scholarly journals Neonatal rat submandibular gland protein SMG-A and parotid secretory protein are alternatively regulated members of a salivary protein multigene family.

1992 ◽  
Vol 267 (4) ◽  
pp. 2679-2687
Author(s):  
L Mirels ◽  
W D Ball
Keyword(s):  
Submandibular Gland ◽  
Multigene Family ◽  
Secretory Protein ◽  
Salivary Protein ◽  
Neonatal Rat ◽  
Parotid Secretory Protein ◽  
Rat Submandibular Gland

Molecular Cloning of Developmentally Regulated Neonatal Rat Submandibular Gland Proteins

1993 ◽  
Vol 4 (3) ◽  
pp. 525-530 ◽  
Author(s):  
Lily Mirels ◽  
Lisa R. Girard ◽  
William D. Ball
Keyword(s):  
Molecular Cloning ◽  
Submandibular Gland ◽  
Cdna Library ◽  
Protein C ◽  
Salivary Protein ◽  
Neonatal Rat ◽  
Salivary Proteins ◽  
Developmentally Regulated ◽  
Rat Submandibular Gland

At birth, the rat submandibular gland (SMG) contains two transient secretory cell types that produce several characteristic salivary proteins. Proteins SMG-A, B1, and B2 (23.5, 26 and 27.5 kDa) are products of the neonatal type III cells, but not the adult acinar cells. Protein C (89 kDa), a major product of the neonatal type I cells, is either absent or present at greatly diminished levels in the secretory cells of the adult gland. The decrease in biosynthesis of these neonatal salivary proteins occurs concomitantly with the increase in levels of characteristic adult SMG products. In order to understand these developmentally regulated changes in SMG salivary protein gene expression, we have initiated the molecular cloning and characterization of neonatal submandibular gland proteins from a 5-d-old rat submandibular gland cDNA library. Clones encoding SMG-A were isolated by homology to the mouse parotid secretory protein (PSP). SMG-A was shown to be derived from a salivary protein multigene family that also includes PSP. Cloning and characterization of additional neonatal rat submandibular gland proteins was initiated by screening the 5-d-old rat submandibular gland cDNA library with first strand cDNA prepared from 1-d-old rat submandibular glands. Clones corresponding to a highly abundant 3 kb transcript present in the neonatal rat SMG, but not in adult submandibular, sublingual, or parotid gland have been identified. The size, abundance, and organ specificity of this transcript suggest that it may encode protein C. One clone derived from an unknown transcript that is developmentally regulated in the neonatal SMG and is present in the adult parotid, submandibular, and sublingual glands was also identified.

scholarly journals Systematic nomenclature for the PLUNC/PSP/BSP30/SMGB proteins as a subfamily of the BPI fold-containing superfamily

2011 ◽  
Vol 39 (4) ◽  
pp. 977-983 ◽  
Author(s):  
Colin D. Bingle ◽  
Ruth L. Seal ◽  
C. Jeremy Craven
Keyword(s):  
Submandibular Gland ◽  
Secretory Protein ◽  
Salivary Protein ◽  
Reliable Data ◽  
Nasal Epithelium ◽  
Hugo Gene Nomenclature Committee ◽  
Gene Nomenclature ◽  
Nomenclature Committee ◽  
Systematic Nomenclature ◽  
Parotid Secretory Protein

We present the BPIFAn/BPIFBn systematic nomenclature for the PLUNC (palate lung and nasal epithelium clone)/PSP (parotid secretory protein)/BSP30 (bovine salivary protein 30)/SMGB (submandibular gland protein B) family of proteins, based on an adaptation of the SPLUNCn (short PLUNCn)/LPLUNCn (large PLUNCn) nomenclature. The nomenclature is applied to a set of 102 sequences which we believe represent the current reliable data for BPIFA/BPIFB proteins across all species, including marsupials and birds. The nomenclature will be implemented by the HGNC (HUGO Gene Nomenclature Committee).

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.

Cytochemical Evidence for Presynatic β-Adrenergic Regulation of Secretion in the Developing Rat Submandibular Gland

1977 ◽  
Vol 35 ◽  
pp. 430-431
Author(s):  
L.S. Cutler
Keyword(s):  
Cyclic Amp ◽  
Adenylate Cyclase ◽  
Submandibular Gland ◽  
Neonatal Rat ◽  
Cyclase Activity ◽  
Adenylate Cyclase Activity ◽  
Parotid Glands ◽  
Adrenergic Agonist ◽  
Rat Submandibular Gland

Many studies previously have shown that the B-adrenergic agonist isoproterenol and the a-adrenergic agonist norepinephrine will stimulate secretion by the adult rat submandibular (SMG) and parotid glands. Recent data from several laboratories indicates that adrenergic agonists bind to specific receptors on the secretory cell surface and stimulate membrane associated adenylate cyclase activity which generates cyclic AMP. The production of cyclic AMP apparently initiates a cascade of events which culminates in exocytosis. During recent studies in our laboratory it was observed that the adenylate cyclase activity in plasma membrane fractions derived from the prenatal and early neonatal rat submandibular gland was retractile to stimulation by isoproterenol but was stimulated by norepinephrine. In addition, in vitro secretion studies indicated that these prenatal and neonatal glands would not secrete peroxidase in response to isoproterenol but would secrete in response to norepinephrine. In contrast to these in vitro observations, it has been shown that the injection of isoproterenol into the living newborn rat results in secretion of peroxidase by the SMG (1).

The BPI-like/PLUNC family proteins in cattle

2011 ◽  
Vol 39 (4) ◽  
pp. 1006-1011 ◽  
Author(s):  
Thomas T. Wheeler ◽  
Brendan J. Haigh ◽  
Marita K. Broadhurst ◽  
Kylie A. Hood ◽  
Nauman J. Maqbool
Keyword(s):  
Protein Gene ◽  
Current Knowledge ◽  
Physiological Role ◽  
Secretory Protein ◽  
Salivary Protein ◽  
Ancestral Gene ◽  
Bacterial Aggregation ◽  
Parotid Secretory Protein ◽  
Pathogen Exposure

Members of the protein family having similarity to BPI (bactericidal/permeability increasing protein) (the BPI-like proteins), also known as the PLUNC (palate, lung and nasal epithelium clone) family, have been found in a range of mammals; however, those in species other than human or mouse have been relatively little characterized. Analysis of the BPI-like proteins in cattle presents unique opportunities to investigate the function of these proteins, as well as address their evolution and contribution to the distinct physiology of ruminants. The present review summarizes the current understanding of the nature of the BPI-like locus in cattle, including the duplications giving rise to the multiple BSP30 (bovine salivary protein 30 kDa) genes from an ancestral gene in common with the single PSP (parotid secretory protein) gene found in monogastric species. Current knowledge of the expression of the BPI-like proteins in cattle is also presented, including their pattern of expression among tissues, which illustrate their independent regulation at sites of high pathogen exposure, and the abundance of the BSP30 proteins in saliva and salivary tissues. Finally, investigations of the function of the BSP30 proteins are presented, including their antimicrobial, lipopolysaccharide-binding and bacterial aggregation activities. These results are discussed in relation to hypotheses regarding the physiological role of the BPI-like proteins in cattle, including the role they may play in host defence and the unique aspects of digestion in ruminants.

scholarly journals The parotid secretory protein BPIFA2 is a salivary surfactant that affects LPS action

2020 ◽  
Author(s):  
Seshagiri R. Nandula ◽  
Ian Huxford ◽  
Thomas T. Wheeler ◽  
Conrado Aparicio ◽  
Sven-Ulrik Gorr
Keyword(s):  
Surface Tension ◽  
Systemic Disease ◽  
Physiological Role ◽  
Hydrophobic Surface ◽  
Secretory Protein ◽  
Salivary Protein ◽  
Lipid Binding ◽  
Wild Type ◽  
Parotid Secretory Protein ◽  
Dry Food

AbstractSaliva plays important roles in the mastication, swallowing and digestion of food, speech and lubrication of oral mucosa, antimicrobial and anti-inflammatory activity and control of body temperature in grooming animals. The salivary protein BPIFA2 (BPI fold containing family A member 2; former names: Parotid Secretory Protein, PSP, SPLUNC2, C20orf70) is related to lipid-binding and LPS-binding proteins expressed in mucosa. Indeed, BPIFA2 binds LPS but the physiological role of BPIFA2 remains to be determined. To address this question, Bpifa2 knockout (Bpifa2tm1(KOMP)Vlcg) (KO) mice were phenotyped with a special emphasis on saliva and salivary glands. Saliva collected from KO mice was less able to spread on a hydrophobic surface than wild-type saliva and the surface tension of KO saliva was close to that of water. These data suggest that BPIFA2 is a salivary surfactant that is mainly responsible for the low surface tension of mouse saliva. The reduced surfactant activity of KO saliva did not affect consumption of dry food or grooming, but saliva from KO mice contained less LPS than wild-type saliva. Indeed, mice lacking BPIFA2 responded to ingested LPS with an increased stool frequency, suggesting that BPIFA2 plays a role in the solubilization and activity of ingested LPS. Consistent with these findings, BPIFA2-depleted mice also showed increased insulin secretion and metabolomic changes that were consistent with a mild endotoxemia. These results support the distal physiological function of a salivary protein and reinforce the connection between oral biology and systemic disease.

Parotid secretory protein is an HDL-associated protein with anticandidal activity

2005 ◽  
Vol 288 (5) ◽  
pp. R1306-R1315 ◽  
Author(s):  
Weerapan Khovidhunkit ◽  
Jean Pierre Hachem ◽  
Katalin F. Medzihradszky ◽  
Philippe N. Duchateau ◽  
Judy K. Shigenaga ◽  
...  
Keyword(s):  
Low Density Lipoprotein ◽  
Density Lipoprotein ◽  
Secretory Protein ◽  
Salivary Protein ◽  
Low Density ◽  
Parotid Glands ◽  
Transfer Protein ◽  
Proteomic Approach ◽  
Phospholipid Transfer ◽  
Parotid Secretory Protein

High-density lipoprotein (HDL) is part of innate immunity, protecting against infection and inflammation. Using a proteomic approach, we identified an amino acid sequence in a hamster HDL protein that showed homology to rat and mouse parotid secretory protein (PSP), a salivary protein secreted from the parotid glands. We cloned the cDNA encoding a putative hamster homolog of rat and mouse PSP. Searches for conserved domains of the protein showed that the COOH terminus of hamster PSP contains a region homologous to the NH2termini of a family of HDL-associated proteins, including LPS-binding protein, cholesteryl ester transfer protein, and phospholipid transfer protein. In mice, PSP was also associated with HDL but was not detected in very-low-density lipoprotein, low-density lipoprotein, or lipoprotein-deficient sera. In addition to salivary glands, we found that PSP mRNA was expressed in lung, testis, and ovary. The level of PSP in HDL was increased after endotoxin injection in hamsters, but not in mice. Recombinant PSP inhibits growth of Candida albicans in culture. In summary, our results showed that PSP is a novel anticandidal protein associated with HDL.

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