Further Studies of Salivary Polymorphisms in the Japanese Population

Tsuchida, Shuichi; Ikemoto, Shigenori

doi:10.1159/000153836

Cited by 3 publications

(3 citation statements)

References 14 publications

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“…Similarly, the proteolytically derived peptides of histatin 3-1 that are shown in Figure 1 are renamed histatins 4-1, 5-1, and 6-1. A possible histatin "4-like" derivative of histatin 3-2 is also identified as histatin 4-2. are present in all samples and are not polymorphic (Azen, 1972;Pals and Pronk, 1979;Pronk et al, 1984;Tsuchida and Ikemoto, 1989). Histatin 3-1 and proteolytically derived polypeptides, histatins 4-1, 5-1, and 6-1 , are present in the HIS2l homozygous and HIS2'-HIS22 heterozygous samples.…”

Section: Nomenclaturementioning

confidence: 96%

“…We here report the nucleotide and derived protein sequences of the HIS22 allele. HIS2' codes for the variant histatin 3-2 protein (formerly termed Pb c) that is found primarily and in high frequencies in Black populations (Azen, 1972;Pals and Pronk, 1979;Pronk et al, 1984;Tsuchida and Ikemoto, 1989). Two single nucleotide mutations (separated by only 18 bp) were found in exon 5 of the HIS2' allele, which could fully explain the electrophoretic differences between the variant histatin 3-2 protein and the common allelic histatin 3-1 protein (a product of the HIS2l allele).…”

Section: Introductionmentioning

confidence: 99%

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Two coding change mutations in theHIS22 allele characterize the salivary histatin 3-2 protein variant

Sabatini

Azen

1994

Hum. Mutat.

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The decoded amino acid sequence of a salivary protein variant, histatin 3-2 (formerly termed Pb c), that is found primarily and in high frequency in Black populations was determined by genomic PCR and direct sequencing of the HIS2(2) allele. Two different mutations that cause coding changes were found in exon 5. The first mutation is a single nucleotide (T-->A) substitution that causes a TAT (Tyr)-->TAA (Stop) change at residue 28. This premature stop mutation results in a 27 amino acid histatin 3-2 protein, which is 5 amino acids smaller than the common histatin 3-1 allelic protein (a product of the HIS2(1) allele). The second mutation, a single nucleotide (G-->A) substitution (located only 19 nucleotides upstream of the first mutation) causes a CGA (Arg)-->CAA (Gln) change at residue 22, which eliminates a proteolytic cleavage site. These two mutations explain the differences in electrophoretic patterns of HIS2(1) versus HIS2(2) coded histatin peptides and may have functional significance. Each mutation alters a different DNA restriction site, and this provides a DNA-based test for the mutations. This test should greatly simplify population and family studies of this protein polymorphism, since the saliva-based test is considerably more problematic. Elucidation here of the derived protein sequence of the variant histatin 3-2 protein may also facilitate functional studies.

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Section: Nomenclaturementioning

confidence: 96%

Section: Introductionmentioning

confidence: 99%

Two coding change mutations in theHIS22 allele characterize the salivary histatin 3-2 protein variant

Sabatini

Azen

1994

Hum. Mutat.

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“…The expression of these two alleles is autosomal-codominant (Azen, 1972(Azen, , 1973. The HIS22 allele is found primarily, and in high frequencies, in Black populations (Azen, 1972;Peters et al, 1977;Pals and Pronk, 1979;Pronk et al, 1984;Tsuchida and Ikemoto, 1989 HISI and part of the HIS21 genes by screening a genomic DNA library made from HIS22 homozygous and HIS21 homozygous individuals, respectively. The putative genomic fragment containing the HIS22 gene was also isolated but was not sequenced.…”

Section: (I) Introductionmentioning

confidence: 99%

Human Salivary Histatins: Promising Anti-Fungal Therapeutic Agents

Tsai

Bobek

1998

Critical Reviews in Oral Biology & Medicine

142

115

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Histatins constitute a group of small, cationic multifunctional proteins present in the saliva of human and some nonhuman primates. The most significant function of histatins may be their anti-fungal activity against Candida albicans and Cryptococcus neoformans. Histatins have been extensively studied at both the protein and gene levels. The structure-function relationship of histatins with respect to their candidacidal activity has also been studied by means of recombinant histatin variants, as well as by chemically synthesized histatin fragments. The mechanism of histatins' action on Candida albicans is not clear, but it appears to be different from that of azole-based anti-fungal drugs which interrupt ergosterol synthesis. During the past 20 years, fungal infections have become more prevalent as a result of the emergence of AIDS, as well as, paradoxically, modern medical advances. The toxicity of current anti-fungal medicine, the emergence of drug-resistant strains, and the availability of only a few types of antifungal agents are the major disadvantages of current anti-fungal therapy. Therefore, the importance of the search for new, broadspectrum anti-fungals with little or no toxicity cannot be overemphasized. The following properties make histatins promising antifungal therapeutic agents: (1) They have little or no toxicity; (2) they possess high cidal activities against azole-resistant fungal species and most of the fungal species tested; and (3) their candidacidal activity is similar to that of azole-based antifungals.Current research efforts focus on the development of improved histatins with enhanced cidal activity and stability, and of suitable and effective histatin delivery systems. These and other approaches may help to outpace the growing list of drug-resistant and opportunistic fungi causing life-threatening, disseminating diseases. The histatins with improved protective properties may also be used as components of artificial saliva for patients with salivary dysfunction.

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