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Central nervous system-specific glycosylation of the type A natriuretic peptide receptor.
- Muller D, Middendorff R, Olcese J, Mukhopadhyay AK
Endocrinology. 2002 Jan;143(1):23-9.
Physiological effects of atrial natriuretic peptide
(ANP) are thought to be mediated by binding
to and activation
of a widely expressed membrane receptor,
termed guanylyl cyclase (GC)-A. During comparative analyses of ANP receptor
expression in various rat and bovine
tissues, by UV
light-induced affinity cross-linking to (125)I-ANP, we uncovered a size heterogeneity
of GC-A, detectable as a 130-kDa protein
in peripheral
and as a 122-kDa protein
in central nervous system
tissues. This heterogeneity
could be explained by differences in N-linked glycosylation,
because treatments with N-glycosidase F
reduced the apparent molecular weights of both receptor
variants to the same value of 116,000. As judged by displacement experiments, the two receptor
glycoforms did not differ in their binding
affinities for natriuretic
peptides.
Assessments of GC activities did not reveal any difference in ANP-induced generation of the second messenger,
cyclic GMP.
The examination of GC-A expression in brain during ontogeny
revealed an alteration of the apparent molecular mass during early postnatal
development from the 130-kDa to the 122-kDa form, suggesting a change in oligosaccharide
processing. This study provides a reliable method for characterizing GC-A expression and identifies, for the first time, a differential
glycosylation
of this receptor
in vivo.
This abstract at PubMed.