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16: J Cell Sci. 1992 Jun;102 ( Pt 2):307-14.

<http://www.ncbi.nlm.nih.gov/sites/entrez?Db=pubmed & DbFrom=pubmed & Cmd=Link & LinkN\

ame=pubmed_pubmed & LinkReadableName=Related%20Articles & IdsFromResult=1383244 & ordi\

nalpos=16 & itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_RVAbstra\

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http://jcs.biologists.org/cgi/reprint/102/2/307

*Mitochondrial gene expression in the human gastrointestinal tract.*

In the human gastrointestinal epithelium, in situ hybridisation

demonstrates that 12 S and 16 S mitochondrial ribosomal RNAs show

maximal steady-state levels on the surface epithelial cells of the

normal small intestine and colon. The mitochondrial mRNAs,

cytochrome b and NADH dehydrogenase (IV) have a uniform distribution

throughout the crypt and surface (villus) epithelial cells of the

small intestine and colon. Histochemical stains for the activity of

the mitochondrial respiratory chain enzymes succinate dehydrogenase

and cytochrome oxidase also show almost uniform activities

throughout the crypt-surface epithelial cell axis in the small and

large intestines. In sections of normal human oesophagus the levels

of mitochondrial ribosomal RNAs, mitochondrial mRNAs and the

activities of mitochondrial respiratory chain enzymes are maximal

over the basal cells of the stratified squamous epithelium. These

results show a relative increase in mitochondrial ribosomal RNA

expression compared with mitochondrial mRNAs in surface cells of

simple intestinal epithelia.

PMID: 1383244

1: Indian J Pediatr. 2006 Dec;73(12):1112-4.

<http://www.ncbi.nlm.nih.gov/sites/entrez?Db=pubmed & DbFrom=pubmed & Cmd=Link & LinkN\

ame=pubmed_pubmed & LinkReadableName=Related%20Articles & IdsFromResult=17202642 & ord\

inalpos=1 & itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_RVAbstra\

ct>

http://www.ijppediatricsindia.org/text.asp?2006/73/12/1112/29665

*Mitochondrial neuro-gastrointestinal encephalopathy syndrome.*

Mitochondrial neurogastrointestinal encephalomyopathy is a rare

disorder affecting the pediatric age group with a heterogeneous

multisystem involvement. We happen to manage a young child with

symptoms of constipation since infancy along with cachexia, seizures

and peripheral neuropathy. The child later went into encephalopathy

preterminally. This clinical syndrome fitted very well with

mitochondrial neurogastrointestinal encephalomyopathy. The child had

elevated lactate levels and electron microscopy of the rectal biopsy

was suggestive of a mitochondrial disorder To the best of our

knowledge there is no case report of this syndrome from India and

since this presents with diagnostic difficulties so is being reported.

PMID: 17202642

2: Turk J Gastroenterol. 2005 Sep;16(3):163-6.

<http://www.ncbi.nlm.nih.gov/sites/entrez?Db=pubmed & DbFrom=pubmed & Cmd=Link & LinkN\

ame=pubmed_pubmed & LinkReadableName=Related%20Articles & IdsFromResult=16245230 & ord\

inalpos=2 & itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_RVAbstra\

ct>

http://www.turkgastro.org/text.php?id=407

*Mitochondrial neurogastrointestinal encephalomyopathy.*

Mitochondrial neurogastrointestinal encephalomyopathy is an

autosomal recessive disease characterized by progressive

ophthalmoplegia, peripheral neuropathy, mitochondrial abnormalities

and gastrointestinal involvement. We describe a 19-year-old male

having chronic intestinal pseudoobstruction associated with

ophthalmoplegia and proximal muscle weakness. The clinical and

radiologic features suggested the diagnosis of mitochondrial

neurogastrointestinal encephalomyopathy. Mitochondrial genetic

defects should be considered in the differential diagnosis of

unexplained chronic gastrointestinal symptoms accompanied by

neurological findings, especially in families where there is more

than one individual with the same kind of symptoms.

PMID: 16245230

3: Am J Physiol Gastrointest Liver Physiol. 2004 May;286(5):G804-13.

<http://www.ncbi.nlm.nih.gov/sites/entrez?Db=pubmed & DbFrom=pubmed & Cmd=Link & LinkN\

ame=pubmed_pubmed & LinkReadableName=Related%20Articles & IdsFromResult=15068964 & ord\

inalpos=3 & itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_RVAbstra\

ct>

http://ajpgi.physiology.org/cgi/content/full/286/5/G804

*Paradoxical decrease of mitochondrial DNA deletions in epithelial

cells of active ulcerative colitis patients.*

Ulcerative colitis (UC) is a condition characterized by chronic

inflammation targeted at the epithelial layer. In addition to being

involved in immune phenomena, UC epithelial cells exhibit decreased

oxidation of butyrate, downregulation of oxidative pathway

regulatory genes, and overexpression of mitochondrial (mt) genes. We

investigated whether these events, which translate an altered energy

metabolism, are associated with an abnormal pattern of mtDNA

deletions. Highly purified colonocytes were isolated from surgically

resected control, involved and uninvolved inflammatory bowel disease

mucosa. The frequency, type, and number of mtDNA deletions were

assessed by PCR amplification, Southern blot analysis, and cloning

and sequencing of amplified DNA fragments. The 4977 mtDNA deletion

was less frequent in UC than control and Crohn's disease (CD)

epithelium, regardless of patient age. Several other deletions were

detected, but all were less common in UC than control and CD cells.

The frequency, variety, and number of mtDNA deletions were

invariably lower in colonocytes isolated from inflamed mucosa than

in autologous cells from noninflamed mucosa. In conclusion, in the

absence of inflammation, UC colonocytes exhibit an mtDNA deletion

pattern similar to that of control cells, indicating a normal

response to physiological levels of oxidative stress. In active

inflammation, when oxidative stress increases, the frequency,

variety, and number of mtDNA deletions decrease. Because comparable

abnormalities are absent in active CD, the mtDNA deletion pattern of

active UC suggests that colonocytes respond uniquely to

inflammation-associated stress in this condition.

PMID: 15068964

4: Am J Physiol Gastrointest Liver Physiol. 2004 Apr;286(4):G671-82.

Epub 2003 Oct 30.

<http://www.ncbi.nlm.nih.gov/sites/entrez?Db=pubmed & DbFrom=pubmed & Cmd=Link & LinkN\

ame=pubmed_pubmed & LinkReadableName=Related%20Articles & IdsFromResult=14592946 & ord\

inalpos=4 & itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_RVAbstra\

ct>

http://ajpgi.physiology.org/cgi/content/full/286/4/G671

*Characteristics of intermittent mitochondrial transport in guinea

pig enteric nerve fibers.*

Enteric neurons controlling various gut functions are prone to

oxidative insults that might damage mitochondria (e.g., intestinal

inflammation). To resume local energy supply, mitochondria need to

be transported. We used MitoTracker dyes and confocal microscopy to

investigate basic characteristics of mitochondrial transport in

guinea pig myenteric neurites. During a 10-s observation of 1 mm

nerve fiber, on average, three mitochondria were transported at an

average speed of 0.41 +/- 0.02 microm/s. Movement patterns were

clearly erratic, and velocities were independent of mitochondrial

size. The velocity oscillated periodically ( approximately 6 s) but

was not consistently affected by structures such as en route

boutons, bifurcations, or stationary mitochondria. Also,

mitochondria transported in opposite directions did not necessarily

affect each others' mobility. Transport was blocked by microtubule

disruption (100 microM colchicine), and destabilization (1 microM

cytochalasin-D) or stabilization (10 microM phalloidin) of actin

filaments, respectively, decreased (0.22 +/- 0.02 microm/s, P <

0.05) or increased (0.53 +/- 0.02 microm/s, P < 0.05) transport

speed. Transport was inhibited by TTX (1 microM), and removal of

extracellular Ca(2+) (plus 2 mM EGTA) had no effect. However,

depletion of intracellular stores (thapsigargin) reduced (to 33%)

and slowed the transport significantly (0.18 +/- 0.02 microm/s, P <

0.05), suggesting an important role for stored Ca(2+) in

mitochondrial transport. Transport was also reduced (to 21%) by the

mitochondrial uncoupler FCCP (1 microM) in a time-dependent fashion

and slowed by oligomycin (10 microM). We conclude that mitochondrial

transport is remarkably independent of structural nerve fiber

properties. We also show that mitochondrial transport is TTX

sensitive and speeds up by stabilizing actin and that functional

Ca(2+) stores are required for efficient transport.

PMID: 14592946

7: Ann Intern Med. 2002 Oct 15;137(8):703-4.

http://www.annals.org/cgi/reprint/137/8/703.pdf

*Intestinal pseudo-obstruction in a diabetic man: role of the

mitochondrial A3243G mutation.*

PMID: 12379086

10: J Histochem Cytochem. 1999 Apr;47(4):517-24.

http://www.jhc.org/cgi/content/full/47/4/517

<http://www.ncbi.nlm.nih.gov/entrez/utils/fref.fcgi?PrId=3051 & itool=Abstract-def\

& uid=10082753 & db=pubmed & url=http://www.jhc.org/cgi/pmidlookup?view=long & pmid=100\

82753>

*Cell-specific expression of mitochondrial carbonic anhydrase in the

human and rat gastrointestinal tract.*

**

<http://www.ncbi.nlm.nih.gov/sites/entrez?Db=pubmed & Cmd=Search & Term=%22Saarnio%2\

0J%22%5BAuthor%5D & itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_\

RVAbstract>Mitochondrial

carbonic anhydrase V (CA V) in liver provides HCO3- to pyruvate

carboxylase for the first step in gluconeogenesis and HCO3- to

carbamyl phosphate synthetase I for the first step in ureagenesis.

Because carbamyl phosphate synthetase I and ornithine

transcarbamylase are also expressed in enterocytes, we tested the

hypothesis that CA V is expressed in the gastrointestinal tract in

addition to liver. Polyclonal rabbit antisera were raised against a

polypeptide of 17 C-terminal amino acids of human CA V and against

purified recombinant mouse isozyme and were used in Western blotting

and immunoperoxidase staining of human and rat tissues.

Immunohistochemistry showed that CA V is expressed cell-specifically

in the alimentary canal mucosa from stomach to rectum.

Immunoreactions for CA V were detected in the parietal cells and

gastrin-producing G-cells of the stomach and in intestinal

enterocytes. Western blotting of human and rat gastrointestinal

tissues with isozyme-specific antibodies showed positive signals for

CA V with the expected molecular mass. The findings in human tissues

paralleled those in rat. The cell-specific pattern of CA V

expression suggests a role for CA V in alimentary canal physiology.

We propose that mitochondrial CA V participates in the

detoxification of ammonia produced in the gastrointestinal tract by

providing bicarbonate to carbamyl phosphate synthetase I. (J

Histochem Cytochem 47:517-524, 1999)

PMID: 10082753

11: J Nutr. 1998 Aug;128(8):1368-75.

<http://www.ncbi.nlm.nih.gov/sites/entrez?Db=pubmed & DbFrom=pubmed & Cmd=Link & LinkN\

ame=pubmed_pubmed & LinkReadableName=Related%20Articles & IdsFromResult=9687558 & ordi\

nalpos=11 & itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_RVAbstra\

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http://jn.nutrition.org/cgi/content/full/128/8/1368

<http://www.ncbi.nlm.nih.gov/entrez/utils/fref.fcgi?PrId=3051 & itool=Abstract-def\

& uid=9687558 & db=pubmed & url=http://jn.nutrition.org/cgi/pmidlookup?view=long & pmid\

=9687558>

*Dietary protein level regulates expression of the mitochondrial

branched-chain aminotransferase in rats.*

The first step in the degradation of branched-chain amino acids

(BCAA) is transamination catalyzed by the branched-chain

aminotransferase (BCAT), which is located in extrahepatic tissues.

Studies of the effect of dietary protein on BCAT activity have given

contradictory results. Therefore, we established the levels of BCAT

activity and mitochondrial BCAT (BCATm) mRNA expression in different

organs and tissues of rats. We then determined the effect of

different levels of dietary protein in well-nourished rats, the

effect of feeding a 0.5% casein diet for 5 wk (protein-malnourished

rats) and nutritional rehabilitation of these rats with different

levels of dietary protein on BCAT activity and BCATm mRNA expression

in selected tissues. Finally, the response of tissue BCAT activity

and BCATm mRNA levels in rats fed a 10% casein diet and injected

with glucagon (4 d) or hydrocortisone (7 d) was determined. The

highest concentration of BCATm mRNA was found in stomach, followed

by kidney, heart, muscle, brain, skin and lung. Low levels were

found in intestine, and no BCATm mRNA was detectable in liver.

Although BCAT activity was significantly higher in muscle, kidney

and brain from rats adapted to consume a 50% casein diet for 7 h/d

for 10 d than in rats fed 6, 18 or 35% casein diets, only muscle had

significantly higher levels of BCATm mRNA. In protein-malnourished

rats, BCAT activity and BCATm mRNA expression in kidney, muscle and

heart were not different from those of rats with free access to an

18% casein diet. Nutritional rehabilitation of the

protein-malnourished rats with 50% casein for 21 d significantly

increased the BCAT activity and BCATm mRNA expression in muscle.

Neither hydrocortisone nor glucagon injection affected BCAT activity

or BCATm mRNA concentrations in rat kidney, muscle or heart. We

conclude that the nutritional regulation of BCATm is extrahepatic,

tissue specific and may involve transcriptional and

post-translational mechanisms.

PMID: 9687558

12: Gut. 1997 Sep;41(3):344-53.

<http://www.ncbi.nlm.nih.gov/sites/entrez?Db=pubmed & DbFrom=pubmed & Cmd=Link & LinkN\

ame=pubmed_pubmed & LinkReadableName=Related%20Articles & IdsFromResult=9378390 & ordi\

nalpos=12 & itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_RVAbstra\

ct>

http://gut.bmj.com/cgi/content/full/41/3/344

<http://www.ncbi.nlm.nih.gov/entrez/utils/fref.fcgi?PrId=3051 & itool=Abstract-def\

& uid=9378390 & db=pubmed & url=http://gut.bmj.com/cgi/pmidlookup?view=long & pmid=9378\

390>

*Mitochondrial damage: a possible mechanism of the " topical " phase

of NSAID induced injury to the rat intestine.*

BACKGROUND: The " topical " effect of non-steroidal anti-inflammatory

drugs (NSAIDs) seems to be an important cause of NSAID induced

gastrointestinal damage. AIM: To examine the possible mechanism of

the " topical " phase of damage in the small intestine. METHODS:

Electron microscopy and subcellular organelle marker enzyme studies

were done in rat small intestine after oral administration of

indomethacin (doses varied between 5 and 30 mg/kg). The effect of

conventional and non-acidic NSAIDs on rat liver mitochondrial

respiration was measured in vitro in a e-type oxygen electrode.

RESULTS: The subcellular organelle marker enzymes showed

mitochondrial and brush border involvement within an hour of

indomethacin administration. Electron microscopy showed dose

dependent mitochondrial changes following indomethacin

administration consistent with uncoupling of oxidative

phosphorylation (or inhibition of electron transport) which were

indistinguishable from those seen with the uncoupler dinitrophenol.

Parenteral indomethacin caused similar changes, but not in rats with

ligated bile ducts. A range of NSAIDs, but not paracetamol or

non-acidic NSAIDs which have a favourable gastrointestinal

tolerability profile, uncoupled oxidative phosphorylation in vitro

at micromolar concentrations and inhibited respiration at higher

concentrations. In vivo studies with nabumetone and aspirin further

suggested that uncoupling or inhibition of electron transport

underlies the " topical " phase of NSAID induced damage. CONCLUSION:

Collectively, these studies suggest that NSAID induced changes in

mitochondrial energy production may be an important component of the

" topical " phase of damage induction.

PMID: 9378390

13: Endocrinology. 1995 Dec;136(12):5520-6.

http://endo.endojournals.org/cgi/reprint/136/12/5520

<http://www.ncbi.nlm.nih.gov/entrez/utils/fref.fcgi?PrId=3051 & itool=Abstract-def\

& uid=7588303 & db=pubmed & url=http://endo.endojournals.org/cgi/pmidlookup?view=long\

& pmid=7588303>

*Tissue-specific regulation by vitamin D status of nuclear and

mitochondrial gene expression in kidney and intestine.*

**

<http://www.ncbi.nlm.nih.gov/sites/entrez?Db=pubmed & Cmd=Search & Term=%22Chou%20SY\

%22%5BAuthor%5D & itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_RV\

Abstract>Vitamin

D is responsible, through the actions of its metabolite, 1

alpha,25-dihydroxyvitamin D3 [1 alpha,25-(OH)2D3], for the

generation of a wide array of biological responses, particularly in

the intestine, kidney, and bone. 1 alpha,25-(OH)2D3 is known to

interact with its nuclear receptor to mediate the regulation of gene

transcription. Although many genes and gene products have been shown

to be regulated by 1 alpha,25-(OH)2D3 (e.g. calbindin-D28K in the

intestine and kidney; collagen, osteocalcin,and osteopontin in

bone), their recognition has been largely the result of empirical

testing. In this report we have used subtractive hybridization

analysis of complementary DNA libraries prepared from messenger RNA

(mRNA) isolated from the intestine and kidney of vitamin D-replete

or vitamin D-deficient chicks to identify genes for novel proteins

whose steady state mRNA levels are regulated by dietary vitamin D

status. In the kidney we observed the down-regulated expression of

at least seven mitochondrially encoded transcripts and the

up-regulated expression of five nuclear encoded genes, two of which

are metallothionein and the beta-subunit of aldolase. In the

intestine, six mitochondrially encoded transcripts are up-regulated,

and seven nuclear encoded transcripts were either up- or

down-regulated. Thus, in addition to identifying new nuclear encoded

genes whose mRNAs are regulated by vitamin D status, our approach

has demonstrated the tissue-specific regulation of mitochondrial

gene expression in the intestine and kidney.

PMID: 7588303

14: Biochem J. 1995 Jun 1;308 ( Pt 2):665-71.

<http://www.ncbi.nlm.nih.gov/sites/entrez?Db=pubmed & DbFrom=pubmed & Cmd=Link & LinkN\

ame=pubmed_pubmed & LinkReadableName=Related%20Articles & IdsFromResult=7539612 & ordi\

nalpos=14 & itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_RVAbstra\

ct>

http://www.pubmedcentral.nih.gov/picrender.fcgi?artid=1136978 & blobtype=pdf

<http://www.ncbi.nlm.nih.gov/entrez/utils/fref.fcgi?PrId=3494 & itool=Abstract-non\

def & uid=7539612 & db=pubmed & url=http://www.pubmedcentral.nih.gov/articlerender.fcg\

i?tool=pubmed & pubmedid=7539612>

*Mitochondrial gene expression in small intestinal epithelial cells.*

Most mitochondrial genes are transcribed as a single large

transcript from the heavy strand of mitochondrial DNA, and are

subsequently processed into the proximal mitochondrial (mt) 12 S and

16 S rRNAs, and the more distal tRNAs and mRNAs. We have shown that

in intestinal epithelial biopsies the steady-state levels of mt 12 S

and 16 S rRNA are an order of magnitude greater than those of mt

mRNAs. Fractionation of rat small intestinal epithelial cells on the

basis of their maturity has shown that the greatest ratios of 12 S

mt rRNA/cytochrome b mt mRNA or 12 S mt rRNA/cytochrome oxidase I mt

mRNA are found in the surface mature enterocytes, with a progressive

decrease towards the crypt immature enteroblasts. Cytochrome b and

cytochrome oxidase I mt mRNA levels are relatively uniform along the

crypt-villus axis, but fractionation experiments showed increased

levels in the crypt base. The levels of human mitochondrial

transcription factor A are also greater in immature crypt

enteroblasts compared with mature villus enterocytes. These results

show that the relative levels of mt rRNA and mRNA are distinctly

regulated in intestinal epithelial cells according to the

crypt-villus position and differentiation status of the cells, and

that there are higher mt mRNA and mt TFA levels in the crypts,

consistent with increased transcriptional activity during

mitochondrial biogenesis in the immature enteroblasts.

PMID: 7539612

17: Proc Natl Acad Sci U S A. 1989 Jul;86(14):5296-300.

<http://www.ncbi.nlm.nih.gov/sites/entrez?Db=pubmed & DbFrom=pubmed & Cmd=Link & LinkN\

ame=pubmed_pubmed & LinkReadableName=Related%20Articles & IdsFromResult=2748585 & ordi\

nalpos=17 & itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_RVAbstra\

ct>

http://www.pnas.org/cgi/reprint/86/14/5296

<http://www.ncbi.nlm.nih.gov/entrez/utils/fref.fcgi?PrId=3051 & itool=Abstract-def\

& uid=2748585 & db=pubmed & url=http://www.pnas.org/cgi/pmidlookup?view=long & pmid=274\

8585>

*Glutathione metabolism in the lung: inhibition of its synthesis

leads to lamellar body and mitochondrial defects.*

Mice treated with buthionine sulfoximine, an inhibitor of

glutathione synthesis, showed striking alterations of morphology of

lung type 2 cell lamellar bodies (swelling and disintegration) and

mitochondria (degeneration) and of lung capillary endothelial cells

(mitochondrial swelling). These effects probably may be ascribed to

glutathione deficiency; administration of glutathione monoester

protects against them. Measurements of arteriovenous plasma

glutathione levels across the lung indicate that the net uptake of

glutathione by this organ is substantial. Thus, glutathione exported

from the liver to the blood plasma is utilized by the lung which,

like the liver, kidney, and lymphocytes (and unlike skeletal

muscle), exhibits a high overall rate of glutathione turnover.

Intraperitoneal injection of glutathione into buthionine

sulfoximine-treated mice leads to very high levels of plasma

glutathione without significant increase in the glutathione levels

of liver, lung, and lymphocytes; on the other hand, administration

of glutathione monoester leads to markedly increased tissue and

mitochondrial levels of glutathione. Administration of glutathione

monoester (in contrast to glutathione) to control mice also

increases mitochondrial glutathione levels. The findings indicate

that glutathione is required for mitochondrial integrity and that it

probably also functions in the processing and storage of surfactant

in lamellar bodies. The morphological changes observed after

treatment with buthionine sulfoximine and their prevention by

glutathione monoester as well as findings on glutathione metabolism

indicate that this tripeptide plays an important role in the lung.

The previously observed failure of buthionine sulfoximine-treated

mice to gain weight is mainly due to glutathione deficiency in the

intestinal mucosa.

PMID: 2748585