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High Expression of the HNK‐1/L2 Carbohydrate Epitope in the Major Glycoproteins of Shark Myelin
Author(s) -
Zand Dina,
Hammer Jeffrey,
Gould Robert,
Quarles Richard
Publication year - 1991
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1991.tb08260.x
Subject(s) - myelin associated glycoprotein , epitope , glycoprotein , myelin , polyclonal antibodies , monoclonal antibody , antiserum , biochemistry , biology , myelin basic protein , microbiology and biotechnology , chemistry , antibody , immunology , central nervous system , endocrinology
The major 24‐ and 28‐kDa glycoproteins in shark PNS and CNS myelin express high levels of the adhesion‐associated HNK‐1/L2 carbohydrate epitope. The 28‐kDa protein, but not the 24‐kDa protein, cross‐reacts strongly with one of two anti‐bovine P O antisera not previously tested against fish myelin proteins. Shark PNS and CNS myelin also contains smaller amounts of high‐molecular‐weight HNK‐1‐positive proteins, including a prominent broad band in the 65–85‐kDa range. Although myelin‐associated glycoprotein (MAG) is well known to react with HNK‐1 in some mammals, monoclonal and polyclonal anti‐MAG antibodies did not react with the high‐molecular‐weight HNK‐1‐positive material in shark myelin, a result suggesting that it is not a MAG‐like protein. The high expression of the HNK‐1/L2 epitope in glycoproteins of shark myelin, including the major P o ‐related ones, suggests that this adhesion‐related carbohydrate structure may have had an important role in the molecular evolution of the myelinating process.