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Humanicsxian Economics Is Here Here
All-For-One and One-For-All
Jessie May Peters
First Published: September 24: 2015
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The Humanion UK Online Daily

 

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What Does Not Die

 

 

 

 

 

 

 

 

 

 

In Hampshire in an autumn wood the squirrel I found that came to say hello
In New Hampshire life’s voices went rippling human joys and sorrows and
In Union Square I saw the sun painting the green leaves with photon-paints
Allwhere life is a song written and sung in many a form in many a rainbow
A rainbow it is always allwhere marking the same shape of life-expressions

It is always in units of atoms
Units of photons and of cells
DNAs RNAs and neurons
Always the same rises ee falls
Always it is the song of cells

And the Empire State Building raised a spectacle in Manhattan skyline as
The traffic lit the air in all its expressions in the evening and in Scotland I
Saw heather and hyacinth in Swansea the light and its spread the same
Light the same song written and sung in many a form in many a rainbow
And it is the same that drives us to strive to stretch to reach to risk to rise

It is always magnetic
Always electric and
Chemical and active
Biochemical it is as
It shapes the cell-rise

I saw grace in human faces in Prague in Granada in Dhaka in Rome or in
London Manchester or York and found moss on city brick walls and saw
Butterflies on squeezed in greens of tiny spaces in town gardens and saw
Waters mining for life poetry in silence music in the ferns climbing onto
The trellis of light heard seagulls’ cries as human babies in all-everyday

In everyday momentary miracles
I saw life’s rainbow biochemistry
Unfolding noughts in paperboats
It is always the same song of love
That never dies and forever lives

:Munayem Mayenin: November 07: 2015

Mutations in Plasma Cells Play a Key Role in Light Chain Amyloidosis Fatal Over-production of Antibodies

 

 

 

|| Tuesday: March 10: 2020 || ά. Bone marrow plasma cells produce antibodies. These comprise two long and two short protein chains. The pathological proliferation of plasma cells can lead to an over-production of the short chains. These associate to fibrils and deposit in organs. The result is fatal organ failure. A research team from the Technical University of Munich:TUM and Heidelberg University has now identified the mutation, behind the disease in a patient. Antibodies are vital for the survival of human beings. They, typically, consist of two longer and, thus, heavier amino acid chains and two lighter ones. In rare cases, the plasma cells multiply excessively, flooding the body with light antibody chains.

In people suffering from light chain amyloidosis or AL amyloidosis, these light chains are deposited as extremely fine fibres, so-called amyloid fibrils, in tissue or in organs. The disease is, often, recognised, only, after the deposits already compromise the function of organs. In many cases AL amyloidosis is fatal. "To date, little was known about the exact cause of this amyloidosis." says Professor Johannes Buchner, of bio-technology at the Technical University of Munich. “Depending on the organ affected, the symptoms vary considerably. Furthermore, each patient produces different types of antibodies. The disease is, thus, difficult to diagnose at an early stage.”

Using various analytical and database-supported methods, the team of scientists succeeded in identifying eleven mutations, caused by the disease in the antibodies of a patient with advanced AL amyloidosis. Further investigations showed that exactly one mutation was responsible for the destabilisation and formation of the disease-causing amyloid fibrils. This mutation causes the unstable light chain to lose its structure after breaking into fragments, which, then, form the deadly amyloid fibrils.

"Our Study shows that mutations, that lead to unstable light chains, are an important factor in the occurrence of amyloidosis." says Ms Pamina Kazman, who carried out the majority of the measurements. "In the long term, we hope that these and other studies will lead to new, earlier diagnostic methods and, possibly, even, new treatment options."

The Paper: Fatal amyloid formation in a patient’s antibody light chain is caused by a single point mutation: Pamina Kazman, Marie-Theres Vielberg, María Daniela Pulido Cendales, Lioba Hunziger, Benedikt Weber, Ute Hegenbart, Martin Zacharias, Rolf Köhler, Stefan Schönland, Michael Groll, Johannes Buchner: Published in eLife online https://doi.org/10.7554/eLife.52300

The research was funded by the German Research Foundation:DFG. The protein structures were determined at the synchrotron radiation sources of the Paul Scherrer Institute in Villigen in Switzerland and the European synchrotron radiation source in Grenoble in France.

::: Caption: 01: PhD student Ms Pamina Kazman examines the folding and stability of antibody domains with the circular dichroism spectrometer of the Chair of Bio-technology; 02: At the Lab: 03: Compared to the normal antibody fragment, left, that of the patient, right, has a significantly larger hydrophobic area, red. Due to its lower stability, this fragment can form the dangerous amyloid fibrils: Image: P Kazman:TUM :::: 10.03.2020

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New Collaboration in Drug Development Offers Hope for the Patients of Alzheimer's Disease

 

 

|| February 22: 2019: University of Dundee News || ά. The University of Dundee’s Drug Discovery Unit has announced a partnership with Takeda, Japan’s largest pharmaceutical company, to develop possible new therapeutic treatments for tau pathology, an underlying feature in several forms of neuro-degeneration, including, Alzheimer’s Disease. Tau pathology occurs when the normal cellular protein, tau, misfolds and forms insoluble fibrils. It is found in the brains of sufferers of more than 20 different neuro-degenerative diseases, of which Alzheimer’s Disease is the most common.

Tau pathology is, increasingly, thought to be an important driver of disease progression. Recent studies demonstrate that tau pathology can spread from diseased to healthy cells in a seeding process, which is the focus of this collaboration. Alzheimer’s Disease affects 50 million people worldwide, yet, there are currently no disease-modifying treatments. Numbers of sufferers are expected to increase dramatically in the coming decades, thus, representing a vast and growing unmet medical need. Working in collaboration with Dr Will McEwan at the University of Cambridge and Dr Leo James at the MRC Laboratory of Molecular Biology, the Drug Discovery Unit has identified drug-like molecules, that prevent seeded misfolding of tau.

The partnership with Takeda will accelerate the progression of these drug-like molecules towards clinical development, with the potential to become much-needed therapies in diseases where tau is implicated, including, Alzheimer’s Disease. Dr David Gray, the Head of Innovative Targets at the Drug Discovery Unit, said, “Our mission is to bridge the gap between innovative life science research and drug development in areas of unmet clinical need and Alzheimer’s Disease is at the top of the list.

With support from Medical Research Council we are able to work with leading investigators, such as, Dr Will McEwan in Cambridge and Dr Leo James at the MRC Laboratory of Molecular Biology to deliver programmes, that are ready for industry to take forward. Teaming up with Takeda means we’ll get further, faster, bringing a potential treatment for this debilitating condition one step closer.”

The University of Dundee Drug Discovery Unit  is a fully integrated drug discovery group, established in 2006 to translate world-class biology research into novel drug targets and candidate drugs.  Housed within purpose-built facilities the Unit has the full repertoire of professional, industry-standard expertise and infrastructure required for preclinical small molecule drug discovery and to bridge the gap between academic research and pharmaceutical development.:::ω.

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Neuro-endocrine Tumours: New Comparative Study Conducted to Help Doctors Choose Better Therapies for Their Patients

 

 

|| February 18: 2019: University of Geneva News || ά. Which treatment for which patient? Researchers from a cluster of universities formed of Geneva, Bern and Basel, the HUG and Inselpital Bern has performed systematic comparisons between the therapies available for neuro-endocrine tumours in order to offer patients the most appropriate ones. An increasing number of new anti-cancer drugs are made available each year. During the authorisation process, such new drugs, usually, undergo comparisons to one but, only, rarely, to multiple established drugs.

This practice leads to a lack of comparisons between therapies and makes it, increasingly, difficult for physicians to choose the best treatment for their patients. To address this, researchers of these universities have conducted an extensive comparison of all drugs, used in the treatment of neuro-endocrine tumours. Their Study, published in JAMA Oncology, aims of guiding physicians through all available treatment options. Neuro-endocrine tumours can develop anywhere in the body from hormone-producing cells. Their prevalence is increasing and new therapies are regularly beefing up therapeutic options.

“The growing number of new therapies constitutes a great opportunity, obviously. However, the fact that few comparative studies are carried out between these different drugs, creates a dilemma for doctors when it comes to finding the best option for each patient.” says Professor Martin A Walter, at the University of Geneva Faculty of Medicine and the Head of the Nuclear Medicine and Molecular Imaging Division at the HUG, who initiated and co-ordinated this Study.

“Indeed, it is, actually, sufficient to establish the superiority of a new molecule over a single established drug or, even, over a placebo, to obtain approval from the regulatory authorities and enter the market.’’

“In such a situation, a network meta-analysis can be a valuable tool to generate indirect comparisons for therapies, that have not yet been directly compared. They, also, make it possible to use all existing data to identify the most effective treatments.” says Dr Reto Kaderli, the Head of Endocrine Surgery, Department of Visceral Surgery and Medicine, Bern University Hospital and University of Bern. Dr Kaderli is the First Author of the Study.

Swiss researchers collaborated with Cochrane, a global organisation, that aims to facilitating clinical decision-making, through systematic reviews of health interventions and with researchers at McMaster University in Hamilton, Canada, where some of the key methodologies for the analysis of evidence-based medicine have been developed.

“One of the most striking results of our Study is the high and, often, underestimated, efficacy of combination therapies. And, equally, striking was that these combination therapies were under-represented in international guidelines.” says Dr Kaderli. Indeed, studies, combining drugs produced by different pharmaceutical companies are mainly conducted by independent researchers and their results are less taken into account in treatment guidelines than studies conducted by the pharmaceutical industry.

“As a specialist in Nuclear Medicine, however, I am delighted with the promising results of our radioactive therapeutics.” says Professor Walter. Such a step still needs to be taken for surgical options, for which randomised controlled trials in combination with other therapies are still lacking.

“Our work, thus, marks an important step in the search for the best therapeutic option for patients with neuro-endocrine tumours and highlights the need for independent evidence-based medicine.” researchers put forward.:::ω.

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New Research Gains New Insight Into the Workings of An Antibody in Coronavirus-Induced Severe Acute Respiratory Syndrome

 

 

 

|| February 06: 2019: University of Washington News || ά. Studies of human monoclonal antibodies, isolated from survivors of Coronavirus-Induced Severe Acute Respiratory Syndrome:SARS or Middle-East Respiratory Syndrome:MERS are showing surprising immune defense tactics against fatal viruses. Atomic and molecular information about the workings of the highly potent antibodies, may, provide insights to prevent these serious and, sometimes, deadly lung infections. Currently, no vaccine or specific treatment is available for any of the six coronaviruses, that can infect humans. 

Some of these coronaviruses cause, only, common-cold like symptoms but, others provoke lethal pneumonias. Past deadly outbreaks in several countries foreshadow the possibility of coronavirus-mediated pandemics. Additionally, genetic surveillance of coronaviruses in bats and the fact that the MERS coronavirus, naturally, circulates in dromedary camels, suggest that  previous outbreaks, may, not be, unusual incidences. The animal:human species barrier is likely to be crossed again and lead to new emerging coronaviruses in the future.

As part of anticipation and preparation initiatives, infectious disease research groups are trying to develop an anti-coronavirus arsenal. An international research team, headed by the University’s Medicine scientists is among those, attempting to understand how SARS and MERS coronaviruses infect humans and how their presence elicits a response from the immune system. The research group is, particularly, interested in how neutralising antibodies target the coronavirus’ cell-invasion machinery.

Their most recent findings appear in the online edition of Cell, January 31. Coronaviruses have multi-functional surface spikes, that recognise and attach to receptors on the surface of a host cell. They, then, fuse the virus and cellular membranes. They use these trimeric spike glycoproteins as their molecular break-in tool.

The spike glycoprotein densely decorates the surface of coronaviruses.  The numerous projections resemble burrs on a seed-pod.  The spikes are key to the infectivity and pathogenicity of the coronavirus. They are the target of neutralising antibodies and the main focus of sub-unit vaccine design.

Previous studies in the Veesler Lab at the University’s Medicine looked at the structural states, that occur in the coronavirus spike before and after the membrane fusion reaction. The researchers saw large conformational changes in the spike glycoprotein. Details about activation of the membrane fusion cascade, however, remained unclear.

Using cryo-electron microscopy and other powerful technologies, the researchers gained insight into how the neutralising monoclonal antibodies from the SARS and MERS survivors inhibit the viruses at the molecular level. Their findings, also, helped elucidate the unusual nature of coronavirus membrane fusion activation.

The researchers found that both the SARS and the MERS coronavirus antibodies blocked the virus spikes from interacting with the receptors on the host cell membrane.  The SARS coronavirus antibody, also, did something unexpected: it, functionally, mimicked receptor-attachment and induced the spike to undergo conformational changes, leading to membrane fusion.  This trigger seems to be driven by a molecular ratcheting mechanism.

The researchers suggest that the finding is an unprecedented example of functional mimicry, whereby, an antibody activates membrane fusion by recapitulating the action of the receptor.

This study used molecular imaging to characterise the structures of both SARS and MERS coronavirus spike glycoproteins in a complex with their respective antibodies. The researchers, also, provided a blueprint of the carbohydrates, that bedeck the spike glycoproteins, in the context of whole viruses. Coronaviruses use this strategy to mask the vulnerable portion of their fusion apparatus to limit antibody access to it and expose it only to carry out the recognition and infection of host cells.

This study was supported by the National Institute of General Medical Sciences, National Institute of Allergy and Infectious Diseases, Pew Biomedical Scholars Award, Investigators in the Pathogenesis of Infectious Disease Award from the Burroughs Wellcome Fund, the Netherlands Organisation for Scientific, European Molecular Biology Organisation, Zoonoses Anticipation and Preparedness Initiative, Pasteur Institute, Centre National de la Recherche Scientifique and the LabEx Integrative Biology of Emerging Infectious Diseases, University of Washington Arnold and Mabel Beckman cryoEM Centre and Proteomics Resource and Beamline 5.0.1 at the Advanced Light Source at Lawrence Berkeley National Laboratory.:::ω.

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