New insights into salivary lactate dehydrogenase of human subjects.

Lactate dehydrogenase (LDH) is a ubiquitous enzyme that plays a significant role in the clinical diagnosis of pathologic processes. The purpose of the current study was to examine LDH activity and isoenzyme profile of whole saliva and to compare it with the LDH activity of salivary glands and plasma before and after exposure to cigarette smoke (CS). The range of LDH activity in whole saliva at rest was 360 to 430 U/L. The mean +/- SEM of LDH activity in parotid and submandibular/sublingual salivary secretions was 41.3 +/- 19.2 U/L and 77.5 +/- 30.4 U/L, respectively, which implied that 75% of the whole-saliva LDH originated from an extra-salivary gland source. The profile of salivary LDH isoenzymes was found to have an entirely different pattern from that found in plasma, similar to that found in oral epithelium, indicating that the major source of salivary LDH is probably the oral epithelium-shedding cells. Therefore, salivary LDH may be evaluated for possible oral mucosal pathologies in a manner similar to that used for evaluating other tissue pathologies--such as those in heart, muscle, or liver--that can be detected in plasma. Exposure of whole saliva to CS in vitro resulted in a 41% reduction in LDH activity. However, CS exposure had no effect on LDH activity in plasma. Whole saliva, in contrast to plasma, contains redox-active metal ions such as iron and copper that may enhance LDH loss of activity. Therefore we conclude that whole saliva in the presence of CS becomes a potent protein-modifying agent that can destroy some of its endogenous components.