anti basal ganglia test

[evie]

Has anyone ever heard of the 'anti basal ganglia test'? I was doing some research and came across a post on a forum regarding this blood test. You can view the post over here:

 

http://www.wemove.org/cgi-bin/ultimatebb.c...13;t=000173;p=0

 

I would like to contact the poster of this thread, but before I do, has anyone ever come across such a thing in the US?

 

--Evie

[P_Mom]

I read the posts you were referring to and it sounds to me like the "anti-basal ganglia" tests are what they call our ASO and AntiDNAase B titer tests. Just the same with these tests being negative and kids still having PANDAS.......same goes for ASO and AntiDNAase titer.

[PANDAS_Denmark]

I read the posts you were referring to and it sounds to me like the "anti-basal ganglia" tests are what they call our ASO and AntiDNAase B titer tests. Just the same with these tests being negative and kids still having PANDAS.......same goes for ASO and AntiDNAase titer.

 

Hi :-)

I agree that it could simply be a ASO and AntiDNAase B titer test.

But maybe it could also be a test of the levels of CAMkinase II activity ?

You can find a description of the test here - as well as the argumentation of using that test : http://www.csus.edu/bios/faculty/Kirvan/Ki...JNI_article.pdf.

My son (PANDAS) had that test a year ago (on several blodtests taken over the past two years), showing remarkable high levels of CAMkinase II activity at the times when he had had PANDASbursts.

I know that this test can be done only at very few laboratories in the world.

As such my sons blodtests was tested/analyzed in US (we live in Denmark).

Best wishes to you all !

[kim]

Pandas Denmark,

 

Thank you so much for posting that study.

 

Something that really interests me, is one article that I found that said that Heparan reduced levels of CAMkinase II. I have a particular interest in heparan/heparan sulfate.

 

 

I hope you all don't mind me dropping this here. It's something that I don't want to lose so I can find it when I have the brain energy to try to figure out what it is all saying. After quicly reading throught the study PANDAS DENMARK posted, I know c-Ret phosphorylation is mentioned, and I have no idea what it is.

 

http://jcs.biologists.org/cgi/content/full/115/23/4495

Key words: GDNF, Glycosaminoglycan, Heparan sulphate, c-Ret

 

Glial cell line-derived neurotrophic factor, GDNF, is vital to the development and maintenance of neural tissues; it promotes survival of sympathetic, parasympathetic and spinal motor neurons during development, protects midbrain dopaminergic neurons from apoptosis well enough to be a promising treatment for Parkinson's disease, and controls renal and testicular development. Understanding how GDNF interacts with its target cells is therefore a priority in several fields. Here we show that GDNF requires glycosaminoglycans as well as the already-known components of its receptor complex, c-Ret and GFR-1. Without glycosaminoglcyans, specifically heparan sulphate, c-Ret phosphorylation fails and GDNF cannot induce axonogenesis in neurons, in PC-12 cells, or scatter of epithelial cells. Furthermore, exogenous heparan sulphate inhibits rather than assists GDNF signalling. The involvement of heparan sulphates in GDNF signalling raises the possibility that modulation of heparan expression may modulate signalling by GDNF in vivo.

 

 

 

http://ajprenal.physiology.org/cgi/content...8/1/F142?ck=nck

 

Heparin exerts an antiproliferative effect in smooth muscle cells, and the Ca2+/calmodulin-dependent protein kinase (CaMK) signaling pathway is heparin sensitive. Here, we report that transfection with a truncated 326-amino acid fragment of CaMK-II increases basal activity of CaMK-II in mesangial cells. Ionomycin increased CaMK-II activity in both transfected and untransfected cells, with a concomitant increase in activated Ca2+/calmodulin. Heparin (1 µg/ml), but not chondroitin or dermatan sulfate, significantly attenuated both serum- or ionomycin-induced CaMK-II activity, and attendant c-fos mRNA expression, but did not affect upstream Ca2+/calmodulin. Autophosphorylation of Thr286 generates an autonomously active CaMK-II. Both serum and ionomycin increased phosphorylation at this site and increased CaMK-II activity in antiphosphothreonine immunoprecipitates. Heparin (1 µg/ml) did not inhibit phosphorylation of Thr286 (although much higher concentrations did). Replacement of Thr286 with Asp produces a constitutively active mutant that was insensitive to ionomycin but was inhibited by heparin maximally at 1 µg/ml. These results suggest that heparin at physiological concentrations acts at or downstream of CaMK-II to suppress its activity independent of an effect on autophosphorylation

[kim]

http://www.newscientist.com/channel/health...=mg19426074.500

 

Previous studies suggested that glucosamine, a dietary supplement commonly taken by people with osteoarthritis, has some immunosuppressive effects. This led Michael Demetriou and colleagues at the University of California, Irvine, to investigate a similar but more potent compound called N-acetylglucosamine (GlcNAc)

[kim]

?

 

http://en.wikipedia.org/wiki/N-Acetylglucosamine

 

GlcNAc is the monomeric unit of the polymer chitin, which forms the outer coverings of insects and crustaceans. GlcNAc is also of note in neurotransmission, where it is thought to be an atypical neurotransmitter functioning in nocioceptive (pain) pathways.

 

It has been proposed as a treatment for autoimmune diseases.[1

 

From the PANDAS study (bolding mine)

 

http://www.csus.edu/bios/faculty/Kirvan/Ki...JNI_article.pdf

 

Most importantly, PANDAS CSF showed highly elevated

levels of CaM kinase II induction similar to that of positive

control SC CSF (Fig. 4a). Non-PANDAS CSF showed no

activation of CaM kinase II. PANDAS CSF-induced CaM

kinase II activity was blocked by the streptococcal associated

GlcNAc epitope, but not by group A streptococcal serotype

5 M protein, suggesting that antibodies directed against an

epitope of the group A carbohydrate of Streptococcus

pyogenes may be important in mediating cell signaling

(Fig. 4b). Therefore, signaling activity found in behavior and

movement disorders during the symptomatic phase of

disease suggests that antibodies present in the sera and

CSF were associated with and may contribute to the clinic

symptoms in acute phases of disease.

 

I don't have a clue what this is saying, but looks important

 

http://www.jneurosci.org/cgi/content/abstract/13/2/559

 

Overexpression of Ca2+/calmodulin-dependent protein kinase II in Neuro2a and

NG108-15 neuroblastoma cell lines promotes neurite outgrowth and growth cone

motility

[kim]

In addition to last post, I wanted to leave this here too. The interactions btwn bacteria and host, and what were talking about here (extends to other pathogen too...trying to piece together varicella in this mess) seems the way GAGS (glucosaminoglycans) interact with each is be important. I know Carolyn N. just hit on some of this info in regards to hormones, it's not always illness.

 

 

http://www.blackwell-synergy.com/doi/full/...33.2003.03600.x

 

Several microbial pathogens have been reported to interact with glycosaminoglycans (GAGs) on cell surfaces and in the extracellular matrix. Here we demonstrate that M protein, a major surface-expressed virulence factor of the human bacterial pathogen, Streptococcus pyogenes, mediates binding to various forms of GAGs. Hence, S. pyogenes strains expressing a large number of different types of M proteins bound to dermatan sulfate (DS), highly sulfated fractions of heparan sulfate (HS) and heparin, whereas strains deficient in M protein surface expression failed to interact with these GAGs. Soluble M protein bound DS directly and could also inhibit the interaction between DS and S. pyogenes. Experiments with M protein fragments and with streptococci expressing deletion constructs of M protein, showed that determinants located in the NH2-terminal part as well as in the C-repeat region of the streptococcal proteins are required for full binding to GAGs. Treatment with ABC-chondroitinase and HS lyase that specifically remove DS and HS chains from cell surfaces, resulted in significantly reduced adhesion of S. pyogenes bacteria to human epithelial cells and skin fibroblasts. Together with the finding that exogenous DS and HS could inhibit streptococcal adhesion, these data suggest that GAGs function as receptors in M protein-mediated adhesion of S. pyogenes.

[kim]

Diagram GlcNAC discussed in article PANDAS Denmark posted and the condition I'm looking at, AND

 

http://www.newscientist.com/data/images/ar...07/26074501.jpg

 

 

These guys are working on this ($10,000,000 grant) The studies are clickable on the left

 

http://www.researchcrossroads.com/index.ph...amp;user=640119

 

autosomal dominant bone disorder that is caused by defective HS synthesis due to mutations of the GlcNAc/GIcA co-polymerase EXT1. Interestingly, there have been clinical reports indicating that HME patients associate autistic traits.

[kim]

If you google UK antibasal ganglia test, I felt it was pretty apparent that they were not talking about ASO/antiDnase levels (in regards to original posters question)

 

This one helps explain some of the questions about the study that Panda's Denmark posted.

 

Autoimmunity

 

Streptococcal mimicry and antibody-mediated cell

signaling in the pathogenesis of Sydenham's chorea

 

http://intramural.nimh.nih.gov/pdn/pubs/pub-15.pdf

 

Recent Publications

http://intramural.nimh.nih.gov/pdn/recent_publications.htm

 

 

http://www.ncbi.nlm.nih.gov/pubmed/16158191

 

Gangliosides, a heterogeneous family of glycosphingolipids abundant in the brain, have been shown to affect neuronal plasticity during development, adulthood and aging. This review will examine old and recent evidence that exogenous gangliosides and in particular GM1, the prototype member of this family, exhibit multimodal neurotrophic effects.

[kim]

here is one study on this subject regarding strep

 

http://www.ingentaconnect.com/content/bsc/...000010/art00021

 

Several microbial pathogens have been reported to interact with glycosaminoglycans (GAGs) on cell surfaces and in the extracellular matrix. Here we demonstrate that M protein, a major surface-expressed virulence factor of the human bacterial pathogen, Streptococcus pyogenes, mediates binding to various forms of GAGs. Hence, S. pyogenes strains expressing a large number of different types of M proteins bound to dermatan sulfate (DS), highly sulfated fractions of heparan sulfate (HS) and heparin, whereas strains deficient in M protein surface expression failed to interact with these GAGs. Soluble M protein bound DS directly and could also inhibit the interaction between DS and S. pyogenes. Experiments with M protein fragments and with streptococci expressing deletion constructs of M protein, showed that determinants located in the NH2-terminal part as well as in the C-repeat region of the streptococcal proteins are required for full binding to GAGs. Treatment with ABC-chondroitinase and HS lyase that specifically remove DS and HS chains from cell surfaces, resulted in significantly reduced adhesion of S. pyogenes bacteria to human epithelial cells and skin fibroblasts. Together with the finding that exogenous DS and HS could inhibit streptococcal adhesion, these data suggest that GAGs function as receptors in M protein-mediated adhesion of S. pyogenes.

[kim]

Here is the one on herpes viruses

 

http://www.jci.org/108/4/503?content_type=full

 

Herpesviruses and heparan sulfate: an intimate relationship in aid of viral entry

[CSP]

WOW!

 

The only time I have ever heard of GAG was for people suffering from poor bladder health.

 

I'm trying to understand all the benefits to the intramax and the protien/sugar matrix. The essential sugars N-acetylgalactosamine, N-acetyglucosamine and N-acetylneuramaminic acid. I'm having a hard time understanding all this, but had a feeling this dietary supplement would be very benefical to my son's impaired protein synthesis and significantly impaired sugar and carbohydrate tolerance. My son's mineral analysis suggests an impaired immune system that may contribute to chronic or recurrent viral, bacterial or fungal infections. I'm a little confused about this as he is never sick other then a cold or stomach bug.

 

This has me really hopeful that the anti-microbial, anti-fungal, anti-parasitic, anti-viral, and anti-bacterial properties to this intramax may really benefit my son. Not to mention balence him out.

 

If I have hit on something that you think I would benefit knowing please let me know, I'll be checking back in tomorrow.

 

Thanks Kim,

C.P.