Discussion:
Mark A. Kukucka's Anonymous Smear Campaigns
(too old to reply)
Mark Thorson
2008-09-23 19:19:13 UTC
Permalink
http://findarticles.com/p/articles/mi_qn4183/is_20051128/ai_n15872662/print

Baltimore-based Belfort Instruments suing fired worker

Caryn Tamber

A Baltimore manufacturer of weather instruments
is suing a fired employee it claims is on an
anonymous Internet rampage. Belfort Instrument
says Mark A. Kukucka has been harassing current
Belfort employees via e-mail, calling the
company's customers and partners alleging
unethical business practices, and posting trade
secrets on the Internet. Defendant Kukucka has
an alarming history of engaging in such 'anonymous'
Internet attacks against those who he believes may
have slighted him (including past employers), and,
absent a TRO, will continue his historical pattern
of making outrageous and harmful attacks against
the material business interests of Belfort
Instrument, reads Belfort's complaint, filed
earlier this month in Baltimore County Circuit
Court. Belfort, which obtained a temporary
restraining order against Kukucka on Nov. 15, is
suing him for misappropriating trade secrets,
breach of contract, defamation and tortious
interference with contractual relations. The
company is seeking $1 million. After consulting
with his client, Belfort attorney Douglas W.
Desmarais declined to speak about the case.
My client's position is that this is a dispute
that they have chosen to resolve through legal
channels, and they're going to let it play out
through legal channels, Desmarais said. Kukucka
could not be located for comment; his phone
number is unlisted and a reverse search of his
Kingsville address produced no results. According
to the complaint, when Kukucka started working
for Belfort in 2001, he signed a contract
promising that, if he left the company, for two
years afterward he would not say negative things
about it; if he did, he would face court action.
He is also bound by the Maryland Uniform Trade
Secrets Act not to divulge privileged information,
Belfort says. Kukucka was fired on Oct. 20 of
this year and then started to harass his
ex-girlfriend, still a Belfort employee, via
e-mail, the suit reads. He also allegedly
e-mailed the company's general mailbox anonymously,
promising to fight back against the company and
drive it out of business. The company also claims
he called their customers and made untrue
allegations. Kukucka also used an Internet
newsgroup to criticize the Belfort product he had
been in charge of marketing, the DigiWx AWOS
digital weather transmitter, calling it Digi$H*T,
Belfort claims. He also allegedly listed which of
Belfort's customers were using DigiWx. The motion
does not state how Belfort knows that Kukucka is
behind the anonymous e-mails, phone calls and
Internet postings, but a letter from Desmarais to
Kukucka warns that Belfort can easily trace the
communications to Kukucka. Belfort also claims
that Kukucka has a history of using pseudonyms
to criticize whoever has offended [him] on a
particular day. Indeed, a search of Google's
newsgroups shows lots of chatter about Kukucka,
including several posts purporting to unmask him
as the anonymous source of negative comments
about Baltimore and a Japan-based company called
Shimadzu, for which he allegedly worked at one
point.
i***@yahoo.com
2008-09-26 14:42:44 UTC
Permalink
Mark Kukucka's lawsuit dismissed: I think that says it all!
Mark Thorson's lawsuit: Mark Thorson LOST and had to publish
RETRACTION!

That's what I thought Mark Thorson, you have no other real
publications except your retraction!
This Mark Thorson must have a "hard-on" for Dr. Kukucka!


This is the first report regarding quantitation of enzymatic (eg.
superoxide dismutase, glutathione reductase & glucose-6-phosphate
dehydrogenase) and non-enzymatic (eg. glutathione) antioxidant levels
in isolated Leydig cells that I can find in the scientific literature:

Mechanisms by which hypoxia augments Leydig cell viability and
differentiated cell function in vitro (PhD Dissertation, 1993)

by Mark A. Kukucka, MS, DVM, PhD

Department of Biomedical Sciences
Virginia-Maryland Regional College of Veterinary Medicine
Virginia Polytechnic Institute & State University
Blacksburg, Virginia 24061-0442


ABSTRACT:

The 1980s heralded the discovery and identification of extra-pituitary
sources of the neurohypophysial hormone oxytocin in non-neural tissues
of several animal species. The presence, location and biosynthesis of
significant amounts of oxytocin in the ovarian corpus luteum was
followed by the immunocytochemical demonstration of an oxytocin-like
peptide in the testicular interstitial cells. Leydig cells, which
comprise up to 80% of the testicular intertubular cell population, are
known to synthesize testosterone in situ. Indirect evidence indicated
that an oxytocin-like peptide was also present in Leydig cells. The
question arose whether this peptide was synthesized de novo by Leydig
cells or was taken up and stored by the cells following biosynthesis
at some other intra- and/or
extra-gonadal source(s). Since luteinizing hormone (LH) and ascorbate
are known to augment the production of oxytocin in ovarian granulose
cells, varying concentrations of these two stimulants were used to
monitor the biosynthesis of oxytocin from isolated Leydig cells in
culture.

Highly enriched populations of guinea pig Leydig cells were isolated
using a method that employed enzymatic dissociation and Percoll
gradient centrifugation. Since ambient oxygen tensions are toxic to
cultured Leydig cells leading to decreased steroidogenic capacity, the
antioxidant defense system of isolated Leydig cells was discerned.
Decreased levels of several antioxidants including superoxide
dismutase, glutathione reductase, glucose-6-phosphate dehydrogenase
and total glutathione were measured. Using
the dichlorofluorescin (DCF-DA) assay, it was determined that isolated
Leydig cells were capable of accumulating hydrogen peroxide (H2O2).
Leydig cells maintained in an atmosphere composed of 19% oxygen
produced H2O2 at a faster rate than similar cells incubated at 3%
oxygen.

Using a polyclonal antibody (Ab)-based immunoaffinity column, oxytocin
biosynthesis was monitored in Leydig cells incubated with a mildly
stimulating dose (0.1 ng/ml) of ovine LH for 24, 48 and 72 hours in
the presence of increasing concentrations of sodium ascorbate (1- 500
mM) under culture conditions of hypoxia and normoxia. Following solid
phase extraction and immunoaffinity purification, sample supernatants
were analyzed for both testosterone and oxytocin content as measured
by radioimmunoassay (RIA) and high performance liquid chromatography-
electrochemical detection (HPLC-ECD) respectively. Hypoxic culture
conditions and low (1-10 mM) concentrations of sodium ascorbate
augmented the production of oxytocin from Leydig cells in culture.
Higher (50-500 mM) levels of ascorbate and normoxic culture conditions
suppressed both testosterone and oxytocin production in isolated
Leydig cells. Because oxytocin synthesis was found to be cycloheximide-
sensitive, we conclude that Leydig cells possess the
biosynthetic machinery necessary to manufacture oxytocin. The isolated
oxytocin peptide was purified by HPLC with fraction collection
followed by polyclonal-Ab immunoaffinity column chromatography.
Comparison of the amino acid sequence of the isolated octapeptide with
authentic oxytocin provides unequivocal evidence that Leydig cells
synthesize oxytocin de novo. Considering the widespread use of vitamin
C as a dietary supplement, the research reported yields valuable
mechanistic information on the reproductive biologic role of vitamin C
in gonadal steroid and peptide hormone metabolism.

http://scholar.lib.vt.edu/theses/available/etd-06062008-170416/


Vitamin C (aka ascorbate) is another non-enzymatic antioxidant found
in significant levels within the testes. As an antioxidant,
ascorbate's primary role is donate electrons to neutralize reactive
species of oxygen including superoxide (to H2O2) and hydroxyl free
radicals (to H2O). When ascorbate acts as a scavenger (by donating an
electron to a free radical), ascorbate is oxidized in the process to
the ascorbate free radical and dehydro-ascorbate. The ascorbate free
radical and the dehydro-ascorbate are reduced back to ascorbate either
by NADH catalyzed by semidehydroascorbate reductase (and forming NAD)
or reduced glutathione (GSH) catalyzed by dehydroascorbate reductase
(and forming oxidized glutathione (GSSG)).

n.b. Vitamin C also works along with glutathione peroxidase (a major
free radical-fighting enzyme) to revitalize vitamin E.

Interestingly, Kukucka et. al. reported finding significant levels of
oxytocin (a disulfide containing octapeptide) in isolated Leydig
cells. Kukucka theorized in the introduction of his PhD dissertation
(back in 1993) that open chain oxytoceine (the reduced form of
oxytocin) may also act as a scavenger (by donating an electron to a
free radical), oxytoceine may then be oxidized back to oxytocin. As
noted above, the ascorbate free radical and the dehydro-ascorbate are
reduced back to ascorbate either by NADH catalyzed by
semidehydroascorbate reductase (and forming NAD) or reduced
glutathione (GSH) catalyzed by dehydroascorbate reductase (and forming
oxidized glutathione (GSSG)).... why couldn't the ascorbate free
radical and dehydro-ascorbate be reduced back to ascorbate by reduced
oxytoceine (forming closed-ring oxytocin)?

Thus, the redox potential of oxytocin <---> oxytoceine may drive
ascorbate <---> dehydro-ascorbate or vice versa as part of the non-
enzymatic antioxidant defense system.


Other publications by Dr. Mark A. Kukucka
http://www.nextbio.com/b/literature/literature.nb?author=MA+Kukucka
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