Galectin-1 is a component of neurofilamentous lesions in sporadic and familial amyotrophic lateral sclerosis

Takeo Kato, Keiji Kurita, Tomomi Seino, Manabu Wada, Toru Kawanami, Makoto Daimon, Toshihiko Kadoya, Hidenori Horie, Asao Hirano

Research output: Contribution to journalArticlepeer-review

32 Scopus citations

Abstract

In amyotrophic lateral sclerosis (ALS), abnormal accumulation of neurofilaments induces pathological changes such as axonal spheroids, cord-like neurite swellings, and perikaryal conglomerate inclusions in degenerating motor neurons of the spinal cord, and the accumulation seems to cause motor neuron degeneration in this disease. Such ALS lesions were intensely labeled with HepSS-1, a monoclonal antibody to heparan sulfate. Since the identification of HepSS-1-immunoreactive substance seems to be an important step for understanding the molecular pathology of ALS, we purified the substance from human spinal cord tissue to homogeneity. Amino acid sequence of the protein was consistent with that of galectin-1. Immunohistochemistry using antibodies against recombinant human galectin-1 showed that galectin-1 was accumulated in these lesions in ALS. Although HepSS-1 was believed to be specific for heparan sulfate, it reacted with recombinant human galectin-1 which has no heparan sulfate moiety. The results show that galectin-1 is a component of the neurofilamentous lesions in ALS. Since galectin-1 has axonal regeneration-enhancing activity, the abnormal accumulation of galectin-1 to the lesions seems to be related to the pathological process of ALS.

Original languageEnglish (US)
Pages (from-to)166-172
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume282
Issue number1
DOIs
StatePublished - 2001

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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