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IGFBP-3 induced by ribotoxic stress is not secreted prior to nuclear localization in mammary epithelial cells
Descriptive
TitleInfo
Title
IGFBP-3 induced by ribotoxic stress is not secreted prior to nuclear localization in mammary epithelial cells
Name
(type = personal)
NamePart
(type = family)
Skorupa
NamePart
(type = given)
Jennifer A.
NamePart
(type = date)
1990-
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Jennifer A. Skorupa
Role
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(authority = RULIB)
author
Name
(type = personal)
NamePart
(type = family)
Cohick
NamePart
(type = given)
Wendie S
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Wendie S Cohick
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Advisory Committee
Role
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(authority = RULIB)
chair
Name
(type = personal)
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(type = family)
Belden
NamePart
(type = given)
William J
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William J Belden
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Advisory Committee
Role
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(authority = RULIB)
internal member
Name
(type = personal)
NamePart
(type = family)
Bello
NamePart
(type = given)
Nicholas T
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Nicholas T Bello
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Advisory Committee
Role
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(authority = RULIB)
internal member
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NamePart
Rutgers University
Role
RoleTerm
(authority = RULIB)
degree grantor
Name
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NamePart
School of Graduate Studies
Role
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school
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Text
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theses
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2018
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2018-01
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2018
Place
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xx
Language
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eng
Abstract
(type = abstract)
Ribotoxic stressors such as anisomycin (ANS) and deoxynivalenol (DON) induce apoptosis in MAC-T cells. These agents also increase IGFBP-3 expression and knockdown of IGFBP-3 mitigates the apoptotic effects of these toxins. IGFBP-3 contains both a signal sequence and a nuclear localization sequence (NLS) and is thus both secreted and localized to the nucleus. Nuclear IGFBP-3 has been proposed to be important in its apoptotic effect. Following treatment with DON and ANS, nuclear IGFBP-3 is glycosylated, a hallmark of the secretory pathway. However, how it escapes the secretory pathway to traffic to the nucleus is unknown. Some studies have reported that extracellular IGFBP-3 is rapidly internalized and delivered to the nucleus, suggesting IGFBP-3 may require secretion and re-internalization prior to nuclear localization. To study trafficking of the endogenous protein, MAC-T cells were treated with ANS or DON. Fluorescent microscopy and Western immunoblot analysis demonstrated that ANS and DON induced nuclear localization of IGFBP-3. Treatment of nuclear IGFBP-3 with the deglycosylation enzyme Endoglycosidase H (Endo H) resulted in a lower molecular weight band indicating nuclear IGFBP-3 contains a mannose or hybrid type glycan. In contrast, the sugar of secreted IGFBP-3 was not truncated using Endo H, but was deglycosylated using PNGase indicating complex-type glycosylation. Cells treated with Brefeldin A (BFA), an inhibitor of anterograde transport from the ER to the Golgi, still showed nuclear movement of IGFBP-3. Glycosylation and BFA data indicate that IGFBP-3 is not secreted and re-internalized prior to nuclear localization during ribotoxic stress.
Subject
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Topic
Endocrinology and Animal Biosciences
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Title
Rutgers University Electronic Theses and Dissertations
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ETD_8617
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electronic resource
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application/pdf
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text/xml
Extent
1 online resource (xii, 61 p. : ill.)
Note
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M.S.
Note
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Includes bibliographical references
Note
(type = statement of responsibility)
by Jennifer A. Skorupa
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TitleInfo
Title
School of Graduate Studies Electronic Theses and Dissertations
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rucore10001600001
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NjNbRU
Identifier
(type = doi)
doi:10.7282/T3D50R5W
Genre
(authority = ExL-Esploro)
ETD graduate
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Rights
RightsDeclaration
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The author owns the copyright to this work.
RightsHolder
(type = personal)
Name
FamilyName
Skorupa
GivenName
Jennifer
MiddleName
A.
Role
Copyright Holder
RightsEvent
Type
Permission or license
DateTime
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(qualifier = exact);
(point = start)
2018-01-04 16:50:18
AssociatedEntity
Name
Jennifer Skorupa
Role
Copyright holder
Affiliation
Rutgers University. School of Graduate Studies
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Type
License
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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.
RightsEvent
DateTime
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2018-01-31
DateTime
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2019-01-31
Type
Embargo
Detail
Access to this PDF has been restricted at the author's request. It will be publicly available after January 31st, 2019.
Copyright
Status
Copyright protected
Availability
Status
Open
Reason
Permission or license
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Technical
RULTechMD
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ETD
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windows xp
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1.4
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2018-01-04T21:44:43
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2018-01-04T21:44:43
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