We have known for over 30 years that minoxidil stimulates hair growth, yet our understanding of its mechanism of action on the hair follicle is very limited. In animal studies, topical minoxidil shortens telogen, causing premature entry of resting hair follicles into anagen, and it probably has a similar action in humans. Minoxidil may also cause prolongation of anagen and increases hair follicle size. Orally administered minoxidil lowers blood pressure by relaxing vascular smooth muscle through the action of its sulphated metabolite, minoxidil sulphate, as an opener of sarcolemmal KATP channels. There is some evidence that the stimulatory effect of minoxidil on hair growth is also due to the opening of potassium channels by minoxidil sulphate, but this idea has been difficult to prove and to date there has been no clear demonstration that KATP channels are expressed in the hair follicle. A number of in vitro effects of minoxidil have been described in monocultures of various skin and hair follicle cell types including stimulation of cell proliferation, inhibition of collagen synthesis, and stimulation of vascular endothelial growth factor and prostaglandin synthesis. Some or all of these effects may be relevant to hair growth, but the application of results obtained in cell culture studies to the complex biology of the hair follicle is uncertain. In this article we review the current state of knowledge on the mode of action of minoxidil on hair growth and indicate lines of future research.

A protein, which can agglutinate a Streptococcus mutans serotype c strain, was isolated from parotid saliva by affinity adsorption of the salivary agglutinin to the microorganism followed by a desorption with a 10 mM phosphate buffer. The agglutinin was subjected to preparative ultracentrifugation, gel filtration, and ultrafiltration. The native purified agglutinin is active only in the presence of Ca. Polyacrylamide gel electrophoresis, analytical centrifugation, and analyses of amino acids and carbohydrates showed that the native agglutinin was a fucose-rich glycoprotein with a carbohydrate content of 45 % and with a molecular weight of at least 5 x lo6. After sodium dodecyl sulphate treatment the molecular weight was 4.4 x 10'. There was a low content of proline and a high content of aspartic acid, serine and threonine. The concentration of agglutinin in parotid saliva is less than 0.5 % of total protein. It has high biological activity: 0.1 pg agglutinin causes a rapid aggregation of approximately lo8 bacteria.The compositions of secretions produced by different exocrine cells in various mucosal tissues are remarkably alike. The characteristics are the presence of potentially antibacterial systems, like secretory IgA, lactoperoxidase, lactoferrin and lysozyme, as well as of high-molecular-weight glycoproteins, which traditionally have been ascribed the role of lubricants. However, it has become evident that some of the highmolecular-weight glycoproteins also carry antibacterial properties [I, 21. Like secretory IgA, and under some conditions lysozyme also, they serve as bacterial agglutinins.The high-molecular-weight glycoproteins bind to surface receptor sites on microorganisms and under certain conditions they cause aggregation of microorganisms [2]. Aggregation or mere coating of microorganisms by salivary bacteriaaggregating glycoproteins or secretory IgA is suggested to contribute to the elimination of microorganisms from the oral cavity by blocking attachment sites on the bacterial surface. It has been suggested [I] that similarity in chemical structure between soluble glycoproteins and epithelial surface receptors, which recognize bacteria, would give rise to an intersepting mechanism, which prevents the bacteria from becoming attached to the epithelial surface.On the other hand, agglutinins, incorporated in the glycoprotein coat of the mucosa or in the acquired pellicle of the tooth surface, may favour attachment of bacteria [I, 3, 41. The balance between clearance and attachment of bacteria results in a selection of the bacteria colonizing the different surfaces [l -3, 51. It is, therefore, of prime interest to study the selecting mechanisms leading to retention of pathogenic microorganisms.In the present study we have isolated and characterized a glycoprotein which agglutinates a serotype c strain of Streptococcus mutans. Serotype c strains of S. mutam are recognized as cariogenic (for review see [6] significance of and some characteristics for the agglutinin specific for these strains have been de...

This study investigated the effect of a surface active compound, delmopinol, on plaque formation and established plaque in vitro, on the bacterial acid production from glucose and on the total viable bacterial counts in saliva. The antimicrobial effect was compared with that of chlorhexidine. The plaque-inhibiting effect was evaluated in an artificial mouth system, and the effect on bacterial acid production was registered as a decrease of pH in bacterial suspensions with various concentrations of delmopinol. It was shown that delmopinol is able to prevent plaque formation, to dissolve established plaque in vitro, and that it has 5-125 times higher minimum inhibitory concentrations than chlorhexidine. Saliva samples collected 1 min after rinsing with delmopinol showed on differences in the total number of bacteria in saliva as compared with controls. It was also shown that the bacterial acid production from glucose was reduced successively with increasing concentrations of delmopinol. The results indicate that delmopinol might be as effective as chlorhexidine against plaque formation and that delmopinol is capable of penetrating established plaque, thus promoting a more effective mechanical cleansing.

Delmopinol is a new surface active anti-plaque agent that has demonstrated a low antimicrobial effect in vitro. By use of a vitality staining technique, the antimicrobial effect on bacteria in plaque samples was tested after rinsing with delmopinol or chlorhexidine. 6 healthy male subjects volunteered to rinse for 4 days using a double-blind cross-over study design with a wash-out period between the rinsing regimens. No oral hygiene measures were allowed during the test periods and each test period started with a professional tooth cleaning procedure 2 days before the start of rinsing to allow for plaque formation. Rinsing was performed with 0.2% delmopinol hydrochloride or 0.2% chlorhexidine digluconate 2 x a day. Small samples of plaque were collected from the buccal surfaces of premolars and 1st molars before the first rinse on day 1 and then before and 1, 2, 4, 7, and 24 h after the last rinse on the 4th day. The plaque samples were immediately stained with propidium iodide and fluorescein diacetate to visualize dead and vital microorganisms respectively. The vitality of the microflora was evaluated using a fluorescence microscope. The baseline vitality values were 91% for chlorhexidine and 86% for delmopinol. At day 4, the plaque vitality for chlorhexidine was approximately 40% up to 4 h and 50% at 7 h and 60% at 24 h after the last rinse. Corresponding values for plaque vitality after delmopinol rinsing were between 70 and 80% on all sampling occasions.(ABSTRACT TRUNCATED AT 250 WORDS)

Previous studies have suggested that both secretory immunoglobulin A (sIgA) and various nonimmunoglobulin salivary glycoproteins are capable of agglutinating a variety of bacteria. The present study was designed to compare the nature of the agglutinins for Streptococcus mutans and Salmonella typhimurium in parotid saliva and colostrum. S. mutans was aggregated by saliva and colostrum, whereas S. typhimurium was aggregated only by saliva as detected by a spectrophotometric method. The principal salivary agglutinin for both S. mutans and S. typhimurium was calcium dependent and could be desorbed in phosphate-buffered saline (pH 6.8). In contrast, the colostral agglutinin was calcium independent and not readily desorbed. The agglutinin activities of saliva and colostrum for S. mutans were additive, suggesting independent target sites on the bacterial surface. The agglutinin activity of colostrum was totally associated with sIgA as was suggested by blocking of the agglutinating activity with anti-a-chain serum and the absence of blocking with an antibody specific for salivary agglutinin. Interestingly, anti-a-chain serum removed all agglutinating activity from saliva, but not from the phosphate-buffered saline-desorbed agglutinin. Dialysis of parotid saliva against 0.1 M disodium EDTA eliminated the agglutinin blocking activity of anti-a,-chain serum but not that of the antiagglutinin antibody. The ability of anti-a-chain serum to block agglutination of the EDTA-dialyzed saliva could be restored by the addition of calcium chloride, suggesting that sIgA and salivary agglutinin are associated through a calcium-mediated interaction. These results indicate that bacterial agglutinating activity of colostrum, as detected spectrophotometrically, is mediated by sIgA, and that of saliva is mainly dependent upon a calcium-dependent nonimmunoglobulin agglutinin. The agglutinating activities of sIgA and parotid agglutinin seem to be additive, and their calcium-dependent association may favor the enhancement of their respective activities.