 Vincent Manganiello
M.D., Ph.D., Johns Hopkins University,
1967
National Institutes of Health
10 Center Drive, Building 10 / Room 5N307
Bethesda, Maryland 20892-1434
Phone Number: 301-496-1770
Fax Number: 301-402-1610
Email Address: manganiv@nhlbi.nih.gov
Research Interest(s):
Molecular & Cellular Biology
Animal Models & Pathology
Endocrinology & Reproduction
Immunology
Pulmonary / Respiratory Diseases
Research Description:
Cyclic Nucleotide Phosphodiesterases
in Health and Disease
Our research focuses on cyclic nucleotide
phosphodiesterases (PDEs), a large superfamily
of enzymes that catalyze the hydrolysis
of cAMP and cGMP, and, thus, are critical
regulators of the intracellular concentrations
of these important second messengers,
and of the signaling pathways and cellular
functions modulated by them. We are especially
interested in the PDE3 gene family, and
are using cell culture model systems and
PDE3 knockout mice to study the role of
PDE3 in regulation of important biological
processes such as insulin secretion and
oocyte maturation, as well as several
critical physiological actions of insulin
and IGF-1. State-of-the art molecular
and cellular biological techniques are
also being utilized to study mechanisms
for regulation of PDE3 gene expression
during differentiation of adipocytes and
human monocytes/macrophages and for intracellular
localization and membrane association
of PDE3 isoforms, as well as to identify
signaling pathways, interacting partners,
and structural determinants involved in
covalent modification/activation and regulation
of PDE3 isoforms. Because of the known
inhibitory effects of cAMP on various
inflammatory responses, microarrays and
proteomics are being employed to discover
new therapeutic targets, and translational
clinical research studies are in progress
to assess the potential utility of PDE
inhibitors in the treatment of pulmonary
diseases such as sarcoidosis.
Selected Publications:
A Role for Phosphodiesterase 3B in the
Antilipolytic Action of Insulin. E Degerman,
T Rahn-Landstrom, L Stenson-Holst, O Goransson,
F Ahmad, Y Shakur, Y Kenan, VC Manganiello.
In D. LeRoith, S.I. Taylor, J.M. Olefsky
(eds): Diabetes Mellitus: A Fundamental
and Clinical Text, Lippincott, Williams
and Wilkins, Philadelphia, PA, :284-291(2000).
Regulation and Function of the Cyclic
Nucleotide Phosphodiesterase (PDE3) Gene
Family. Y Shakur, LS Holst, TR Landstrom,
M Movsesian, E Degerman, V Manganiello.
Progress in Nucleic Acid Research and
Molecular Biology 66:241-277(2000). PubMed
Functions of the N-terminal Region of
Cyclic Nucleotide Phosphodiesterase 3
(PDE3) Isoforms. Y Kenan, T Murata, Y
Shakur, E Degerman, VC Manganiello. Journal
of Biological Chemistry 275:12331-12338
(2000). PubMed
Membrane Localization of Cyclic Nucleotide
Phosphodiesterase 3 (PDE3). Two N-terminal
domains are required for the efficient
targeting to, and association of PDE3
with Endoplasmic Reticulum. Y Shakur,
K Takeda, Y Kenan, ZX Yu, G Rena, D Brandt,
MD Houslay, E Degerman, VJ Ferans, VC
Manganiello, V.C. Journal of Biological
Chemistry 275:38749-38761(2000). PubMed
Cyclic Nucleotide Phosphodiesterase 3B
is a Downstream Target of Protein Kinase
B and may be Involved in Regulation of
Effects of Protein Kinase B on Thymidine
Incoporation in FDCP2 cells. F Ahmad,
LN cong, L Stenson-Holst, LM Wang, T Rahn-Landstrom,
JH Pierce, MJ Quon, E Degerman, VC Manganiello.
Journal of Immunology 64:4678-4688(2000). PubMed
Last updated August 29, 2002 |
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