanding of the protein, and by extension the neurodegenerative diseases it causes.Support or Funding InformationRI‐INBREThis abstract is from the Experimental Biology 2018 Meeting. There is no full text article associated with this abstract published in The FASEB Journal.
Expression and Purification of human Neuronal PAS domain protein 2 (hNPAS2)
Authors: Moriel Karla , Xi Dongman , Sarabia Alejandro , Chauhan Neha , Ray Supriyo , Xiao Chuan 
Published: June 2021

The circadian rhythm is an internal clock responsible for a variety of physiological processes occurring within a 24‐hour cycle. Synchronized by a master clock in the brain, the circadian rhythm consists of a transcriptional‐translational feedback loop (TTFL) capable of inducing oscillating gene expression in all the cells throughout the organism. The TTFL begins with the heterodimerization of two transcription factors, BMAL1 and CLOCK, resulting in the transcription and translation of many circadian‐related genes. The target protein of interest, human neuronal PAS domain protein 2 (hNPAS2) is a paralog of CLOCK that can serve as a positive regulator of the circadian rhythm by heterodimerizing with BMAL1. Previous research suggests that disruption in the expression of hNPAS2 may result in improper circadian functioning and development of sleeping and mental disorders. In this study, the full‐length eukaryotic form of hNPAS2 was cloned into a bacterial expression vector. However, bacterial expression has led to misfolding and aggregation of the recombinant hNPAS2, becoming the central issue of the study. In an effort to obtain soluble and homogeneous hNPAS2, multiple expression and purification methods have been developed. The resultant purified soluble protein will enable future structural and functional studies, which can bring new insights to the regulatory mechanisms of the circadian rhythm and understanding of circadian‐related disorders. Additionally, a portion of this research was integrated into a teaching module delivered by the leading student researcher to a senior undergraduate advanced biochemistry course. Multiple novel pedagogic techniques were employed in the teaching module with the objective of raising the students' interests to research as well as their abilities to apply the principles and concepts of biochemistry learned in the course in a real scientific study.Support or Funding InformationResearch reported in this poster was supported by the National Institute of General medical Sciences of the National Institutes of Health under linked Award Numbers RL5GM118969, TL4GM118971, AND UL1GM118970. The content is solely the responsibility of the authors and does not necessarily represent the official views of the National Institutes of Health Research reported in this poster was supported by the National Research of General Medical Sciences of NIH under award number SC3GM109870 Research reported in this poster was supported has used core facility at BBRC supported by National Institute of Minority Health and Health Disparities under award number 5G12MD007592This abstract is from the Experimental Biology 2018 Meeting. There is no full text article associated with this abstract published in The FASEB Journal.
The IAPP Toxicity on Rats, Raccoons and Degus in HeLa Cells
Authors: Munoz Crystabel 
Published: June 2021

Type 2 diabetes is the most common form of diabetes, where the body suffers from insulin resistance. The islet amyloid polypeptide (IAPP) is a secretory product of beta cells in pancreatic islets of Langerhans that also inhibits glucagon and insulin secretion. The aggregation of IAPP is present in pancreatic islet amyloid deposits seen especially in Type 2 diabetes, in humans and other mammalian species. The objective of this study was to determine the effects of the animal toxicity on mammalian cells. In this work, the human IAPP sequence and the effect on mammalian cells was compared to the IAPP from degu, rat, and raccoon. Molecular techniques such as MTT and LDH Cytotoxicity assay were used to test the effect of human and animal IAPP on HeLa cells. The MTT results show a consistent drop in cell viability as the concentration of IAPP from a human, degu, rat and raccoon increases. LDH cytotoxicity shows the highest toxicity in human IAPP compared to the rest of the studied animals. Although when mixing both the human and animal IAPPs, the toxicity of the human IAPP decreased whereas the viability had no significant effect. Further molecular analysis is necessary to determine the correlation between animal IAPP toxicity and the incidence of Type 2 diabetes.This abstract is from the Experimental Biology 2018 Meeting. There is no full text article associated with this abstract published in The FASEB Journal.
A Catalytic Null Splice Variant of Human Leucyl‐tRNA Synthetase with Enhanced Non‐Canonical Function
Authors: Forsyth Connor Mackenzie , Baymiller Maxwell , Martinis Susan A. 
Published: June 2021

At the center of translation are the ancient and essential aminoacyl‐tRNA synthetases (AARS). These proteins set the genetic code by attaching amino acids to their cognate tRNAs with very high accuracy. Over a lengthy evolutionary time, AARS have developed functions beyond aminoacylation through the addition of new domains and repurposing of existing structural motifs. Non‐canonical functions of AARS are especially widespread in eukaryotes and range from cell signaling to transcription and translation regulation. For example, human cytoplasmic leucyl‐tRNA synthetase (LeuRS) has been adapted as an intracellular leucine sensor for the mammalian target of the rapamycin complex 1 (mTORC1) master regulatory pathway (Han, 2012). Ten alternatively‐spliced variants of cytoplasmic LeuRS were identified in humans using RNA Seq (Lo, 2014). It is possible that each of these splice variants contributes to novel and idiosyncratic functions. We have found that one of these variants, LeuRS AS04, is overexpressed in both Jurkat T cells and peripheral blood mononuclear cells (PBMC), suggesting a potential immune‐cell specific role. Despite the absence of key catalytic residues, LeuRS AS04 is a potent and specific activator of mTORC1. In particular, downstream phosphorylation of mTORC1 target ribosomal protein S6 kinase beta‐1 (p70S6K1) was significantly enhanced in cells overexpressing AS04 compared to those overexpressing full‐length LeuRS. We hypothesize that this alternately spliced LeuRS variant might have evolved to enhance and regulate the non‐canonical function of LeuRS‐dependent mTORC1 signaling.Support or Funding InformationW.M. Keck Foundation Biomedical Research GrantThis abstract is from the Experimental Biology 2018 Meeting. There is no full text article associated with this abstract published in The FASEB Journal.
Characterization of pathogenic mutations in human mitochondrial alanyl‐tRNA synthetase
Authors: Chihade Joseph , Kennicott Hannah , Jessica Makori , de Leon Samuel Diaz , Donnell Isaac , Heath Jacob 
Published: June 2021

Translation in mitochondria is dependent on a set of mitochondrial specific aminoacyl‐tRNA synthetases. Defects in these enzymes are related to a range of human diseases. For example, mutations in the human mitochondrial alanyl‐tRNA synthetase (AARS2) have been associated with infantile cardiomyopathy and with adult‐onset leukoencephalopathy. Structural analysis of homology models and haplotype analysis suggests that all pathogenic mutations result to some degree in loss of AARS2 function, and that the severity of the mutation correlates with the observed disease phenotype.(1) We are testing this hypothesis in vitro by examining protein stability, RNA binding, and aminoacylation activity of these mutants.This abstract is from the Experimental Biology 2018 Meeting. There is no full text article associated with this abstract published in The FASEB Journal.
The effects of peroxide exposure on the transfer RNA of radiotrophic C. neoformans
Authors: Kelley Melissa , Myers Ryan , Jora Manasses , Addepalli Balasubramanyam , Limbach Patrick 
Published: June 2021

Cryptococcus neoformans is a radiotrophic fungi capable of surviving in extreme environments. Understanding post‐transcriptional RNA modifications may lead to insight on translational regulation and protein synthesis. Little is known about the role of transfer RNA (tRNA) modifications in C. neoformans. Modification profiles change during oxidative stress and may play biological roles in cell survival. Here, the impact of peroxide exposure on C. neoformans tRNA is investigated through liquid chromatography coupled with mass spectrometry.Support or Funding InformationDepartment of Defense: Defense Threat Reduction Agency (DTRA)University of CincinnatiThis abstract is from the Experimental Biology 2018 Meeting. There is no full text article associated with this abstract published in The FASEB Journal.