Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P56851 (epididymal)
 11,273 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Previous studies of experimental diabetes have demonstrated changes in the levels of specific salivary proteins. The present study is part of a larger effort aimed at elucidating the mechanism(s) by which insulin regulates salivary protein expression in the rat parotid gland. Diabetes was induced in 2-3-month-old male Fischer 344 rats by injection of streptozotocin (STZ). After 30 days one group of rats was given insulin for 7 days. Untreated rats served as controls. As previously observed, parotid acinar cells from diabetic rats accumulated lipid and contained occasional crystalloid lysosomes. Quantitative immunogold labeling of secretory granules in diabetic glands revealed decreases of 30-60% for proline-rich-proteins (PRPs), amylase and parotid secretory protein (PSP), but labeling for acidic epididymal glycoprotein (AEG) was unchanged. The response to insulin treatment was variable: amylase and PSP labeling were partly restored, but PRP and AEG labeling showed little change. Photoaffinity labeling of cyclic AMP receptor proteins (cARP) showed changes in several tissues including a consistent increase in the diabetic parotid gland. Immunogold labeling of secretory granules with antibody to cARP was similar in control and diabetic parotids, but nuclear and cytoplasmic label was decreased in diabetic acinar cells. These results indicate that STZ-diabetes and insulin reconstitution cause variable changes in the expression of parotid secretory proteins. Changes in cARP levels suggest that the insulin and cyclic AMP pathways may interact in regulating expression of salivary secretory proteins.
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PMID:Expression and distribution of parotid secretory proteins in experimental diabetes. 982 30

Cysteine-rich secretory proteins (CRISPs) represent a family of evolutionarily conserved proteins which may play a role in the innate immune system and are transcriptionally regulated by androgens in several tissues. Transcripts for all three members of the CRISP family have now been identified in the murine lacrimal gland. RT-PCR using primers able to discriminate between the related CRISP forms allowed the amplification of fragments with the expected length. DNA sequencing revealed a complete identity with the hitherto characterized epididymal CRISP-1, testicular CRISP-2, and salivary gland CRISP-3. An analysis of several mouse strains indicated that all expressed the three CRISP forms, but in differing amounts. RT-PCR analysis of RNA isolated from acinar cells of lacrimal glands revealed that they expressed CRISP-1 and CRISP-2. Semiquantitative and quantitative analyses furthermore showed higher CRISP-1 and CRISP-3 mRNA levels in the lacrimal glands of male BALB/c and NOD mice when compared to females. Testosterone treatment of C3H/HeJ female mice was followed by an upregulation of the steady-state CRISP-1 but not CRISP-2 transcript levels. A comparable stimulation was observed for the mRNAs coding for parotid secretory protein (PSP), a factor previously shown to exhibit sexual dimorphism in the murine lacrimal gland. The expression of CRISP transcripts in the lacrimal gland is consistent with a function in the innate immune system.
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PMID:Expression of transcripts for cysteine-rich secretory proteins (CRISPs) in the murine lacrimal gland. 998 83