A contactin-receptor-like protein tyrosine phosphatase β complex mediates adhesive communication between astroglial cells and gonadotrophin-releasing hormone neurones

A. S. Parent, A. E. Mungenast, Alejandro Lomniczi, U. S. Sandau, E. Peles, M. A. Bosch, Oline Ronnekleiv, Sergio Ojeda

Research output: Contribution to journalArticle

32 Citations (Scopus)

Abstract

Although it is well established that gonadotrophin-releasing hormone (GnRH) neurones and astrocytes maintain an intimate contact throughout development and adult life, the cell-surface molecules that may contribute to this adhesiveness remain largely unknown. In the peripheral nervous system, the glycosylphosphatidyl inositol (GPI)-anchored protein contactin is a cell-surface neuronal protein required for axonal-glial adhesiveness. A glial transmembrane protein recognised by neuronal contactin is receptor-like protein tyrosine phosphatase β (RPTPβ), a phosphatase with structural similarities to cell adhesion molecules. In the present study, we show that contactin, and its preferred in cis partner Caspr1, are expressed in GnRH neurones. We also show that the RPTPβ mRNA predominantly expressed in hypothalamic astrocytes encodes an RPTPβ isoform (short RPTPβ) that uses its carbonic anhydrase (CAH) extracellular subdomain to interact with neuronal contactin. Immunoreactive contactin is most abundant in GnRH nerve terminals projecting to both the organum vasculosum of the lamina terminalis and median eminence, implying GnRH axons as an important site of contactin-dependent cell adhesiveness. GT1-7 immortalised GnRH neurones adhere to the CAH domain of RPTPβ, and this adhesiveness is blocked when contactin GPI anchoring is disrupted or contactin binding capacity is immunoneutralised, suggesting that astrocytic RPTPβ interacts with neuronal contactin to mediate glial-GnRH neurone adhesiveness. Because the abundance of short RPTPβ mRNA increases in the female mouse hypothalamus (but not in the cerebral cortex) before puberty, it appears that an increased interaction between GnRH axons and astrocytes mediated by RPTPβ-contactin is a dynamic mechanism of neurone-glia communication during female sexual development.

Original languageEnglish (US)
Pages (from-to)847-858
Number of pages12
JournalJournal of Neuroendocrinology
Volume19
Issue number11
DOIs
StatePublished - Nov 2007

Fingerprint

Receptor-Like Protein Tyrosine Phosphatases
Contactins
Gonadotropin-Releasing Hormone
Adhesives
Communication
Neurons
Adhesiveness
Neuroglia
Astrocytes
Carbonic Anhydrases
Inositol
Axons
Messenger RNA
Median Eminence
Sexual Development
Peripheral Nervous System
Cell Adhesion Molecules
Puberty
Phosphoric Monoester Hydrolases
Cerebral Cortex

Keywords

  • Adhesion molecules
  • Astrocytes
  • GnRH neurones
  • Hypothalamus

ASJC Scopus subject areas

  • Endocrinology
  • Neuroscience(all)

Cite this

A contactin-receptor-like protein tyrosine phosphatase β complex mediates adhesive communication between astroglial cells and gonadotrophin-releasing hormone neurones. / Parent, A. S.; Mungenast, A. E.; Lomniczi, Alejandro; Sandau, U. S.; Peles, E.; Bosch, M. A.; Ronnekleiv, Oline; Ojeda, Sergio.

In: Journal of Neuroendocrinology, Vol. 19, No. 11, 11.2007, p. 847-858.

Research output: Contribution to journalArticle

@article{dc4ac37c57c5448a9e866a741919e1f4,
title = "A contactin-receptor-like protein tyrosine phosphatase β complex mediates adhesive communication between astroglial cells and gonadotrophin-releasing hormone neurones",
abstract = "Although it is well established that gonadotrophin-releasing hormone (GnRH) neurones and astrocytes maintain an intimate contact throughout development and adult life, the cell-surface molecules that may contribute to this adhesiveness remain largely unknown. In the peripheral nervous system, the glycosylphosphatidyl inositol (GPI)-anchored protein contactin is a cell-surface neuronal protein required for axonal-glial adhesiveness. A glial transmembrane protein recognised by neuronal contactin is receptor-like protein tyrosine phosphatase β (RPTPβ), a phosphatase with structural similarities to cell adhesion molecules. In the present study, we show that contactin, and its preferred in cis partner Caspr1, are expressed in GnRH neurones. We also show that the RPTPβ mRNA predominantly expressed in hypothalamic astrocytes encodes an RPTPβ isoform (short RPTPβ) that uses its carbonic anhydrase (CAH) extracellular subdomain to interact with neuronal contactin. Immunoreactive contactin is most abundant in GnRH nerve terminals projecting to both the organum vasculosum of the lamina terminalis and median eminence, implying GnRH axons as an important site of contactin-dependent cell adhesiveness. GT1-7 immortalised GnRH neurones adhere to the CAH domain of RPTPβ, and this adhesiveness is blocked when contactin GPI anchoring is disrupted or contactin binding capacity is immunoneutralised, suggesting that astrocytic RPTPβ interacts with neuronal contactin to mediate glial-GnRH neurone adhesiveness. Because the abundance of short RPTPβ mRNA increases in the female mouse hypothalamus (but not in the cerebral cortex) before puberty, it appears that an increased interaction between GnRH axons and astrocytes mediated by RPTPβ-contactin is a dynamic mechanism of neurone-glia communication during female sexual development.",
keywords = "Adhesion molecules, Astrocytes, GnRH neurones, Hypothalamus",
author = "Parent, {A. S.} and Mungenast, {A. E.} and Alejandro Lomniczi and Sandau, {U. S.} and E. Peles and Bosch, {M. A.} and Oline Ronnekleiv and Sergio Ojeda",
year = "2007",
month = "11",
doi = "10.1111/j.1365-2826.2007.01597.x",
language = "English (US)",
volume = "19",
pages = "847--858",
journal = "Journal of Neuroendocrinology",
issn = "0953-8194",
publisher = "Wiley-Blackwell",
number = "11",

}

TY - JOUR

T1 - A contactin-receptor-like protein tyrosine phosphatase β complex mediates adhesive communication between astroglial cells and gonadotrophin-releasing hormone neurones

AU - Parent, A. S.

AU - Mungenast, A. E.

AU - Lomniczi, Alejandro

AU - Sandau, U. S.

AU - Peles, E.

AU - Bosch, M. A.

AU - Ronnekleiv, Oline

AU - Ojeda, Sergio

PY - 2007/11

Y1 - 2007/11

N2 - Although it is well established that gonadotrophin-releasing hormone (GnRH) neurones and astrocytes maintain an intimate contact throughout development and adult life, the cell-surface molecules that may contribute to this adhesiveness remain largely unknown. In the peripheral nervous system, the glycosylphosphatidyl inositol (GPI)-anchored protein contactin is a cell-surface neuronal protein required for axonal-glial adhesiveness. A glial transmembrane protein recognised by neuronal contactin is receptor-like protein tyrosine phosphatase β (RPTPβ), a phosphatase with structural similarities to cell adhesion molecules. In the present study, we show that contactin, and its preferred in cis partner Caspr1, are expressed in GnRH neurones. We also show that the RPTPβ mRNA predominantly expressed in hypothalamic astrocytes encodes an RPTPβ isoform (short RPTPβ) that uses its carbonic anhydrase (CAH) extracellular subdomain to interact with neuronal contactin. Immunoreactive contactin is most abundant in GnRH nerve terminals projecting to both the organum vasculosum of the lamina terminalis and median eminence, implying GnRH axons as an important site of contactin-dependent cell adhesiveness. GT1-7 immortalised GnRH neurones adhere to the CAH domain of RPTPβ, and this adhesiveness is blocked when contactin GPI anchoring is disrupted or contactin binding capacity is immunoneutralised, suggesting that astrocytic RPTPβ interacts with neuronal contactin to mediate glial-GnRH neurone adhesiveness. Because the abundance of short RPTPβ mRNA increases in the female mouse hypothalamus (but not in the cerebral cortex) before puberty, it appears that an increased interaction between GnRH axons and astrocytes mediated by RPTPβ-contactin is a dynamic mechanism of neurone-glia communication during female sexual development.

AB - Although it is well established that gonadotrophin-releasing hormone (GnRH) neurones and astrocytes maintain an intimate contact throughout development and adult life, the cell-surface molecules that may contribute to this adhesiveness remain largely unknown. In the peripheral nervous system, the glycosylphosphatidyl inositol (GPI)-anchored protein contactin is a cell-surface neuronal protein required for axonal-glial adhesiveness. A glial transmembrane protein recognised by neuronal contactin is receptor-like protein tyrosine phosphatase β (RPTPβ), a phosphatase with structural similarities to cell adhesion molecules. In the present study, we show that contactin, and its preferred in cis partner Caspr1, are expressed in GnRH neurones. We also show that the RPTPβ mRNA predominantly expressed in hypothalamic astrocytes encodes an RPTPβ isoform (short RPTPβ) that uses its carbonic anhydrase (CAH) extracellular subdomain to interact with neuronal contactin. Immunoreactive contactin is most abundant in GnRH nerve terminals projecting to both the organum vasculosum of the lamina terminalis and median eminence, implying GnRH axons as an important site of contactin-dependent cell adhesiveness. GT1-7 immortalised GnRH neurones adhere to the CAH domain of RPTPβ, and this adhesiveness is blocked when contactin GPI anchoring is disrupted or contactin binding capacity is immunoneutralised, suggesting that astrocytic RPTPβ interacts with neuronal contactin to mediate glial-GnRH neurone adhesiveness. Because the abundance of short RPTPβ mRNA increases in the female mouse hypothalamus (but not in the cerebral cortex) before puberty, it appears that an increased interaction between GnRH axons and astrocytes mediated by RPTPβ-contactin is a dynamic mechanism of neurone-glia communication during female sexual development.

KW - Adhesion molecules

KW - Astrocytes

KW - GnRH neurones

KW - Hypothalamus

UR - http://www.scopus.com/inward/record.url?scp=35048889059&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=35048889059&partnerID=8YFLogxK

U2 - 10.1111/j.1365-2826.2007.01597.x

DO - 10.1111/j.1365-2826.2007.01597.x

M3 - Article

C2 - 17927663

AN - SCOPUS:35048889059

VL - 19

SP - 847

EP - 858

JO - Journal of Neuroendocrinology

JF - Journal of Neuroendocrinology

SN - 0953-8194

IS - 11

ER -