This is a long post.

1. A scholar.google.com search for "Multiple
Myeloma"+Dexamethasone+rapamycin resulted in 726 finds -
http://tinyurl.com/ywtjqz

2. Rapamycin sensitizes multiple myeloma cells to apoptosis induced by
dexamethasone -
http://bloodjournal.hematologylibrary.org/cgi/content/full/103/8/3138
http://bloodjournal.hematologylibrary.org/cgi/reprint/103/8/3138
This article has been cited  50 times - http://tinyurl.com/2w6hx4

3. Mechanism by Which Mammalian Target of Rapamycin Inhibitors Sensitize
Multiple Myeloma Cells to Dexamethasone-Induced Apoptosis  -
http://cancerres.aacrjournals.org/cgi/content/full/66/4/2305

4. This is the general link to the journal: Cancer Biology & Therapy
http://www.landesbioscience.com/journals/cbt/

5. http://www.landesbioscience.com/index.php - I used the search routine
at this site for multiple myeloma and there were some finds.

a. Interleukin-7 Induces MUC1 -
http://www.landesbioscience.com/journals/cbt/article/durum2-2.pdf

b. DF3/MUC1 Signaling In Multiple Myeloma Cells Is Regulated by
Interleukin-7 -
http://www.landesbioscience.com/journals/cbt/article/kufe2-2.pdf
Yongqing Li, Wen Chen, Jian Ren, Wei-hsuan Yu, Quan Li, Kiyotsugu
Yoshida and Donald Kufe

volume 2 | issue 2
march/april 2003
Pages: 187 - 193

The human DF3/MUC1 transmembrane protein is aberrantly expressed in
multiple myeloma cells and other B cell malignancies. The regulation of
MUC1 in B cells and its potential function as a signaling molecule are
unknown. The present results demonstrate that interleukin-7 (IL-7)
stimulates MUC1 expression in multiple myeloma cells. The results also
demonstrate the IL-7 induces binding of MUC1 to the Lyn tyrosine kinase.
The MUC1 C-terminal subunit binds directly to Lyn through interactions
with the Lyn SH3 and SH2 domains. Activation of Lyn in response to IL-7
stimulation results in increased tyrosine phosphorylation of the MUC1
C-terminal subunit. In vitro and in vivo studies show that Lyn
phosphorylates MUC1, at least in large part, on a YEKV site in the MUC1
cytoplasmic tail. The functional significance of the MUC1-Lyn
interaction is supported by the demonstration that Lynmediated
phosphorylation of MUC1 on YEKV induces binding of MUC1 and the
b-catenin signaling protein. In concert with these results, IL-7
treatment is associated with binding of MUC1 to b-catenin and targeting
of the MUC1 b-catenin complex to the nucleus. These findings indicate
that IL-7 regulates MUC1 expression and function in multiple myeloma cells.

Key Words

MUC1, IL-7, multiple myeloma, Lyn, •-catenin.

c. Signal Transduction and Myeloma: New Targets, New Hope -
http://www.landesbioscience.com/journals/cbt/article/lonial2-4.pdf
Sagar Lonial, Edmund K Waller, Jonathan W Simons and L.T. Heffner Jr.

volume 2 | issue 4
july/august 2003
Pages: 310 - 319

Multiple Myeloma is a hematologic malignancy characterized by the
abnormal proliferation of plasma cells. Therapy for this disease has
largely been palliative, and chances for long term survival after
initiation of treatment have been quite limited. In the era of molecular
therapies, a better understanding of the molecular biology resulting in
the development of myeloma have shed light on a number of novel and
potentially exciting therapeutic options for this disease which
previously had limited options. This review will discuss some of the
basic mechanisms of current therapy such as corticosteroids and
alkylating agents, as well as developing such as the proteasome
inhibitors, thalidomide and its analogs, arsenic trioxide, anti-sense
technology, and others. The final section will assess the potential for
new targeted approaches to treatment for mechanisms which have yet to be
fully explored, and for agents which are in early phase I development.
We now provide open access to journal articles published online for one
year or more. This article may be downloaded at the following link:

Click here to view the open access version of this article
http://www.landesbioscience.com/journals/5/article/425

There were finds using 1. immunoglobulin, 2. Mammalian target of
rapamycin in this sites search routine.

d. Rapamycins: Mechanisms of Action and Cellular Resistance -
http://www.landesbioscience.com/journals/cbt/article/huang2-3.pdf
No results were returned for alpha lipoic acid, coumain, or warfarin.

e. A scholar.google search for "Multiple Myeloma"+Cells+Interleukin-7
resulted in 749 finds - http://tinyurl.com/ytf4xc
f. "Multiple Myeloma"+MUC1+transmembrane+protein: 440 finds -
http://tinyurl.com/24pj38.
g. "Multiple Myeloma"+alpha+"lipoic acid" 182 finds -
http://tinyurl.com/2y6yd6
h. "Multiple Myeloma"+alpha+"lipoic acid"+warfarin 31 finds -
http://tinyurl.com/yo5gpm including Turning Point in the PatientWith
Relapsed Multiple Myeloma: Identifying Specific Targeted Therapies to
Potentially Overcome Drug Resistance and Improve Outcomes -
http://www.ons.org/Cecentral/pdf/MM_issue1_web.pdf
i. "lipoic acid"+warfarin+INR 29 finds - http://tinyurl.com/23zu62

6. Subject: Re: More on mTOR and HIF-1 Mammalian target of rapamycin is
activated in human gastric cancer and serves as a target for therapy in
an experimental model (Part 1)

Circ Res. 2007 Jan 5;100(1):79-87. Epub 2006 Nov 16. Links
Hypoxia-induced endothelial proliferation requires both mTORC1 and
mTORC2.Li W, Petrimpol M, Molle KD, Hall MN, Battegay EJ, Humar R.
Department of Research, University Hospital Basel, Hebelstrasse 20,
CH-4031 Basel, Switzerland.

A central regulator of cell growth that has been implicated in
responses to stress such as hypoxia is mTOR (mammalian Target Of
Rapamycin). We have shown previously that mTOR is required for
angiogenesis in vitro and endothelial cell proliferation in response
to hypoxia. Here we have investigated mTOR-associated signaling
components under hypoxia and their effects on cell proliferation in
rat aortic endothelial cells (RAECs). Hypoxia (1% O(2)) rapidly (>30
minutes) and in a concentration-dependent manner promoted rapamycin-
sensitive and sustained phosphorylation of mTOR-Ser2448 followed by
nuclear translocation in RAECs. Similarly, hypoxia induced
phosphorylation of the mTORC2 substrate Akt-Ser473 (3 to 6 hours at 1%
O(2)) and a brief phosphorylation peak of the mTORC1 substrate S6
kinase-Thr389 (10 to 60 minutes). Phosphorylation of Akt was inhibited
by mTOR knockdown and partially with rapamycin. mTOR knockdown,
rapamycin, or Akt inhibition specifically and significantly inhibited
proliferation of serum-starved RAECs under hypoxia (P<0.05; n> or =4).
Similarly, hypoxia induced Akt-dependent and rapamycin-sensitive
proliferation in mouse embryonic fibroblasts. This response was
partially blunted by hypoxia-inducible factor-1alpha knockdown and not
affected by TSC2 knockout. Finally, mTORC2 inhibition by rictor
silencing, especially (P<0.001; n=7), and mTORC1 inhibition by raptor
silencing, partially (P<0.05; n=7), inhibited hypoxia-induced RAEC
proliferation. Thus, mTOR mediates an early response to hypoxia via
mTORC1 followed by mTORC2, promoting endothelial proliferation mainly
via Akt signaling. mTORC1 and especially mTORC2 might therefore play
important roles in diseases associated with hypoxia and altered
angiogenesis.

PMID: 17110594 [PubMed - indexed for MEDLINE]

Related LinksPRR5, a novel component of mTOR complex 2, regulates
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[J Biol Chem. 2007]Ablation in mice of the mTORC components raptor,
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FOXO and PKCalpha, but not S6K1. [Dev Cell. 2006]Hypoxia enhances
vascular cell proliferation and angiogenesis in vitro via rapamycin
(mTOR)-dependent signaling. [FASEB J. 2002]ASCT2 silencing regulates
mammalian target-of-rapamycin growth and survival signaling in human
hepatoma cells. [Am J Physiol Cell Physiol. 2007]Activation of
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7. Subject: More on mTOR and HIF-1 Mammalian target of rapamycin is
activated in human gastric cancer and serves as a target for therapy in
an experimental model (Part 2)

Int J Cancer. 2007 Apr 15;120(8):1803-10. Links
Mammalian target of rapamycin is activated in human gastric cancer and
serves as a target for therapy in an experimental model.Lang SA,
Gaumann A, Koehl GE, Seidel U, Bataille F, Klein D, Ellis LM, Bolder
U, Hofstaedter F, Schlitt HJ, Geissler EK, Stoeltzing O.
Department of Surgery, University of Regensburg, Medical Center,
Regensburg, Germany.

The mammalian target of rapamycin (mTOR) has become an interesting
target for cancer therapy through its influence on oncogenic signals,
which involve phosphatidylinositol-3-kinase and hypoxia-inducible
factor-1alpha (HIF-1alpha). Since mTOR is an upstream regulator of
HIF-1alpha, a key mediator of gastric cancer growth and angiogenesis,
we investigated mTOR activation in human gastric adenocarcinoma
specimens and determined whether rapamycin could inhibit gastric
cancer growth in mice. Expression of phospho-mTOR was assessed by
immunohistochemical analyses of human tissues. For in vitro studies,
human gastric cancer cell lines were used to determine S6K1, 4E-BP-1
and HIF-1alpha activation and cancer cell motility upon rapamycin
treatment. Effects of rapamycin on tumor growth and angiogenesis in
vivo were assessed in both a subcutaneous tumor model and in an
experimental model with orthotopically grown tumors. Mice received
either rapamycin (0.5 mg/kg/day or 1.5 mg/kg/day) or diluent per intra-
peritoneal injections. In addition, antiangiogenic effects were
monitored in vivo using a dorsal-skin-fold chamber model.
Immunohistochemical analyses showed strong expression of phospho-mTOR
in 60% of intestinal- and 64% of diffuse-type human gastric
adenocarcinomas. In vitro, rapamycin-treatment effectively blocked
S6K1, 4E-BP-1 and HIF-1alpha activation, and significantly impaired
tumor cell migration. In vivo, rapamycin-treatment led to significant
inhibition of subcutaneous tumor growth, decreased CD31-positive
vessel area and reduced tumor cell proliferation. Similar significant
results were obtained in an orthotopic model of gastric cancer. In the
dorsal-skin-fold chamber model, rapamycin-treatment significantly
inhibited tumor vascularization in vivo. In conclusion, mTOR is
frequently activated in human gastric cancer and represents a
promising new molecular target for therapy. (c) 2007 Wiley-Liss, Inc.

PMID: 17230506 [PubMed - indexed for MEDLINE]

Related LinksInhibition of heat shock protein 90 impairs epidermal
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2007]Significance of Akt phosphorylation on tumor growth and vascular
endothelial growth factor expression in human gastric carcinoma.
[Pathobiology. 2006]Role of hypoxia-inducible factor 1alpha in gastric
cancer cell growth, angiogenesis, and vessel maturation. [J Natl
Cancer Inst. 2004]Akt1 activation can augment hypoxia-inducible
factor-1alpha expression by increasing protein translation through a
mammalian target of rapamycin-independent pathway. [Mol Cancer Res.
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