Basic proline-rich proteins of murine parotid glands. Induction of mRNA by isoprenaline and post-secretion processing
Basic proline-rich proteins of murine parotid glands. Induction of mRNA by isoprenaline and post-secretion processing
Five major basic polypeptides with characteristics typical of proline-rich proteins, accumulated in parotid glands after long term isoprenaline treatment of Balb C mice. They were studied by two-dimensional gel electrophoresis and designated B1 degree, B2' degrees, B2 degrees, B3 degrees and B4 degrees on the basis of pI-dependent mobility. They were not observed in the glands of normal mice and were precipitated when glands were homogenized in 10% trichloroacetic acid unlike the three isoprenaline-induced proline-rich proteins of murine parotid glands reported previously. Isoprenaline induced six proline-rich in vitro translation products which were absent normally. Four of these species had pI-dependent mobilities almost identical to B1 degree, B2 degrees, B3 degrees and B4 degrees, indicating not only precursor/product relationships, but also that isoprenaline induced the accumulation of the proteins by regulating the mRNA. Identical salivary counterparts of the basic glandular proline-rich proteins were not detected whereas a series of smaller and more basic isoprenaline-induced polypeptides were observed in saliva (major speices B1s-B4s). The glandular proline-rich proteins were secreted from parotid tissue in vitro and the data indicate that proline-rich proteins are synthesised as precursors and processed into salivary form in the parotid glands after secretion. The relationships between the B-type in vitro translation products, parotid gland precursors and salivary proteins were also confirmed immunologically.
Animals Electrophoresis, Gel, Two-Dimensional Electrophoresis, Polyacrylamide Gel Isoproterenol/*pharmacology Male Mice Mice, Inbred BALB C Molecular Weight Parotid Gland/drug effects/*metabolism Peptide Biosynthesis Peptides/*genetics/isolation & purification Phosphoproteins/*genetics Proline-Rich Protein Domains *RNA Processing, Post-Transcriptional RNA, Messenger/biosynthesis/drug effects/*genetics Reference Values Saliva/analysis Transcription, Genetic/*drug effects
371-379
Bannister, A. J.
10690686-0eb6-4f35-81ad-d8e9a5859430
Divecha, N.
5c2ad0f8-4ce7-405f-8a15-2fc4ab96d787
Ashmore, M.
b802743a-7501-4982-bdc5-4c08b65034aa
McDonald, C. J.
fd9f9d68-ad7a-4e82-a88d-a2dbc623ce91
1989
Bannister, A. J.
10690686-0eb6-4f35-81ad-d8e9a5859430
Divecha, N.
5c2ad0f8-4ce7-405f-8a15-2fc4ab96d787
Ashmore, M.
b802743a-7501-4982-bdc5-4c08b65034aa
McDonald, C. J.
fd9f9d68-ad7a-4e82-a88d-a2dbc623ce91
Bannister, A. J., Divecha, N., Ashmore, M. and McDonald, C. J.
(1989)
Basic proline-rich proteins of murine parotid glands. Induction of mRNA by isoprenaline and post-secretion processing.
European Journal of Biochemistry, 181 (2), .
(doi:10.1111/j.1432-1033.1989.tb14734.x).
Abstract
Five major basic polypeptides with characteristics typical of proline-rich proteins, accumulated in parotid glands after long term isoprenaline treatment of Balb C mice. They were studied by two-dimensional gel electrophoresis and designated B1 degree, B2' degrees, B2 degrees, B3 degrees and B4 degrees on the basis of pI-dependent mobility. They were not observed in the glands of normal mice and were precipitated when glands were homogenized in 10% trichloroacetic acid unlike the three isoprenaline-induced proline-rich proteins of murine parotid glands reported previously. Isoprenaline induced six proline-rich in vitro translation products which were absent normally. Four of these species had pI-dependent mobilities almost identical to B1 degree, B2 degrees, B3 degrees and B4 degrees, indicating not only precursor/product relationships, but also that isoprenaline induced the accumulation of the proteins by regulating the mRNA. Identical salivary counterparts of the basic glandular proline-rich proteins were not detected whereas a series of smaller and more basic isoprenaline-induced polypeptides were observed in saliva (major speices B1s-B4s). The glandular proline-rich proteins were secreted from parotid tissue in vitro and the data indicate that proline-rich proteins are synthesised as precursors and processed into salivary form in the parotid glands after secretion. The relationships between the B-type in vitro translation products, parotid gland precursors and salivary proteins were also confirmed immunologically.
This record has no associated files available for download.
More information
Published date: 1989
Keywords:
Animals Electrophoresis, Gel, Two-Dimensional Electrophoresis, Polyacrylamide Gel Isoproterenol/*pharmacology Male Mice Mice, Inbred BALB C Molecular Weight Parotid Gland/drug effects/*metabolism Peptide Biosynthesis Peptides/*genetics/isolation & purification Phosphoproteins/*genetics Proline-Rich Protein Domains *RNA Processing, Post-Transcriptional RNA, Messenger/biosynthesis/drug effects/*genetics Reference Values Saliva/analysis Transcription, Genetic/*drug effects
Identifiers
Local EPrints ID: 479393
URI: http://eprints.soton.ac.uk/id/eprint/479393
ISSN: 0014-2956
PURE UUID: db45440e-8a8d-439f-82d6-040fb8f7e979
Catalogue record
Date deposited: 20 Jul 2023 17:41
Last modified: 17 Mar 2024 02:59
Export record
Altmetrics
Contributors
Author:
A. J. Bannister
Author:
M. Ashmore
Author:
C. J. McDonald
Download statistics
Downloads from ePrints over the past year. Other digital versions may also be available to download e.g. from the publisher's website.
View more statistics