bony tumors/cysts

[MARYANN]

My daughter had a mole, shaped as a lake with bumps around it. Little larger than a pencil eraser.

When the doctor saw it he said he never saw a child have this kind of mole. Scared me! Tested everything fine. Also; when she had the ticcing with her neck and I did not know it was a tic I took her to the orthopedic. When he gave her the x-ray, he sent her for a MRI because he said she might have extra bone. The doctor sent me to pediatric orthopedic specialist and she had MRI.

He sent me for MRI for the pain not for what ever this was on her neck. I kept asking about it

and it was like no concern. After she got the MRI I asked what is on her neck, he said it is

either calcifacation or benein tumor. Nothing to w0rry about if anything was wrong it would light up like a christimas tree. Now, of course since this topic is here im doing some research and benign tumor should be watched. This doctor is suppose to be one of the best so im confused.

I'm a little confused about this topic but it is interesting if there is some kind of connection.

[kim]

I can't tell you how much I appreciate those of you who are contributing to this discussion!

 

bmom, I wanted to post and say "take it back!" Your husband does too have a bony tumor, because I need it to be a bony tumor!

 

For anyone who has a little spare time, lol, read thru this.

 

 

Growth factor

 

http://en.wikipedia.org/wiki/Growth_factor

[kim]

MARYANN,

 

I feel the same way, you need to keep an eye on something like that but if it is the same thing that my son has, the incidence of it turning into something threatening (osteosarcoma) is very low. If there is an increase in size, pain, etc. it should be checked out again. What actually interests me more (at this point)is what other implications that genetic mutation could have. My son has 3 things that are considered relatively rare, with tics probably being the most common!

If there aren't some dots to be connected, I'd be a little surprised. I just wish there was someone who did this type of thing. I looked it up, and saw the word "Doctor" mentioned, but I tried a few of those, and apparently, that is not part of the job

[bmom]

Hi Kim, I will tell you that all this did send me searching on the computer and I panicked as I read about something called neurofibromatosis 1. I thought if my son had 3 caffe latte spots and my husband had a bony tumor was I once again looking at something that my son could have? Anyway, as I researched it, I then realized that it was not even a bony tumor and more of a fatty one. A little bit of relief for me! I did read a little about alternative treatments for fatty tumors which mentioned toxins as a reason.

[kim]

Hi Kim and bmom,

I have antiphospholipid antibody syndrome and took heparin and/or lovenox while pregnant with my three children (also had 2 miscarriages). This is why I'm thinking my ds got the double whammy from both of us- my auto-immune disorder coupled with dh's "tics" that he had has a child (nothing that was ever diagnosed or that ever interfered with his daily life; he has just now realized that he might have had something similar to ds on a lesser scale when he was younger. I have never seen any sign of tics in the 10 years that we've been together.).

 

Kim, does this mean anything?? You are so smart and I am so thankful to have you on "my team".

 

Thanks,

tlk

 

 

 

I missed this! Wanted to bring it forward, in case others did too. I didn't want anyone to miss tlk saying i was smart! LOL.

 

Ok, there is way too much talk here about this clotting thing.

 

I HAVE to add, that i had asked the ped allergist if the fish oil was thinning my oldest son's blood too much. I know vit e and fish oil can thin blood. Pycnogenol, which we have discussed in relationship to an immune booster, also has the ability to keep platelets from sticking together. I wasn't using that at the time, but thought I would mention it.

 

The Dr. said that the amts my son was taking would not effect the thickness of his blood. He said, even if you used enough to thin it, it would not effect clotting time.

At the time, he was having a lot of bloody noses. I chalked it up to allergy irritation, but why so hard to stop? He is not having them anywhere near as frequently now, but I still find these strange little splatters of blood on his comfortor/sheet/pillowcases.

 

In reading about the MTHFR and antiphospholipid antibody, i get the impression that this isn't an area that a lot of Dr.s are educated in or at least there is some confusion. Hope you all will add anything else that you can think of.

[kim]

In that last post, I meant to say that there is too much talk about clotting to be a coincidence, it would seem. From the little I read, that isn't really a common condition either, although possibly more prevalent that what is thought?

 

I have read that a MTHFR mutation is not all that uncommon, however.

 

Guess i better see what i can find on antiphospholipid antibody syndrome. I'm assuming it, too, causes excessive clotting?

[kim]

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

[kim]

Sunshine mentioned that her son has a CBS mutation. Faith mentions MTHFR mutation.

 

I remember bits and pieces about the CBS mutation from reading the Yasko forum. Look at the 2nd cite that I clicked on, when searching it.

 

http://www.med.uiuc.edu/hematology/PtHomocysteinemia.htm

 

 

Carolyn N just mentioned NAC that she became interested in from her sulfur research. Seems were onto something here!

[kim]

PROTEOGLYCANS IN THE DEVELOPING NERVOUS SYSTEM

 

http://www.burnham.org/print.asp?contentID=196

 

excerpts

 

http://www.burnham.org/print.asp?contentID=196

 

PROTEOGLYCANS IN THE DEVELOPING NERVOUS SYSTEM

Proteoglycans are a family of glycoproteins that carry sulfated polysaccharides (glycosaminoglycans). There are four classes of glycosaminoglycans, namely heparan sulfate, chondroitin sulfate, keratan sulfate, and hyaluronan. Proteoglycans have been implicated in various biological processes, such as the modulation of growth factor/morphogen signaling during development and tissue remodeling, regulation of cell proliferation, adhesion, and migration. Our laboratory has been studying the role of proteoglycans in neural development and physiology.

 

and

 

Analysis of the role of heparan sulfate in development using a conditional knockout system

To understand the role of heparan sulfate in mammalian nervous system, we created loxP-modified Ext1 allele by homologous recombination. Ext1 encodes an enzyme essential for heparan sulfate synthesis. As the first conditional knockout study using this system, we performed a developing brain-targeted Ext1 knockout using the nestin-Cre driver transgene. All the nestinCre-Ext1 conditional knockout mice died at birth, presumably due to respiratory failure. The brain of conditional knockout mice exhibited various patterning defects that are composites of those caused by mutations of multiple heparan sulfate-binding morphogens. Furthermore, these brains displayed severe guidance errors in major commissural tracts, revealing a pivotal role of heparan sulfate in midline axon guidance (5). [This paper was featured in Signal Transduction Knowledge Environment (STKE): Sci. STKE, November 11, 2003.]

 

 

http://www.ncbi.nlm.nih.gov/pubmed/1637821...ed_Discovery_RA

 

1: Med Microbiol Immunol. 2006 Sep;195(3):133-41. Epub 2005 Dec 24. Links

Heparan sulfate proteoglycans mediate Staphylococcus aureus interactions with intestinal epithelium.Hess DJ, Henry-Stanley MJ, Erlandsen SL, Wells CL.

Department of Surgery, University of Minnesota, Minneapolis, MN 55455, USA.

 

Staphylococcus aureus can be internalized by non-professional phagocytes, and may colonize the intestine in normal and antibiotic-treated individuals. Intestinal colonization may depend on the interactions of S. aureus with the intestinal epithelium. The best described mechanism of S. aureus binding to eukaryotic cells involves S. aureus fibronectin binding proteins (FnBPs), using fibronectin as a bridging molecule to beta1 integrins on the eukaryotic cell surface. Because S. aureus can be internalized by enterocytes, and because S. aureus is known to bind heparan sulfate (HS), we hypothesized that heparan sulfate proteoglycans (HSPGs) widely expressed on epithelia may mediate S. aureus interactions with intestinal epithelial cells. Internalization of S. aureus RN6390 by cultured intestinal epithelial cells was inhibited in a dose-dependent fashion by the HS mimic heparin, and by HS itself. Internalization of S. aureus DU5883, which lacks expression of staphylococcal FnBPs, was also inhibited by heparin. S. aureus adherence to ARH-77 cells, transfected to express the HSPG syndecan-1, was greatly increased when compared to adherence to plasmid control ARH-77 cells which have little detergent extractable HS. In addition, compared to wild-type HS-expressing Chinese hamster ovary (CHO) cells, internalization of S. aureus was decreased using mutant CHO cells with decreased HS expression. These findings are consistent with a model wherein S. aureus internalization by intestinal epithelial cells (and perhaps other epithelia) is mediated by S. aureus binding to the HS moiety of cell-surface HSPGs, and this interaction appears independent of fibronectin binding.

 

 

 

 

http://www.ncbi.nlm.nih.gov/pubmed/1631738...ed_Discovery_RA

 

Ability of the heparan sulfate proteoglycan syndecan-1 to participate in bacterial translocation across the intestinal epithelial barrier.Henry-Stanley MJ, Hess DJ, Erlandsen SL, Wells CL.

Department of Laboratory Medicine and Pathology, University of Minnesota, Minneapolis, MN 55455-0374, USA.

 

Although hundreds of microbial species reside in the human intestinal tract, comparatively few (e.g., Escherichia coli and other enterobacteria, Enterococcus faecalis, etc.) are typically associated with systemic infection in postsurgical, shock, and trauma patients. Syndecan-1 is the predominant cell surface heparan sulfate proteoglycan expressed on epithelia, and there is substantial evidence that heparan sulfate participates in interactions of a variety of frankly pathogenic microbes with mammalian cells. To investigate the role of syndecan-1 in interactions of enteric flora with intestinal epithelium, bacteria that might use the enterocyte as a portal of entry for systemic infection (including E. faecalis, E. coli, and other enterobacteria, and several species of staphylococci and streptococci) were studied for their abilities to interact with syndecan-1. Streptococcus bovis, S. agalactiae, S. pyogenes, Staphylococcus aureus, and S. epidermidis showed increased adherence to ARH-77 cells transfected to express syndecan-1. Heparin, a heparan sulfate analog, inhibited internalization of S. bovis, S. agalactiae, S. pyogenes, and S. aureus by HT-29 enterocytes (prominent syndecan-1 expression), but not Caco-2 enterocytes (relatively low syndecan-1 expression). Data from experiments with Chinese hamster ovary cells with altered glycosaminoglycan expression indicated that heparan sulfate and chondroitin sulfate (glycosaminoglycans on the syndecan-1 ectodomain) participated in bacterial interactions with mammalian cells. Thus, although E. faecalis, E. coli, and other gram-negative enterobacteria did not appear to interact with syndecan-1, this heparan sulfate proteoglycan may mediate enterocyte interactions with some staphylococci and streptococci that are known to cause systemic infections in specific populations of high-risk, immunosuppressed, postsurgical, and trauma patientsNOT ONLINE YET 2008 study

This Article:

Craig N. Morrell, Henry Sun, Masahiro Ikeda, Jean-Claude Beique, Anne Marie Swaim, Emily Mason, Tanika V. Martin, Laura E. Thompson, Oguz Gozen, David Ampagoomian, Rolf Sprengel, Jeffrey Rothstein, Nauder Faraday, Richard Huganir, and Charles J. Lowenstein

 

 

http://www.ncbi.nlm.nih.gov/pubmed/3290104...ed_Discovery_RA

 

Heparin-inhibitable basement membrane-binding protein of Streptococcus pyogenes.Bergey EJ, Stinson MW.

Department of Microbiology, School of Medicine and Biomedical Sciences, State University of New York, Buffalo 14214.

 

Solubilized surface proteins of Streptococcus pyogenes serotype M6 were found by indirect immunofluorescence assays to bind selectively to proteoglycan-containing regions of basement membranes of kidney and cardiac muscle in vitro. Epithelial, endothelial, and interstitial cells were unstained. Binding of streptococcal protein to basement membranes was competitively inhibited by heparin and, to a lesser extent, by heparan sulfate. Weak inhibition was also observed with other glycosaminoglycans, including dermatan sulfate, chondroitin sulfate, and hyaluronic acid. Type IV collagen, gelatin, serum fibronectin, glucuronic acid, and a selection of monosaccharides had no significant effects on binding. The heparin-inhibitable basement membrane-binding protein was purified by affinity chromatography on heparin-Sepharose 6-B. Polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate and urea dissociated the affinity-purified protein into two polypeptides of 9,000 and 15,000 mrs. Chemical analyses revealed that the purified protein was devoid of cysteine, amino and neutral sugars, and phosphate. Thus, the polypeptides are not glycosylated or complexed with trace amounts of lipoteichoic acid or polysaccharide. Binding of purified protein to tissue was determined by direct radioassay and indirect immunofluorescence and was inhibitable by heparin. Although the in vivo effects of this streptococcal component remain to be determined, its deposition on basement membranes in vitro supports the hypothesis that it contributes to the pathogenesis of poststreptococcal glomerulonephritis or acute rheumatic fever.

 

 

 

 

 

Glutamate mediates platelet activation through the AMPA receptor

 

J. Cell Biol. 2008 180: i13

Similiar articles

 

http://www.jcb.org/cgi/search?qbe=jcb;JCB1...p;minscore=5000

 

 

 

 

http://cat.inist.fr/?aModele=afficheN&cpsidt=17332123

 

Heparin, a heparan sulfate analog, inhibited internalization of S. bovis, S. agalactiae, S. pyogenes, and S. aureus by HT-29 enterocytes (prominent syndecan-1 expression), but not Caco-2 enterocytes (relatively low syndecan-1 expression). Data from experiments with Chinese hamster ovary cells with altered glycosaminoglycan expression indicated that heparan sulfate and chondroitin sulfate (glycosaminoglycans on the syndecan-1 ectodomain) participated in bacterial interactions with mammalian cells.

 

 

http://www.nature.com/nature/journal/v414/...bs/414648a.html

 

 

Streptococcus pyogenes (also known as group A Streptococcus, GAS), the agent of streptococcal sore throat and invasive soft-tissue infections, attaches to human pharyngeal or skin epithelial cells through specific recognition of its hyaluronic acid capsular polysaccharide by the hyaluronic-acid-binding protein CD44 (refs 1, 2). Because ligation of CD44 by hyaluronic acid can induce epithelial cell movement on extracellular matrix3, 4, 5, we investigated whether molecular mimicry by the GAS hyaluronic acid capsule might induce similar cellular responses. Here we show that CD44-dependent GAS binding to polarized monolayers of human keratinocytes induced marked cytoskeletal rearrangements manifested by membrane ruffling and disruption of intercellular junctions. Transduction of the signal induced by GAS binding to CD44 on the keratinocyte surface involved Rac1 and the cytoskeleton linker protein ezrin, as well as tyrosine phosphorylation of cellular proteins. Studies of bacterial translocation in two models of human skin indicated that cell signalling triggered by interaction of the GAS capsule with CD44 opened intercellular junctions and promoted tissue penetration by GAS through a paracellular route. These results support a model of host cytoskeleton manipulation and tissue invasion by an extracellular bacterial pathogen.

 

 

http://ajp.amjpathol.org/cgi/content/abstract/161/6/2219

 

CD44 is a major cell-surface receptor for hyaluronic acid (HA), a glycosaminoglycan component of extracellular matrix. HA-CD44 interactions have been implicated in leukocyte extravasation into an inflammatory site

 

 

 

 

SEARCH TITLE....LOSS O SULFATED GAGS STREP A INFECTION

 

http://lib.bioinfo.pl/meid:13671

 

Infect Immun. 1980 Feb ;27 (2):444-8 6991416 (P,S,E, Cited:58 Growth characteristics of group A streptococci in a new chemically defined medium.

 

I van de Rijn, R E Kessler

A new chemically defined medium for the growth of group A streptococci has been formulated. The advantages of this new medium over previously described defined media are: (i) rates of growth (i.e., doubling times) of 20 strains were comparable to the rates of growth in complex media; (ii) each strain grew to a higher culture density in the new defined medium than in complex media; (iii) transfer from complex media with small inocula was possible without any prior adaptation regimen; and (iv) the production of virulence factors (i.e., M protein and hyaluronic acid) and extracellular enzymes during growth in this new medium was comparable to that in complex media.

Mesh-terms: Bacterial Proteins :: biosynthesis; Culture Media; Deoxyribonucleases :: biosynthesis; Hyaluronic Acid :: biosynthesis; Kinetics; Streptococcus pyogenes :: growth & development; Streptococcus pyogenes :: metabolism; Streptolysins :: biosynthesis; Support, U.S. Gov't, P.H.S.;

 

 

http://lib.bioinfo.pl/auth:Sj%C3%B6bring,U

 

Eur J Biochem. 2003 May ;270 (10):2303-11 12752450 (P,S,E, Cited:1 Interactions between M proteins of Streptococcus pyogenes and glycosaminoglycans promote bacterial adhesion to host cells.

 

Inga-Maria Frick, Artur Schmidtchen, Ulf Sjöbring

Department of Cell and Molecular Biology, Section for Molecular Pathogenesis, Lund University, Sweden. Inga-Maria.Frick@medkem.lu.se

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.

Mesh-terms: Bacterial Adhesion; Bacterial Proteins :: chemistry; Bacterial Proteins :: metabolism; Cell Adhesion; Dermatan Sulfate :: chemistry; Dermatan Sulfate :: metabolism; Dose-Response Relationship, Drug; Electrophoresis, Polyacrylamide Gel; Epithelial Cells :: cytology; Gene Deletion; Glycosaminoglycans :: chemistry; Glycosaminoglycans :: metabolism; Human; Protein Binding; Streptococcus pyogenes :: metabolism; Support, Non-U.S. Gov't; Tumor Cells, Cultured; Virulence Factors :: chemistry;

 

 

http://www.blackwell-synergy.com/doi/pdf/1...0.x?cookieSet=1

 

Interactions between M proteins of Streptococcus pyogenes

and glycosaminoglycans promote bacterial adhesion to host cells

 

 

 

 

http://www3.interscience.wiley.com/cgi-bin...017607/ABSTRACT

 

Keywords

glycosaminoglycan • hyaluronan • chondroitin • heparin or heparan • synthase • polysaccharide • glycosyltransferase • extracellular matrix

 

 

Abstract

Glycosaminoglycans (linear polysaccharides with a repeating disaccharide backbone containing an amino sugar) are essential components of extracellular matrices of animals. These complex molecules play important structural, adhesion, and signaling roles in mammals. Direct detection of glycosaminoglycans has been reported in a variety of organisms, but perhaps more definitive tests for the glycosyltransferase genes should be utilized to clarify the distribution of glycosaminoglycans in metazoans. Recently, glycosyltransferases that form the hyaluronan, heparin/heparan, or chondroitin backbone were identified at the molecular level. The three types of glycosyltransferases appear to have evolved independently based on sequence comparisons and other characteristics. All metazoans appear to possess heparin/heparan. Chondroitin is found in some worms, arthropods, and higher animals. Hyaluronan is found only in two of the three main branches of chordates. The presence of several types of glycosaminoglycans in the body allows multiple communication channels and adhesion systems to operate simultaneously. Certain pathogenic bacteria produce extracellular coatings, called capsules, which are composed of glycosaminoglycans that increase their virulence during infection. The capsule helps shield the microbe from the host defenses and/or modulates host physiology. The bacterial and animal polysaccharides are chemically identical or at least very similar. Therefore, no immune response is generated, in contrast to the vast majority of capsular polymers from other bacteria. In microbial systems, it appears that in most cases functional convergent evolution of glycosaminoglycan glycosyltransferases occurred, rather than direct horizontal gene transfer from their vertebrate hosts. Anat Rec 268:317-326, 2002. © 2002 Wiley-Liss, Inc.

[kim]

http://www.md-journal.com/pt/re/medicine/a...#33;8091!-1

 

Chorea in the Antiphospholipid Syndrome: Clinical, Radiologic, and Immunologic Characteristics of 50 Patients from Our Clinics and the Recent Literature.

 

 

http://lup.sagepub.com/cgi/content/abstract/8/2/127 (bolding mine)

 

Y Shoenfeld

 

Department of Medicine B and Research Unit of Autoimmune Diseases, Sheba Medical Center, Tel Hashomer, Israel

 

A D Korczyn

 

Department of Physiology and Pharmacology, Sackler Faculty of Medicine, Tel Aviv University, Ramat Aviv 69978, Tel Hashomer, Israel

 

IgG from this patient as well as IgG from two elderly patients with high levels of aPL were subsequently shown to permeabilize the synaptosomes to labeled nicotinamide adenine dinucleotide(NAD) and pertussis toxin-ADP-ribose transferase (PTX-A protein) as assayed by labeled ADP-ribosylation of G-proteins in the membranes. No such effects were seen with the control IgG. aPL may thus have the potential to disrupt neuronal function by direct action on nerve terminals. These results may explain some of the non-thromboembolic CNS manifestations of the antiphospholipid syndrome

 

 

http://www.annalsnyas.org/cgi/content/abstract/1109/1/473

 

2-glycoprotein-I (2-GPI, also known as apolipoprotein H) is a major autoantigen in the antiphospholipid syndrome (APS), a disease commonly affecting the central nervous system.

and

 

IgG from most APS patients bound to HRGP, which shares distinct biochemical properties with 2-GPI, is present in the brain and may be an important autoantigen.

 

 

more articles on this subject

 

 

http://www.google.com/search?hl=en&rls...ion&spell=1