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Heparan Sulfate Heterogeneity in Skeletal Muscle Basal Lamina:
Demonstration by Phage Display-Derived Antibodies
Guido J.
Jenniskens,
Arie
Oosterhof,
Ricardo
Brandwijk,
Jacques H.
Veerkamp, and
Toin H.
van Kuppevelt
Department of Biochemistry, Faculty of Medical Sciences, University
of Nijmegen, 6500 HB Nijmegen, The Netherlands
The basal lamina (BL) enveloping skeletal muscle fibers contains
different glycoproteins, including proteoglycans. To obtain more
information on the glycosaminoglycan moiety of proteoglycans, we have
selected a panel of anti-heparan sulfate (HS) antibodies from a
semisynthetic antibody phage display library by panning against
glycosaminoglycan preparations derived from skeletal muscle. Epitope
recognition by the antibodies is strongly dependent on O- and N-sulfation of the heparan
sulfate. Immunostaining with these antibodies showed a distinct
distribution of heparan sulfate epitopes in muscle basal lamina of
various species. Clear differences in staining intensity were observed
between neural, synaptic, and extrasynaptic basal laminae. Moreover,
temporal and regional changes in abundancy of heparan sulfate epitopes
were observed during muscle development both in vitro
and in vivo. Taken together, these data suggest a role
for specific heparan sulfate domains/species in myogenesis and
synaptogenesis. Detailed analysis of the functions of heparan sulfate
epitopes in muscle morphogenesis has now become feasible with the
isolation of antibodies specific for distinct heparan sulfate epitopes.
Key words:
heparan sulfate proteoglycan; glycosaminoglycan; basal
lamina; neuromuscular junction; myogenesis; synaptogenesis
Copyright © 2000 Society for Neuroscience 0270-6474/00/20114099-13$05.00/0
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