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Details on Person Histatins (HTNs) is a family of small histidine-rich peptide...

Class:Id	Summation:6807151
_displayName	Histatins (HTNs) is a family of small histidine-rich peptide...
_timestamp	2016-02-20 01:03:39
created	[InstanceEdit:6807178] Shamovsky, Veronica, 2015-10-29
literatureReference	[LiteratureReference:6807160] A cascade of 24 histatins (histatin 3 fragments) in human saliva. Suggestions for a pre-secretory sequential cleavage pathway [LiteratureReference:6807174] Characterization of histatin 5 with respect to amphipathicity, hydrophobicity, and effects on cell and mitochondrial membrane integrity excludes a candidacidal mechanism of pore formation [LiteratureReference:6807163] Histatin-derived monomeric and dimeric synthetic peptides show strong bactericidal activity towards multidrug-resistant Staphylococcus aureus in vivo [LiteratureReference:6807146] Histatins, a novel family of histidine-rich proteins in human parotid secretion. Isolation, characterization, primary structure, and fungistatic effects on Candida albicans [LiteratureReference:6807155] Salivary histatin as an inhibitor of a protease produced by the oral bacterium Bacteroides gingivalis [LiteratureReference:6807172] Structural relationship between human salivary histatins [LiteratureReference:6807201] Synthetic histatin analogues with broad-spectrum antimicrobial activity [LiteratureReference:6807157] The effects of histatin-derived basic antimicrobial peptides on oral biofilms [LiteratureReference:6807180] The assessment of sIgA, histatin-5, and lactoperoxidase levels in saliva of adolescents with dental caries [LiteratureReference:6807158] Human antimicrobial peptides: defensins, cathelicidins and histatins [LiteratureReference:6807179] Human salivary histatin-5 exerts potent fungicidal activity against Cryptococcus neoformans [LiteratureReference:8861782] Growth-inhibitory and bactericidal effects of human parotid salivary histidine-rich polypeptides on Streptococcus mutans [LiteratureReference:8861781] Selective effects of histidine-rich polypeptides on the aggregation and viability of Streptococcus mutans and Streptococcus sanguis [LiteratureReference:8861767] Inhibitory effects of human salivary histatins and lysozyme on coaggregation between Porphyromonas gingivalis and Streptococcus mitis [LiteratureReference:8861775] P-113D, an antimicrobial peptide active against Pseudomonas aeruginosa, retains activity in the presence of sputum from cystic fibrosis patients [LiteratureReference:8861763] Inhibitory effect of synthetic histatin 5 on leukotoxin from Actinobacillus actinomycetemcomitans [LiteratureReference:8861771] In vitro activity of the histatin derivative P-113 against multidrug-resistant pathogens responsible for pneumonia in immunocompromised patients
modified	[InstanceEdit:8861796] Shamovsky, Veronica, 2016-02-20
text	Histatins (HTNs) is a family of small histidine-rich peptides (18-28 mol%) that present in the saliva and secreted by parotid, sub-mandibular and sub-lingual salivary glands (Oppenheim FG et al. 1988; Troxler RF 1990; Gornowicz A et al. 2014). The members of HTN family are structurally related peptides of which histatin 1 and 3 are full-length proteins encoded by closely related loci of two distinct genes, HTN1 and HTN3 (Oppenheim FG et al. 1988; Troxler RF 1990; Sabatini LM et al 1993). The smaller peptides are generated by proteolytic cleavage of parent HTN1 and HTN3 proteins by salivary proteases during secretion (Troxler RF 1990; Castagnola M et al. 2004). HTNs exhibited antibacterial activity in vitro against various bacteria, including S. mutans, P. gingivalis, A. actinomycetemcomitans, P. aeruginosa and St. aureus (MacKay BJ et al. 1984; Murakami Y et al. 1991; Payne JB et al. 1991; Nishikata MH et al. 1991; Sajjan US et al. 2001; Murakami Y et al. 2002; Giacometti A et al. 2005; Welling MM et al. 2007). HTNs were also active against complex mixtures of bacteria, such as those present in saliva and plaque (Helmerhorst EJ et al. 1999). The antibacterial activity of HTNs is thought to rely on electrostatic interactions of cationic HTNs with anionic phospholipids, such as phosphatidylglycerol and cardiolipin on the bacterial cell surface (De Smet K & Contreras R 2005). HTNs have also been shown to possess a fungicidal activity (Oppenheim FG et al. 1988; Troxler RF 1990). HTN5 (a product of HTN3 gene) is the most potent among all histatin family members with regard to its antifungal activity against C.albicans and C.neoformans (Xu T et al. 1991; Tsai H & Bobek LA 1997; Helmerhorst EJ et al. 2001).
(summation)	[Reaction:6807144] HTN1,HTN3 or HTN5 binds the bacterial anionic surface [Homo sapiens]
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