The non-receptor tyrosine kinase Lyn is localised in the developing murine blood-brain barrier

M. G. Achen, Matthias Clauss, H. Schnurch, W. Risau

Research output: Contribution to journalArticle

24 Citations (Scopus)

Abstract

The blood-brain barrier, formed by brain endothelium, is critical for brain function. The development of the blood-brain barrier involves brain angiogenesis and endothelial cell differentiation, processes which require active signal transduction pathways. The differentiation of brain endothelial cells to the 'blood-brain-barrier phenotype' involves cytoskeletal changes which modulate the tightness of the barrier. In order to identify signal transduction proteins involved in blood-brain barrier development, cDNA from bovine and murine brain endothelial cells was used in a polymerase chain reaction for cloning of DNA encoding Src homology 3 domains. Src homology 3 domains are structural domains found in many signal transduction proteins. These domains often mediate interaction of signaling proteins with the cytoskeleton and therefore may play a role in the regulation of the cytoskeletal changes which occur during blood-brain-barrier development. Unexpectedly, all bovine and murine clones analyzed from polymerase chain reactions encoded the Src homology 3 domain of one protein, namely the non-receptor tyrosine kinase, Lyn, which is involved in signal transduction in cells of the hemopoietic system. In situ hybridization analyses confirmed the presence of lyn mRNA in developing blood vessels in embryonic and early post-natal mouse brain, but not in endothelium outside the brain. In bovine brain endothelial cells in primary culture, p53(lyn) is highly abundant and present in two forms which have different patterns of tyrosine phosphorylation. These data suggest that Lyn may be involved in transduction of growth and differentiation signals required for blood-brain-barrier development.

Original languageEnglish (US)
Pages (from-to)15-24
Number of pages10
JournalDifferentiation
Volume59
Issue number1
DOIs
StatePublished - 1995
Externally publishedYes

Fingerprint

Blood-Brain Barrier
Protein-Tyrosine Kinases
Brain
src Homology Domains
Signal Transduction
Endothelial Cells
Endothelium
Proteins
Polymerase Chain Reaction
Cytoskeleton
In Situ Hybridization
Blood Vessels
Tyrosine
Organism Cloning
Cell Differentiation
Complementary DNA
Clone Cells
Phosphorylation
Phenotype
Messenger RNA

ASJC Scopus subject areas

  • Pathology and Forensic Medicine
  • Developmental Biology
  • Cell Biology

Cite this

The non-receptor tyrosine kinase Lyn is localised in the developing murine blood-brain barrier. / Achen, M. G.; Clauss, Matthias; Schnurch, H.; Risau, W.

In: Differentiation, Vol. 59, No. 1, 1995, p. 15-24.

Research output: Contribution to journalArticle

@article{ca446b8b4a9c45bbaf407941152e2da6,
title = "The non-receptor tyrosine kinase Lyn is localised in the developing murine blood-brain barrier",
abstract = "The blood-brain barrier, formed by brain endothelium, is critical for brain function. The development of the blood-brain barrier involves brain angiogenesis and endothelial cell differentiation, processes which require active signal transduction pathways. The differentiation of brain endothelial cells to the 'blood-brain-barrier phenotype' involves cytoskeletal changes which modulate the tightness of the barrier. In order to identify signal transduction proteins involved in blood-brain barrier development, cDNA from bovine and murine brain endothelial cells was used in a polymerase chain reaction for cloning of DNA encoding Src homology 3 domains. Src homology 3 domains are structural domains found in many signal transduction proteins. These domains often mediate interaction of signaling proteins with the cytoskeleton and therefore may play a role in the regulation of the cytoskeletal changes which occur during blood-brain-barrier development. Unexpectedly, all bovine and murine clones analyzed from polymerase chain reactions encoded the Src homology 3 domain of one protein, namely the non-receptor tyrosine kinase, Lyn, which is involved in signal transduction in cells of the hemopoietic system. In situ hybridization analyses confirmed the presence of lyn mRNA in developing blood vessels in embryonic and early post-natal mouse brain, but not in endothelium outside the brain. In bovine brain endothelial cells in primary culture, p53(lyn) is highly abundant and present in two forms which have different patterns of tyrosine phosphorylation. These data suggest that Lyn may be involved in transduction of growth and differentiation signals required for blood-brain-barrier development.",
author = "Achen, {M. G.} and Matthias Clauss and H. Schnurch and W. Risau",
year = "1995",
doi = "10.1046/j.1432-0436.1995.5910015.x",
language = "English (US)",
volume = "59",
pages = "15--24",
journal = "Differentiation",
issn = "0301-4681",
publisher = "Elsevier BV",
number = "1",

}

TY - JOUR

T1 - The non-receptor tyrosine kinase Lyn is localised in the developing murine blood-brain barrier

AU - Achen, M. G.

AU - Clauss, Matthias

AU - Schnurch, H.

AU - Risau, W.

PY - 1995

Y1 - 1995

N2 - The blood-brain barrier, formed by brain endothelium, is critical for brain function. The development of the blood-brain barrier involves brain angiogenesis and endothelial cell differentiation, processes which require active signal transduction pathways. The differentiation of brain endothelial cells to the 'blood-brain-barrier phenotype' involves cytoskeletal changes which modulate the tightness of the barrier. In order to identify signal transduction proteins involved in blood-brain barrier development, cDNA from bovine and murine brain endothelial cells was used in a polymerase chain reaction for cloning of DNA encoding Src homology 3 domains. Src homology 3 domains are structural domains found in many signal transduction proteins. These domains often mediate interaction of signaling proteins with the cytoskeleton and therefore may play a role in the regulation of the cytoskeletal changes which occur during blood-brain-barrier development. Unexpectedly, all bovine and murine clones analyzed from polymerase chain reactions encoded the Src homology 3 domain of one protein, namely the non-receptor tyrosine kinase, Lyn, which is involved in signal transduction in cells of the hemopoietic system. In situ hybridization analyses confirmed the presence of lyn mRNA in developing blood vessels in embryonic and early post-natal mouse brain, but not in endothelium outside the brain. In bovine brain endothelial cells in primary culture, p53(lyn) is highly abundant and present in two forms which have different patterns of tyrosine phosphorylation. These data suggest that Lyn may be involved in transduction of growth and differentiation signals required for blood-brain-barrier development.

AB - The blood-brain barrier, formed by brain endothelium, is critical for brain function. The development of the blood-brain barrier involves brain angiogenesis and endothelial cell differentiation, processes which require active signal transduction pathways. The differentiation of brain endothelial cells to the 'blood-brain-barrier phenotype' involves cytoskeletal changes which modulate the tightness of the barrier. In order to identify signal transduction proteins involved in blood-brain barrier development, cDNA from bovine and murine brain endothelial cells was used in a polymerase chain reaction for cloning of DNA encoding Src homology 3 domains. Src homology 3 domains are structural domains found in many signal transduction proteins. These domains often mediate interaction of signaling proteins with the cytoskeleton and therefore may play a role in the regulation of the cytoskeletal changes which occur during blood-brain-barrier development. Unexpectedly, all bovine and murine clones analyzed from polymerase chain reactions encoded the Src homology 3 domain of one protein, namely the non-receptor tyrosine kinase, Lyn, which is involved in signal transduction in cells of the hemopoietic system. In situ hybridization analyses confirmed the presence of lyn mRNA in developing blood vessels in embryonic and early post-natal mouse brain, but not in endothelium outside the brain. In bovine brain endothelial cells in primary culture, p53(lyn) is highly abundant and present in two forms which have different patterns of tyrosine phosphorylation. These data suggest that Lyn may be involved in transduction of growth and differentiation signals required for blood-brain-barrier development.

UR - http://www.scopus.com/inward/record.url?scp=0029145620&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0029145620&partnerID=8YFLogxK

U2 - 10.1046/j.1432-0436.1995.5910015.x

DO - 10.1046/j.1432-0436.1995.5910015.x

M3 - Article

C2 - 7589891

AN - SCOPUS:0029145620

VL - 59

SP - 15

EP - 24

JO - Differentiation

JF - Differentiation

SN - 0301-4681

IS - 1

ER -