Protein oxidation in aging and age-related diseases.

[Guest guest]

Hi All,

 

Interesting papers relating less active enzymes as we age with free radical

damage and not increased pancreatic enzyme

production caused by not eating enough active food based enzymes as Dr. Howell

suggests.

 

And a second showing CRONing (which reduced free radical levels better than any

anti-oxidant) enhances enzyme and

protein activity in old age.

 

That said, food based active digestive enzymes will assist more rapid digestion

in the gut and may help to improve

health via better breakdown of proteins into non active amino acids building

blocks.

 

Here is a good moving graphic showing protein to amino digestion:

Exocrine Secretions of the Pancreas

http://arbl.cvmbs.colostate.edu/hbooks/pathphys/digestion/pancreas/exocrine.html

 

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http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve & db=PubMed & list_uids=1\

1795513 & dopt=Abstract

Ann N Y Acad Sci 2001 Apr;928:22-38 Related Articles, Books, LinkOut

Protein oxidation in aging and age-related diseases.

Stadtman ER.

Laboratory of Biochemistry, National Heart, Lung, and Blood Institute, National

Institutes of Health, Bethesda, Maryland

20892-0342, USA. erstadtman

 

Although different theories have been proposed to explain the aging process, it

is generally agreed that there is a

correlation between aging and the accumulation of oxidatively damaged proteins,

lipids, and nucleic acids.

 

Oxidatively modified proteins have been shown to increase as a function of age.

 

Studies reveal an age-related increase in the level of protein carbonyl content,

oxidized methionine, protein

hydrophobicity, and cross-linked and glycated proteins as well as the

accumulation of less active enzymes that are more

susceptible to heat inactivation and proteolytic degredation.

 

Factors that decelerate protein oxidation also increase the life span of animals

and vice versa.

 

Furthermore, a number of age-related diseases have been shown to be associated

with elevated levels of oxidatively

modified proteins.

 

The chemistry of reactive oxygen species- [ROS or free radicals..gw] mediated

protein modification will be discussed.

 

The accumulation of oxidatively modified proteins may reflect deficiencies in

one or more parameters of a complex

function that maintains a delicate balance between the presence of a

multiplicity of prooxidants, antioxidants, and

repair, replacement, or elimination of biologically damaged proteins.

 

PMID: 11795513 [PubMed - in process]

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http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve & db=PubMed & list_uids=1\

1795521 & dopt=Abstract

Ann N Y Acad Sci 2001 Apr;928:296-304 Related Articles, Books, LinkOut

Calorie restriction enhances the expression of key metabolic enzymes associated

with protein renewal during aging.

Spindler SR.

Department of Biochemistry, University of California, Riverside 92521, USA.

spindler

 

Our studies show that dietary caloric restriction (CR) alters the expression of

key metabolic enzymes in a manner

consistent with an increased rate of extrahepatic protein turnover and renewal

during aging.

 

Of the key hepatic gluconeogenic enzyme genes affected by CR, glucose

6-phosphatase mRNA increased 1.7- and 2.3-fold in

young and old CR mice.

 

Phosphoenolpyruvate carboxykinase mRNA increased 2-fold in young mice, and its

mRNA and activity increased 2.5- and

1.7-fold in old mice.

 

These changes indicate that CR enhances the enzymatic capacity for

gluconeogenesis.

 

The carbon required for gluconeogenesis appears to be generated from peripheral

protein turnover.

 

Muscle glutamine synthetase mRNA increased 1.3- and 2.1-fold in young and old CR

mice, suggesting increased disposal of

nitrogen and carbon derived from protein catabolism for energy.

 

mRNA for the key liver nitrogen disposal enzymes glutaminase, carbamyl phosphate

synthase I, and tyrosine

aminotransferase were increased by 2.4-, 1.8-, and 1.8-fold in CR mice.

 

Consistent with increased hepatic nitrogen disposal, hepatic glutamine

synthetase mRNA and activity were each decreased

about 40% in CR mice.

 

Together, these and our other published data suggest that CR enhances and

maintains protein turnover, and thus protein

renewal, into old age.

 

These effects are likely to resist the well-documented decline in whole body

protein renewal with age.

 

Enhanced renewal may reduce the level of damaged and toxic proteins that

accumulate during aging, contributing to the

extension of life span by CR.

 

PMID: 11795521 [PubMed - in process]

 

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Good health & long life,

Greg Watson,

http://optimalhealth.cia.com.au