Expression and anti-bacterial activity of human parotid secretory protein (PSP)

2003 ◽  
Vol 31 (4) ◽  
pp. 815-818 ◽  
Author(s):  
C. Geetha ◽  
S.G. Venkatesh ◽  
B.H. Fasciotto Dunn ◽  
S.-U. Gorr
Keyword(s):  
Parotid Gland ◽  
Human Saliva ◽  
Secretory Protein ◽  
Bacterial Activity ◽  
Parotid Glands ◽  
Related Sequence ◽  
Human Parotid Gland ◽  
Bactericidal Effects ◽  
Parotid Secretory Protein ◽  
Rat Parotid

Parotid secretory protein (PSP) is an abundant protein in mouse and rat parotid glands. A related sequence (C20orf70) was identified on human chromosome 20. The goal of this study was to determine if PSP is expressed in the human parotid gland. The cDNA for human PSP was amplified from a human parotid cDNA sample. A peptide antibody, raised to the C-terminal peptide of PSP, identified the protein in human parotid tissue by immunofluorescence microscopy. Immunoaffinity chromatography suggested that PSP was expressed in human saliva. PSP is related to bactericidal/permeability-increasing protein (BPI). To test if PSP exhibits anti-bacterial activity, epitope-tagged PSP was expressed in rat GH4C1 cells. The secretion medium exhibited bacteristatic or bactericidal effects on Pseudomonas aeruginosa in a colony-forming assay when compared with secretion medium from GH4C1 cells that did not express PSP. These results suggest that PSP is expressed in the human parotid gland and saliva, where it functions as a BPI-like anti-bacterial protein.

scholarly journals Effects of Diabetes and Insulin on α-amylase Messenger RNA Levels in Rat Parotid Glands

1990 ◽  
Vol 69 (8) ◽  
pp. 1500-1504 ◽  
Author(s):  
S.K. Kim ◽  
L.M. Cuzzort ◽  
R.K. McKean ◽  
E.D. Allen
Keyword(s):  
Parotid Gland ◽  
Beta Cell ◽  
Messenger Rna ◽  
Secretory Protein ◽  
Diabetic Rats ◽  
Mrna Levels ◽  
Mrna Synthesis ◽  
Parotid Glands ◽  
Protein Levels ◽  
Rat Parotid

Previous studies have shown that amylase levels are reduced significantly in the pancreas and parotid gland of diabetic rats and that insulin reverses this effect and increases the secretory protein levels. In the pancreas, these changes in amylase protein levels are accompanied by parallel changes in amylase mRNA levels. In the present study, the effects of diabetes and subsequent insulin treatments on contents ( per cell) of amylase protein and its mRNA in parotid glands were compared in rats rendered diabetic with an injection of a beta-cell toxin, streptozotocin (STZ). Both amylase protein and its mRNA contents were reduced significantly in diabetic rats, compared with control rats, and this reduction was reversed following insulin injections of diabetic rats. In insulin-injected diabetic rats, amylase protein contents increased before a detectable increase in amylase mRNA levels was seen. The mRNA contents of a non-secretory protein, actin, did not change during diabetogenesis or subsequent insulin treatments. The reductions in parotid contents of amylase and its mRNA in diabetic rats and the reversal of these changes by insulin are similar to those changes that occur in the pancreas under the same conditions. However, the magnitude of these changes in parotid glands was much smaller than in the pancreas, and the effect of insulin on amylase mRNA synthesis was not as immediate as in the latter gland.

Regulatory Aspects of N-linked Glycoproteins

1987 ◽  
Vol 66 (2) ◽  
pp. 552-556 ◽  
Author(s):  
E.E. Kousvelari ◽  
P.C. Fox ◽  
B.J. Baum
Keyword(s):  
Parotid Gland ◽  
Secretory Protein ◽  
Parotid Glands ◽  
Adrenergic Stimulation ◽  
Regulatory Aspects ◽  
Parotid Acinar Cells ◽  
Extracellular Signaling ◽  
Rat Parotid Gland ◽  
Secretory Glycoproteins ◽  
Rat Parotid

Activation of β-adrenoreceptors in rat parotid acinar cells leads to copious exocrine protein secretion. Additionally, β-adrenergic stimulation dramatically increases specific secretory protein synthesis and enhances N-linked glycosylation of secretory glycoproteins. Recently, efforts have been directed toward understanding the mechanisms underlying these biosynthetic events. We have been particularly interested in the receptor-mediated regulation of glycosylation. In this report, we evaluate available mechanistic information from the rat parotid gland and present initial data examining the ability of various regulatory agents to modulate N-linked glycosylation in enzymatically-dispersed cell aggregates from surgical specimens of human parotid glands. We conclude that glycosylation of human parotid N-linked glycoproteins may be regulated by extracellular signaling similar to that operative in the rat parotid gland.

Differential aggregation properties of secretory proteins that are stored in exocrine secretory granules of the pancreas and parotid glands

2004 ◽  
Vol 286 (2) ◽  
pp. C365-C371 ◽  
Author(s):  
S. G. Venkatesh ◽  
Darrin J Cowley ◽  
Sven-Ulrik Gorr
Keyword(s):  
Secretory Granules ◽  
Secretory Protein ◽  
Low Ph ◽  
Secretory Proteins ◽  
Parotid Glands ◽  
Granule Membrane ◽  
Parotid Secretory Protein ◽  
Rat Parotid ◽  
Ph Range ◽  
Induced Aggregation

Low-pH- and calcium-induced aggregation of regulated secretory proteins has been proposed to play a role in their retention and storage in secretory granules. However, this has not been tested for secretory proteins that are stored in the exocrine parotid secretory granules. Parotid granule matrix proteins were analyzed for aggregation in the presence or absence of calcium and in the pH range of 5.5 to 7.5. Amylase did not aggregate under these conditions, although <10% of parotid secretory protein (PSP) aggregated below pH 6.0. To test aggregation directly in isolated granules, rat parotid secretory granules were permeabilized with 0.1% saponin in the presence or absence of calcium and in the pH range of 5.0 to 8.4. In contrast to the low-pH-dependent retention of amylase in exocrine pancreatic granules, amylase was quantitatively released and most PSP was released from parotid granules under all conditions. Both proteins were completely released upon granule membrane solubilization. Thus neither amylase nor PSP show low-pH- or calcium-induced aggregation under physiological conditions in the exocrine parotid secretory granules.

Isoproterenol downregulation of statin-related gene expression in the rat parotid gland

1991 ◽  
Vol 100 (3) ◽  
pp. 641-647
Author(s):  
D.K. Ann ◽  
A. Wechsler ◽  
H.H. Lin ◽  
E. Wang
Keyword(s):  
Parotid Gland ◽  
Nuclear Protein ◽  
Immunofluorescence Microscopy ◽  
Nuclear Staining ◽  
Parotid Glands ◽  
Cells In Culture ◽  
Indirect Immunofluorescence Microscopy ◽  
Wide Range ◽  
Parotid Cells ◽  
Rat Parotid

Statin, a 57 kilodalton (kDa) nuclear protein, is characteristically found in nonproliferating cells in culture as well as nondividing cells of a wide range of highly differentiated tissues. Moreover, cells in culture that are statin positive lose this statin expression when re-entering the cell-cycle traverse. In this work, statin expression was investigated in the parotid gland of untreated rats and those treated with isoproterenol (IPR), a proliferation-inducing catecholamine. Indirect immunofluorescence microscopy revealed specific nuclear staining with anti-statin monoclonal antibody (S-44) in the acinar and ducts cells of the untreated rats but significantly reduced in those induced with isoproterenol. To characterize the protein recognized by S-44, protein extracts from both tissues were immunoblotted and incubated with S-44. The antibody reacted specifically with a 48 kDa protein in the extract of the parotid glands from untreated rats while no reaction was detected in that of the proliferation-induced ones. These observations along with the result that a statin-like (S1) transcript is downregulated by isoproterenol in the parotid glands further support the notion that the disappearance of statin-related expression is associated with the IPR-induced proliferation in the rat parotid glands. The discrepancy between the apparent molecular mass of the protein identified by S-44 in nonproliferating parotid cells and that of statin originally found in fibroblasts, suggests that either a modified form of statin may be present in the parotid gland, or this 48 kDa protein may be a member of the nonproliferative statin-like family.

scholarly journals Sympathetic denervation impairs agonist-stimulated phosphatidylinositol metabolism in rat parotid glands

1983 ◽  
Vol 214 (3) ◽  
pp. 865-870 ◽  
Author(s):  
C P Downes ◽  
M D Dibner ◽  
M R Hanley
Keyword(s):  
Substance P ◽  
Parotid Gland ◽  
Membrane Lipid ◽  
Sympathetic Denervation ◽  
Parotid Glands ◽  
Surface Receptors ◽  
Alpha Adrenoceptor ◽  
Inositol Phospholipids ◽  
Rat Parotid Gland ◽  
Rat Parotid

Substance P, muscarinic and alpha-adrenoceptor agonists stimulated the incorporation of [3H]inositol into phosphatidylinositol in rat parotid gland slices. Surgical denervation of the sympathetic input to the rat parotid gland by superior cervical ganglionectomy produced marked reductions in these responses. The stimulated incorporation of radiolabelled precursors into phosphatidylinositol is a measure of its resynthesis after receptor-mediated breakdown of inositol phospholipids. We therefore examined the enzymic site of the lesion induced by sympathetic denervation using parotid gland slices labelled with either [3H]inositol or [32P]phosphate and stimulated with substance P. Receptor-activated phospholipase C attack upon [3H]inositol phospholipids was assayed by measuring the formation of [3H]inositol 1-phosphate in the presence of 10 mM-Li+ to inhibit further breakdown. It was not affected by denervation. Substance P elicited a rapid breakdown of phosphatidylinositol 4,5-bisphosphate and this response was reduced in the denervated gland. The second step in stimulated phosphatidylinositol turnover, phosphorylation of diacylglycerol to phosphatidate was not affected by denervation. Sympathetic denervation appears to induce a specific enzymic lesion in the parotid gland that impairs receptor-stimulated resynthesis of phosphatidylinositol from phosphatidate. This change in membrane lipid metabolism may be related to a number of the effects of sympathetic denervation, such as agonist supersensitivity, reduced gland cell proliferation and induction of new surface receptors.

scholarly journals INHERITANCE OF A PAROTID SECRETORY PROTEIN IN MICE AND ITS USE IN DETERMINING SALIVARY AMYLASE QUANTITATIVE VARIANTS

Genetics ◽  
1980 ◽  
Vol 95 (1) ◽  
pp. 129-141
Author(s):  
David Owerbach ◽  
J Peter Hjorth
Keyword(s):  
Cyanogen Bromide ◽  
Inbred Strains ◽  
Secretory Protein ◽  
Major Protein ◽  
Chromosome 2 ◽  
Parotid Glands ◽  
Salivary Amylase ◽  
Inbred Strains Of Mice ◽  
Mendelian Factor ◽  
Parotid Secretory Protein

ABSTRACT Among inbred strains of mice, a major protein, PSP, produced and secreted by the parotid glands, shows variation in electrophoretic mobility and in the peptides produced by cyanogen bromide treatment. This variation is inherited as a single Mendelian factor with two alleles showing co-dominant expression. In genetic crosses, it segregates independently from the amylase complex and is closely linked to the agouti locus on chromosome 2. The protein ratios between amylase and PSP in saliva, obtained by scanning of electrophoretic gel separations, were found to reflect genetic differences in salivary amylase production in strains YBR/Cv and C3H/As.

Secretory protein expression patterns during rat parotid gland development

1998 ◽  
Vol 252 (3) ◽  
pp. 485-497 ◽  
Author(s):  
Savithri Sivakumar ◽  
Lily Mirels ◽  
Abigail J. Miranda ◽  
Arthur R. Hand
Keyword(s):  
Parotid Gland ◽  
Protein Expression ◽  
Expression Patterns ◽  
Secretory Protein ◽  
Rat Parotid Gland ◽  
Rat Parotid ◽  
Gland Development

Deamination of Adenosine 5′-Phosphate and Adenosine as a Possible Source of Ammonia in Human and Bovine Parotid Glands

1981 ◽  
Vol 60 (5) ◽  
pp. 565-569 ◽  
Author(s):  
Z. Bereznowski ◽  
A. Stankiewicz ◽  
W. Makarewicz
Keyword(s):  
Parotid Gland ◽  
Adenosine Deaminase ◽  
Inorganic Phosphate ◽  
Incubation Mixture ◽  
Amp Deaminase ◽  
Parotid Glands ◽  
Enzyme Preparations ◽  
Human Parotid Gland ◽  
Adenosine Phosphate

1. The liberation of ammonia from adenosine 5′-phosphate (AMP) and adenosine and the release of inorganic phosphate from AMP were investigated in homogenates of bovine and human parotid glands. 2. Adenosine phosphate deaminase (AMP deaminase) was purified from bovine and human parotid glands. The enzyme preparations obtained were free from adenosine deaminase and 5′-nucleotidase activities. 3. AMP incubated with human parotid gland homogenate produced inosine 5′-phosphate, adenosine, inosine and ammonia. The amount of ammonia accumulating in the incubation mixture was equal to the sum of inosine 5′-phosphate plus inosine. 4. These results demonstrate the presence in human parotid of AMP deaminase and adenosine deaminase.

scholarly journals Inositol 1,2-cyclic 4,5-trisphosphate is not a product of μscarinic receptor-stimulated phosphatidylinositol 4,5-bisphosphate hydrolysis in rat parotid glands

1987 ◽  
Vol 243 (1) ◽  
pp. 211-218 ◽  
Author(s):  
P T Hawkins ◽  
C P Berrie ◽  
A J Morris ◽  
C P Downes
Keyword(s):  
Parotid Gland ◽  
Inositol Phosphates ◽  
Inositol Phosphate ◽  
Water Soluble ◽  
Parotid Glands ◽  
Inositol 1 ◽  
Inositol 1,4,5 Trisphosphate ◽  
Cyclic Phosphate ◽  
Rat Parotid ◽  
Cyclic Compounds

We have employed a neutral-pH extraction technique to look for inositol 1,2-cyclic phosphate derivatives in [3H]inositol-labelled parotid gland slices stimulated with carbachol. The incubations were terminated by adding cold chloroform/methanol (1:2, v/v), the samples were dried under vacuum and inositol phosphates were extracted from the dried residues by phenol/chloroform/water partitioning. Water-soluble inositol metabolites were separated by h.p.l.c. at pH 3.7. 32P-labelled inositol phosphate standards (inositol 1-phosphate, inositol 1,2-cyclic phosphate, inositol 1,4,5-trisphosphate and inositol 1,2-cyclic 4,5-trisphosphate) were quantitively recovered through both extraction and chromatography steps. Treatment of inositol cyclic phosphate standards with 5% (w/v) HClO4 for 10 min prior to chromatography resulted in formation of the expected non-cyclic compounds. [3H]Inositol 1-phosphate and [3H]inositol 1,4,5-trisphosphate were both present in parotid gland slices and both increased during stimulation with 1 mM-carbachol. There was no evidence for significant quantities of [3H]inositol 1,2-cyclic phosphate or [3H]inositol 1,2-cyclic 4,5-trisphosphate in control or carbachol-stimulated glands. Parotid gland homogenates rapidly converted inositol 1,4,5-trisphosphate to inositol bisphosphate and inositol tetrakisphosphate, but metabolism of the inositol cyclic trisphosphate was much slower. The results suggest that inositol 1,4,5-trisphosphate, but not inositol 1,2-cyclic 4,5-trisphosphate, is the water-soluble product of muscarinic receptor-stimulated phospholipase C in rat parotid glands.

The B1-Immunoreactive Proteins of the Perinatal Submandibular Gland: Similarity to the Major Parotid Gland Protein, RPSP

1993 ◽  
Vol 4 (3) ◽  
pp. 517-524 ◽  
Author(s):  
William D. Ball ◽  
Arthur R. Hand ◽  
Jorge E. Moreira ◽  
Jeanne M. Iversen ◽  
Murray R. Robinovitch
Keyword(s):  
Submandibular Gland ◽  
Polyclonal Antibodies ◽  
Secretory Protein ◽  
Biochemical Properties ◽  
Type I ◽  
Parotid Glands ◽  
Sds Page ◽  
Parotid Secretory Protein ◽  
Rat Submandibular Gland ◽  
I Cells

The B1-immunoreactive proteins of type in cells of the perinatal rat submandibular gland are immunologically cross-reactive with proteins of both the sublingual and parotid glands; in particular, protein SMG-A appears similar to a major parotid protein. We isolated SMG-A and the parotid protein (known as M1 or leucine-rich protein), prepared polyclonal antibodies to them, and compared their biochemical properties and immunological reactivities. They were identical in their molecular weight on SDS-PAGE (23.5 kDa), tenacious binding to Affi-gel Blue, isoelectric point (pH 4.53), and proteolysis to a 14 kDa peptide: Antibodies to SMG-A showed reactivity with protein SMG-C, a product of the neonatal type I cells, as well as with proteins SMG-B1 and SMG-B2, contrasted with the absence of reactivity of anti-M1 IgG with these proteins. Anti-M1 reacted with the "parotid secretory protein" (PSP) of the mouse, and M1 appears to be the homologue, in the rat, of mouse PSP.

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