Characterization of pituitary IGF-I receptors: modulation of prolactin and growth hormone
1 Department of Zoology, North Carolina State University, Raleigh 27695-7617; and 2 Department of Medicine, Division of Gastroenterology, Duke University Medical Center, Durham, North Carolina 27710 There have been no studies in any vertebrate that have localized insulin-like growth factor (IGF)-I...
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| Veröffentlicht in: | American journal of physiology. Regulatory, integrative and comparative physiology integrative and comparative physiology, 2002-08, Vol.283 (2), p.468-R476 |
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| container_title | American journal of physiology. Regulatory, integrative and comparative physiology |
| container_volume | 283 |
| creator | Fruchtman, Shira McVey, Douglas C Borski, Russell J |
| description | 1 Department of Zoology, North Carolina State
University, Raleigh 27695-7617; and 2 Department of
Medicine, Division of Gastroenterology, Duke University Medical
Center, Durham, North Carolina 27710
There have
been no studies in any vertebrate that have localized insulin-like
growth factor (IGF)-I receptors in prolactin (PRL) cells or that have
correlated pituitary binding to the potency of IGF-I in regulating both
PRL and growth hormone (GH) secretion. We show that IGF-I binds with
high affinity and specificity to the pituitary gland of hybrid striped
bass ( Morone saxatilis × M. chrysops ).
IGF-I and IGF-II were equipotent in inhibiting saturable 125 I-IGF-I binding, whereas insulin was ineffective. IGF-I
binds with similar affinity to the rostral pars distalis (>95% PRL
cells) as the whole pituitary gland and immunohistochemistry
colocalizes IGF-I receptors and PRL in this same region.
Des(1-3)IGF-I, a truncated analog of IGF-I that binds
with high affinity to IGF-I receptors but weakly to IGF-I binding
proteins (IGFBPs), showed a similar inhibition of saturable
125 I-IGF-I binding, but it was more potent than IGF-I in
stimulating PRL and inhibiting GH release. These results are the first
to localize IGF-I receptors to PRL cells, correlate IGF-I binding to
its efficacy in regulating GH and PRL secretion, as well as demonstrate
that IGFBPs may play a significant role in modulating the disparate
actions of IGF-I on PRL and GH secretion.
signal transduction; teleost; insulin-like growth factor binding
proteins; Morone ; secretion |
| doi_str_mv | 10.1152/ajpregu.00511.2001 |
| format | Article |
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University, Raleigh 27695-7617; and 2 Department of
Medicine, Division of Gastroenterology, Duke University Medical
Center, Durham, North Carolina 27710
There have
been no studies in any vertebrate that have localized insulin-like
growth factor (IGF)-I receptors in prolactin (PRL) cells or that have
correlated pituitary binding to the potency of IGF-I in regulating both
PRL and growth hormone (GH) secretion. We show that IGF-I binds with
high affinity and specificity to the pituitary gland of hybrid striped
bass ( Morone saxatilis × M. chrysops ).
IGF-I and IGF-II were equipotent in inhibiting saturable 125 I-IGF-I binding, whereas insulin was ineffective. IGF-I
binds with similar affinity to the rostral pars distalis (>95% PRL
cells) as the whole pituitary gland and immunohistochemistry
colocalizes IGF-I receptors and PRL in this same region.
Des(1-3)IGF-I, a truncated analog of IGF-I that binds
with high affinity to IGF-I receptors but weakly to IGF-I binding
proteins (IGFBPs), showed a similar inhibition of saturable
125 I-IGF-I binding, but it was more potent than IGF-I in
stimulating PRL and inhibiting GH release. These results are the first
to localize IGF-I receptors to PRL cells, correlate IGF-I binding to
its efficacy in regulating GH and PRL secretion, as well as demonstrate
that IGFBPs may play a significant role in modulating the disparate
actions of IGF-I on PRL and GH secretion.
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University, Raleigh 27695-7617; and 2 Department of
Medicine, Division of Gastroenterology, Duke University Medical
Center, Durham, North Carolina 27710
There have
been no studies in any vertebrate that have localized insulin-like
growth factor (IGF)-I receptors in prolactin (PRL) cells or that have
correlated pituitary binding to the potency of IGF-I in regulating both
PRL and growth hormone (GH) secretion. We show that IGF-I binds with
high affinity and specificity to the pituitary gland of hybrid striped
bass ( Morone saxatilis × M. chrysops ).
IGF-I and IGF-II were equipotent in inhibiting saturable 125 I-IGF-I binding, whereas insulin was ineffective. IGF-I
binds with similar affinity to the rostral pars distalis (>95% PRL
cells) as the whole pituitary gland and immunohistochemistry
colocalizes IGF-I receptors and PRL in this same region.
Des(1-3)IGF-I, a truncated analog of IGF-I that binds
with high affinity to IGF-I receptors but weakly to IGF-I binding
proteins (IGFBPs), showed a similar inhibition of saturable
125 I-IGF-I binding, but it was more potent than IGF-I in
stimulating PRL and inhibiting GH release. These results are the first
to localize IGF-I receptors to PRL cells, correlate IGF-I binding to
its efficacy in regulating GH and PRL secretion, as well as demonstrate
that IGFBPs may play a significant role in modulating the disparate
actions of IGF-I on PRL and GH secretion.
signal transduction; teleost; insulin-like growth factor binding
proteins; Morone ; secretion</description><subject>Animals</subject><subject>Bass</subject><subject>Binding, Competitive - drug effects</subject><subject>Crosses, Genetic</subject><subject>Dose-Response Relationship, Drug</subject><subject>Growth Hormone - analysis</subject><subject>Growth Hormone - biosynthesis</subject><subject>Immunohistochemistry</subject><subject>In Vitro Techniques</subject><subject>Insulin - pharmacokinetics</subject><subject>Insulin-Like Growth Factor Binding Proteins - metabolism</subject><subject>Insulin-Like Growth Factor I - pharmacokinetics</subject><subject>Insulin-Like Growth Factor II - pharmacokinetics</subject><subject>Peptide Fragments - pharmacokinetics</subject><subject>Pituitary Gland - chemistry</subject><subject>Pituitary Gland - cytology</subject><subject>Pituitary Gland - drug effects</subject><subject>Pituitary Gland - metabolism</subject><subject>Prolactin - analysis</subject><subject>Prolactin - biosynthesis</subject><subject>Radioligand Assay</subject><subject>Receptor, IGF Type 1 - chemistry</subject><subject>Receptor, IGF Type 1 - metabolism</subject><subject>Substrate Specificity</subject><issn>0363-6119</issn><issn>1522-1490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kL1u2zAURomiRe2kfYEMgaZucvgniexWGLFjwECBwh06ETRFWjQkUSEpOM7Tl66deCo43IHnfLj3A-AOwRlCBX6Q-8Hr3TiDsEBohiFEH8A0feAcUQ4_gikkJclLhPgE3ISwhxBSQslnMEE4PVbCKfgzb6SXKmpvX2W0rs-cyQYbRxulP2ar5SJfZV4rPUTnw_esc_XYXkHv2iTbPpN9ne28O8Qma5zvXK-_gE9GtkF_vcxb8HvxuJk_5eufy9X8xzpXtCAxl9ooWEtWsZLWHGtT1NCwLdWSb1GhtiWt0qwqTrg0rOKKMVNUDJFkKUUKcgu-nXPTMs-jDlF0NijdtrLXbgyiQhwjSnkC8RlU3oXgtRGDt126UiAoToWKS6HiX6HiVGiS7i_p47bT9VW5NJiA_Aw0dtccrNdiaI7Butbtju-BmBGBxS9assTz__OLsW03-iW-iVdPDLUhfwFJspnB</recordid><startdate>20020801</startdate><enddate>20020801</enddate><creator>Fruchtman, Shira</creator><creator>McVey, Douglas C</creator><creator>Borski, Russell J</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20020801</creationdate><title>Characterization of pituitary IGF-I receptors: modulation of prolactin and growth hormone</title><author>Fruchtman, Shira ; McVey, Douglas C ; Borski, Russell J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c453t-aefc0da87864d92ef5d0f8b4ea9b15cb647b1577939af879c88f57813c0dcc353</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Animals</topic><topic>Bass</topic><topic>Binding, Competitive - drug effects</topic><topic>Crosses, Genetic</topic><topic>Dose-Response Relationship, Drug</topic><topic>Growth Hormone - analysis</topic><topic>Growth Hormone - biosynthesis</topic><topic>Immunohistochemistry</topic><topic>In Vitro Techniques</topic><topic>Insulin - pharmacokinetics</topic><topic>Insulin-Like Growth Factor Binding Proteins - metabolism</topic><topic>Insulin-Like Growth Factor I - pharmacokinetics</topic><topic>Insulin-Like Growth Factor II - pharmacokinetics</topic><topic>Peptide Fragments - pharmacokinetics</topic><topic>Pituitary Gland - chemistry</topic><topic>Pituitary Gland - cytology</topic><topic>Pituitary Gland - drug effects</topic><topic>Pituitary Gland - metabolism</topic><topic>Prolactin - analysis</topic><topic>Prolactin - biosynthesis</topic><topic>Radioligand Assay</topic><topic>Receptor, IGF Type 1 - chemistry</topic><topic>Receptor, IGF Type 1 - metabolism</topic><topic>Substrate Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Fruchtman, Shira</creatorcontrib><creatorcontrib>McVey, Douglas C</creatorcontrib><creatorcontrib>Borski, Russell J</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>American journal of physiology. 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University, Raleigh 27695-7617; and 2 Department of
Medicine, Division of Gastroenterology, Duke University Medical
Center, Durham, North Carolina 27710
There have
been no studies in any vertebrate that have localized insulin-like
growth factor (IGF)-I receptors in prolactin (PRL) cells or that have
correlated pituitary binding to the potency of IGF-I in regulating both
PRL and growth hormone (GH) secretion. We show that IGF-I binds with
high affinity and specificity to the pituitary gland of hybrid striped
bass ( Morone saxatilis × M. chrysops ).
IGF-I and IGF-II were equipotent in inhibiting saturable 125 I-IGF-I binding, whereas insulin was ineffective. IGF-I
binds with similar affinity to the rostral pars distalis (>95% PRL
cells) as the whole pituitary gland and immunohistochemistry
colocalizes IGF-I receptors and PRL in this same region.
Des(1-3)IGF-I, a truncated analog of IGF-I that binds
with high affinity to IGF-I receptors but weakly to IGF-I binding
proteins (IGFBPs), showed a similar inhibition of saturable
125 I-IGF-I binding, but it was more potent than IGF-I in
stimulating PRL and inhibiting GH release. These results are the first
to localize IGF-I receptors to PRL cells, correlate IGF-I binding to
its efficacy in regulating GH and PRL secretion, as well as demonstrate
that IGFBPs may play a significant role in modulating the disparate
actions of IGF-I on PRL and GH secretion.
signal transduction; teleost; insulin-like growth factor binding
proteins; Morone ; secretion</abstract><cop>United States</cop><pmid>12121860</pmid><doi>10.1152/ajpregu.00511.2001</doi></addata></record> |
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| ispartof | American journal of physiology. Regulatory, integrative and comparative physiology, 2002-08, Vol.283 (2), p.468-R476 |
| issn | 0363-6119 1522-1490 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_71921449 |
| source | MEDLINE; American Physiological Society; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals |
| subjects | Animals Bass Binding, Competitive - drug effects Crosses, Genetic Dose-Response Relationship, Drug Growth Hormone - analysis Growth Hormone - biosynthesis Immunohistochemistry In Vitro Techniques Insulin - pharmacokinetics Insulin-Like Growth Factor Binding Proteins - metabolism Insulin-Like Growth Factor I - pharmacokinetics Insulin-Like Growth Factor II - pharmacokinetics Peptide Fragments - pharmacokinetics Pituitary Gland - chemistry Pituitary Gland - cytology Pituitary Gland - drug effects Pituitary Gland - metabolism Prolactin - analysis Prolactin - biosynthesis Radioligand Assay Receptor, IGF Type 1 - chemistry Receptor, IGF Type 1 - metabolism Substrate Specificity |
| title | Characterization of pituitary IGF-I receptors: modulation of prolactin and growth hormone |
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