Cyrex Array 7 and Consultation – Joint Autoimmune
Joint autoimmune test can assist in the early detection of mixed connective tissue disorders as well as helping to assess the effectiveness of treatment protocols for conditions such as osteoarthritis and the management of mixed connective tissue disorders
No- This test is done at home and comes with prepaid shipping materials and everything you need to ensure proper delivery to the lab.
Web results are posted within 7-14 business days. Our office will notify you when test results have been reported.
Yes. The kit comes with easy to follow instructions
Yes. Dr Hagmeyer will review the test result with you. Each test comes with a 30-45 minute post-test review/explanation.
One we have placed the order for the test we are unable to issue a refund.
Hormone imbalances in men can contribute to:
Decreased muscle mass and strength
General fatigue/decreased energy
Increased risk for coronary artery disease or heart attack
Hair loss or thinning
Increased fat accumulation
Decreased bone density or osteoporosis
Compromised immune function
Irritability and depression
- Sample collection must be performed by a phlebotomist Monday – Thursday only.
- Information about scheduling a blood draw can be found HERE.
- You may need to pay a separate fee for phlebotomy.
- Do not eat a high-fat meal prior to your blood draw.
- Hydrate prior to your blood draw.
- If you are taking immunosuppressants or corticosteroid drugs, contact your healthcare provider regarding the timing of this test.
Antigens Tested (IgG + IgA Combined)
- Myelin Basic Protein
- Alpha + Beta Tubulin
Myelin basic protein (MBP)
Myelin is the protective sheath surrounding nerves. Myelin basic protein (MBP) is believed to be important in the process of myelination, the building of myelin sheaths. Thus, MBP is often a target in the demyelination process in various neuroimmune disorders.
Known Cross-Reactions: Chlamydia pneumoniae, Herpes-6;5 streptococcal protein;5, 6 gliadin;7 Acinetobacter;8 Mycobacterium avium;9 IgG and IgM to tissue-bound-Bisphenol A (BPA)10
MBP antibodies are detected in various neuroimmune disorders including multiple sclerosis. Consequently, antibodies to MBP are accepted markers of inflammation in various neuroimmune disorders.
In possible cases of multiple sclerosis (MS) the measurement of antibodies against MBP may predict early conversion to clinically definite MS; in a study by Berger et al patients who were seropositive for both antibodies, anti-MBP and anti-myelin oligodendrocyte glycoprotein, had clinically definite MS within a mean of 7.5 months.2
To increase the sensitivity and specificity of MS diagnosis, a combination of antibodies, lymphocyte activation or cytokine production assessments along with an MRI, should be utilized.2, 5 Autism Spectrum Disorder (ASD) presents with multiple biomolecular manifestations including neurological dysfunction.
Compared to control subjects, ASD patients possess significantly higher levels of anti-brain antibodies, such as MBP, serotonin receptor, and brain endothelial cells or blood-brain barrier.1
Due to cross-reactivity to Streptococcal protein, MBP antibody is also found in PANDAS (pediatric autoimmune neuropsychiatric disorder associated with group A streptococcal infection), its adult version ANDAS and Obsessive Compulsive Disorder (OCD).6
Indeed, the similarities of peptide sequences between Streptococcal proteins and MBP result in cross- reactivity.
This autoimmune response triggers inflammation via myelin basic protein-specific T-cells, thus compromising the blood-brain barrier.3, 5
A point of interest is that the administration of myelin basic protein artificially increases blood-brain barrier permeability and is under research as a possible treatment for rabies virus, which enters the brain to replicate itself.4
- Multiple sclerosis2, 5
- PANDAS / ANDAS / OCD6
- Toxin exposure
Gangliosides are glycosphingolipids. Asialo GM1 has important physiological properties and impacts neuronal plasticity and repair mechanisms, as well as the release of neurotrophins in the brain. Asialo GM1 acts as the site of binding for both Cholera toxin and E. coli.
Known Cross-Reactions: Campylobactor jejuni,3 Streptococcal proteins,4 gliadin6
- Chronic Inflammatory Demyelinating Polyneuropathy 2
- Cerebrovascular Accidents 1
- Cranial Trauma 1
- Guillain Barré Syndrome 3
- Miller Fisher Syndrome 3
- Motor Neuron Disease1, 2 MMNBC1
- Multifocal Motor Neuropathy 2
- Multiple Sclerosis 1
- Myasthenia Gravis 1
- PANDAS / ANDAS / OCD5
- Rheumatoid Arthritis 1
- Sensorimotor Neuropathy 2
- Systemic Lupus
- Erythematosus 1, 2
GM1 is exposed at the surface of spinal motor neurons, and in the peripheral nerves, it is limited to the node and paranodal region.
Low levels of antibodies can be found in normal individuals and in patients with certain autoimmune disorders, however, high titers may be helpful in the diagnosis of multifocal motor neuropathy with conduction block (MMNCB),2 and paraproteinenia including motor neuron disease and multifocal motor neuropathy.1
Autoantibodies to ganglioside GM1 are thought to be involved in the pathophysiology of some motor neuropathies due to relatively high level detection prior to therapeutic intervention, and a subsequent decrease of antibodies concurrent with clinical improvement.1
High titers of IgM Antiganglioside GM1 may be etiologically important in certain types of motor neuropathy, while on the other hand, low levels of antibodies may represent B-cell dysfunctional regulation.2
The origin of anti-ganglioside antibodies is unknown, however, it is speculated that they can be formed against certain infectious microorganisms.
Campylobacter jejuni has been identified as a frequent cause of Guillain Barré syndrome and Miller Fisher syndrome; during infectionof C. jejuni anti-GM1 antibodies bind with whole cells of different C. jejuni isolates.4 Likewise, this occurs with Streptococcal infection, which is a trigger for PANDAS, the adult version, ANDAS and OCD.4, 5
ALPHA + BETA TUBULIN
Tubulin is a building block protein and a major component of a cell’s internal cytoskeleton, called microtubules.
These structures play key roles in many cellular functions including, interaction with guanine, lateral contacts, interaction with beta and gamma phosphates of nucleotides, interaction with gamma phosphate, longitudinal contacts, backbone interactions with a and b phosphates, hydrophobic contact of conserved residues, nucleotide contacts, MAP-binding domain and acetylation site.
Known Cross-Reactions: Streptococcal Protein 7
- Alcoholic liver disease1
- Demyelinating disease1
- Graves’ disease1, 5
- Hashimoto’s thyroiditis1, 5
- Infectious agent exposure1,
- Rheumatoid arthritis1
- Recent onset diabetes type
- 16 Toxin exposure7
Tubulin’s basic function as a component of microtubules explains its appearance in a variety of unrelated disorders, which can affect organ tissues, as well as, neuronal structures.3, 4
Quantitative increases in anti- tubulin antibodies are thought to be due to autoimmune reactions to the patient’s own tubulin, or to the polyclonal activation of B cells associated with diseases and disorders listed above.1
A surprising similarity between the structures of tubulin and bacterial protein FtsZ (filamenting temperature-sensitive mutant Z) has spawned a variety of studies linking infectious agent exposure with tubulin antibodies.4 Elevated anti- tubulin antibody levels were found in sera from patients who presented with a number of infections, including leishmaniasis, African trypanosomiasis, onchocerciasis, schistosomiasis and leprosy.1
Tubulin may be altered during the course of an infection, thus rendering it immunogenic. Infectious agents due to antigenic similarity may illicit a cross-reaction autoimmune response.
Tubulin cross-reacts with Streptococcal protein, which can lead to autoimmunity and the neurological dysfunction associated withPANDAS/ANDAS/OCD.7
Tubulin is also a neuronal target of autoantibodies in Sydenham’s Chorea, in which these autoantibodies alter the blood-brain barrier, thus increasing permeability of the blood-brain barrier.3
This event results in cell signaling, dopamine release, and movement and neuropsychiatric abnormalities. Antibodies against nerve cell Tubulin have been demonstrated in patients with toxic chemical exposure, including mercury and other heavy metals.
Anti- tubulin antibodies are also detected in a high ratio of patients with recent onset type 1 diabetes, but decrease or disappear during the course of the disease.6 Anti-tubulin antibody was detected in 56% of patients with Hashimoto’s thyroiditis and in 41% of patients with Graves’ disease.5
Cerebellum is the part of the brain controlling movement and balance. Inside the cerebellar cortex there are large neurons called Purkinje’s cells. The Cerebellar antibodies test measures antibodies against the cerebellum Purkinje’s Cell Antigens
- Celiac Disease 5
- Gluten Ataxia 5, 7
- Opsoclonus-Myoclonus Syndrome 3
Known Cross-Reactions: gliadin, 6-8 tumor cells,3 Milk butyrophilin 6, 7
Elevated Cerebellar antibodies are an indication of neuroautoimmunity. Infection, or exposure to toxic chemicals, can induce production of antibodies against Purkinje’s cells.5
Due to cross-reactivity between Gliadin and Cerebellar antigens or peptides, an autoimmune reaction occurs. 7
Medical conditions related to Purkinje cells range from toxic exposure (mercury, alcohol) to autoimmune disorders (Celiac disease), and from genetic mutations (spinocerebellar ataxias) to neurodegenerative diseases of no known genetic basis (cerebellar multiple system atrophy, sporadic ataxias).
Although the etiology of paraneoplastic cerebellar degeneration (PCD), which generally occurs in patients with neoplasms of the lung, breast, ovary, or with Hodgkin’s disease, is unknown, scientists speculate it is autoimmune in nature.4
The known cross-reactivity between cerebellar peptides and gliadin and milk butyrophilin, as seen in patients with gluten sensitivity, which includes many individuals with autism spectrum disorder (ASD), may be responsible for molecular level gluten ataxia,6 7 tremors and alterations of coordination, balance and sensations.2, 6, 7
Exacerbating cerebellar degeneration, and bringing about the subsequent clinical conditions in ASD patients is mercury –induced disruption in cerebellar synaptic transmission between parallel fibers or climbing fibers of Purkinje cells.2
According to Bernard and colleagues, due to the anti-cerebellar antibodies present in the sera of ASD patients, ongoing damage may arise as these antibodies find and react with neuronal antigens.2
Synapsin I, also known as phosphosynaspin I, is a major immunoreactive protein found in most neurons of the central and peripheral nervous systems. It is a member of a group of neuronal phosphoproteins involved in the regulation of neurotransmitter release.
Synapsin I is present in the nerve terminal of axons, specifically in the membranes of synaptic vesicles.
- Demyelinating Diseases 2
- Inhibited Neurotransmitter Release 4
- Lupus 4
- Multiple Sclerosis 2
Known Cross-Reactions: Gliadin1,5
Antibodies against Synapsin can contribute to neuronal damage2, 4 as well as non-neuronal tissues.3
There is a similarity between Synapsin I and Gliadin (a protein of wheat) in that they both have high frequencies of proline and glutamine residues, thus, cross-reactivity occurs between Synapsin I and Gliadin.1,5
This molecular mimicry triggers autoimmunity resulting in neurological deficits often associated with gluten sensitivity and, in genetically susceptible patients, with Celiac Disease.
Non-neuronal Synapsin I has also been identified in the liver and is thought to be associated with the trans-Golgi network-derived compartment.3
This placement suggests that Synapsin I plays a role in modulating post-trans-Golgi network trafficking pathways of secreted proteins.3