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 HUGO Gene Nomenclature Committee (HGNC)

2001 ◽  
Vol 109 (6) ◽  
pp. 678-680 ◽  
Author(s):  
Sue Povey ◽  
Ruth Lovering ◽  
Elspeth Bruford ◽  
Mathew Wright ◽  
Michael Lush ◽  
...  
Keyword(s):  
Hugo Gene Nomenclature Committee ◽  
Gene Nomenclature ◽  
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.

scholarly journals HUGO Gene Nomenclature Committee (HGNC) recommendations for the designation of gene fusions

Leukemia ◽  
2021 ◽  
Author(s):  
Elspeth A. Bruford ◽  
Cristina R. Antonescu ◽  
Andrew J. Carroll ◽  
Arul Chinnaiyan ◽  
Ian A. Cree ◽  
...  
Keyword(s):  
Cancer Cells ◽  
Scientific Community ◽  
Scientific Literature ◽  
Gene Fusions ◽  
Hugo Gene Nomenclature Committee ◽  
Fusion Genes ◽  
Gene Nomenclature ◽  
Nomenclature Committee ◽  
Gene Symbols

AbstractGene fusions have been discussed in the scientific literature since they were first detected in cancer cells in the early 1980s. There is currently no standardized way to denote the genes involved in fusions, but in the majority of publications the gene symbols in question are listed either separated by a hyphen (-) or by a forward slash (/). Both types of designation suffer from important shortcomings. HGNC has worked with the scientific community to determine a new, instantly recognizable and unique separator—a double colon (::)—to be used in the description of fusion genes, and advocates its usage in all databases and articles describing gene fusions.

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.

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.

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.

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

Electromyography Monitoring of Patients With Salivary Gland Diseases

2005 ◽  
Vol 133 (6) ◽  
pp. 869-873 ◽  
Author(s):  
Michael Vaiman ◽  
Oded Nahlieli ◽  
Samuel Segal ◽  
Ephraim Eviatar
Keyword(s):  
Salivary Gland ◽  
Parotid Gland ◽  
Healthy Volunteers ◽  
Submandibular Gland ◽  
Study Design ◽  
Flow Rate ◽  
Surface Electromyography ◽  
Salivary Flow ◽  
Reliable Data ◽  
Salivary Gland Diseases

OBJECTIVE: To provide a description of surface electromyography (sEMG) of spontaneous saliva swallowing (SSS) and monitoring of swallow rate in patients with salivary gland diseases. STUDY DESIGN: Numbers of SSS obtained during 2 hours of sEMG monitoring were compared with sialometry data for healthy volunteers (n = 100), patients with Sjögren syndrome (n = 10), and patients after parotid gland (n = 15) and submandibular gland (n = 16) surgery. RESULTS: Normative: 1 SSS every 2 minutes and 15 seconds; Sjögren: 1 SSS every 13 minutes ( P < 0.001); parotid gland surgery: 1 SSS every 3 minutes and 24 seconds ( P = 0.26); submandibular gland surgery: 1 SSS every 5 minutes and 04 seconds ( P < 0.05). Sjögren patients and patients after submandibular surgery had hyposalivation correlated with less SSS. CONCLUSION: The established normal rate of SSS makes this modality applicable for evaluating salivary flow for potentially identifying and ruling out abnormalities. Parotid gland surgery does not significantly affect salivary flow rate. Sialometry combined with sEMG monitoring give a clinician more reliable data to evaluate salivary gland disorders than sialometry alone. EBM RATING: B-2

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