Smoker's face describes the characteristic changes that happen to the faces of many people who smoke tobacco products. [1] [2] Smoking causes damage to the skin by depleting the skin of oxygen and nutrients. [3] The general appearance is of accelerated ageing of the face, with a characteristic pattern of facial wrinkling and sallow coloration.
A summary of a study published by the National Institutes of Health found that certain facial features appeared in about 46% of continuing smokers and 8% of former smokers who had smoked a full decade while those same features were absent in a control group of non-smokers. [4]
Matrix metalloproteinases (MMP's) are enzymes that promote breakdown of the extracellular matrix. [5] This matrix contains important nutrients and proteins like collagen, elastin, and proteoglycans. All of which are involved in skin health and structure. [6] The MMP levels in a smoker are elevated, causing over breakdown of the matrix. Therefore, those essential proteins and antioxidants, like Vitamin C, also begin to disappear. [7] [8] This leaves the skin empty and depleted of its structure, causing hollowness and sagging of the skin. [3]
Nearby blood vessels can become damaged by the tobacco extracts and then constrict, reducing flow of oxygen to the face. [3] Oxygen breakdown without circulation causes reactive oxygen species, or ROS and free radicals, to build up. Then skin, now deplete of antioxidants, cannot clean up the free radicals leaving them to build up in the tissues. [9] This eventually leads to oxidative stress. [10] [9] This is attributed to what is called extrinsic aging; known to be caused by external and environmental factors. [8] This can cause skin allergies, skin thinning, wrinkles, issues with pigmentation, cancers and more. [10] Important enzymes like glutathione peroxidase and glutathione reductase, which help clean up the extracellular matrix also become reduced. [10]
Matrix metalloproteinases (MMPs), also known as matrix metallopeptidases or matrixins, are metalloproteinases that are calcium-dependent zinc-containing endopeptidases; other family members are adamalysins, serralysins, and astacins. The MMPs belong to a larger family of proteases known as the metzincin superfamily.
Tobacco products, especially when smoked or used orally, have negative effects on human health. Researchers have addressed concerns about these effects for a long time. They have focused primarily on cigarette smoking.
Smoking is a practice in which a substance is combusted and the resulting smoke is typically inhaled to be tasted and absorbed into the bloodstream of a person. Most commonly, the substance used is the dried leaves of the tobacco plant, which have been rolled with a small rectangle of paper into an elongated cylinder called a cigarette. Other forms of smoking include the use of a smoking pipe or a bong.
Matrix metalloproteinase-9 (MMP-9), also known as 92 kDa type IV collagenase, 92 kDa gelatinase or gelatinase B (GELB), is a matrixin, a class of enzymes that belong to the zinc-metalloproteinases family involved in the degradation of the extracellular matrix. In humans the MMP9 gene encodes for a signal peptide, a propeptide, a catalytic domain with inserted three repeats of fibronectin type II domain followed by a C-terminal hemopexin-like domain.
72 kDa type IV collagenase also known as matrix metalloproteinase-2 (MMP-2) and gelatinase A is an enzyme that in humans is encoded by the MMP2 gene. The MMP2 gene is located on chromosome 16 at position 12.2.
Matrix metalloproteinase-14 is an enzyme that in humans is encoded by the MMP14 gene.
Matrilysin also known as matrix metalloproteinase-7 (MMP-7), pump-1 protease (PUMP-1), or uterine metalloproteinase is an enzyme in humans that is encoded by the MMP7 gene. The enzyme has also been known as matrin, putative metalloproteinase-1, matrix metalloproteinase pump 1, PUMP-1 proteinase, PUMP, metalloproteinase pump-1, putative metalloproteinase, MMP). Human MMP-7 has a molecular weight around 30 kDa.
Stromelysin-2 also known as matrix metalloproteinase-10 (MMP-10) or transin-2 is an enzyme that in humans is encoded by the MMP10 gene.
Matrix metalloproteinase-26 also known as matrilysin-2 and endometase is an enzyme that in humans is encoded by the MMP26 gene.
Stromelysin-3 (SL-3) also known as matrix metalloproteinase-11 (MMP-11) is an enzyme that in humans is encoded by the MMP11 gene.
Matrix metalloproteinase-25 is an enzyme that in humans is encoded by the MMP25 gene.
Matrix metalloproteinase 28 also known as epilysin is an enzyme that in humans is encoded by the MMP28 gene.
Matrix metalloproteinase-24 is an enzyme that in humans is encoded by the MMP24 gene.
Matrix metalloproteinase-20 (MMP-20) also known as enamel metalloproteinase or enamelysin is an enzyme that in humans is encoded by the MMP20 gene.
Metalloprotease inhibitors are cellular inhibitors of the Matrix metalloproteinases (MMPs). MMPs belong to a family of zinc-dependent neutral endopeptidases. These enzymes have the ability to break down connective tissue. The expression of MMPs is increased in various pathological conditions like inflammatory conditions, metabolic bone disease, to cancer invasion, metastasis and angiogenesis. Examples of diseases are periodontitis, hepatitis, glomerulonephritis, atherosclerosis, emphysema, asthma, autoimmune disorders of skin and dermal photoaging, rheumatoid arthritis, osteoarthritis, multiple sclerosis, Alzheimer's disease, chronic ulcerations, uterine involution, corneal epithelial defects, bone resorption and tumor progression and metastasis. Due to the role of MMPs in pathological conditions, inhibitors of MMPs may have therapeutic potential. Several other proteins have similar inhibitory effects, however none as effective. They might have other biological activities which have yet been fully characterised.
Matrix metalloproteinase-21 (MMP-21) is an enzyme that in humans is encoded by the MMP21 gene.
Matrix metallopeptidase 27 also known as MMP-27 is an enzyme which in humans is encoded by the MMP27 gene.
Matrix metalloproteinase 15 also known as MMP15 is an enzyme that in humans is encoded by the MMP15 gene.
Photoaging or photoageing is a term used for the characteristic changes to skin induced by chronic UVA and UVB exposure. Tretinoin is the best studied retinoid in the treatment of photoaging.
Diabetic foot ulcer is a breakdown of the skin and sometimes deeper tissues of the foot that leads to sore formation. It may occur due to a variety of mechanisms. It is thought to occur due to abnormal pressure or mechanical stress chronically applied to the foot, usually with concomitant predisposing conditions such as peripheral sensory neuropathy, peripheral motor neuropathy, autonomic neuropathy or peripheral arterial disease. It is a major complication of diabetes mellitus, and it is a type of diabetic foot disease. Secondary complications to the ulcer, such as infection of the skin or subcutaneous tissue, bone infection, gangrene or sepsis are possible, often leading to amputation.