Facial Tightening With an Advanced 4-MHz Monopolar Radiofrequency Device
November 2012 | Volume 11 | Issue 11 | Original Article | 1288 | Copyright © November 2012
Background:Over the past 10 years, radiofrequency (RF) technology has been utilized for nonablative treatments for the treatment of
rhytides and skin laxity. This manuscript reviews the scientific background of collagen synthesis in vivo and in response to RF energy as
well as a clinical study of 17 patients receiving a series of facial treatments with a 4-MHz monopolar RF (Pellevé,Ellman International,
Inc, Oceanside, NY). Clinical methods, results, and a review of the literature for RF aesthetic treatments of the face are presented.
Methods:Seventeen patients were treated in one site with 6 total treatments scheduled as follows:1 session was performed every
15 days for 2 consecutive sessions, 1 session every month for 2 consecutive sessions, and 1 session every 2 months for 2 consecutive
sessions. Both the treating physician and the patients via live viewing and comparison with baseline photographs performed assessment
of results. Results are reported as averages across the 17 patients.
Results: Two weeks after the first treatment,patients noted an overall average of 25% to 30% improvement. Just before the last or
sixth treatment, there was an average of 50% improvement noted by the physician, with patients ranking an average self-improvement
of 48%. The treating physician rated average improvement of 46% compared with baseline,whereas the patients ranked average
improvement of 30% compared with baseline at 1 year after treatment was initiated (6 months after the final treatment).Patients find
this treatment to be very well tolerated, with minimal to no discomfort and no downtime or significant side effects.
Conclusions: The Pellevé 4-MHz monopolar RF device is effective, safe, and very well tolerated for treating laxity, texture, and wrinkles
of the skin without complication or discomfort. Evidence in the literature supports the scientific mechanism of action of acute collagen
modification and continued neocollagenesis observed with the system. In this cohort, patients maintain approximately 50% improvement
on average at 6 months and a 30% to 50% improvement 1 year after beginning the treatments, 6 months after completion.
Skin is more than 15% of body weight1 and is primarily
composed of types I and III collagen. Type I collagen is
80% to 85% of the dermal collagen. Type III collagen is primarily
observed in the papillary dermis and makes up 10% to
15% of the dermal collagen.
The amount of soluble collagen declines with age, while the insoluble
collagen increases; this change is caused by the increase
in stable multichain cross-linking and leads to a loss of skin elasticity.2 The added stable cross-links also produce an increase in
collagen tensile strength with age.3 The amount of new collagen
production decreases with age as a result of fibroblast collapse.4 The collagen content of the dermis also decreases as a result
of increased proteinases that degrade collagen.5These changes
lead to decreased collagen turnover, thickening of collagen fibers,
more disorganized bundles, and thinning of the dermis.
The epidermis also thins, and there is a loss of the rete ridges,
which normally extend downward between the dermal papillae.
The ratio of type I to type III collagen decreases because of the
selective reduction of type I collagen.6
The exposure to ultraviolet (UV) radiation adds to these changes in
the skin, resulting in accumulation of elastotic material in the papillary
dermis and middermis; this process is termed solar elastosis. Exposure to UV radiation leads to activation of proteinases that
degrade existing collagen.7 Collagen synthesis is also reduced; this
may be related to fibroblast damage and protein oxidation.8
Nonablative radiofrequency (RF) treatment utilizes heat modification
of collagen for the treatment of rhytides and lax skin. As
collagen is heated, the intramolecular heat-labile bonds forming
the chain cross-links are broken, while the heat-stable intermolecular
cross-links are maintained.9 This unravels the triple helix
and shortens the molecule. Electron microscopy has shown an
increase in size of the collagen fibrils and a loss of distinct borders
among the fibrils, with some fibrils merging together.10,11 The initial effect of heating to sufficient temperature stimulates
neocollagenesis; however, if the temperature is too high, irreversible
denaturation converts the orderly crystalline structure
of collagen into the random form, gelatin. Even higher temperatures
produce necrosis, scarring, and burning.