Re: A bit more about The Proteome Project � Human Protein

[Guest guest]

I shouldn't have to be searching for this kind of stuff -but reading some things

that I read just drives me nuts!

More proteomic studies that may be of interest to those of us that are curious

as to perhaps why nutriiveda is " working " Keep your eyes open for

" lactoferrin " from the whey, especially when combined with other nutrients -

something I haven't talked about much but another possible theory for

http://pursuitofresearch.org/science.html

This is not limited for those who have seizure issues and 'why' or 'how' is

nutriiveda stopping seizures -but fortunately it is being studied and has been

-nutrition links to stopping seizures. YAY!!! There is hope for western

medicine!

For all our children, perhaps in addition to all else -it's the lactoferrin from

the whey mixed with the other nutrients as in this study they used 50 g dose of

orally administered lactoferrin! Below this is a brand new study just published

today on the proteome project! It's interesting how these nutrients are

combining which may explain why this is working better than just those that have

used whey protein alone. Interesting stuff!!

Volume 70, Issue 4, Pages 876-879 (2008)

Potentiation of brain serotonin activity may inhibit seizures, especially in

drug-resistant epilepsy

P. MainardiCorresponding Author Informationemail address, A. Leonardi, C. Albano

Received 18 June 2007; accepted 18 June 2007. published online 10 September

2007.

Summary

In spite of the large number of antiepileptic drugs (AEDs) actually available,

the problem of drug-resistant epilepsy has not been solved. No AEDs are

efficacious in patients with pharmacoresitant epilepsy, so new hypothesises

about the mechanisms of pharmacoresistance are needed.

In the last years the ideas on the role of brain serotonin in epilepsy have been

turned upside down: increasing the available brain serotonin is thought now to

have an antiepileptic effect. Antidepressant drugs like selective serotonin

re-uptake inhibitors, i.e., fluoxetine, have proved to be useful in seizure

control.

Tryptophan (Trp), an essential amino acid, is the only brain precursor of

serotonin, it competes with the other large neutral amino acids (LNAAs) for the

carrier of blood†" brain barrier (BBB). Our own data has shown a lowering of

plasmatic LNAA levels in epileptic patients, on the basis of these results we

could estimate a decrease of a 1/3 in the Trp brain intake rate in epileptics in

respect to controls.

Increasing plasmatic Trp levels increases brain serotonin synthesis. Trp and

5-hydroxytryptophan (5-HTP) were tested as an add on in epilepsy, but the

clinical outcome was controversial. Free amino acids are not fully adsorbed by

the gastro-intestinal system, furthermore LNAAs, and also 5-HTP is a LNAA,

compete to cross the intestinal membrane for the same carrier, like for the BBB.

The best way to increase the plasmatic Trp level is a protein rich in Trp and

poor in the other LNAAs. Unfortunately Trp is a limited amino acid in proteins.

We report the clinical results obtained by adding a whey protein to the

antiepileptic therapy of drug-resistant epileptic patients: alpha-lactoalbumin,

rich in Trp and poor in the other LNAAs.

Public release date: 15-Jun-2010

Contact: Jesus Delgado

Jesus.Delgado@...

34-935-814-049

Universitat Autonoma de Barcelona

Protein extremes gain relevance in massive proteomic studies

Researchers at University of Ghent, Belgium, and Universitat Autònoma de

Barcelona (UAB) develop a new procedure to identify the two extremes of protein

molecules and their processing and maturing in in-vivo and ex-vivo massive

proteomic studies. The research has been published online at Nature Methods,

under the title of " Complementary Positional Proteomics for Screening of Endo-

and Exoproteases " .

The world of proteins is one of the most complex and fundamental in living

beings given that these biomolecules carry out and control or intervene in most

biological functions. The massive identification and characterisation in a

multitude of live organisms and in different vital stages has been and remains

one of the most important tasks of proteomics, since it allows for further

calibration of their role in biological functions and pathologies/diseases and

to develop control strategies (e.g. drugs and vaccines).

Until recently most proteomic studies were focused on internal regions of

proteins, usually those located in the three-dimensional folding (essential for

many functions) or in the N-terminal (-Nt), with a free amine group (-NH2) at

the start of the linear chain of linked amino acids. Protein molecules can have

either few or hundreds (common in many organisms) and even thousands of linked

amino acids, always in linear form, even if three-dimensional folding later

takes place. This focalised research is due to the fact that procedures and

chemistry needed to study N-terminal and internal regions are easier and can be

developed quicker.

The new method developed by scientists helps to expand studies to C-terminal

proteins (-Ct), proteins with a free carboxyl group, COOH, at the end of the

linear chain of amino acids. The global and integrated strategy was created by

research groups of the University of Ghent, Belgium (Petra van Damme, Kris

Gevaert, et. al.) and UAB (Sílvia Bronsoms and Francesc Xavier Aviles from the

Institute of Biotechnology and Biomedicine and the Department of Biochemistry

and Molecular Biology).

In other words, it is now possible to use massive proteomic methods to study

maturing processes of proteins which often include breaks in their linear

sequence both internally and at their N- and C-termini. Therefore, it will be

possible to assess the specific role of these regions in the processes mentioned

and in other related functions such as generation, activation and deactivation

of hormones, growth factors, neuropeptides, enzymes, membrane receptors and many

other proteins with important biological roles. The strategy developed can be

carried out ex-vivo (in cell extracts) or in-vivo (by transfection and proteomic

analysis). In addition, protein extremes are commonly involved in essential

functions, such as locating and directing cells-tissues, triggering the start of

three-dimensional folding, joining other biomolecules and macrostructures,

post-generation chemical modifications of proteins, etc.

This publication completes previous studies (e.g. on N-terminal regions) carried

out by the Flemish research group, leader in the field of general proteomics, as

well as by researchers at Universitat Autònoma de Barcelona, leaders in the

field of enzymes processing and maturing C-terminal proteins

(carboxypeptidases), who recently published an article on the processing of

C-terminal peptides in the Journal of Biological Chemistry, by S. Tanco, J.

Lorenzo and F. X. Aviles, of UAB, and Ll. Fricker et. al. of Albert Einsten

College of Medicine of New York.

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Reference article: " Complementary Positional Proteomics for Screening of Endo-

and Exoproteases " , Van Damme P. et al (2010) Nature Methods.

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