Publication: Use of lectin-probes for correlative
histochemical and biochemical assessments
of the glycosylation patterns of secretory proteins,
including kallikreins, in salivary glands and saliva
Authors
Garrett, J.R. ; Proctor, G.B. ; Zhang, X.S. ; Shori, D.K. ; Schulte, B.A.
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Publisher
Murcia : F. Hernández
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DOI
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info:eu-repo/semantics/article
Description
Abstract
Labelled lectins were used as probes to study
the glycosylation and secretion of submandibular
glycoproteins not only in sections of fixed glands but
also in glandular extracts and in nerve-induced saliva,
after electrophoretic separations and immobilization in
nitrocellulose membranes.
In cats the glycoproteins in sympathetic saliva
differed considerably from those in parasympathetic
saliva. In sympathetic saliva they were found to
originate mainly from striated ducts, to some extent from
demilunar cells and to a small extent from acinar cells,
whereas in parasympathetic saliva they arose mainly
from acinar-cells añd demilunes and only to a small
extent from striated ducts.
In rat submandibular glands sympathetic stimulation
caused extensive depletion of lectin stainable granules
from granular tubules. Corresponding strong binding
occurred with the same lectins to constituents in saliva
that ran between 25 and 35 kD on SDS gel electrophoresis
and were shown to contain tissue kallikreins.
Their binding patterns suggested that individual
kallikreins from the same gland may be glycosylated in
different ways. This possibility was tested on five
different kallikreins after separation from submandibular
extracts by isoelectric focussing. Lectin bindings on slot
blot preparations of these kallikreins were tested before
and after N-glycosidase F, sialidase or endo-a-Nacetylgalactosaminidase
digestions. Results showed that,
despite their close genetic and structural similarities, the
kallikreins are in fact differently sialylated and
fucosylated and the novel finding that some contain Oglycosidically
linked side chains as well as the
anticipated N-glycosidically linked side chains was
revealed.
Thus, correlative histochemical and biochemical
Offprint requests to: Professor J.R. Garrett, Secretory and Soft Tissue
Research Unit, Department of Oral Pathology, The Rayne Institute,
KCSMD, 123 Coldharbour Lane, London, SE5 9NU, England
assessments of bindings with lectin probes has provided
important new information about differences in the
glycosylation pattems of individual glycoproteins stored
within the same secretory granules.
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