Human monoclonal antibodies to myelin-associated glycoprotein are directed against the polypeptide and not the carbohydrate moiety

Murray, Norman; Steck, Andreas; Page, Nicole; Perruisseau, Geneviève

doi:10.1016/s0165-5728(84)80003-x

Cited by 8 publications

(3 citation statements)

References 16 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The HNKl antibody was generated to a human lymphoblastoma and is used to identify a subset of human lymphocytes with natural killer activity (Abo and Balch, 1981). The demonstration that it also reacts with the myelin associated glycoprotein (McGany et al, 1983;Murray et al, 1984;Sat0 et al, 1985) revealed that it identifies an antigen shared by the immune system and the nervous system. Subsequent studies showed that the epitope recognized by HNKl and related antibodies was in the carbohydrate moieties of MAG, some glycolipids, and several other glycoproteins of the nervous system implicated in cell adhesion, including neural cell adhesion molecule (N-CAM) (Ilyas et al, 1984;Inuzuka et al, 1984;Kruse et al, 1984Kruse et al, , 1985Nobile-Orazio et al, 1984;Noronha et al, 1986).…”

Section: Discussionmentioning

confidence: 99%

Immunoreactivity of PMP‐22, P0, and other 19 to 28 kDa glycoprotens in peripheral nerve myelin of mammals and fish with HNK1 and related antibodies

Hammer

O’Shannessy

León³

et al. 1993

J of Neuroscience Research

View full text Add to dashboard Cite

Mammalian peripheral nervous system (PNS) myelin contains several glycoproteins with molecular weights of 19 to 28 kDa, including the major 28 kDa P0 glycoprotein and a recently cloned protein called PMP-22. Some glycoproteins in this M(r) range in humans, cats and some other mammals react with HNK1, a mouse monoclonal antibody that identifies a carbohydrate epitope shared between the immune system and a number of adhesion proteins in the nervous system. A variety of antibodies to P0, PMP-22, and the carbohydrate determinants reacting with HNK1 were used to characterize immunochemically these 19 to 28 kDa glycoproteins of cat PNS myelin. The HNK1-reactive components include P0 and two slightly smaller 23 to 26 kDa proteins that are immunologically related to P0. However, HNK1 reacts most strongly with a lower molecular weight glycoprotein that does not react with the antibodies to P0 and was identified as PMP-22. Since the carbohydrate structure reacting with HNK1 is generally expressed on adhesion molecules, this result suggests that PMP-22 may function in cell-cell or membrane-membrane interactions. Furthermore, the related human anti-MAG monoclonal IgM antibodies from patients with neuropathy also react strongly with PMP-22, suggesting that it may be a target antigen in the pathogenesis of this disease. Purified PNS and CNS myelin from bony fish (toadfish and trout) were also shown to contain major glycoproteins, in the same 19 to 28 kDa M(r) range, that react very strongly with HNK1. It is shown that fish myelin has major proteins of this size that are immunologically and structurally related to mammalian P0, and it is demonstrated here that one of the strongly HNK1-positive proteins reacted well with an antiserum raised to bovine P0. The presence of high levels of the adhesion-related HNK1 epitope on these major myelin proteins of fish suggests that this carbohydrate structure may have played a role in the molecular evolution of myelin.

show abstract

Section: Discussionmentioning

confidence: 99%

Immunoreactivity of PMP‐22, P0, and other 19 to 28 kDa glycoprotens in peripheral nerve myelin of mammals and fish with HNK1 and related antibodies

Hammer

O’Shannessy

León³

et al. 1993

J of Neuroscience Research

View full text Add to dashboard Cite

show abstract

“…This evidence is derived from experiments showing that M A G deglycosylated in solution with trifluoromethane-sulphonic acid reacts with antibodies directed against the polypeptide but not with the human IgM antibodies [8]. However, using a different approach, we were unable to confirm these results [18], perhaps because deglycosylation was incomplete.…”

Section: Monoclonal Antibodies To Magmentioning

confidence: 76%

Monoclonal antibodies to myelin-associated glycoprotein reveal antigenic structures and suggest pathogenic mechanisms

Steck

Murray

1985

Springer Semin Immunopathol

Self Cite

View full text Add to dashboard Cite

“…Anti-HNK-1 has been thought to be one of the markers of human natural killer (NK) cells (20). In patients with anti-MAG M proteinernia and polyneuropathy, although there has been a report of a marked decrease in the number of circulating HNK-1-positive cells (27), no reports have appeared on the NK activity in peripheral blood. In addition, we have reported that rabbit polyclonal anti-MAG antiserum has stained approximately 9% of mononuclear cells in human peripheral blood (23) and a dual-color immunofluorescence study revealed that most MAG-positive cells were also stained with anti-HNK-1 (24).…”

Section: Discussionmentioning

confidence: 99%

Anti-myelin-associated glycoprotein antibody in sera from patients with demyelinating diseases

Sato¹,

Baba²,

Ishii³

et al. 1986

Acta Neurologica Scandinavica

View full text Add to dashboard Cite

An enzyme-linked immunosorbent assay (ELISA) was developed for quantitating anti-myelin-associated glycoprotein (MAG) IgM antibody in human sera. Absorbance values of anti-MAG antibody were higher than 0.2 at 1:80 of serum dilution in sera from some patients with demyelinating diseases of the central or peripheral nervous systems including multiple sclerosis, subacute sclerosing panencephalitis, Guillain-Barré syndrome, chronic relapsing polyradiculoneuritis and carcinomatous polyneuropathy and also some patients with autoimmune diseases such as collagen diseases and myasthenia gravis. However, absorbance values of anti-MAG antibody in sera from control individuals and patients with some other neurological diseases were less than 0.2 and considered as negative. Because of the reported existence of a cross antigenicity between MAG and lymphocyte, and especially natural killer cells, the possibility of the functional importance of anti-MAG antibody on cellular immunity is discussed with particular reference to the demyelinating diseases.

show abstract

Human monoclonal antibodies to myelin-associated glycoprotein are directed against the polypeptide and not the carbohydrate moiety

Cited by 8 publications

References 16 publications

Immunoreactivity of PMP‐22, P0, and other 19 to 28 kDa glycoprotens in peripheral nerve myelin of mammals and fish with HNK1 and related antibodies

Immunoreactivity of PMP‐22, P0, and other 19 to 28 kDa glycoprotens in peripheral nerve myelin of mammals and fish with HNK1 and related antibodies

Monoclonal antibodies to myelin-associated glycoprotein reveal antigenic structures and suggest pathogenic mechanisms

Anti-myelin-associated glycoprotein antibody in sera from patients with demyelinating diseases

Contact Info

Product

Resources

About