Determination of the human salivary peptides histatins 1, 3, 5 and statherin by high-performance liquid chromatography and by diode-array detection

Castagnola, Massimo; Congiu, D.; Denotti, Gloria; Nunzio, A. Di; Fadda, Maria Benedetta; Melis, S.; Messana, Irene; Misiti, Francesco; Murtas, R.; Olianas, Alessandra; Piras, Vincenzo; Pittau, A.; Puddu, G.

doi:10.1016/s0378-4347(00)00466-7

Cited by 36 publications

(44 citation statements)

References 28 publications

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“…Sample Collection and Treatment-Whole human saliva was collected between 2 and 4 p.m. from four normal adult informed volunteers according to a standard protocol (11). Collection time was standardized in order to reduce concentration variability connected to circadian rhythms of secretion.…”

Section: Methodsmentioning

confidence: 99%

A Cascade of 24 Histatins (Histatin 3 Fragments) in Human Saliva

Castagnola

Inzitari²,

Rossetti³

et al. 2004

Journal of Biological Chemistry

102

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The systematic search by tandem mass spectrometry of human saliva from four different subjects, of 136 possible fragments originated from histatin 3, allowed the detection of 24 different peptides. They include, with the exception of histatin 4, all the known histatin 3 fragments, namely histatins 5-12 and the peptides corresponding to 15-24, 26 -32, 29 -32 residues, and 13 new fragments corresponding to 1-11, 1-12, 1-13, 5-13, 6 -11, 6 -13, 7-11, 7-12, 7-13, 14 -24, 14 -25, 15-25, and 28 -32 residues of histatin 3. On the contrary, none of 119 possible fragments of histatin 1, including histatin 2, was detected. The results suggest that the genesis of histatin 3-related peptides, being under the principal action of trypsin-like activities, is probably not a random process but rather follows a sequential fragmentation pathway. Lack of detection of C-terminal fragments, with the exception of 26 -32, 28 -32, and 29 -32 fragments, suggested that arginine 25 should be the first cleavage site, generating histatin 6 and 26 -32 fragments. The genesis of 28 -32 and 29 -32 fragments and histatin 5 should implicate a subsequent exo-protease action. Similarly, lack of detection of fragments having Lys-5 and Arg-6 at the N terminus and Arg-25 at the C terminus strongly suggested that sequences KRKF (11-14 residues) and AKR (4 -6 residues) should be the second and the third cleavage sites, respectively. Lys-17 and Arg-22 are not cleaved at all.Histatins are a class of salivary peptides probably present only in higher primates (1), deriving their name from the high histidine content (2, 3). The powerful antifungal action of this class of peptides stimulated intense investigations concerning their properties, activity, structure, and secretion (4). Until now, only two human genes, HTN1 (HIS1) and HTN2 (HIS2), localized on chromosome 4q13, have been recognized as responsible for their synthesis (1, 5). The products of these two genes are histatin 1 and histatin 3, respectively. The former is a peptide of 38 amino acids, phosphorylated at Ser-2, whereas the latter, 32 amino acid long with a sequence very similar to histatin 1, is not phosphorylated. Many other peptides of this family have been identified in human saliva, all sharing a sequence common to the two parent peptides. Although different classifications have been proposed, the current preferred nomenclature derives from the study of Troxler et al. (6), who identified in human saliva a peptide corresponding to the C-terminal 26 residues of histatin 1, named histatin 2, and nine peptides, all related to the sequence of histatin 3 and named histatins 4 -12. Except for histatin 2, the other minor histatins likely originated by proteolytic cleavages from histatin 3. Among them, histatin 5, showing a sequence identical to the first 24 amino acids of histatin 3, represents the major fragment because it is present in human saliva at a higher concentration than the other fragments. Moreover, it appears to display the highest specific activity against Candida albicans species wit...

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Section: Methodsmentioning

confidence: 99%

A Cascade of 24 Histatins (Histatin 3 Fragments) in Human Saliva

Castagnola

Inzitari²,

Rossetti³

et al. 2004

Journal of Biological Chemistry

102

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“…1) biologically important in living systems, 20 as an Different analytical methods have been developed to quantify cysteamine and there metabolites in biological matrices (urine, human salivary, blood), pharmaceutical preparation and foods. The most commonly employed techniques are the chromatographic such as liquid chromatography (LC), [28][29][30][31][32][33] and gas chromatography (GC). 34 Many of these methods require several manipulation steps which are time-consuming and use significant amounts of solvent, and they require sophisticated instrumentation and training.…”

Section: -19mentioning

confidence: 99%

Electrochemical Investigation of Cysteamine at Carbon Fiber Microdisk Electrode

El-Hallag

Al‐Youbi

Obaid

et al. 2011

J. Chil. Chem. Soc.

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The electrooxidation of cysteamine compound was carried out using convolutive cyclic voltammetry, linear sweep voltammetry and chronoamperomtry techniques at a carbon fiber microdisk electrode in 0. 1 M perchloric acid. The electrooxidation potential (E 0'' ) of cysteamine occurs at + 0.921 V. The mechanistic pathway of electrooxidation process at carbon fiber microelectrode is loss of 1 electron per molecule. The electrode process is controlled mainly by diffusion. The chemical and electrochemical parameters of the investigated system were determined experimentally and verified theoretically via digital simulation method.

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“…The most abundant identified proteins are proline-rich-proteins (PRPs; 60 %), -amylase and cystatins (20 %). The last group consists mainly of histatins, mucins and statherins [12]. Salivary proteins are mainly secreted by the parotid, submandibular and sublingual glands, but microorganisms, blood and mucosal tissue also contribute to its composition [13,14].…”

Section: Introductionmentioning

confidence: 99%

Analysis of the Human Salivary Peptidome by Differential Peptide Display and LC-MS/MS Overview Sequencing

Yondre¹,

Tammen²,

Hess³

et al. 2008

TOPROTJ

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Abstract:In recent years interest in the characterization of the human salivary proteome has increased in order to explore its diagnostic potential. Major constituents of human saliva are highly polymorphic proteins that may have biological roles in oral lubrication and protection, e.g. proline-rich proteins (PRPs), statherins, histatins and cystatins. Interestingly, many of theses proteins are rapidly degraded in the oral cavity by host-and bacteria-or viral-derived proteases. Thus, comprehensive analysis of peptides up to 15 kDa (peptidomics) of whole saliva may yield basic information on proteolytic patterns. By employing a LC-ESI-MS/MS approach a total of 107 native peptides from 17 distinct protein precursors was identified from whole saliva. Subsequently the catalog of peptides was used to analyze inter-individual differences in saliva samples from four donors by differential peptide display technology. Genetic polymorphisms were found in peptides from the PRB4M_HUMAN and PROL4_HUMAN precursors. Analysis of the proposed N-and C-termini of the peptides revealed frequent cleavage after Lys or Arg which is characteristic for salivary kallikrein enzymes. Furthermore, we highlight the cleavage motif Gln/Gly in the PRP-C precursor, which suggests a new proteolytic pattern in saliva.

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Determination of the human salivary peptides histatins 1, 3, 5 and statherin by high-performance liquid chromatography and by diode-array detection

Cited by 36 publications

References 28 publications

A Cascade of 24 Histatins (Histatin 3 Fragments) in Human Saliva

A Cascade of 24 Histatins (Histatin 3 Fragments) in Human Saliva

Electrochemical Investigation of Cysteamine at Carbon Fiber Microdisk Electrode

Analysis of the Human Salivary Peptidome by Differential Peptide Display and LC-MS/MS Overview Sequencing

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