Phylogenetic conservation of the cell-type-specific Lan3-2 glycoepitope in Caenorhabditis elegans

Harper C. Vansteenhouse, Zachary A. Horton, Robert O'Hagan, Mei Hui Tai, Birgit Zipser

Research output: Contribution to journalArticleResearchpeer-review

Abstract

The biological function of a cell-type-specific glycosylation of an adhesion molecule belonging to the L1CAM immunoglobulin superfamily was previously determined in the nervous system of the embryonic leech, Hirudo medicinalis. The Lan3-2 glycoepitope is a surface marker of sensory afferent neurons and is required for their appropriate developmental collateral branching and synaptogenesis in the CNS. The chemical structure of the Lan3-2 glycoepitope consists of β-(1,4)-linked mannopyranose. Here, we show the conservation of the cell-type-specific expression of this mannose polymer in Caenorhabditis elegans. The Lan3-2 glycoepitope is expressed on the cell surface of a subset of dissociated embryonic neurons and, in the adult worm, by the pharyngeal motor neuron, M5, and the chemosensory afferents, the amphids. Additionally, the vulval epithelium expresses the Lan3-2 glycoepitope in late L4 larvae and in adult hermaphrodites. To investigate proteins carrying this restrictively expressed glycoepitope, worm extract was immunoaffinity purified with Lan3-2 monoclonal antibody and Western blotted. A polyclonal antibody reactive with the cytoplasmic tail of LAD-1/SAX-7, a C. elegans member of the L1CAM family, recognizes a 270 kDa protein band while Lan3-2 antibody also recognizes a 190 kDa glycoform, its putative Lan3-2 ectodomain. Thus, in C. elegans, as in leech, the Lan3-2 epitope is located on a L1CAM homologue. The cell-type-specific expression of the Lan3-2 glycoepitope shared by leech and C. elegans will be useful for understanding how cell-type-specific glycoepitopes mediate cell-cell interactions during development.

Original languageEnglish
Pages (from-to)77-87
Number of pages11
JournalDevelopment Genes and Evolution
Volume220
Issue number3-4
DOIs
StatePublished - 1 Sep 2010

Fingerprint

Caenorhabditis elegans
Neural Cell Adhesion Molecule L1
Leeches
Mannose
Hirudo medicinalis
Afferent Neurons
Antibodies
Motor Neurons
Sensory Receptor Cells
Glycosylation
Cell Communication
Nervous System
Larva
Tail
Immunoglobulins
Epitopes
Polymers
Proteins
Epithelium
Monoclonal Antibodies

Keywords

  • Glycans
  • Glycomics
  • L1CAM
  • Leech
  • Mannose

Cite this

Vansteenhouse, Harper C. ; Horton, Zachary A. ; O'Hagan, Robert ; Tai, Mei Hui ; Zipser, Birgit. / Phylogenetic conservation of the cell-type-specific Lan3-2 glycoepitope in Caenorhabditis elegans. In: Development Genes and Evolution. 2010 ; Vol. 220, No. 3-4. pp. 77-87.
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abstract = "The biological function of a cell-type-specific glycosylation of an adhesion molecule belonging to the L1CAM immunoglobulin superfamily was previously determined in the nervous system of the embryonic leech, Hirudo medicinalis. The Lan3-2 glycoepitope is a surface marker of sensory afferent neurons and is required for their appropriate developmental collateral branching and synaptogenesis in the CNS. The chemical structure of the Lan3-2 glycoepitope consists of β-(1,4)-linked mannopyranose. Here, we show the conservation of the cell-type-specific expression of this mannose polymer in Caenorhabditis elegans. The Lan3-2 glycoepitope is expressed on the cell surface of a subset of dissociated embryonic neurons and, in the adult worm, by the pharyngeal motor neuron, M5, and the chemosensory afferents, the amphids. Additionally, the vulval epithelium expresses the Lan3-2 glycoepitope in late L4 larvae and in adult hermaphrodites. To investigate proteins carrying this restrictively expressed glycoepitope, worm extract was immunoaffinity purified with Lan3-2 monoclonal antibody and Western blotted. A polyclonal antibody reactive with the cytoplasmic tail of LAD-1/SAX-7, a C. elegans member of the L1CAM family, recognizes a 270 kDa protein band while Lan3-2 antibody also recognizes a 190 kDa glycoform, its putative Lan3-2 ectodomain. Thus, in C. elegans, as in leech, the Lan3-2 epitope is located on a L1CAM homologue. The cell-type-specific expression of the Lan3-2 glycoepitope shared by leech and C. elegans will be useful for understanding how cell-type-specific glycoepitopes mediate cell-cell interactions during development.",
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Phylogenetic conservation of the cell-type-specific Lan3-2 glycoepitope in Caenorhabditis elegans. / Vansteenhouse, Harper C.; Horton, Zachary A.; O'Hagan, Robert; Tai, Mei Hui; Zipser, Birgit.

In: Development Genes and Evolution, Vol. 220, No. 3-4, 01.09.2010, p. 77-87.

Research output: Contribution to journalArticleResearchpeer-review

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T1 - Phylogenetic conservation of the cell-type-specific Lan3-2 glycoepitope in Caenorhabditis elegans

AU - Vansteenhouse, Harper C.

AU - Horton, Zachary A.

AU - O'Hagan, Robert

AU - Tai, Mei Hui

AU - Zipser, Birgit

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AB - The biological function of a cell-type-specific glycosylation of an adhesion molecule belonging to the L1CAM immunoglobulin superfamily was previously determined in the nervous system of the embryonic leech, Hirudo medicinalis. The Lan3-2 glycoepitope is a surface marker of sensory afferent neurons and is required for their appropriate developmental collateral branching and synaptogenesis in the CNS. The chemical structure of the Lan3-2 glycoepitope consists of β-(1,4)-linked mannopyranose. Here, we show the conservation of the cell-type-specific expression of this mannose polymer in Caenorhabditis elegans. The Lan3-2 glycoepitope is expressed on the cell surface of a subset of dissociated embryonic neurons and, in the adult worm, by the pharyngeal motor neuron, M5, and the chemosensory afferents, the amphids. Additionally, the vulval epithelium expresses the Lan3-2 glycoepitope in late L4 larvae and in adult hermaphrodites. To investigate proteins carrying this restrictively expressed glycoepitope, worm extract was immunoaffinity purified with Lan3-2 monoclonal antibody and Western blotted. A polyclonal antibody reactive with the cytoplasmic tail of LAD-1/SAX-7, a C. elegans member of the L1CAM family, recognizes a 270 kDa protein band while Lan3-2 antibody also recognizes a 190 kDa glycoform, its putative Lan3-2 ectodomain. Thus, in C. elegans, as in leech, the Lan3-2 epitope is located on a L1CAM homologue. The cell-type-specific expression of the Lan3-2 glycoepitope shared by leech and C. elegans will be useful for understanding how cell-type-specific glycoepitopes mediate cell-cell interactions during development.

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