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

2020 ◽  
Vol 105 (8) ◽  
pp. 1280-1292
Author(s):  
Seshagiri Rao Nandula ◽  
Ian Huxford ◽  
Thomas T. Wheeler ◽  
Conrado Aparicio ◽  
Sven‐Ulrik Gorr
Keyword(s):  
Secretory Protein ◽  
Parotid Secretory Protein

Bovine parotid secretory protein: structure, expression and relatedness to other BPI (bactericidal/permeability-increasing protein)-like proteins

2003 ◽  
Vol 31 (4) ◽  
pp. 781-784 ◽  
Author(s):  
T.T. Wheeler ◽  
K. Hood ◽  
K. Oden ◽  
J. McCracken ◽  
C.A. Morris
Keyword(s):  
Minor Salivary Gland ◽  
Secretory Protein ◽  
Protein Family ◽  
Sequence Information ◽  
The Family ◽  
Salivary Gland Protein ◽  
Full Length Sequence ◽  
Parotid Secretory Protein ◽  
Restricted Pattern

Members of the family of BPI (bactericidal/permeability-increasing protein)-like proteins are as yet incompletely characterized, particularly in cattle, where full-length sequence information is available for only three of the 13 family members known from other species. Structural bioinformatic analyses incorporating bovine homologues of several members of the BPI-like protein family, including two forms of bovine parotid secretory protein (PSP), showed that this family is also present in cattle. Expression analyses of several members of the BPI-like protein family in cattle, including PSP (Bsp30), von Ebner's minor salivary gland protein (VEMSGP) and lung-specific X protein (LUNX), showed a restricted pattern of expression, consistent with earlier hypotheses that these proteins function in the innate immune response to bacteria. The possible role of bovine PSP in susceptibility to pasture bloat in cattle is discussed.

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.

Four BPI (bactericidal/permeability-increasing protein)-like genes expressed in the mouse nasal, oral, airway and digestive epithelia

2003 ◽  
Vol 31 (4) ◽  
pp. 801-805 ◽  
Author(s):  
E.E. LeClair
Keyword(s):  
Salivary Gland ◽  
Minor Salivary Gland ◽  
Secretory Protein ◽  
Chromosome 2 ◽  
Specific Expression ◽  
Tissue Specific Expression ◽  
Oral Airway ◽  
Structural Identity ◽  
Salivary Gland Protein ◽  
Parotid Secretory Protein

A cluster of related genes whose products show structural identity with bactericidal permeability-increasing protein (BPI) has been identified in the genomes of both mice (on chromosome 2) and humans (on chromosome 20). Genes in the cluster include those encoding parotid secretory protein (PSP), von Ebner minor salivary gland protein (VEMSGP) and sequences in the PLUNC (palate, lung and nasal epithelium clone) family, among others. This mini-review addresses the tissue-specific expression of these genes in the mouse.

Psp and Smgb: a model for developmental and functional regulation in the rat major salivary glands

2003 ◽  
Vol 31 (4) ◽  
pp. 777-780 ◽  
Author(s):  
W.D. Ball ◽  
L. Mirels ◽  
A.R. Hand
Keyword(s):  
Salivary Glands ◽  
Secretory Protein ◽  
Developmental Expression ◽  
Regulatory Mechanisms ◽  
Lipopolysaccharide Binding Protein ◽  
Functional Regulation ◽  
Parotid Secretory Protein ◽  
Biochemical Features ◽  
Lipopolysaccharide Binding

This paper summarizes past work detailing the developmental expression, cell and organ localization and biochemical features of the proteins parotid secretory protein (PSP) and isoforms of submandibular gland protein B (SMGB), and describes the molecular characterization of the genes that encode them, Psp and Smgb. These genes appear to be related to the BPI (bactericidal/permeability-increasing protein)/LBP (lipopolysaccharide-binding protein)/PLUNC (palate, lung and nasal epithelial clone) gene family found in the oral and respiratory organs of humans, rodents and cattle. We have emphasized the diverse patterns of expression of these genes among the submandibular, sublingual and parotid salivary glands of the rat, and their potential usefulness in defining and identifying genomic regulatory mechanisms of salivary development. While Psp is expressed similarly in the mouse, the putative Smgb gene of the mouse seems not to be expressed, apparently due to the insertion, between exons 1 and 2, of a gene for a retroviral protein.

Structure of human BPI (bactericidal/permeability-increasing protein) and implications for related proteins

2003 ◽  
Vol 31 (4) ◽  
pp. 791-794 ◽  
Author(s):  
L.J. Beamer
Keyword(s):  
Three Dimensional ◽  
Structural Features ◽  
Secretory Protein ◽  
Sequence Database ◽  
Dimensional Model ◽  
Three Dimensional Model ◽  
X Ray ◽  
Fold Family ◽  
Parotid Secretory Protein ◽  
Related Proteins

Human bactericidal/permeability-increasing protein (BPI) belongs to a family of mammalian lipopolysaccharide-binding and lipid transport proteins. Recent sequence database searches indicate that several other protein families, including the palate, lung and nasal epithelial clone (PLUNC), parotid secretory protein (PSP) and BPI-like proteins, are likely to share the BPI fold, which was determined through X-ray crystallographic studies. As the single representative of its fold family of known structure, the three-dimensional model of BPI suggests structural features that are likely to be conserved across this large and varied group of proteins.

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 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.

Analysis of cDNA sequence, protein structure and expression of parotid secretory protein in pig

2003 ◽  
Vol 48 (13) ◽  
pp. 1358-1363 ◽  
Author(s):  
Haifang Yin ◽  
Baoliang Fan ◽  
Zhihui Zhao ◽  
Zhaoliang Liu ◽  
Jing Fei ◽  
...  
Keyword(s):  
Protein Structure ◽  
Cdna Sequence ◽  
Secretory Protein ◽  
Parotid Secretory Protein
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