COLLAGEN: STRUCTURE, METABOLISM, PRODUCTION AND INDUSTRIAL APPLICATION

This review presents the current scientific literature data about structure, properties, and functions of collagen, which is known as one of the most abundant human and animal proteins. The building of collagen molecule from the primary structure to submolecular formations, the main stages of its synthesis and biodegradation are briefly described. The information about collagen diversity, its features and metabolic ways in various tissues, including skin, tendons, bones, etc. is presented. The problems of pathologies caused by collagen synthesis and breakdown disorders as well as age-related changes in collagen properties and their causes are discussed. A comparative analysis of the advantages and disadvantages of collagen and its derivatives obtaining from various sources (animals, marine, and recombinant) is given. The most productive methods for collagen extraction from various tissues are shown. The concept of collagen hydrolysis conditions influence on the physicochemical properties and biological activity of the obtained products is described. The applications of collagen and its products in various fields of industrial activity, such as pharmaceutical, cosmetic industry and medicine, are discussed. Further prospective directions of fundamental and applied investigations in this area of research are outlined.

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Age-related changes in collagen synthesis and degradation in rat tissues. Importance of degradation of newly synthesized collagen in regulating collagen production

Biochemical Journal ◽

10.1042/bj2760307 ◽

1991 ◽

Vol 276 (2) ◽

pp. 307-313 ◽

Cited By ~ 120

Author(s):

P K Mays ◽

R J McAnulty ◽

J S Campa ◽

G J Laurent

Keyword(s):

Skeletal Muscle ◽

Collagen Synthesis ◽

Rat Tissues ◽

Age Related ◽

Developmental Growth ◽

Cross Links ◽

Fractional Synthesis ◽

Synthesis And Degradation ◽

Age Related Changes

During developmental growth, collagens are believed to be continuously deposited into an extracellular matrix which is increasingly stabilized by the formation of covalent cross-links throughout life. However, the age-related changes in rates of synthetic and degradative processes are less well understood. In the present study we measured rates of collagen synthesis in vivo using a flooding dose of unlabelled proline given with [14C]proline and determining production of hydroxy[14C]proline. Degradation of newly synthesized collagen was estimated from the amount of free hydroxy [14C]proline in tissues 30 min after injection. Collagen fractional synthesis rates ranged from about 5%/day in skeletal muscle to 20%/day in hearts of rats aged 1 month. At 15 months of age, collagen fractional synthesis rates had decreased markedly in lung and skin, but in skeletal muscle and heart, rates were unchanged. At 24 months of age, synthesis rates had decreased by at least 10-fold in all tissues, compared with rates at 1 month. The proportion of newly synthesized collagen degraded ranged from 6.4 +/- 0.4% in skin to 61.6 +/- 5.0% in heart at 1 month of age. During aging the proportion degraded increased in all tissues to maximal values at 15 months, ranging from 56 +/- 7% in skin to 96 +/- 1% in heart. These data suggest that there are marked age-related changes in rates of collagen metabolism. They also indicate that synthesis is active even in old animals, where the bulk of collagens produced are destined to be degraded.

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