The Role of Matrix Metalloproteinases in Human Body

Matrix Metalloproteinase enzymes (MMPs) were discovered, in 1962, by Jerome Gross and Charles M. Lapierre while studying the degradation of triple-helical collagen during the metamorphosis of a tadpole tail. The collagen was cleaved by an enzyme known as interstitial collagenase. This enzyme was first isolated from human skin in the inactive form, pro-MMP (also called MMP zymogen), in 1968. It was later found in both invertebrates and plants. In 1990, it was discovered a cysteine switch mechanism was responsible for regulating the enzyme in its inactive form. After the complete sequencing of the human genome, it was determined that twenty-four different genes encoded a set of all human MMPs. MMPs are Zn dependent proteases. MMPs have 27 types and each type has a special character. MMPs also called matrixinis [1]. MMPs play big role in morphogenesis, embryonic development, embryonic invasion to endometrium, renew extracellular matrix elements, wound healing, tissue repair, and remodeling of new tissue after myocardial infarction and MMPs also participate progression of disease such as rheumatoid arthritis, caries, cardiovascular diseases, atherosclerosis, Parkinson, Alzheimer diseases, atheroma, cancer, metastasis. All of MMPs kind is multi-domain proteins and their activities are regulated by tissue inhibitor of metalloproteinase. The prevention of the pathologies which is created by MMPs used some synthetic and naturally inhibitors This review will explain to reader attitude MMPs and some chemical and physical factor which there to being high level and low could affect to MMPs activity and synthesis as caffeine one of snake venom components, melatonin, serotonin, stress factor, E and C vitamins.

Author(s): Hafiz Hasanov, Khayala Mammadova, Firangiz Guliyeva, Ulviya Azizova and Nigar Mikailova

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