Tudca / Tauroursodeoxycholic Acid

Insights and discussion from the cutting edge with reference to journal articles and other research papers.
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jjnz
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Tudca / Tauroursodeoxycholic Acid

Post by jjnz »

I don't see much discussion on this fairly readily available bile salt.
Supposedly it inhibits apoptosis.
from https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4030606/

"TUDCA improves apolipoprotein E4 (APOE4) macrophage survival and function. APOE4 and APOE3 have important functions in binding to LDL receptors. APOE is a protein associated with several classes of plasma lipoproteins expressed in the liver and other tissues, including those of the central nervous system, vascular smooth muscle cells, adrenals, macrophages, and adipocytes. It contributes to cholesterol transport and modulates metabolic disease progression via lipid transport-independent mechanisms. APOE3 and APOE4 are isoforms of the polymorphic APOE that bind to LDL receptors and other LDL receptor family proteins with similar affinity. However, APOE3 appears to protect against metabolic disorders while APOE4 is a major genetic risk factor of inflammatory metabolic diseases, including atherosclerosis, diabetes, and Alzheimer's disease (AD). Increased cell death was observed in APOE4 macrophages when stimulated with LPS or oxidized LDL and was due mainly to potentiation of ER stress signaling and JNK phosphorylation.1 TUDCA attenuated LPS- and oxLDL-induced apoptosis of APOE4 macrophages to levels observed in APOE3 macrophages.

TUDCA acts as a mitochondrial stabilizer and anti-apoptotic agent in several models of neurodegenerative diseases, including AD, Parkinson's diseases (PD), and Huntington's diseases (HD). Based on mechanistic studies conducted primarily in rodent models, TUDCA may provide a novel and effective treatment in neurological disorders with its neuroprotective activities. TUDCA shows cytoprotective properties through the inhibition of apoptosis,2,9 and it has been convincingly demonstrated that T/UDCA crosses the blood brain barrier in humans.10 That said, not everyone is convinced, and there is at least one report recommending that the use of T/UDCA beyond PBC is unjustified.11

Go to:
ALZHEIMER'S DISEASE
Alzheimer's disease is a progressive and untreatable neurodegenerative disease that affects specific areas of the brain, including the hippocampus and frontal cortex. Deficits in memory and other cognitive skills compromise independent living in AD patients. The mechanisms of neuronal dysfunction and cell death in AD are not entirely understood, but there is growing evidence to suggest that apoptosis plays a key role in the loss of cell number. AD is characterized by extracellular accumulation of amyloid β-peptide (Aβ) plaques and intracellular neurofibrillary tangles (NFT) containing hyperphosphorylated tau-proteins. Aβ, a protein derived from the cleavage of the amyloid-precursor protein (APP) in high quantities aggregates to toxic amyloid plaques, affecting physiological mechanisms of the cell and induces neuronal death.

In AD brains, the primary modification of tau has been proposed as the abnormal phosphorylation. Caspase-3 cleavage of tau in the C-terminal region has also been detected in AD brains and promotes tau assembly.12 The rTg4510 mouse model is a taupathy model with massive neurodegeneration in specific cortical and limbic structures. Results from a study of the rTg4510 mouse model suggested that apoptosis is an early event associated with tau cleavage in the hippocampus and the frontal cortex, occurring prior to NFT formation and massive neuronal death. Caspase-3–cleaved intermediate tau species appear to represent a toxic form of the molecule in rTg4510 brains, resulting in protein aggregation in NFT and neuronal dysfunction. Apoptosis and caspase-3 cleavage of tau induced fibrillar Aβ were inhibited significantly by TUDCA.13

Apoptosis, a type of programmed cell death, is an energy-dependent process. There are a series of biochemical and morphological modifications, which include condensation of chromatin, shrinkage of cytoplasm, and the formation of apoptotic bodies. Apoptosis occurs primarily via extrinsic death-receptor and/or intrinsic mitochondrial pathways. Oxidative stress, DNA damage, or protein misfolding leads to mitochondrial membrane permeability, release of apoptogenic factors into the cytoplasm, and disruption of the mitochondrial membrane potential, ultimately resulting in cell death. Currently, there is no effective treatment for patients with AD. Approved drugs can enhance transmitter levels but do not slow disease progression. TUDCA has established itself as a potent inhibitor of apoptosis and may be a possible therapeutic intervention for neurodegenerative diseases such as AD.

Phosphatidylinositide 3'-OH kinase (PI3K) promotes survival downstream of apoptosis-inducing stimuli. A growing number of cellular intermediates are activated by PI3K, including the serine/threonine protein kinase Akt, which are capable of suppressing apoptosis. Aβ peptide is a strong inducer of the Bax pro-apoptotic mitochondrial pathway and a weak activator of Akt phosphorylation.14 There is significant dysregulation of anti-apoptotic Bcl-2 and proapoptotic Bax proteins in human AD tissues.12,13 TUDCA modulates Aβ-induced apoptosis by activating a PI3K survival pathway and thereby suppressing Bax translocation. Rat cortical neuron response to incubation with Aβ show that cytochrome c is significantly depleted from mitochondria. Release of cytochrome c was accompanied by caspase-3 activation, DNA degradation, and nuclear fragmentation. Bax protein levels increased in mitochondria during Aβ-induced apoptosis, and this was associated with increased release of cytochrome c. Rat cortical neurons exposed to Aβ peptide with TUDCA treatment showed significant reduction of Bax translocation, thus inhibited cytochrome c release, caspase activation, and DNA and nuclear fragmentation. In addition, TUDCA activated the PI3K-dependent survival pathway. Most notably, PI3K/Akt activation by TUDCA was sufficient to retain Bax in the cytoplasm after Aβ treatment.14

TUDCA also modulates phosphorylation and translocation of Bad via PI3K in glutamate-induced apoptosis of rat cortical neurons. Glutamate is an excitatory neurotransmitter in the CNS that regulates neuronal plasticity and induction of cell death. Cell death induced by glutamate may be involved in chronic neurodegenerative disorders, such as AD. Rat cortical neurons exposed to glutamate induced cytochrome c release, caspase activation, and morphologic changes of apoptosis. Significant reduction of glutamate-induced apoptosis of rat cortical neurons was observed in pretreatment with TUDCA. The Bcl-2 family of proteins controls the regulation of mitochondrial membrane function. Glutamate modulates the expression of Bcl-2 family proteins and induces cytochrome c release, caspase activation, and nuclear fragmentation. Incubation with TUDCA promoted phosphorylation and translocation of pro-apoptotic Bad from mitochondria to the cytosol, thereby inhibiting apoptosis and suggesting an important target for the anti-apoptotic function of TUDCA. The phosphorylation of Bad by TUDCA was also found to occur through a PI3K-dependent mechanism.15

One of the earliest sites of AD pathology is associated with reduced synapse density, and synaptic loss is highly correlated with cognitive impairment. TUDCA modulates synaptic deficits induced by amyloid and reduced the down-regulation of the postsynaptic density-95 protein (PSD-95) in an AD mouse model. TUDCA also prevented the reduction in dendritic spine number and decrease spontaneous miniature excitatory synaptic activity.16

The mitochondrial membrane is an important target in Aβ-induced cytotoxicity. An electron paramagnetic resonance (EPR) spectroscopy analysis showed that Aβ disrupted the mitochondrial membrane lipid and protein structure, inducing oxidative injury, which increases membrane permeability and release of caspase-activating factors. Lipid polarity and protein mobility were disrupted by Aβ and increased cytochrome c release. Aβ induced distress of mitochondrial function and structure were diminished by pretreatment of TUDCA.17 TUDCA was evaluated in several studies and has been shown to reduce Aβ toxicity by interfering with its production and accumulation. It inhibited Aβ-induced apoptosis by promoting mitochondrial membrane stability and reducing the release of cytochrome c and downstream activation of caspases.

In addition to mitochondria playing a central role in the apoptotic process, ER is also a critical organelle in AD. ER stress as discussed earlier leads to accumulation of unfolded or misfolded proteins like Aβ peptide. UPR is triggered by ER stress, and severe or prolonged activation of UPR results in apoptotic cell death. ER stress also leads to activation of several kinases that have functional effects on neuronal homeostasis, including apoptosis signal–regulating kinase 1 (ASK1), which triggers c-Jun N-terminal kinase (JNK) signaling. ASK1-mediated JNK activation has the potential to stimulate AD pathogenesis. Caspase-2 activation is a requirement of Aβ-induced cell death, and TUDCA prevented its activation. TUDCA also revoked Aβ-induced JNK/caspase-2 signaling and modulated Aβ-induced caspase-12-mediated apoptosis triggered by ER subcellular compartment. ER stress markers down-regulated by Aβ were partially restored by TUDCA.18

Accumulation of Aβ in the brain is associated with mutations in amyloid precursor protein (APP) and pre-senilin 1 (PS1) genes. TUDCA treatment in APP/PS1 mice decreased Aβ production and inhibited accumulation of Aβ deposits in the brain. Decreased Aβ levels were observed in both hippocampus and frontal cortex of TUDCA-treated APP/PSI mice. These findings suggested that TUDCA interferes with Aβ production, possibly by regulation of lipid metabolism mediators. Activation of astrocytes and microglia in areas of Aβ plaques contributes to an inflammatory process that develops around the injury in the brain. Activated astrocytes and microglia were visualized by GFAP immunoreactivity and Iba-I immunoreactivity, respectively, and observed in APP/PSI mice. Significantly less GFAP immunoreactivity and Iba-I immunoreactivity were observed in TUDCA-treated APP/PSI mice, suggesting that TUDCA inhibits activation of astrocytes and microglia. Marked improvement in the integrity of MAP2-positive neuronal fibers was observed around the amyloid plaques in the brains of TUDCA-treated APP/PSI. It was suggested that the rates of neuronal degeneration in APP/PSI mice treated with TUDCA were significantly decreased.19

Memory loss and cognitive decline are major hallmarks observed in AD patients. Learning and working-memory tasks rely predominantly on hippocampal function. TUDCA prevented downstream abnormal conformations of tau, which may have beneficial consequences in slowing cognitive decline.18 Based on the contextual fear-conditioning test, it was suggested that TUDCA may prevent memory deficits in APP/PS1 mice via attenuation of Aβ-associated neurodegeneration.19 Findings from another study in APP/PSI mice suggested that dietary TUDCA supplementation improved the use of spatial search strategies during a maze in APP/PS1 mice. It also showed improvement in social memory and passive avoidance learning in APP/PSI mice.20

Cerebral amyloid angiopathy (CAA) is common feature of AD. This age-associated condition is characterized by the deposition of amyloid peptides in cortical and leptomeningeal vessels that cause capillary disruption and endothelial dysfunction. CAA plays a significant role in intracerebral hemorrhage. There is limited information regarding the effect of amyloid peptides on endothelial vessel wall cells that are in contact with vascular amyloid deposits in CAA. E22Q is a glutamine to glutamic acid substitution at residue 22 and is associated with hereditary cerebral hemorrhage with amyloidosis Dutch type. TUDCA protected brain microvascular endothelial cells from apoptotic insult triggered by the potent vasculotropic E22Q peptide. TUDCA also prevented AβE22Q-induced mitochondrial Bax translocation, cytochrome c release and subsequent cell death.21 Such studies provide new perspectives in modulating amyloid-induced toxicity in CAA and suggest TUDCA as a potential therapeutic intervention for AD"

Interesting, it's dirt cheap and available on the likes of Amazon, has anyone tried it and if so noticed any cholesterol changes?
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Korie
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Re: Tudca / Tauroursodeoxycholic Acid

Post by Korie »

Thanks for posting! This certainly is very interesting. As a newbie, I will have to read up more on this. I wonder if any of our more seasoned posters have an insights??
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Re: Tudca / Tauroursodeoxycholic Acid

Post by NewRon »

Has anyone found any more about TUDCA?
Apo E4/E4, Male, Age 60
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SusanJ
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Re: Tudca / Tauroursodeoxycholic Acid

Post by SusanJ »

NewRon wrote:Has anyone found any more about TUDCA?
Here's a good overview from 2019. I'd say that more research is still needed.
4. Therapeutic Perspectives and Limitations
With all that being said, not every piece of information concerning TUDCA/UDCA activity is so optimistic in pointing to these bile acids as a universal cure for a plenitude of diseases. Although in the vast majority of research TUDCA is presented as a very efficient and promising agent in pharmacological management of many disorders, there is one report saying that the utilization of UDCA beyond primary biliary cholangitis is unjustified [193]. The unsuspected side effects of UDCA treatment seem to include e.g., cholangitis, hepatitis, ascites, pruritus, vanishing bile duct syndrome, liver cell failure, severe watery diarrhea, immune-suppression, and mutagenic effects. On the molecular level, UDCA was implied to inhibit DNA repair, phagocytosis, and NOS induction, as well as suppress activation of co-enzyme A, cyclic AMP, and p53 [193]. Also, pro-carcinogenic potential of UDCA has been suggested [194]. Regarding this information, one should keep in mind that similar results have not been presented for TUDCA, however, close structural proximity of both bile acids raises some doubts and suggests treating the results of pre-clinical studies with sufficient caution.
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6952947/
NewRon
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Re: Tudca / Tauroursodeoxycholic Acid

Post by NewRon »

"...cholangitis, hepatitis, ascites, pruritus, vanishing bile duct syndrome, liver cell failure, severe watery diarrhea, immune-suppression, and mutagenic effects."

Cripes!
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Sara Barthel
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Re: Tudca / Tauroursodeoxycholic Acid

Post by Sara Barthel »

jjnz wrote:I don't see much discussion on this fairly readily available bile salt.
Supposedly it inhibits apoptosis.
from https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4030606/

"TUDCA improves apolipoprotein E4 (APOE4) macrophage survival and function. APOE4 and APOE3 have important functions in binding to LDL receptors. APOE is a protein associated with several classes of plasma lipoproteins expressed in the liver and other tissues, including those of the central nervous system, vascular smooth muscle cells, adrenals, macrophages, and adipocytes. It contributes to cholesterol transport and modulates metabolic disease progression via lipid transport-independent mechanisms. APOE3 and APOE4 are isoforms of the polymorphic APOE that bind to LDL receptors and other LDL receptor family proteins with similar affinity. However, APOE3 appears to protect against metabolic disorders while APOE4 is a major genetic risk factor of inflammatory metabolic diseases, including atherosclerosis, diabetes, and Alzheimer's disease (AD). Increased cell death was observed in APOE4 macrophages when stimulated with LPS or oxidized LDL and was due mainly to potentiation of ER stress signaling and JNK phosphorylation.1 TUDCA attenuated LPS- and oxLDL-induced apoptosis of APOE4 macrophages to levels observed in APOE3 macrophages.

TUDCA acts as a mitochondrial stabilizer and anti-apoptotic agent in several models of neurodegenerative diseases, including AD, Parkinson's diseases (PD), and Huntington's diseases (HD). Based on mechanistic studies conducted primarily in rodent models, TUDCA may provide a novel and effective treatment in neurological disorders with its neuroprotective activities. TUDCA shows cytoprotective properties through the inhibition of apoptosis,2,9 and it has been convincingly demonstrated that T/UDCA crosses the blood brain barrier in humans.10 That said, not everyone is convinced, and there is at least one report recommending that the use of T/UDCA beyond PBC is unjustified.11

Go to:
ALZHEIMER'S DISEASE
Alzheimer's disease is a progressive and untreatable neurodegenerative disease that affects specific areas of the brain, including the hippocampus and frontal cortex. Deficits in memory and other cognitive skills compromise independent living in AD patients. The mechanisms of neuronal dysfunction and cell death in AD are not entirely understood, but there is growing evidence to suggest that apoptosis plays a key role in the loss of cell number. AD is characterized by extracellular accumulation of amyloid β-peptide (Aβ) plaques and intracellular neurofibrillary tangles (NFT) containing hyperphosphorylated tau-proteins. Aβ, a protein derived from the cleavage of the amyloid-precursor protein (APP) in high quantities aggregates to toxic amyloid plaques, affecting physiological mechanisms of the cell and induces neuronal death.

In AD brains, the primary modification of tau has been proposed as the abnormal phosphorylation. Caspase-3 cleavage of tau in the C-terminal region has also been detected in AD brains and promotes tau assembly.12 The rTg4510 mouse model is a taupathy model with massive neurodegeneration in specific cortical and limbic structures. Results from a study of the rTg4510 mouse model suggested that apoptosis is an early event associated with tau cleavage in the hippocampus and the frontal cortex, occurring prior to NFT formation and massive neuronal death. Caspase-3–cleaved intermediate tau species appear to represent a toxic form of the molecule in rTg4510 brains, resulting in protein aggregation in NFT and neuronal dysfunction. Apoptosis and caspase-3 cleavage of tau induced fibrillar Aβ were inhibited significantly by TUDCA.13

Apoptosis, a type of programmed cell death, is an energy-dependent process. There are a series of biochemical and morphological modifications, which include condensation of chromatin, shrinkage of cytoplasm, and the formation of apoptotic bodies. Apoptosis occurs primarily via extrinsic death-receptor and/or intrinsic mitochondrial pathways. Oxidative stress, DNA damage, or protein misfolding leads to mitochondrial membrane permeability, release of apoptogenic factors into the cytoplasm, and disruption of the mitochondrial membrane potential, ultimately resulting in cell death. Currently, there is no effective treatment for patients with AD. Approved drugs can enhance transmitter levels but do not slow disease progression. TUDCA has established itself as a potent inhibitor of apoptosis and may be a possible therapeutic intervention for neurodegenerative diseases such as AD.

Phosphatidylinositide 3'-OH kinase (PI3K) promotes survival downstream of apoptosis-inducing stimuli. A growing number of cellular intermediates are activated by PI3K, including the serine/threonine protein kinase Akt, which are capable of suppressing apoptosis. Aβ peptide is a strong inducer of the Bax pro-apoptotic mitochondrial pathway and a weak activator of Akt phosphorylation.14 There is significant dysregulation of anti-apoptotic Bcl-2 and proapoptotic Bax proteins in human AD tissues.12,13 TUDCA modulates Aβ-induced apoptosis by activating a PI3K survival pathway and thereby suppressing Bax translocation. Rat cortical neuron response to incubation with Aβ show that cytochrome c is significantly depleted from mitochondria. Release of cytochrome c was accompanied by caspase-3 activation, DNA degradation, and nuclear fragmentation. Bax protein levels increased in mitochondria during Aβ-induced apoptosis, and this was associated with increased release of cytochrome c. Rat cortical neurons exposed to Aβ peptide with TUDCA treatment showed significant reduction of Bax translocation, thus inhibited cytochrome c release, caspase activation, and DNA and nuclear fragmentation. In addition, TUDCA activated the PI3K-dependent survival pathway. Most notably, PI3K/Akt activation by TUDCA was sufficient to retain Bax in the cytoplasm after Aβ treatment.14

TUDCA also modulates phosphorylation and translocation of Bad via PI3K in glutamate-induced apoptosis of rat cortical neurons. Glutamate is an excitatory neurotransmitter in the CNS that regulates neuronal plasticity and induction of cell death. Cell death induced by glutamate may be involved in chronic neurodegenerative disorders, such as AD. Rat cortical neurons exposed to glutamate induced cytochrome c release, caspase activation, and morphologic changes of apoptosis. Significant reduction of glutamate-induced apoptosis of rat cortical neurons was observed in pretreatment with TUDCA. The Bcl-2 family of proteins controls the regulation of mitochondrial membrane function. Glutamate modulates the expression of Bcl-2 family proteins and induces cytochrome c release, caspase activation, and nuclear fragmentation. Incubation with TUDCA promoted phosphorylation and translocation of pro-apoptotic Bad from mitochondria to the cytosol, thereby inhibiting apoptosis and suggesting an important target for the anti-apoptotic function of TUDCA. The phosphorylation of Bad by TUDCA was also found to occur through a PI3K-dependent mechanism.15

One of the earliest sites of AD pathology is associated with reduced synapse density, and synaptic loss is highly correlated with cognitive impairment. TUDCA modulates synaptic deficits induced by amyloid and reduced the down-regulation of the postsynaptic density-95 protein (PSD-95) in an AD mouse model. TUDCA also prevented the reduction in dendritic spine number and decrease spontaneous miniature excitatory synaptic activity.16

The mitochondrial membrane is an important target in Aβ-induced cytotoxicity. An electron paramagnetic resonance (EPR) spectroscopy analysis showed that Aβ disrupted the mitochondrial membrane lipid and protein structure, inducing oxidative injury, which increases membrane permeability and release of caspase-activating factors. Lipid polarity and protein mobility were disrupted by Aβ and increased cytochrome c release. Aβ induced distress of mitochondrial function and structure were diminished by pretreatment of TUDCA.17 TUDCA was evaluated in several studies and has been shown to reduce Aβ toxicity by interfering with its production and accumulation. It inhibited Aβ-induced apoptosis by promoting mitochondrial membrane stability and reducing the release of cytochrome c and downstream activation of caspases.

In addition to mitochondria playing a central role in the apoptotic process, ER is also a critical organelle in AD. ER stress as discussed earlier leads to accumulation of unfolded or misfolded proteins like Aβ peptide. UPR is triggered by ER stress, and severe or prolonged activation of UPR results in apoptotic cell death. ER stress also leads to activation of several kinases that have functional effects on neuronal homeostasis, including apoptosis signal–regulating kinase 1 (ASK1), which triggers c-Jun N-terminal kinase (JNK) signaling. ASK1-mediated JNK activation has the potential to stimulate AD pathogenesis. Caspase-2 activation is a requirement of Aβ-induced cell death, and TUDCA prevented its activation. TUDCA also revoked Aβ-induced JNK/caspase-2 signaling and modulated Aβ-induced caspase-12-mediated apoptosis triggered by ER subcellular compartment. ER stress markers down-regulated by Aβ were partially restored by TUDCA.18

Accumulation of Aβ in the brain is associated with mutations in amyloid precursor protein (APP) and pre-senilin 1 (PS1) genes. TUDCA treatment in APP/PS1 mice decreased Aβ production and inhibited accumulation of Aβ deposits in the brain. Decreased Aβ levels were observed in both hippocampus and frontal cortex of TUDCA-treated APP/PSI mice. These findings suggested that TUDCA interferes with Aβ production, possibly by regulation of lipid metabolism mediators. Activation of astrocytes and microglia in areas of Aβ plaques contributes to an inflammatory process that develops around the injury in the brain. Activated astrocytes and microglia were visualized by GFAP immunoreactivity and Iba-I immunoreactivity, respectively, and observed in APP/PSI mice. Significantly less GFAP immunoreactivity and Iba-I immunoreactivity were observed in TUDCA-treated APP/PSI mice, suggesting that TUDCA inhibits activation of astrocytes and microglia. Marked improvement in the integrity of MAP2-positive neuronal fibers was observed around the amyloid plaques in the brains of TUDCA-treated APP/PSI. It was suggested that the rates of neuronal degeneration in APP/PSI mice treated with TUDCA were significantly decreased.19

Memory loss and cognitive decline are major hallmarks observed in AD patients. Learning and working-memory tasks rely predominantly on hippocampal function. TUDCA prevented downstream abnormal conformations of tau, which may have beneficial consequences in slowing cognitive decline.18 Based on the contextual fear-conditioning test, it was suggested that TUDCA may prevent memory deficits in APP/PS1 mice via attenuation of Aβ-associated neurodegeneration.19 Findings from another study in APP/PSI mice suggested that dietary TUDCA supplementation improved the use of spatial search strategies during a maze in APP/PS1 mice. It also showed improvement in social memory and passive avoidance learning in APP/PSI mice.20

Cerebral amyloid angiopathy (CAA) is common feature of AD. This age-associated condition is characterized by the deposition of amyloid peptides in cortical and leptomeningeal vessels that cause capillary disruption and endothelial dysfunction. CAA plays a significant role in intracerebral hemorrhage. There is limited information regarding the effect of amyloid peptides on endothelial vessel wall cells that are in contact with vascular amyloid deposits in CAA. E22Q is a glutamine to glutamic acid substitution at residue 22 and is associated with hereditary cerebral hemorrhage with amyloidosis Dutch type. TUDCA protected brain microvascular endothelial cells from apoptotic insult triggered by the potent vasculotropic E22Q peptide. TUDCA also prevented AβE22Q-induced mitochondrial Bax translocation, cytochrome c release and subsequent cell death.21 Such studies provide new perspectives in modulating amyloid-induced toxicity in CAA and suggest TUDCA as a potential therapeutic intervention for AD"

Interesting, it's dirt cheap and available on the likes of Amazon, has anyone tried it and if so noticed any cholesterol changes?
Wow thank you for sharing this information Jinz! I have been extremely impressed with the quality and efficacy of BodyBio products and just ordered TUDCA and ox bile to take in conjunction with their liquid phosphatidylcholine product (PC) primarily for gut healing and preventative brain health but was not aware of the potentially powerful effects of TUDCA on its own as well.
SarahAnne
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Re: Tudca / Tauroursodeoxycholic Acid

Post by SarahAnne »

Since we’re 3 months since last post here, I’m wondering if anyone is taking TUDCA and noticing any benefits and/or side effects? Or, whether any of the experts here have further info about taking this. Many thx:)
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