Search

Factors related to the concentrations of IgA, IgG and albumin (Alb) in human saliva were studied. Saliva specimens that were strongly positive for the occult blood test contained much more Alb than negative specimens. The concentrations of IgA and IgG in the saliva specimens showed no clear associations with the results of the occult blood test. Although associations were found among the concentrations of individual proteins (IgA, IgG and Alb) in saliva specimens, no association was found between the concentration of these proteins and the DMF (decayed, missing and filled teeth) and PMA (papillary, marginal and attached gingival) indexes. The concentrations and ratios of these proteins were almost the same in saliva specimens from both sexes. The ratios of IgA/Alb and IgG/Alb among those aged less than 20 years old were significantly lower than in older subjects (probability < 0.001). We also found relatively low IgA/Alb value among those 45 years old or older. The ratios of these proteins in saliva stains did not change remarkably after storage for 18 weeks.

Saliva, which contributes to maintaining health in the oral environment, is affected by the physiological functions of the organism and their condition. Dental caries and periodontosis, both of which are oral diseases with frequent occurrence, require the presence of bacteria to occur. SIgA (secretory IgA), an immune globulin that is found in large quantities in substances secreted during salivation, has an antibacterial action. Thus, in conducting a basic investigation on the relationship between these factors, the author investigated what effect the speed of saliva secretion, a physiological factor of the saliva component, has on the SIgA value. Results showed that, regarding the relationship between the salivary SIgA value and the speed of salivary secretion, a negative correlation exists although this is weak in terms of relevance. The fact that the correlation displayed a tendency toward scattering indicates a need to pay attention when measuring the elements in the saliva to those factors that evidently have an effect on the composition of the saliva.

Changes in the concentrations of ions (K+, Cl-, Na+), total protein, amylase activity and flow rate of parotid saliva were observed by tongue stimulation with 3% tartaric acid various intervals in a subject after about one hour rest. The results may be summarized as follows: 1) After about one hour rest state, the values of each item were K+: 42-56 mEq/l, Cl-: 8-28 mEq/l, Na+: 1-10 mEq/l, total protein: 5.7-11 mg/ml, amylase activity: 2-6.5 x 10(3)U/ml and flow rate: 0.03-0.05 ml/min. 2) The changes were classified into two groups based on the recovery from peak to rest values. One group showed short recovery times (Cl-: 20 min., Na+: 8 min. and flow rate: 2 min.) and the other group had rather longer recovery times (K+: 40 min., total protein: 55 min. and amylase activity: 40 min.). The differences between these two groups were clear when the stimulus intervals were 30 sec. to 5 min. 3) When the tongue was stimulated every 15 sec. all items showed first responses, after that, the all values except the flow rate remained unchanged. 4) Different values in ions and protein concentrations and amylase activity were observed when the flow rate was similar before and after stimulation. 5) The recovery time of the responses of protein concentration and amylase activity to stimulation was about one hour, and a rest period of more than one hour is necessary to analyze the concentration of total protein and amylase activity in parotid saliva.

We have been studied the characteristics of protein components in gingival crevicular fluid (GCF) with isoelectric focusing technique. The purpose of this study was to investigate the relationship between those proteins and clinical findings such as Gingival Index (Loe & Sillness), Pocket depth, Plaque Index (Quigley & Hein), Gingival Bleeding Index and Bone Index. GCF, serum and mixed saliva collected from the same subject were analyzed, and following results were obtained. The patterns of protein bands in GCF were similar to those in serum but different from mixed saliva, and the pI of main protein band of GCF and serum were 4.9. No apparent difference was observed on the patterns between clinically healthy gingiva and those received periodontal disease. Protein patterns were compared with the before mentioned clinical findings and GCF volume. Main protein bands were observed on cathode side (pI 8.0-9.0) at the patterns against Gingival Index: 0-1 or greater than 2, Gingival Bleeding Index: + or -, Pocket Depth: 0-1 or greater than 2 and Bone Index: 1 or greater than 3. It was suggested that the study of the proteins on cathode side is important.

During our studies on the active moiety of parotin, we succeeded in purifying MP-parotin (MW = 130000) and parotin-subunit (MW = 45000) from crude parotin. Furthermore, AA-1 (MW = 9100) was isolated after the tryptic cleavage of the parotin-subunit. AA-1 was the smallest unit ever obtained which had serum Ca-decreasing activity and circulating leucocyte-increasing activity together with the nature of specific localization in bone. Therefore, AA-1 was considered to contain the essential residues for parotin activity in its structure. Since crude parotin was also known to show andromimetic action, these parotin components reduced in size were assayed in this regard. A daily injection of MP-parotin (500 micrograms/kg), parotin-subunit (20 micrograms/kg) or AA-1 (20 micrograms/kg) was administered subcutaneously for two weeks to male rats weighing 200 approximately 220 g. The dynamics of the testicular biosynthesis of testosterone from 3H-pregnenolone and 14C-progesterone via delta 4, delta 5-pathway and the transition of delta 5 to delta 4-steroids were measured. MP-parotin and the parotin-subunit stimulated the pathway of pregnenolone----17-hydroxypregnenolone----dehydroepiandrosterone---- androstenedione----testosterone and resulted in the elevation of serum testosterone levels. Cyclic AMP levels in the testicular homogenate and the motility of epididymal sperm were also increased by the treatment. On the other hand, AA-1 showed no effect on these parameters. It was concluded that andromimetic activity, which is involved in MP-parotin or parotin subunit was independent of parotin activity on the bone tissue.

In order to elucidate whether Salivary Protein C and salivary peptide P-C, originally isolated from human saliva were present in tissues other than those of the salivary glands or not, an indirect immunofluorescence technique using both antisera against salivary peptide P-C and Salivary Protein C was carried out on human salivary glands and the human respiratory tract. As salivary peptide P-C-like immunoreactivity was detected in the serous cells of salivary glands by previous immunohistochemical study, the human respiratory tract was closed as model tissue, since tracheal and bronchial glands in the human respiratory tract consist of mucous and serous cells. Furthermore, to check whether salivary peptide P-C is a fragment of Salivary Protein C or not, the same immunohistochemical study was undertaken on the serial sections of salivary glands and the respiratory tract. Salivary peptide P-C and Salivary Protein C-like immunoreactivities were present in the serous cells of human salivary glands and in tracheal and bronchial cells. Furthermore, the same serous cells were immunostained with antisera against salivary peptide P-C, with antisera against Salivary Protein C and with antisera against Salivary Protein C preabsorbed with salivary peptide P-C. In view of the fact that the full sequence of salivary peptide P-C is identical to the COOH terminal 44 amino acid residues of Salivary Protein C, it was suggested that the full sequence of Salivary Protein C was present in the serous cells of human salivary glands and in those of tracheal and bronchial glands and that salivary peptide P-C was a fragment of Salivary Protein C.(ABSTRACT TRUNCATED AT 250 WORDS)

In order to clarify the intracellular localization of salivary peptide P-C like immunoreactivity in the human pancreatic B-cells, an immuno-electronmicroscopical study using protein A-gold technique was carried out on the human foetal pancreas. Salivary peptide P-C like immunoreactivity was present in some of insulin secretory granules while insulin like immunoreactivity was found in all insulin secretory granules. The finding suggested that new substance in addition to insulin and its precursor was present in the insulin secretory granules of the human pancreatic B-cells. Furthermore, the finding seemed to explain the previous study that development of salivary peptide'P-C like immunoreactivity in the foetal pancreatic B-cells was immature in compared to that in the human adult pancreatic B-cells. In addition, to examine whether or not, salivary peptide P-C like immunoreactivity in the human pancreatic B-cells is Salivary Protein C, an indirect immunofluorescence technique using three kinds of antisera against salivary peptide P-C, Salivary Protein C and salivary peptide P-B, and using their antigens was undertaken on the adult pancrease. From the results of the study, it was thought that salivary peptide P-C like immunoreactivity in the human pancreas was neither Salivary Protein C itself, nor salivary peptide P-B itself, but was either salivary peptide P-C itself or unknown substance which had the common antigenic determinant with salivary peptide P-C, P-B and Salivary Protein C, since salivary peptide P-C like immunoreactivity in the human pancreas disappeared in the sections in which P-C antisera preincubated with each of salivary peptide P-C, P-B and Salivary Protein C were used as the primary antisera. Thus, although new substance was present in the insulin secretory granules of the human pancreatic B-cells, its pathophysiological role remained to be elucidated.

It had been reported by authors that salivary gland hormone, parotin, was composed with subunit (parotin-subunit) which showed molecular weight of 45,000, and that parotin-subunit had rabbit serum calcium decreasing activity and the cross reactivity with rabbit anti parotin serum. In the present report, in order to study physiological chemistry of parotin-subunit, the influence of parotin-subunit on serum Ca and 45Ca levels relating to calcium metabolism, the distribution of 131I-parotin-subunit, the effect of parotin-subunit, on adenyl cyclase-cyclicAMP system, the anabolic action, C-terminal amino acid sequence and sugar component of parotin-subunit were investigated. The results are summarized as follows: 1) The decrease of rabbit serum Ca after injection of parotin-subunit was related to change of Ca in stable bone, but not to inhibition of bone resorption. 2) A high concentrated localization of radioactivity of 131I-parotin-subunit was found in liver, kidney and spleen, and as much as 60% of administrated radioactivity was localized in liver at 5 min after the injection. The retention of radioactivity was found in testis, seminal vesicle, prostate, parotid gland and submaxillary gland. 3) Cyclic AMP level increased significantly in metaphysial bone, submaxillary gland and plasma after administration of parotin-subunit but in other organs with localized much radioactivities, the level did not changed. Parotin-subunit activated adenyl cyclase of particular fraction of metaphysial bone. 4) The C-terminal amino acid of parotin-subunit was Leu, and its C-terminal amino acid sequence was -Val-Ser-Ala-Thr- Leu-OH by digestion of carboxypeptidase A. 5) Parotin-subunit included 3.3% of sugar which consisted of amino sugar and uronic acid.