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Activation of the rat luteinizing hormone following substitution of treonine-413 with selective residues
Descriptive
TypeOfResource
Text
TitleInfo
(ID = T-1)
Title
Activation of the rat luteinizing hormone following substitution of treonine-413 with selective residues
Identifier
ETD_2530
Identifier
(type = hdl)
http://hdl.rutgers.edu/1782.1/rucore10001600001.ETD.000053490
Language
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(type = code)
eng
Genre
(authority = marcgt)
theses
Subject
(ID = SBJ-1);
(authority = RUETD)
Topic
Microbiology and Molecular Genetics
Subject
(ID = SBJ-2);
(authority = ETD-LCSH)
Topic
Glycoprotein hormones
Subject
(ID = SBJ-3);
(authority = ETD-LCSH)
Topic
Amino acids
Abstract
(type = abstract)
The glycoprotein hormones lutropin (LH), follitropin (FSH) and thyrotropin (TSH) control the many functions of the ovaries, testes and thyroid (27). Humans have two lutropins, (hLH) and chorionic gonadotropin (hCG). hLH is secreted from the pituitary gland while hCG is a placental protein (27). It has been known since 1989 that the receptor for these lutropins is a G protein-coupled receptor (GPCR), which constitute the largest most-conserved superfamily of signaling molecules (42). High affinity hormone binding results from interactions between residues in the curved portion of the extracellular domain of the receptor and the groove in the hormone formed by the apposition of the second α-subunit loop and the first and third β-subunit loops. Most of the remainder of the hormone is found in the large space between the arms of the extracellular domain and makes few, if any, additional specific contacts with the receptor needed for high affinity binding. Signal transduction is caused by steric or other influences of the hormone on the distance between the arms of the extracellular domain, an effect augmented by the oligosaccharides. Because the extracellular domain is coupled at multiple sites to the transmembrane domain, the change in conformation of the extracellular domain is relayed to the transmembrane domain and subsequently to the cytoplasmic surface of the plasma membrane. Here I will discuss several mutations made of the LHR amino acid Threonine 413 (T413). These six mutations were analyzed by hCG binding and cAMP assays. Since hCG is capable of stimulating steriodogenesis and cyclic AMP formation in the rat testicular tissues (28), it was important that we looked at not only the ability of the mutants created to bind hCG but also their effects on cAMP activation. It is important to study this particular amino acid because it is highly conserved over many species and the unique nature of this residue has not been investigated to our knowledge.
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electronic resource
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v, 87 p. : ill.
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application/pdf
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text/xml
Note
(type = degree)
M.S.
Note
Includes abstract
Note
(type = bibliography)
Includes bibliographical references
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(type = statement of responsibility)
by Nicole Lynn Arnold
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Arnold
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Nicole
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1980-
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author
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Nicole Arnold
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(type = family)
Vershon
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(type = given)
Andrew K
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chair
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Advisory Committee
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Andrew K Vershon
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(type = family)
Moyle
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(type = given)
William R
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internal member
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Advisory Committee
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William R Moyle
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(type = family)
Bernard
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(type = given)
Michael P
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(authority = RULIB)
outside member
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Advisory Committee
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Michael P Bernard
Name
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NamePart
Rutgers University
Role
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degree grantor
Name
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NamePart
Graduate School - New Brunswick
Role
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school
OriginInfo
DateCreated
(qualifier = exact)
2010
DateOther
(qualifier = exact);
(type = degree)
2010
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TitleInfo
Title
Rutgers University Electronic Theses and Dissertations
Identifier
(type = RULIB)
ETD
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(type = host)
TitleInfo
Title
Graduate School - New Brunswick Electronic Theses and Dissertations
Identifier
(type = local)
rucore19991600001
Location
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(displayLabel = Rutgers, The State University of New Jersey)
NjNbRU
Identifier
(type = doi)
doi:10.7282/T35X290F
Genre
(authority = ExL-Esploro)
ETD graduate
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Rights
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The author owns the copyright to this work.
Copyright
Status
Copyright protected
Availability
Status
Open
Reason
Permission or license
RightsHolder
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(type = personal)
Name
FamilyName
Arnold
GivenName
Nicole
Role
Copyright Holder
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(AUTHORITY = rulib)
Type
Permission or license
DateTime
2010-04-12 20:53:08
AssociatedEntity
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(AUTHORITY = rulib)
Role
Copyright holder
Name
Nicole Arnold
Affiliation
Rutgers University. Graduate School - New Brunswick
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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.
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ETD
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application/x-tar
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4341760
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