Basic proline‐rich proteins of murine parotid glands

Bannister, Andrew J.; Divecha, Nullin; Ashmore, Michael; McDonald, Charles J.

doi:10.1111/j.1432-1033.1989.tb14734.x

Cited by 10 publications

(13 citation statements)

References 38 publications

(16 reference statements)

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“…The isolation and characterization of these is described in detail elsewhere (Bannister et al, 1989). However, briefly, mice were injected daily for 10 days with 0.6 mg isoproterenol/mouse (Sigma, Pool, UK).…”

Section: Antigensmentioning

confidence: 99%

“…Injections of isoproterenol increase the expression of PRP genes (Roberts et aI., 1991a, b, c) and after only 3-4 days newly synthesized PRPs make up more than 50% of the secretory products of the glands of mice (Robinovitch et al, 1977). One acidic and six basic PRPs have been identified in the hypertrophied glands of rats (Muenzer et al, 1979a, b) and three different glycosylated forms (Mehansho et al, 1985) and five non-glycosylated forms (Bannister et al, 1989) have been isolated from the parotid glands of mice.…”

Section: Introductionmentioning

confidence: 95%

“…Recently we have identified two PRPs in normal mouse parotid immunologically and have characterized the PRPs from the glands of isoproterenol-treated mice (Bannister et al, 1989;Divecha et al, 1989). In this companion study we have used polyclonal antibodies raised against these induced proteins to localize PRPs in normal mouse parotid glands at the electron microscope level.…”

Section: Introductionmentioning

confidence: 97%

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Electron microscopic immunocytochemical localization of proline-rich proteins in normal mouse parotid salivary glands

et al. 1992

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Rabbit polyclonal antibodies against isoproterenol-induced mouse proline-rich proteins (PRPs) were used to localize PRPs in the parotid salivary glands of normal adult BALB/c mice. The antibodies recognized both acidic-type and basic-type PRPs. Immunoblotting experiments revealed that the glands contained an acidic-type and a basic-type PRP. Parotid gland tissue was fixed with Karnosky's fixative and embedded in Lowicryl resin at low temperature. PRPs were localized at the electron microscope level using an indirect post-embedding staining technique with protein A-gold. The secretion granules of the acinar cells were strongly labelled. Pre-absorption of the antibody with purified acidic-type and basic-type PRPs indicated that the basic-type PRP is mainly located at the periphery of the granules but that the acidic-type PRP is more evenly distributed within the granules. Pre-absorption of the antibody with alpha-amylase did not affect the staining pattern, suggesting minimal cross-reactivity. PRPs were also detected within the rough endoplasmic reticulum and the Golgi apparatus of acinar cells, within the granules of the proacinar cells and in the lumena of the ducts, but not within the intercalated or striated duct cell granules.

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Section: Antigensmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 95%

Section: Introductionmentioning

confidence: 97%

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Electron microscopic immunocytochemical localization of proline-rich proteins in normal mouse parotid salivary glands

et al. 1992

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“…Salivary PRps consist of between 70-80% proline, glutamine and glycine, arranged as 5-15 almost identical repeats of an approximate 18-residue sequence [4]. Their production is constitutive in man, but is at a very low level in some rodents, and can be induced either by isoprenaline [5] or by tannin-rich diets [6].…”

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confidence: 99%

Study of the interaction between salivary proline‐rich proteins and a polyphenol by ¹H‐NMR spectroscopy

Murray

Williamson

Lilley

et al. 1994

European Journal of Biochemistry

215

147

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The interaction between salivary proline-rich proteins and plant polyphenols (tannins) in the oral cavity and their subsequent precipitation influences the taste, texture and nutritional value of food ; it is thought to be responsible for the astringency of many foods and beverages. To investigate the interaction, two-dimensional 'H-NMR studies have been carried out on the binding of a representative polyphenol, pentagalloyl glucose, to two synthetic peptides (19 and 22 residues in length) that are typical of the repeat sequence of mouse salivary proline-rich protein MP5. Intermolecular nuclear Overhauser effects and chemical shift changes show that the main binding sites on the peptides are proline residues together with the preceding amide bond and amino acid. The interaction is principally a hydrophobic association between a galloyl ring and the pyrrolidine ring face containing the Ca proton, but secondary hydrogen-bonding effects help to stabilise the complex. Very similar interactions are seen for both peptides. The conformation of the peptides remains extended on binding. The chemical shift changes seen for many of the peptide protons can be fitted to a simple bindmg curve with dissociation constant of around 40 mM, but some protons show evidence of cooperative binding involving several galloyl groups. Higher concentrations of pentagalloyl glucose lead to a reduced off-rate from the complex and eventual precipitation which implies that precipitation is caused by a kinetic competition between aggregation and dissociation of the complex.Polyphenols (vegetable tannins) are a major constituent of plants, including many that are consumed widely by humans. They are present in foods (e.g. sorghum, millet, fruit, berries, cocoa), beverages (e.g. coffee, tea, beer, wine, cider), folk medicines and herbal remehes. Polyphenols are charactensed by a multiplicity of phenolic groups and have molecular masses in the range 500-5000Da. They have been classified into two groups: the hydrolysable tannins, which are esters, usually with D-glucose, of gallic acid and its derivatives, and the condensed tannins (proanthocyanidins) which are oligomers of the flavan-3-01 skeleton, e.g. epicatechin [l]. Their biological effects are wide-ranging and include inhibition of gut enzymes, inhibition of non-haem iron absorption, influencing the taste and reducing the nutritional value of food, oesophageal cancer, and the effect of astringency, i.e. a feeling of extreme dryness, puckeriness and constriction Abbreviations. PRP, proline-rich protein; Gall,Glc, 1,2,3,4,6-penta-U-galloyl-/I-D-glucopyranose; (C2H3)2S0, (Z&)dimethyl sulphoxide ; ROESY, two-dimensional rotating-frame nuclear Overhauser effect spectroscopy ; TOCSY, two-dimensional total correlation spectroscopy ; NOESY, two-dimensional nuclear Overhauser effect spectroscopy; AS-, maximum chemical shift change; ROE, rotating frame nuclear Overhauser effect; 35HN,. three-bond coupling constant between NH and CaH; AS/AT, chemical shift temperature coefficient; dm, sequential NOE conn...

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“…Production of salivary PRPs is constitutive in many mammals, including man, but can be induced either by isoprenaline [2] or by diets rich in tannins in some species such as rat [3]. The salivary PRPs contain an N-terminal sequence followed by between 5 and 15 repeats of an approximately 18-residue sequence which is almost totally comprised of proline, glutamine and glycine residues and contains at least one basic amino acid [4].…”

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confidence: 99%

Conformational study of a salivary proline‐rich protein repeat sequence

Murray¹,

Williamson²

1994

European Journal of Biochemistry

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Salivary proline-rich proteins have a repetitive primary structure particularly rich in the amino acids proline, glutamine and glycine. One of the biological roles of these proteins is to bind and precipitate polyphenols (vegetable tannins) present in the diet (e.g. tea, coffee, fruit, chocolate) neutralising their harmful actions which include nutritional loss, inhibition of gut enzymes and oesophageal cancer. Two peptides overlapping in sequence, corresponding to the mouse salivary proline-rich protein MP5 repeat sequence : QGPPPQGGPQQRPPQPGNQ and GPQQRPPQPGNQQGPPPQGGPQ have been synthesised and studied in H,0/(2H,)dimethyl sulphoxide (9 : 1, by vol.) using 'H-NMR spectroscopy. Low-temperature far-ultraviolet CD spectroscopy and NMR conformational parameters indicate that the peptides adopt an extended random coil conformation in solution. There is no evidence for a defined polyproline type I1 helix in the peptides, despite the high proline content. NMR data show that the trans-proline isomer predominates to at least 90%.The salivary proline-rich proteins (PRPs) form a major part of the protein content of saliva, constituting up to 70% of the protein in parotid saliva [l]. Production of salivary PRPs is constitutive in many mammals, including man, but can be induced either by isoprenaline [2] or by diets rich in tannins in some species such as rat [3]. The salivary PRPs contain an N-terminal sequence followed by between 5 and 15 repeats of an approximately 18-residue sequence which is almost totally comprised of proline, glutamine and glycine residues and contains at least one basic amino acid [4]. Salivary PRPs have been divided into three categories: acidic and basic (which are distinguished by the nature of the Nterminal region) and glycosylated PRPs.A number of functions have been suggested for the salivary PRPs. The N-terminal regions of acidic PRPs bind to the surface of teeth and are involved in calcium and hydroxyapatite homeostasis and dental pellicle formation [5]. Glycosylated PRPs bind and agglutinate oral bacteria, which is probably mediated by the carbohydrate moiety of the PRPs [6]. When attached to the tooth surface, this bacterial binding ability may be a contributory factor in dental caries. The major function of the extensive proline-rich repeat region of the salivary PRPs appears to be binding to vegetable tannins (polyphenols) present in the diet [7-91. The tannins have a variety of harmful effects, ranging from reducing the nutri- tional value of food to causing oesophageal cancer [lo]; it is thought that the salivary PRPs function by forming insoluble complexes with tannins, so that they can pass harmlessly through the body.The aim of the work described in this and the subsequent paper [ l l ] is to investigate the secondary structure of salivary PRPs and their interaction with a model tannin, as a first step in arriving at an understanding of the molecular mechanisms governing salivary PRP/tannin binding and precipitation. Two peptides were selected for investigation, based on the conse...

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Basic proline‐rich proteins of murine parotid glands

Cited by 10 publications

References 38 publications

Electron microscopic immunocytochemical localization of proline-rich proteins in normal mouse parotid salivary glands

Electron microscopic immunocytochemical localization of proline-rich proteins in normal mouse parotid salivary glands

Study of the interaction between salivary proline‐rich proteins and a polyphenol by ¹H‐NMR spectroscopy

Conformational study of a salivary proline‐rich protein repeat sequence

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Basic proline‐rich proteins of murine parotid glands

Cited by 10 publications

References 38 publications

Electron microscopic immunocytochemical localization of proline-rich proteins in normal mouse parotid salivary glands

Electron microscopic immunocytochemical localization of proline-rich proteins in normal mouse parotid salivary glands

Study of the interaction between salivary proline‐rich proteins and a polyphenol by 1H‐NMR spectroscopy

Conformational study of a salivary proline‐rich protein repeat sequence

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Study of the interaction between salivary proline‐rich proteins and a polyphenol by ¹H‐NMR spectroscopy