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.

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.

Protein-binding elements in the proximal parotid secretory protein gene enhancer essential for salivary-gland-specific expression

2001 ◽  
Vol 357 (2) ◽  
pp. 537-544
Author(s):  
Pia SVENDSEN ◽  
Karsten KRISTIANSEN ◽  
J. Peter HJORTH
Keyword(s):  
Salivary Gland ◽  
Transgenic Mice ◽  
Parotid Gland ◽  
Limit Of Detection ◽  
Specific Binding ◽  
Secretory Protein ◽  
Nuclear Proteins ◽  
Specific Expression ◽  
Adjacent Element ◽  
Parotid Secretory Protein

The murine parotid secretory protein (PSP) gene is expressed at high levels in the parotid gland and at lower levels in the sublingual gland. A proximal enhancer core necessary for tissue-specific expression was identified previously, and it was demonstrated that one element, parotid gland element I (PGE I), exhibited specific binding of parotid gland nuclear proteins. In the present study, we demonstrate that a related adjacent element, PGE II, which binds nuclear proteins in a much less tissue-restricted manner, is able to compete with PGE I for binding of parotid-gland-specific factors. The functional significance of PGE I and PGE II was examined in transgenic mice. Deletion of PGE II reduced transgene expression only in the parotid gland, whereas deletion of PGE I appeared to reduce expression in both of the PSP-expressing salivary glands. Combined deletion of PGE I and PGE II reduced expression below the limit of detection. Thus PGE I and PGE II are functionally important salivary-gland-specific binding elements that are necessary for the salivary-gland-specific expression of a PSP minigene in transgenic mice.

scholarly journals cDNA structure, tissue-specific expression, and chromosomal localization of the murine band 7.2b gene

Blood ◽  
1995 ◽  
Vol 86 (1) ◽  
pp. 359-365 ◽  
Author(s):  
PG Gallagher ◽  
M Romana ◽  
JH Lieman ◽  
DC Ward
Keyword(s):  
Alpha Helix ◽  
Distal Region ◽  
Proximal Region ◽  
Erythrocyte Membranes ◽  
Chromosome 2 ◽  
Specific Expression ◽  
Tissue Specific ◽  
Reading Frame ◽  
Tissue Specific Expression ◽  
Membrane Spanning

Band 7.2b is an integral phosphoprotein absent from the erythrocyte membranes of patients with hydrocytosis, an autosomal, dominantly inherited, hemolytic anemia characterized by stomatocytic red blood cells with abnormal permeability to Na+ and K+. The role of this protein in the erythrocyte membrane is not well understood. To gain additional insight into the structure and function of this protein, we have cloned the murine band 7.2b cDNA and studied its tissue-specific expression. 2,873 bp of cDNA with an open reading frame of 852 bp were isolated. This fragment encodes a protein of 284 amino acids with a predicted molecular weight of 31 kD. The band 7.2b gene had a wide pattern of expression, with high levels of mRNA in heart, liver, skeletal muscle, and testis and low levels in lung, brain, and spleen. Using fluorescent in situ hybridization, the murine band 7.2b gene was mapped to chromosome 2, at the border of the distal region of 2B and proximal region of C1, syntenic to 9q33-q34, the location of the human homologue. Models of the predicted protein structure showed a short NH2- terminal head, a strongly hydrophobic 28-amino acid stretch presumably encoding a single membrane-spanning domain, and a large domain composed of beta sheet and alpha helix. Database searching showed no significant homology of other known proteins to murine or human band 7.2b.

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.

scholarly journals Isolation and characterization of the androgen-dependent mouse cysteine-rich secretory protein-3 (CRISP-3) gene

1995 ◽  
Vol 309 (3) ◽  
pp. 831-836 ◽  
Author(s):  
U Schwidetzky ◽  
B Haendler ◽  
W D Schleuning
Keyword(s):  
Salivary Gland ◽  
Transcription Initiation ◽  
Genomic Library ◽  
Consensus Sequence ◽  
Initiation Site ◽  
Secretory Protein ◽  
Specific Expression ◽  
Isolation And Characterization ◽  
Eukaryotic Genes ◽  
Responsive Element

The mRNA for cysteine-rich secretory protein-3 (CRISP-3) was originally identified in the mouse salivary gland as an androgen-dependent transcript, and is closely related to CRISP-1 and CRISP-2 which are abundantly expressed in the epididymis and testis respectively. Overlapping phage clones encompassing the entire length of the CRISP-3 gene were isolated from a lambda EMBL3 genomic library and analysed. DNA sequencing revealed that the gene consisted of eight exons ranging between 55 and 740 bp in size, and seven introns. All exon-intron junctions conformed to the GT/AG rule established for eukaryotic genes. The length of the introns was determined by PCR and was found to vary between 1.0 and 3.7 kb, indicating that the gene spans over 20 kb of the mouse genome. Primer extension allowed the mapping of the major transcription initiation site to an adenine located at the appropriate position downstream of a bona fide TATA box, in a region corresponding well to the eukaryotic consensus sequence. Over 800 bp of CRISP-3 promoter region were determined and two regions almost exactly matching the androgen-responsive element consensus RGWACANNNTGTWCY detected. In addition, sequences described in the Drosophila melanogaster Sgs-3 gene as being involved in its salivary gland-specific expression as well as two putative OTF- and GATA-binding elements were also found.

scholarly journals Evaluation of Autoantibodies in Patients with Primary and Secondary Sjogren’s Syndrome

2017 ◽  
Vol 11 (1) ◽  
pp. 10-15 ◽  
Author(s):  
Ellen De Langhe ◽  
Xavier Bossuyt ◽  
Long Shen ◽  
Kishore Malyavantham ◽  
Julian L. Ambrus ◽  
...  
Keyword(s):  
Sjögren’S Syndrome ◽  
Lupus Erythematosus ◽  
Sjögren's Syndrome ◽  
Sjogren’S Syndrome ◽  
Secretory Protein ◽  
Sjogren's Syndrome ◽  
Early Disease ◽  
Salivary Gland Protein ◽  
Parotid Secretory Protein ◽  
Sjögren‘S Syndrome

Background: Antibodies to salivary gland protein 1 (SP1), carbonic anhydrase 6 (CA6) and parotid secretory protein (PSP) were discovered in an animal model of Sjogren’s syndrome (SS). Their expression was noted in patients with SS, especially those with lower focus scores on lip biopsies and those with early disease lacking antibodies to Ro and La. Objective: The current studies evaluated these autoantibodies in patients with long-standing SS expressing high levels of anti-Ro antibodies and in patients with Sjogren’s syndrome secondary to systemic lupus erythematosus (SLE), systemic sclerosis (SSc) and mixed connective tissue disease (MCTD). Method: Sera were obtained from patients and evaluated by ELISA for IgG, IgA and IgM antibodies to SP1, CA6 and PSP. Results: IgA anti-CA6 antibodies were noted in 38% of these patients, but anti-SP1, CA6 and PSP IgM or IgG antibodies were identified only in a minority of patients. In patients with secondary SS, antibodies to SP1/CA6/PSP were more sensitive and specific than anti-Ro . Conclusion: While more studies are needed, antibodies to SP1, CA6 and PSP provide valuable markers for the diagnosis of primary and secondary SS, especially early in the course of the disease.

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