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From:
John Dankowych <[log in to unmask]>
Date:
Sat, 20 Nov 1999 01:57:22 -0500
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<<Disclaimer: Verify this information before applying it to your situation.>>

Listmates,

Ok, I received 4 responses to a query I posted about papain on the
autism list.

There were no negative reports.

Here is why I asked:

Please take this is for what it is, only one data point.  You should not
draw any conclusions from a single anectodal report.  Perhaps this might
draw out some other experiences.

The other day my sister-in-law called to tell me that her son had been
moved to another room in the hospital.  (He is the hospital for an acute
bout of ulcerative colitis.)  I mentioned to her that there was an
abstract I had just read in which it was noted that hydrocortisone
inhibited proteoglycan synthesis.  Her daughter came down with arthritis
in one knee and has been getting hydrocortisone shots for it.  In
describing the paper I explained that the experiments began with the
injection of papain to induce injury and thus allow the scientists to
watch the proteoglycans/GAGs being rebuilt.  This rang a bell for her.
She explained that she had been racking her brain over the past 6 months
trying to figure out why two of her kids had gotten ill (arthritis and
ulcerative colitis) at around the same time.  She had already concluded
that the only thing new she had introduced into the family diet last year
was a meat tenderizer whose main ingredient was papain.  Arthritis and
ulcerative colitis followed.  Coincidence?  I did a very quick look at my
enzyme books.  Papain, as you know comes from papaya.  It is used as a
digestive aid in Celiac Disease, as a meat tenderizer and in herniated
lumbar disk surgery to selectively destroy cartlidge.  It is claimed that
it has an ability to select dead tissue and leave living tissue alone.  I
don't know how it could it do that.  Perhaps GAGs that are unsulfated are
viewed as dead tissue while well sulfated GAGs are protected against this
protease.  However, I believe they used heathy rabbits in the experiments
referred to in the attached paper, so you wouldn't expect them to have a
sulfation issue.  Perhaps, in the long run, papain is not such a good
thing for people with gut problems and/or arthritis or even a genetic
(HLA) predisposition to these?  Bromelain (from pineapple) and perhaps
other digestive enzymes would be suspect as wel.l Perhaps even our own
digestive enzymes are an issue under poor sulfation conditions.  Note:  I
did some searching on the web and found vritually no negative reports
except for one comment that suggested that at some level proteases such
as papain would begin to eat away at your own tissue, but that the level
of safety was not known.


Regards,

John Dankowych


Altered chondrocytic oxidative metabolism during the restoration of
depleted intercellular matrix.
 Boussidan F, Nahir AM
 J Exp Pathol (Oxford) 1990 Jun 71:3 395-402

Abstract
 The depletion of proteoglycans (PGs), induced by a single intravenous
injection of papain, is a useful model for studying the response of
chondrocytes in vivo to injury.  The present study concentrated on the
activity of enzymes related to the synthesis of PGs, either directly,
with uridine diphosphoglucose dehydrogenase (UDPGD), or indirectly,
through the general oxidative metabolism of the chondrocytes.  Most of
the enzymes showed diminished activity on day 2; in some, there was
little change in activity, whereas in others there was marked increase in
activity over the following days.  Thus, on day 9 the activities of
glucose-6-phosphate dehydrogenase and of glyceraldehyde-3-phosphate
dehydrogenase were twice the original (day 0) values, and those of
succinate dehydrogenase and of UDPGD were one and a half times greater
than the original activities.  Such increased enzymatic activity preceded
the increase in PG content, which by day 14 reached up to 80% of the
initial value.  Both the increased activity and the replenishment of the
PG content were inhibited when hydrocortisone (10 mg/kg) was injected.

MeSH
 Animal, Cartilage, Extracellular Matrix, Glucosephosphate Dehydrogenase,
Glyceraldehyde-3-Phosphate Dehydrogenases, Hydrocortisone, Lactate
Dehydrogenase, Papain, Proteoglycans, Rabbits, Succinate Dehydrogenase,
Uridine Diphosphate Glucose Dehydrogenase, 3-Hydroxyacyl CoA
Dehydrogenases

 Author Address
 H. Schussheim Rheumatology Research Laboratory, Faculty of Medicine,
Technion-Israel Institute of Technology, Haifa.

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