The BSP30 salivary proteins from cattle, LUNX/PLUNC and von Ebner's minor salivary gland protein are members of the PSP/LBP superfamily of proteins

Wheeler, Thomas T.; Haigh, Brendan; McCracken, Judith Y.; Wilkins, Richard J.; Morris, C. A.; Grigor, Murray R.

doi:10.1016/s0167-4781(02)00508-0

Cited by 52 publications

(55 citation statements)

References 37 publications

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“…psp is produced by mouse salivary glands with similar temporal and cell specificity to rat psp, however, mouse smgb has been silenced through a viral integration event in the first intron (Ball et al 2003) and therefore mice are smgb deficient. Further psp-related proteins have been described in cow saliva and termed bovine salivary protein 30 kDa (bsp30) (Wheeler et al 2002). Cloning studies initially identified two distinct genes, bsp30a and bsp30b, that are highly expressed in the parotid gland and comprise approximately 30% of the protein in bovine saliva.…”

Section: Multiple Splunc2 Bands Are Detectable In Human Salivamentioning

confidence: 99%

“…Cloning studies initially identified two distinct genes, bsp30a and bsp30b, that are highly expressed in the parotid gland and comprise approximately 30% of the protein in bovine saliva. The two forms of bsp30 are highly expressed in the major salivary glands of cattle and appear to be expressed independently of one another (Wheeler et al 2002). bsp30a and bsp30b are highly related at primary sequence level (96% at DNA and 83% at amino acid level) and recent genomic analysis has identified the existence of two further bsp30 genes (bsp30c and bsp30d) and has shown that these four genes have arisen by a series of duplication events (Wheeler et al 2007).…”

Section: Multiple Splunc2 Bands Are Detectable In Human Salivamentioning

confidence: 99%

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Characterisation and expression of SPLUNC2, the human orthologue of rodent parotid secretory protein

Bingle

Barnes

Lunn

et al. 2009

Histochem Cell Biol

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Section: Multiple Splunc2 Bands Are Detectable In Human Salivamentioning

confidence: 99%

Section: Multiple Splunc2 Bands Are Detectable In Human Salivamentioning

confidence: 99%

Characterisation and expression of SPLUNC2, the human orthologue of rodent parotid secretory protein

Bingle

Barnes

Lunn

et al. 2009

Histochem Cell Biol

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“…Each conserved domain is predicted to form an apolar lipid binding pocket, with hydrophilic chains outside and hydrophobic chains inner side, which is a critical structure allowing transfer of apolar ligands in an aqueous environment (Beamer et al, 1997(Beamer et al, , 1999. A pair of cysteine residues, which are thought to form an intramolecular disulfite bond in this family (Beamer et al, 1997;Wheeler et al, 2002), are also found in the N-terminal BPI domain of LPlunc1 (asterisks in Fig. 1A).…”

Section: Isolation Of a Lplunc1 Clone That Belongs To The Bpi/plunc Smentioning

confidence: 99%

Identification of a novel left–right asymmetrically expressed gene in the mouse belonging to the BPI/PLUNC superfamily

Hou

Yashiro

Okazaki

et al. 2004

Developmental Dynamics

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In the process of left-right (L-R) axis formation in the mouse, the node plays a critical role as a structure where the initial breaking of L-R symmetry occurs. Here, we report on the gene LPlunc1, a member of BPI/PLUNC gene superfamily, which is asymmetrically expressed in the developing mouse node. LPlunc1 protein is secreted as a processed form of relative molecular mass 54K-60K and shares sequence features with the other members of BPI/PLUNC superfamily, including the N-terminal and C-terminal homology domains, each of which is considered to form a lipid binding pocket. LPlunc1 is transiently expressed in the crown cells of the node asymmetrically. This expression pattern of Lplunc1 highly overlaps with that of Nodal, a major player during the L-R formation. Interestingly, this asymmetric expression pattern is randomized in the iv mutant and reversed in the inv mutant, indicating that LPlunc1 is downstream of iv and inv. Our results suggest a link between lipid binding/transfer and the axis development.

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“…Studies on saliva have been conducted much more on human saliva, while they have just recently begun to develop on ruminants (Beauchemin et al, 2008;Lamy et al, 2009Lamy et al, , 2010Wheeler et al, 1998Wheeler et al, , 2002Wheeler et al, , 2007Wheeler et al, , 2011Lamy and Mau, 2012). There are many different types of proteins in the ruminant saliva with quite a large range of molecular mass reported elsewhere (Lamy et al, 2009).…”

Section: Introductionmentioning

confidence: 99%

Proteomic Analysis of a 14.2 kDa Protein Isolated from Bali Cattle(Bos Sondaicus/Javanicus)Saliva Using Single Dimension Sodium Dodecyl Sulphate-Polyacrylamide Gel Electrophoresis and Matrix-Assisted Laser Desorption Ionization Time-of-Flight Tandem Mass Spectrometer

Depamede

2013

Italian Journal of Animal Science

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A 14.2 kDa protein isolated from Bali cattle (Bos sondaicus/javanicus) saliva has been reported to have a bactericidal activity. The aim of this study was to analyse the nature of a 14.2 kDa protein using single dimension (1-D) sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and matrix-assisted laser desorption ionization time-of-flight tandem mass spectrometer (MALDI TOF/TOF). The protein was isolated by means of polyethylene glycol (PEG)/sodium sulfate aqueous twophase system, and then determined by 12.5% SDS-PAGE. A band of 14.2 kDa was sliced and analysed by MALDI TOF/TOF mass spectrometer using a 5800 proteomics analyzer. Mascot search and National Center for Biotechnology Information (NCBI) Blast search revealed that the spot of 1-D SDS-PAGE consisted of three proteins: zymogen granule protein 16 homologue B, pancreatic adenocarcinoma upregulated factor-like, and prolactin-inducible protein homologue precursor. The three proteins have been observed in Bos taurus and other species such as mouse. The actual nature of the proteins and their function in Bali cattle (Bos sondaicus/javanicus), as well as the connection with the evolution of bovines need further analysis.

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The BSP30 salivary proteins from cattle, LUNX/PLUNC and von Ebner's minor salivary gland protein are members of the PSP/LBP superfamily of proteins

Cited by 52 publications

References 37 publications

Characterisation and expression of SPLUNC2, the human orthologue of rodent parotid secretory protein

Characterisation and expression of SPLUNC2, the human orthologue of rodent parotid secretory protein

Identification of a novel left–right asymmetrically expressed gene in the mouse belonging to the BPI/PLUNC superfamily

Proteomic Analysis of a 14.2 kDa Protein Isolated from Bali Cattle(Bos Sondaicus/Javanicus)Saliva Using Single Dimension Sodium Dodecyl Sulphate-Polyacrylamide Gel Electrophoresis and Matrix-Assisted Laser Desorption Ionization Time-of-Flight Tandem Mass Spectrometer

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