Staff View
Osteopontin and cell adhesion: role of post-translational modifications and the C-terminal region

Descriptive

TitleInfo
Title
Osteopontin and cell adhesion: role of post-translational modifications and the C-terminal region
Name (type = personal)
NamePart (type = family)
Kazanecki
NamePart (type = given)
Christian Charles
DisplayForm
Christian Kazanecki
Role
RoleTerm (authority = RUETD)
author
Name (type = personal)
NamePart (type = family)
Denhardt
NamePart (type = given)
David
Affiliation
Advisory Committee
DisplayForm
David T. Denhardt
Role
RoleTerm (authority = RULIB)
chair
Name (type = personal)
NamePart (type = family)
Fong
NamePart (type = given)
Dunne
Affiliation
Advisory Committee
DisplayForm
Dunne Fong
Role
RoleTerm (authority = RULIB)
internal member
Name (type = personal)
NamePart (type = family)
Xiao
NamePart (type = given)
Gutian
Affiliation
Advisory Committee
DisplayForm
Gutian Xiao
Role
RoleTerm (authority = RULIB)
internal member
Name (type = personal)
NamePart (type = family)
Sahota
NamePart (type = given)
Amrik
Affiliation
Advisory Committee
DisplayForm
Amrik Sahota
Role
RoleTerm (authority = RULIB)
internal member
Name (type = personal)
NamePart (type = family)
Riman
NamePart (type = given)
Richard
Affiliation
Advisory Committee
DisplayForm
Richard E. Riman
Role
RoleTerm (authority = RULIB)
outside member
Name (type = corporate)
NamePart
Rutgers University
Role
RoleTerm (authority = RULIB)
degree grantor
Name (type = corporate)
NamePart
Graduate School-New Brunswick
Role
RoleTerm (authority = RULIB)
school
TypeOfResource
Text
Genre (authority = marcgt)
theses
OriginInfo
DateCreated (qualifier = exact)
2007
DateOther (qualifier = exact); (type = degree)
2007
Language
LanguageTerm (authority = ISO 639-3:2007); (type = text)
English
PhysicalDescription
Form (authority = marcform)
electronic
InternetMediaType
application/pdf
InternetMediaType
text/xml
Extent
xii, 109 pages
Abstract (type = abstract)
Osteopontin (OPN) is an integrin-binding secreted phosphoglycoprotein found in many tissues and body fluids, where it acts as both a soluble cytokine and a component of mineralized matrices. It exhibits a broad range of functional activities in physiological and pathological processes, many of which are influenced by post-translational modifications. OPN is highly modified by phosphorylation and glycosylation that can vary depending on the source. This study identified two different forms of OPN produced by murine ras-transformed fibroblasts (FbOPN) and differentiating osteoblasts (ObOPN) based on the reactivity of a panel of anti-OPN monoclonal antibodies. By enzymatic dephosphorylation, mass, and sequence analyses, it was shown that FbOPN contained approximately four phosphate groups distributed over 17 potential phosphorylation sites, whereas ObOPN contained approximately 21 phosphate groups distributed over 27 sites. This is the first extensive characterization of OPN produced by transformed cells, and the FbOPN form is the least modified form of OPN that has been characterized to date.

The forms of OPN also differed in their ability to support adhesion of human MDA-MB-435 tumor cells and mouse 275-3-2 ras-transformed fibroblasts. The MDA-MB-435 cells bound with approximately 60% greater efficiency to the FbOPN than ObOPN, whereas the 275-3-2 cells bound the ObOPN with 35% greater efficiency than FbOPN. Inhibition of adhesion with an Arg-Gly-Asp (RGD)-containing peptide inhibited the binding of both lines to the OPN forms, suggesting that different integrins preferentially bind to OPN based upon its phosphorylation state.

This study has also identified a potential role for a novel region of OPN in cell adhesion. Two anti-osteopontin monoclonal antibodies, both of which recognize the C-terminal region of OPN, were shown to inhibit MDA-MB-435 cell adhesion to recombinant human OPN. Synthetic peptides corresponding to this region were bound by cells using a flow cytometry assay, suggesting a receptor interaction in this region of OPN. This interaction is hypothesized to be a signaling interaction because cells were not able to adhere to the synthetic C-terminal peptides and adhesion in the presence of these soluble peptides was not affected.
Note (type = degree)
Ph.D.
Note (type = bibliography)
Includes bibliographical references (p. 86-107).
Subject (authority = RUETD)
Topic
Microbiology and Molecular Genetics
Subject (authority = ETD-LCSH)
Topic
Osteopontin
Subject (authority = ETD-LCSH)
Topic
Cell adhesion molecules
Subject (authority = ETD-LCSH)
Topic
Phosphoproteins
Subject (authority = ETD-LCSH)
Topic
C-peptide
RelatedItem (type = host)
TitleInfo
Title
Graduate School - New Brunswick Electronic Theses and Dissertations
Identifier (type = local)
rucore19991600001
Identifier (type = hdl)
http://hdl.rutgers.edu/1782.2/rucore10001600001.ETD.13493
Identifier
ETD_164
Identifier (type = doi)
doi:10.7282/T3GF0TXZ
Location
PhysicalLocation (authority = marcorg); (displayLabel = Rutgers, The State University of New Jersey)
NjNbRU
Genre (authority = ExL-Esploro)
ETD doctoral
Back to the top

Rights

RightsDeclaration (AUTHORITY = GS); (ID = rulibRdec0006)
The author owns the copyright to this work.
Copyright
Status
Copyright protected
Availability
Status
Open
AssociatedEntity (AUTHORITY = rulib); (ID = 1)
Name
Christian Kazanecki
Role
Copyright holder
Affiliation
Rutgers University. Graduate School-New Brunswick
RightsEvent (AUTHORITY = rulib); (ID = 1)
Type
Permission or license
Detail
Non-exclusive ETD license
AssociatedObject (AUTHORITY = rulib); (ID = 1)
Type
License
Name
Author Agreement License
Detail
I hereby grant to the Rutgers University Libraries and to my school the non-exclusive right to archive, reproduce and distribute my thesis or dissertation, in whole or in part, and/or my abstract, in whole or in part, in and from an electronic format, subject to the release date subsequently stipulated in this submittal form and approved by my school. I represent and stipulate that the thesis or dissertation and its abstract are my original work, that they do not infringe or violate any rights of others, and that I make these grants as the sole owner of the rights to my thesis or dissertation and its abstract. I represent that I have obtained written permissions, when necessary, from the owner(s) of each third party copyrighted matter to be included in my thesis or dissertation and will supply copies of such upon request by my school. I acknowledge that RU ETD and my school will not distribute my thesis or dissertation or its abstract if, in their reasonable judgment, they believe all such rights have not been secured. I acknowledge that I retain ownership rights to the copyright of my work. I also retain the right to use all or part of this thesis or dissertation in future works, such as articles or books.
Back to the top

Technical

Format (TYPE = mime); (VERSION = )
application/x-tar
FileSize (UNIT = bytes)
895488
Checksum (METHOD = SHA1)
07ee30f32bc515ff7f8812e97eb692229340bdbd
ContentModel
ETD
CompressionScheme
other
OperatingSystem (VERSION = 5.1)
windows xp
Format (TYPE = mime); (VERSION = NULL)
application/x-tar
Back to the top
Version 8.5.5
Rutgers University Libraries - Copyright ©2024