On Mon, 30 Oct 2000, Valerie W. McClain, IBCLC wrote:
> I wish Mary that you could be more specific about what you view as hogwash.
> It is very difficult for me to respond without knowing what it is that I am
> writing is wrong.  I am under the impression that you believe that
> biotechnology is not currently capable of genetic engineering human milk
> components.  I believe that recombinant human lactoferrin was first
> genetically engineered in 1985. But I am not sure because statements by
> various companies conflict with one another.  But this is a news item from
> from the University of Buffalo--note the date, production sceduled for 2
> years hence--1997!!

Mostly it is the jumping to the conclusion that everything and anything
must be because of genetic engineering like the recent oats issue.  There
also is no cow's colostrum with human milk proteins being marketed to
consumers.  Dairy cows overproduce colostrum just like they overproduce
milk, and until recently, the colostrum was just a waste product, but now
combined with marketing, a false "need" has been produced to turn that
waste product into marketable product.

Transgenic engineering of the sort used to produce medicines (you put the
gene into a bacteria or yeast and get it to manufacture the medicine, like
human insulin) has been around for awhile, perhaps 20 years.  Transgenic
engineering to move a gene into a higher organism is now cutting edge
science, and is not "decades old".  It's very hit or miss, first you have
to get the gene into the plant or animal, which is nowhere near as easy as
it is to get it into bacteria or yeast, then you have to figure out how to
get it expressed, then you hope that it has the effect you were hoping
for, and not any bad ones.  It's important to draw a distinction between
gene engineering within a species and transgenic engineering (moving a
gene from one species to another).  For the most part, gene engineering
within a species is just a short cut to traditional animal and plant
breeding.  For instance, with DHA, there is no need to engineer DHA into
blue-green algae, because they already produce it (it is an adaptation to
life in cold water, fish get it because they either eat the algae or
something else up the food chain).  Because DHA is a fat, not a protein,
cloning the entire metabolic pathway to produce it would be an incredible
feat.  For commercial production, a company would want to do some
engineering on the algae, the usual reasons being to disable the
regulatory gene so that the algae continually produced DHA, and to make
the algae "weak", dependant on something that will be provided in the lab
but not present in its natural environment so that it can't escape.  These
are all things that could be accomplished without gene engineering, but it
would just take a lot longer and be less certain of success.

In 1981, I toured the Max Planck Institute where they were engaged in
cutting edge research in cloning plants that did not normally reproduce
vegetatively.  The purpose was to allow rapid production of breeding stock
to allow new varieties of plant to go to market sooner, especially those
that reproduced slowly.  Any thought of using this technology in
conjunction with gene engineering was completely science fiction back
then.  In 1989, when I graduated from college, transgenic engineering into
plants was cutting edge research, and there was a firestorm of controversy
over whether transgenic plants should be allowed to be planted outside of
carefully controlled greenhouses.  Transgenic engineering into animals is
now at the stage where a success is major news.  There is no production of
commercially available transgenic animals, everything is still in the lab.
There are very few examples of commercially available transgenic plants,
most of that is still lab work.  But you can see how fast things can move.
When I graduated in 1989, cloning of mammals was still considered to be
one of the "hard" problems due to some features of mammalian cells (some
things everybody can see how to achieve them, it's merely a matter of
doing the work, but some things someone is going to have to have an
unanticipated breakthrough), and now we have Dolly the sheep.

As I said before, genetic engineering is just a tool, to be used for good
or ill.  Whether something is profitable is not relevant to that issue, I
consider the engineering of bacteria to produce human insulin to be a
good, regardless of the fact that it's made a lot of money.  If a company
can clone human lactoferrin and make a medicine out of it, that's a good.
I don't have a problem with the cloning of human milk proteins in general.
The problem lies in the fact that many people don't just think of formula
as food, but as medicine, and the formula companies nurture that belief.
If you're going to successfully fight them, attacking them for using GMO's
to produce the components is not going to work because so many medications
are produced the same way and this is accepted by the vast majority of the
population.  Fight the view of formula as needed medication (for only a
few, of course).  The formula companies love the fact that the content is
regulated by the FDA because it lends to that aura of "medication, not
just food".  Probably a bad idea to remove that one, but continue working
to get doctors and hospitals to stop handing it out like medicine.  The
word "formula" conjures up lots of nice scientific and medical
associations, start using something like "artificial milk" whenever
possible.  It's junk food for babies, and ought to be thought of as such.
Every little step counts, but those in the right direction count for more
than those off on a tangent.

Quite frankly, I have not yet seen an application of transgenic plants or
animals that I would consider "good".  So far it's all been about
marketing creating a need, it doesn't help solve world hunger or produce
medicine to fight disease.  So I'm wholeheartedly with you on that one.
But if you get into a PR war over genetic engineering in general, and
you'll have the pharmaceuticals industry truthfully pointing out that your
position condemns a lot of medications that a lot of people depend on,
and you'll end up looking like an extremist and dismissed.  If you're
going to lead on this issue, get some education in the field so that you
can comment accurately.

Finally, the article below isn't really a news item, it is a press
release, which tend to be rather notorious for more hype than substance.
Does this company actually still exist?  It doesn't appear to be
publically traded, it may have gone bankrupt or been bought out by another
company.  Did they actually manage to scale up to commercial production
(not necessarily a given), and is the product being sold commercially
today?  There is a very big difference between being able to produce
something in the lab, and being able to produce it in commercial
quantities and to get it FDA approved.

> " UB Biologists Clone, Express Key Iron-Binding Protein With Commercial
> Promise
> Release date: Friday, June 9, 1995
> Contact: Ellen Goldbaum, [log in to unmask]
> Phone: 716-645-2626
> Fax: 716-645-3765
> BUFFALO, N.Y. -- A powerful human protein that destroys pathogens by
> depriving them of the iron they need to grow has been cloned, expressed and
> purified by University at Buffalo biologists, who have filed for patent
> protection on the research.
> Recombinant lactoferrin has commercial potential for products ranging from an
> antimicrobial agent to an improved infant formula.
> The research was funded by FerroDynamics, Inc., a biotechnology company in
> Houston that has licensed worldwide rights to recombinant human lactoferrin
> and its commercial uses from the University at Buffalo.
> Found in most physiological fluids, such as tears, mucus and mother's milk,
> the protein's critical feature is its ability to bind iron, making much of it
> unavailable to invading pathogens.
> "Lactoferrin's high affinity for iron makes it a key player in the human
> immune system," explained Darrell Doyle, Ph.D., professor of biological
> sciences at UB who directed the research.
> "It's a natural antibiotic," he said.
> But cloning the human gene for lactoferrin has not been easy.
> "For years, people have tried unsuccessfully to clone a full-length
> lactoferrin gene," noted Marian L. Kruzel, Ph.D., president of FerroDynamics.
> Cloning was difficult because of the large fragment of DNA that had to be
> expressed: The gene that codes for lactoferrin is about 2,000 base pairs
> long.
> Identifying the right expression system for reproducing the protein also was
> critical.
> Because the right kinds of sugars are necessary for the protein to function
> properly, common expression systems like bacteria, which do not glycosylate
> proteins (add sugars to them), cannot be used.
> The UB team was successful when Paul Gollnick, Ph.D., assistant professor of
> biological sciences at UB, and Tomasz Kurecki, Ph.D., senior research support
> specialist, used the PCR (polymerase chain reaction) method to clone the
> full-length human lactoferrin gene.
> Using a picha pastoris yeast expression system, FerroDynamics confirmed the
> ability to produce human lactoferrin on the laboratory scale.
> Now in the process of scaling up from pilot production of lactoferrin,
> FerroDynamics expects to have its first product on the market within two
> years. The company's primary focus is the market for topical antimicrobial
> products.
> At the first sign of infection, white blood cells release lactoferrin, which
> fights bacterial invaders by depriving them of the iron critical to their
> growth.
> Unlike currently available antibiotics, each of which is designed to combat a
> specific type or group of bacteria, lactoferrin is nonspecific.
> According to Kruzel, that provides an important advantage.
> "Over time, bacteria being treated with antibiotics such as penicillin or
> streptomycin can evolve strains that are resistant to specific
> characteristics in those drugs," he explained.
> But human lactoferrin binds to, or sequesters, the iron of all pathogens.
> "Without iron, pathogens cannot survive," he said.
> Among the other lactoferrin products FerroDynamics expects to market is an
> additive to make baby formula more like human milk.
> Studies of breast-fed infants have shown that babies fed human milk, which is
> rich in lactoferrin, absorb iron from it much more efficiently than babies
> fed infant formulas fortified with iron, Doyle explained.
> Other products that are now possible based on the UB research include food
> preservatives, dietary supplements and skin-care products."
>              ***********************************************
> The LACTNET mailing list is powered by L-Soft's renowned
> LISTSERV(R) list management software together with L-Soft's LSMTP(TM)
> mailer for lightning fast mail delivery. For more information, go to:

The LACTNET mailing list is powered by L-Soft's renowned
LISTSERV(R) list management software together with L-Soft's LSMTP(TM)
mailer for lightning fast mail delivery. For more information, go to: