Kininogen and Kallikrein in Saliva of Periodontally-diseased Subjects

Sakamoto, Wataru; Fukuda, Hiroshi; Nishikaze, O

doi:10.1177/00220345810600011101

Cited by 10 publications

(7 citation statements)

References 8 publications

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“…Kininogen levels in saliva from patients with periodontal disease were higher than what was observed in saliva from periodontally healthy patients. Kallikrein activity, however, was approximately the same in the two groups (Sakamoto et al 1981). In another study, an increase in salivary kallikrein and a decrease in salivary kininase activity were found in association with increased severity of periodontal disease (Picarelli et al 1986).…”

Section: Enzymesmentioning

confidence: 89%

Analysis of saliva for periodontal diagnosis

Kaufman

Lamster

2000

J Clinic Periodontology

335

293

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A number of markers show promise as sensitive measures of disease and the effectiveness of therapy. At this time, host-derived enzymes and other inflammatory mediators orginating from the gingival crevice appear to hold the greatest promise as salivary diagnostic tests for periodontal disease. Longer-term longitudinal studies, however, are required to establish the relationship between specific markers and progression of periodontal disease. Furthermore, analysis of saliva may offer a cost-effective approach to assessment of periodontal disease in large populations.

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Section: Enzymesmentioning

confidence: 89%

Analysis of saliva for periodontal diagnosis

Kaufman

Lamster

2000

J Clinic Periodontology

335

293

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“…There is also precedent, however, for the existence of LMWK extravascularly. Thus, LMWK has been detected in human parotid and submaxillary salivas (21) and has been localized by immunofluorescence to the distal nephron of the kidney (10). To date, however, there has been no report of intact HMWK being detected in the absence of plasma.…”

Section: Discussionmentioning

confidence: 99%

“…Allergic individuals (n = 6) and nonallergic controls (n = 5) between the ages of 21 and 45 yr were recruited. They gave informed consent before being included in the study.…”

Section: Subjectsmentioning

confidence: 99%

Influx of kininogens into nasal secretions after antigen challenge of allergic individuals.

et al. 1985

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We have recently demonstrated that kinins are generated in vivo after nasal challenge with antigen of allergic, but not nonallergic, individuals. The present study was undertaken as a first step in determining the mechanism(s) of kinin formation during the allergic reaction and was directed towards establishing the availability and origin of kininogens in nasal secretions. Allergic individuals (n = 6) and nonallergic controls (n = 5) were challenged with antigen; and by using specific radioimmunoassays, nasal washes, obtained before and after challenge, were assayed for high molecular weight kininogen (HMWK), total kininogen (TK), albumin, and kinins. Dramatic increases in HMWK (1,730±510 ng/ml), TK (3,810±1035 ng/ml), kinin (9.46±1.75 ng/ml), and albumin (0.85±0.2 mg/ml) were observed after challenge of allergic individuals which correlated (P < 0.001) with increases in histamine and N-a-tosyl-Larginine methyl esterase activity and with the onset of clinical symptoms. For nonallergic individuals, levels of kininogens, albumin, and all mediators after antigen challenge were not different from base line. Linear regression analysis revealed excellent correlations (P < 0.001 in each case) between increases in HMWK, TK, kinin, and albumin during antigen titration experiments and between the time courses of appearance and disappearance of HMWK, TK, kinin, and albumin after antigen challenge. Gel filtration revealed no evidence of degradation products of kininogens in nasal washes. For each allergic individual the ratio of HMWK/TK in postchallenge nasal washes was similar to the ratio of these two proteins in the same individual's plasma. These data suggest that, during the allergic reaction, there is an increase in vascular permeability and a transudation of kininogens from plasma into nasal secretions, where they can provide substrate for kinin-forming enzymes.

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“…It is not known at the present time whether salivary kallikrein has either a homeostatic or pathophysiologic function in the oral cavity. In this regard, Sakamoto et al (1981) did not observe a significant difference in kallikrein levels in saliva obtained from patients with periodontal disease and from periodontally-healthy individuals.…”

Section: Introductionmentioning

confidence: 55%

Levels of Glandular Kallikrein in Whole Saliva Obtained from Patients with Solid Tumors Remote from the Oral Cavity

et al. 1986

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Glandular kallikrein activity in whole saliva was determined in 16 patients with malignant tumors distant from the oral cavity and in an equal number of healthy control subjects of similar age and sex distribution. The level of glandular kallikrein was significantly greater in saliva obtained from the patients with solid tumours as determined with a tripeptide nitro-anilide substrate, D-Val-Leu-ArgpNA. A basis for the higher levels of glandular kallikrein in saliva obtained from the solid tumor patients has not been established, nor is it possible to establish a role for glandular kallikrein in the pathogenesis of malignant disease. The higher level of glandular kallikrein observed in whole saliva obtained from patients with solid tumors suggests the need for further investigation of the role of kallikrein in malignant disease and the usefulness of salivary measurements of this enzyme as a reflection of systemic changes.

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Kininogen and Kallikrein in Saliva of Periodontally-diseased Subjects

Cited by 10 publications

References 8 publications

Analysis of saliva for periodontal diagnosis

Analysis of saliva for periodontal diagnosis

Influx of kininogens into nasal secretions after antigen challenge of allergic individuals.

Levels of Glandular Kallikrein in Whole Saliva Obtained from Patients with Solid Tumors Remote from the Oral Cavity

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