oxalate/arachidonic acid

[Guest guest]

,

Neathery always shows very high ranges of arachidonic acid. We've been told

repeatedly to keep her away from meats. They funny thing is - she has NEVER

eaten meat. Well, she's eaten maybe 2 or 3 hamburgers over the past 12 1/2 years

but that's it. From what I read of your post - sulfates are connected in

arachidonic acid. Dr. Barry Sears wrote that you can inject a rabbit with every

form of fat and the rabbit is o.k. When a rabbit is injected with arachidonic

acid it dies within 3 hours. Our daughter is just so biologically injured. I

never know what to do anymore. I'm more interested in the sulfate connection

than ever.

Shari

[Guest guest]

Shari,

If the increased arachidonic acid is reflective of what is happening in the

red cell membrane, then your daughter may be experiencing heightened

oxalate transport via red blood cells. This would not be reflected in a

plasma test for oxalate, and we really don't know where oxalate is

travelling that is being transported via red blood cells.

Oxalate transport via red blood cells is also stepped up if you are blood

type O and have exposure to some antigens that are seen in celiac

disease. I am blood type O, and have done so much better since I got off

gluten 12 years ago. My own history makes me wonder if transport of

oxalate via red blood cells might for some reasons traffick oxalate to

places other than the kidney. I never have had kidney issues, but I did

have bone marrow failure!

4: J Am Soc Nephrol. 1999 Nov;10 Suppl 14:S381-4.

Specific modulatory effect of arachidonic acid on human red blood cell oxalate

transport: clinical implications in calcium oxalate nephrolithiasis.

Baggio B, Priante G, Brunati AM, Clari G, Bordin L.

Department of Medical-Surgery Sciences, University of Padua, Italy.

BBaggio@...

Greater arachidonic acid (AA) contents, which were correlated with erythrocyte

transmembrane oxalate (Ox) transport, were observed in plasma and erythrocyte

membrane phospholipids of patients with idiopathic calcium renal stones,

suggesting a link between membrane phospholipid fatty acid composition and

cellular Ox transport. To confirm this hypothesis, the effects of exogenous red

blood cell incorporation of three different fatty acids (i.e., oleic acid, AA,

and eicosapentaenoic acid) on Ox transport and the phosphorylation status of

band 3 protein, which has been shown to mediate red blood cell Ox flux, were

investigated. Preincubation of erythrocytes with AA induced a dose-dependent

increase in the phosphorylation level of band 3 protein and an increase in

transmembrane Ox self-exchange. In contrast, inhibitory effects on both

parameters were observed after the incorporation of oleic and eicosapentaenoic

acids. These data, together with previous observations of dietary effects on

erythrocyte Ox transport and urinary Ox excretion, indicate that genetic and/or

nutritional changes in membrane phospholipid fatty acid composition play a

crucial role in modulating cellular Ox transport in idiopathic calcium Ox

nephrolithiasis.

PMID: 10541268 [PubMed - indexed for MEDLINE]

J Lab Clin Med. 2000 Jan;135(1):89-95. Related Articles, Links

Click here to read

Dietary manipulation of delta-6-desaturase modifies phospholipid

arachidonic acid levels and the urinary excretion of calcium and oxalate in

the rat: insight in calcium lithogenesis.

Gambaro G, Bordoni A, Hrelia S, Bordin L, Biagi P, Semplicini A, Clari

G, Manzato E, Baggio B.

Department of Medical and Surgical Sciences, School of Medicine,

University of Padova, Italy.

An anomalous n-6 polyunsaturated fatty acid composition in plasma and

erythrocyte membrane phospholipids, namely increased levels of arachidonic

acid (AA), has been reported in calcium nephrolithiasis and has been

proposed to play an important role in its pathogenesis. To confirm this, in

rats we modified phospholipid AA levels by dietary manipulation of the

delta-6-desaturase, the rate-limiting enzyme of the fatty acid biosynthetic

pathway, and evaluated the effect on cellular and renal functions

predisposing to lithogenesis. Increased AA levels led to conditions at risk

for nephrolithiasis: higher oxalate flux and lower sodium cotransport in

erythrocytes and a rise in urinary prostaglandin E2, calcium, sodium, and

oxalate levels; reduced AA levels reversed these changes. In vitro, in

human erythrocytes the incorporation of exogenous AA into membranes

increased band 3 protein phosphorylation directly activating the Ser/Thr

protein kinase CK1 and induced a parallel raise in band 3-mediated oxalate

transport. These findings demonstrate the pivotal role of phospholipid AA

in modulating erythrocyte and renal transport of calcium and oxalate.

PMID: 10638699 [PubMed - indexed for MEDLINE]

J Cell Physiol. 1993 Nov;157(2):403-7. Related Articles, Links

ABH antigens as recognition sites for the activation of red blood cell

anion exchange by the lectin ulex europaeus agglutinin I.

Engelmann B.

Physiologisches Institut, Universitat Munchen, Germany.

The blood group antigen H (blood group O) and fucose-specific lectin

Ulex europaeus agglutinin I (UEA1) (10 micrograms/ml) was found to increase

the rate constant of Cl- efflux into 100 mM Na+ oxalate media by about 40%

in erythrocytes taken from antigen H donors. In 100 mM K+ oxalate, 150 mM

Na+ pyruvate and in 150 mM Na+ acetate media the lectin elevated the rate

constant of Cl- efflux by 20-50%. The acceleration of Cl- efflux by UEA1

was completely blocked by 10 microM

4,4'-diisothiocyanato-stilbene-2,2'-disulfonic acid (DIDS) indicating that

the effect of the lectin is mediated by the anion exchanger of human

erythrocytes (band 3 protein). In antigen A1 erythrocytes no significant

stimulation of anion exchange by UEA1 was seen. The activation of Cl-

efflux was completely prevented by addition of 1 mM fucose to the medium.

These results suggest that the effect of UEA1 is mediated through

interaction with the fucose residues of H antigens. Increasing

extracellular Ca++ from 0.5 to 5 mM in Na+ pyruvate or Na+ acetate media

slightly reduced the acceleration of anion exchange by the lectin. On the

other hand, replacing part of extracellular chloride by bicarbonate did not

considerably alter the (previously reported) stimulatory effect of UEA1 on

red blood cell Ca++ uptake. This suggests that the acceleration of anion

exchange and of Ca++ uptake by UEA1, respectively, are mediated by

different mechanisms. It is concluded that UEA1 activates anion exchange of

human erythrocytes most probably by a direct interaction with H antigens

present on extracellular domains of the band 3 protein.

PMID: 7693725 [PubMed - indexed for MEDLINE]

Am J Gastroenterol. 2004 May;99(5):894-904.[] Links

Erratum in:

Am J Gastroenterol. 2004 Jul;99(7):following 1406.

Comment in:

Am J Gastroenterol. 2004 May;99(5):905-6.

Presence of bacteria and innate immunity of intestinal epithelium in

childhood celiac disease.

Forsberg G,

Fahlgren A,

Horstedt P,

Hammarstrom S,

Hernell O,

Hammarstrom ML.

Department of Clinical Microbiology and Immunology, Umea University, Umea,

Sweden.

OBJECTIVES: Exposure to gliadin and related prolamins and appropriate

HLA-DQ haplotype are necessary but not sufficient for contracting celiac

disease (CD). Aberrant innate immune reactions could be contributing risk

factors. Therefore, jejunal biopsies were screened for bacteria and the

innate immune status of the epithelium investigated. METHODS: Children with

untreated, treated, challenged CD, and controls were analyzed. Bacteria

were identified by scanning electron microscopy. Glycocalyx composition and

mucin and antimicrobial peptide production were studied by quantitative

RT-PCR, antibody and lectin immunohistochemistry. RESULTS: Rod-shaped

bacteria were frequently associated with the mucosa of CD patients, with

both active and inactive disease, but not with controls. The lectin Ulex

europaeus agglutinin I (UEAI) stained goblet cells in the mucosa of all CD

patients but not of controls. The lectin peanut agglutinin (PNA) stained

glycocalyx of controls but not of CD patients. mRNA levels of mucin-2

(MUC2), alpha-defensins HD-5 and HD-6, and lysozyme were significantly

increased in active CD and returned to normal in treated CD. Their

expression levels correlated to the interferon-gamma mRNA levels in

intraepithelial lymphocytes. MUC2, HD-5, and lysozyme proteins were seen in

absorptive epithelial cells. beta-defensins hBD-1 and hBD-2,

carcinoembryonic antigen (CEA), CEA cell adhesion molecule-1a (CEACAM1a),

and MUC3 were not affected. CONCLUSIONS: Unique carbohydrate structures of

the glycocalyx/mucous layer are likely discriminating features of CD

patients. These glycosylation differences could facilitate bacterial

adhesion. Ectopic production of MUC2, HD-5, and lysozyme in active CD is

compatible with goblet and Paneth cell metaplasia induced by high

interferon-gamma production by intraepithelial lymphocytes.

PMID: 15128357 [PubMed - indexed for MEDLINE]

\At 10:19 AM 5/14/2007, you wrote:

>,

>Neathery always shows very high ranges of arachidonic acid. We've been

>told repeatedly to keep her away from meats. They funny thing is - she has

>NEVER eaten meat. Well, she's eaten maybe 2 or 3 hamburgers over the past

>12 1/2 years but that's it. From what I read of your post - sulfates are

>connected in arachidonic acid. Dr. Barry Sears wrote that you can inject a

>rabbit with every form of fat and the rabbit is o.k. When a rabbit is

>injected with arachidonic acid it dies within 3 hours. Our daughter is

>just so biologically injured. I never know what to do anymore. I'm more

>interested in the sulfate connection than ever.

>Shari

>

>

[Guest guest]

My mother just had a bone marrow transplant - actually two from the same donor.

She was diagnosed with Acute Myeloid Leukemia 16 months ago.

Shari

Re: oxalate/arachidonic acid

Shari,

If the increased arachidonic acid is reflective of what is happening in the

red cell membrane, then your daughter may be experiencing heightened

oxalate transport via red blood cells. This would not be reflected in a

plasma test for oxalate, and we really don't know where oxalate is

travelling that is being transported via red blood cells.

Oxalate transport via red blood cells is also stepped up if you are blood

type O and have exposure to some antigens that are seen in celiac

disease. I am blood type O, and have done so much better since I got off

gluten 12 years ago. My own history makes me wonder if transport of

oxalate via red blood cells might for some reasons traffick oxalate to

places other than the kidney. I never have had kidney issues, but I did

have bone marrow failure!

4: J Am Soc Nephrol. 1999 Nov;10 Suppl 14:S381-4.

Specific modulatory effect of arachidonic acid on human red blood cell oxalate

transport: clinical implications in calcium oxalate nephrolithiasis.

Baggio B, Priante G, Brunati AM, Clari G, Bordin L.

Department of Medical-Surgery Sciences, University of Padua, Italy.

BBaggio@...

Greater arachidonic acid (AA) contents, which were correlated with erythrocyte

transmembrane oxalate (Ox) transport, were observed in plasma and erythrocyte

membrane phospholipids of patients with idiopathic calcium renal stones,

suggesting a link between membrane phospholipid fatty acid composition and

cellular Ox transport. To confirm this hypothesis, the effects of exogenous

red

blood cell incorporation of three different fatty acids (i.e., oleic acid, AA,

and eicosapentaenoic acid) on Ox transport and the phosphorylation status of

band 3 protein, which has been shown to mediate red blood cell Ox flux, were

investigated. Preincubation of erythrocytes with AA induced a dose-dependent

increase in the phosphorylation level of band 3 protein and an increase in

transmembrane Ox self-exchange. In contrast, inhibitory effects on both

parameters were observed after the incorporation of oleic and eicosapentaenoic

acids. These data, together with previous observations of dietary effects on

erythrocyte Ox transport and urinary Ox excretion, indicate that genetic

and/or

nutritional changes in membrane phospholipid fatty acid composition play a

crucial role in modulating cellular Ox transport in idiopathic calcium Ox

nephrolithiasis.

PMID: 10541268 [PubMed - indexed for MEDLINE]

J Lab Clin Med. 2000 Jan;135(1):89-95. Related Articles, Links

Click here to read

Dietary manipulation of delta-6-desaturase modifies phospholipid

arachidonic acid levels and the urinary excretion of calcium and oxalate in

the rat: insight in calcium lithogenesis.

Gambaro G, Bordoni A, Hrelia S, Bordin L, Biagi P, Semplicini A, Clari

G, Manzato E, Baggio B.

Department of Medical and Surgical Sciences, School of Medicine,

University of Padova, Italy.

An anomalous n-6 polyunsaturated fatty acid composition in plasma and

erythrocyte membrane phospholipids, namely increased levels of arachidonic

acid (AA), has been reported in calcium nephrolithiasis and has been

proposed to play an important role in its pathogenesis. To confirm this, in

rats we modified phospholipid AA levels by dietary manipulation of the

delta-6-desaturase, the rate-limiting enzyme of the fatty acid biosynthetic

pathway, and evaluated the effect on cellular and renal functions

predisposing to lithogenesis. Increased AA levels led to conditions at risk

for nephrolithiasis: higher oxalate flux and lower sodium cotransport in

erythrocytes and a rise in urinary prostaglandin E2, calcium, sodium, and

oxalate levels; reduced AA levels reversed these changes. In vitro, in

human erythrocytes the incorporation of exogenous AA into membranes

increased band 3 protein phosphorylation directly activating the Ser/Thr

protein kinase CK1 and induced a parallel raise in band 3-mediated oxalate

transport. These findings demonstrate the pivotal role of phospholipid AA

in modulating erythrocyte and renal transport of calcium and oxalate.

PMID: 10638699 [PubMed - indexed for MEDLINE]

J Cell Physiol. 1993 Nov;157(2):403-7. Related Articles, Links

ABH antigens as recognition sites for the activation of red blood cell

anion exchange by the lectin ulex europaeus agglutinin I.

Engelmann B.

Physiologisches Institut, Universitat Munchen, Germany.

The blood group antigen H (blood group O) and fucose-specific lectin

Ulex europaeus agglutinin I (UEA1) (10 micrograms/ml) was found to increase

the rate constant of Cl- efflux into 100 mM Na+ oxalate media by about 40%

in erythrocytes taken from antigen H donors. In 100 mM K+ oxalate, 150 mM

Na+ pyruvate and in 150 mM Na+ acetate media the lectin elevated the rate

constant of Cl- efflux by 20-50%. The acceleration of Cl- efflux by UEA1

was completely blocked by 10 microM

4,4'-diisothiocyanato-stilbene-2,2'-disulfonic acid (DIDS) indicating that

the effect of the lectin is mediated by the anion exchanger of human

erythrocytes (band 3 protein). In antigen A1 erythrocytes no significant

stimulation of anion exchange by UEA1 was seen. The activation of Cl-

efflux was completely prevented by addition of 1 mM fucose to the medium.

These results suggest that the effect of UEA1 is mediated through

interaction with the fucose residues of H antigens. Increasing

extracellular Ca++ from 0.5 to 5 mM in Na+ pyruvate or Na+ acetate media

slightly reduced the acceleration of anion exchange by the lectin. On the

other hand, replacing part of extracellular chloride by bicarbonate did not

considerably alter the (previously reported) stimulatory effect of UEA1 on

red blood cell Ca++ uptake. This suggests that the acceleration of anion

exchange and of Ca++ uptake by UEA1, respectively, are mediated by

different mechanisms. It is concluded that UEA1 activates anion exchange of

human erythrocytes most probably by a direct interaction with H antigens

present on extracellular domains of the band 3 protein.

PMID: 7693725 [PubMed - indexed for MEDLINE]

Am J Gastroenterol. 2004 May;99(5):894-904.[] Links

Erratum in:

Am J Gastroenterol. 2004 Jul;99(7):following 1406.

Comment in:

Am J Gastroenterol. 2004 May;99(5):905-6.

Presence of bacteria and innate immunity of intestinal epithelium in

childhood celiac disease.

Forsberg G,

Fahlgren A,

Horstedt P,

Hammarstrom S,

Hernell O,

Hammarstrom ML.

Department of Clinical Microbiology and Immunology, Umea University, Umea,

Sweden.

OBJECTIVES: Exposure to gliadin and related prolamins and appropriate

HLA-DQ haplotype are necessary but not sufficient for contracting celiac

disease (CD). Aberrant innate immune reactions could be contributing risk

factors. Therefore, jejunal biopsies were screened for bacteria and the

innate immune status of the epithelium investigated. METHODS: Children with

untreated, treated, challenged CD, and controls were analyzed. Bacteria

were identified by scanning electron microscopy. Glycocalyx composition and

mucin and antimicrobial peptide production were studied by quantitative

RT-PCR, antibody and lectin immunohistochemistry. RESULTS: Rod-shaped

bacteria were frequently associated with the mucosa of CD patients, with

both active and inactive disease, but not with controls. The lectin Ulex

europaeus agglutinin I (UEAI) stained goblet cells in the mucosa of all CD

patients but not of controls. The lectin peanut agglutinin (PNA) stained

glycocalyx of controls but not of CD patients. mRNA levels of mucin-2

(MUC2), alpha-defensins HD-5 and HD-6, and lysozyme were significantly

increased in active CD and returned to normal in treated CD. Their

expression levels correlated to the interferon-gamma mRNA levels in

intraepithelial lymphocytes. MUC2, HD-5, and lysozyme proteins were seen in

absorptive epithelial cells. beta-defensins hBD-1 and hBD-2,

carcinoembryonic antigen (CEA), CEA cell adhesion molecule-1a (CEACAM1a),

and MUC3 were not affected. CONCLUSIONS: Unique carbohydrate structures of

the glycocalyx/mucous layer are likely discriminating features of CD

patients. These glycosylation differences could facilitate bacterial

adhesion. Ectopic production of MUC2, HD-5, and lysozyme in active CD is

compatible with goblet and Paneth cell metaplasia induced by high

interferon-gamma production by intraepithelial lymphocytes.

PMID: 15128357 [PubMed - indexed for MEDLINE]

\At 10:19 AM 5/14/2007, you wrote:

>,

>Neathery always shows very high ranges of arachidonic acid. We've been

>told repeatedly to keep her away from meats. They funny thing is - she has

>NEVER eaten meat. Well, she's eaten maybe 2 or 3 hamburgers over the past

>12 1/2 years but that's it. From what I read of your post - sulfates are

>connected in arachidonic acid. Dr. Barry Sears wrote that you can inject a

>rabbit with every form of fat and the rabbit is o.k. When a rabbit is

>injected with arachidonic acid it dies within 3 hours. Our daughter is

>just so biologically injured. I never know what to do anymore. I'm more

>interested in the sulfate connection than ever.

>Shari

>

>