HYACOLL TYPE II COLLAGEN

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Collagen

HEALTH-PROMOTING EFFECTS OF
HYACOLL TYPE II COLLAGEN

Collagen is a generic term for a large group of extracellular proteins, so-called cell-binding proteins, which are very common in humans and animals. In humans, collagen is the main connective tissue protein and accounts for approximately one third of the total protein mass. The properties of collagen related to its high thermostability, mechanical strength, elasticity and ability to interact with various biomolecules [1] make it the main fibrillar building block of skin, bone, tendons and cartilage [2]. This fact is used in the pharmaceutical and cosmetic industries, where this protein is an ingredient in many pharmaceuticals, dietary supplements and cosmetics.

Synkol - the company is certified and listed by the General Veterinary Inspectorate in accordance with Regulation ( EC) 853/2004 in Section XV- Collagen.

Knee joints

Structure of tendons

Movement system

Back pain

Skin, hair and nails

TYPE II COLLAGEN
KEY INFORMATION

1.

Collagen structure

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The amino acid sequence of collagen is unusual and is distinguished by its very regular arrangement. Characteristically, there are large amounts of glycine (Gly), proline (Pro) and two amino acids formed by post-translational hydroxylation of proline and lysine in the endoplasmic reticulum: hydroxyproline (Hyp) and hydroxylysine (Hyl) [2; 5]. Glycine is almost always present as every third amino acid radical, and proline together with hydroxyproline make up about 22 % of the primary structure of collagen [1; 4]. In addition, the aforementioned amino acid radicals occur in the sequence of each α-chain of the protein in regular repeats: Gly-Pro-Y or Gly-X-Hyp (X; Y – any amino acid radical). A particularly common one is the triad: Gly-Pro-Hyp (accounts for 10.5%) [1; 4], which is characteristic of only a few fibrillar protein types [4]. The regularity of the triads in the sequence is the cause of the interactions between the three left-handed α collagen chains, causing them to spontaneously twist and form units called tropocollagen (Fig. 1). Therefore, collagen molecules are multi-domain proteins [1-3].

Schemat budowy tropokolagenu z charakterystyczną triadą: glicyna – prolina – hydroksyprolina.
Figure 1 Schematic of tropocollagen structure with the characteristic triad: glycine - proline - hydroxyproline. Modified from [4].

The resulting right-handed coild-coil helix of tropocollagen is approximately 1.5 nm thick with a 0.3 nm pitch, and each chain is over 1,400 amino acids long [4]. Spontaneous aggregation of tropocollagen leads to the formation of filamentous structures and collagen fibres sequentially [1] (Fig. 2). Stabilisation of the collagen helix takes place through covalent and hydrogen bonds formed by hydroxyproline and hydroxylysine [1-2].

Schemat organizacji włókien kolagenowych.
Figure 2 Schematic of collagen fibre organisation. Modified from [6].

2.

Collagen classification

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More than twenty types of collagen are currently known. The extensive classification is related to the widespread occurrence of this protein in many tissue types and its diverse functions [1; 5; 7]. Table I provides basic information on the structure, locations and pathologies associated with abnormalities of known collagen types [5; 7].

Pattern Type Construction Occurrence Pathology
I Fibrillar α1[I]2α2[I] Abundantly and commonly found in: dermis, bones, ligaments and tendons Ehlers-Danlos syndrome, osteoporosis
II Fibrillar α1[II]3 Cartilage, vitreous body Osteoarthrosis, chondrodysplasia
III Fibrillar α1[III]3 Skin, blood vessels, intestine Ehlers-Danlos syndrome, aneurysm
IV Mesh α1[IV]2α2[IV] α3[IV]α4[IV]α5[IV]α5[IV]2α6[IV] Basement membrane Alporta syndrome
V Fibrillar α1[V]3
α1[V]2α2[V] α1[V]α2[V]α3[V] 		Commonly found in: bone, dermis, cornea, placenta. It complements collagen I Ehlers-Danlos syndrome
VI Mesh α1[VI]α2[VI]α3[VI] α1[VI]α2[VI]α4[VI] Commonly found in: bone, cartilage, cornea, dermis Bethlem myopathy
VII Fibrillar, anchor α1[VII]2α2[VII] Dermis, bladder Acquired vesicular separation of the epidermis
VIII Mesh α1[VIII]3
α2[VIII]3
α1[VIII]2α2[VIII] 		Commonly found in: dermis, brain, heart and kidneys Corneal endothelial dystrophy
IX FACITs α1[IX]α2[IX]α3[IX] Cartilage, cornea, vitreous body Osteoarthrosis, epiphyseal dysplasia
X Mesh α1[X]3 Cartilage Chondrodysplasia
XI Fibrillar α1[XI]α2[XI]α3[XI] Cartilage, intervertebral disc Chondrodysplasia, osteoarthrosis
XII FACITs α1[XII]3 Dermis, tendons -
XIII MACITs - Endothelial cells, dermis, eyes, heart -
XIV FACITs α1[XIV]3 Commonly found in: bones, dermis and cartilage -
XV Composed of multiple domains, with gaps in triple helixes - Capillaries, testes, kidneys, heart -
XVI FACITs - Dermis, kidneys -
XVII MACITs α1[XVII]3 Haemidesmosomes in epithelial cells Generalised, atrophic, blistering separation of the epidermis
XVIII Composed of multiple domains, with gaps in triple helixes - Basement membrane, liver Knobloch syndrome
XIX FACITs - Basement membrane -
XX FACITs - Cornea -
XXI FACITs - Stomach, kidneys -
XXII FACITs - Nodes -
XXIII MACITs - Heart, retina -
XXIV Fibrillar - Bones, cornea -
XXV MACITs - Brain, heart, testicles Amyloid plaque formation???
XXVI FACITs - Ovaries, testicles -
XXVII Fibrillar - Cartilage -
XXVIII - - Dermis, sciatic nerves Neurodegenerative diseases???
Table I. Classification of collagens found in vertebrates. FACITs - collagen bound to fibrils with interrupted triple helixes; MACITs - collagen bound to the cell membrane with interrupted triple helixes. Based on [1; 5].

3.

Properties of collagen and its uses

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Due to its widespread occurrence in various types of tissue and its characteristics of high thermostability, deformability and mechanical strength, collagen has many applications.
In the food industry, collagen is primarily used in the production of gelatine, which is an ingredient in many food, pharmaceutical and cosmetic products, as well as the casings used in the creation of cured meats.
Collagen has been used very widely as a dietary supplement to strengthen joints and improve the elasticity and resistance of skin and nails. In addition, it is used in medicine - in orthopaedics, dentistry, in the production of skin substitutes and in burn surgery, where it is designed to accelerate skin regeneration. Collagen is used as a natural, hypoallergenic wound dressing, which has antimicrobial properties to protect against wound infection [9]. According to some research groups [10], oral administration of type II collagen alleviates the symptoms of rheumatoid arthritis. The study was conducted on a group of 60 patients and a reduction in swelling and joint tenderness was observed in those receiving the study preparation compared with the placebo group. Disease remission was achieved in four patients. There were also no side effects of the proposed therapy [10]. Other studies indicate [11] that oral intake of low molecular weight collagen type II hydrolysate, chondroitin sulphate and hyaluronic acid reduces the discomfort associated with arthritis and osteoarthritis. The product is well tolerated and its intake increased joint mobility in the study patients compared to the placebo group [11].
Unfortunately, from the age of 25 onwards, the body's collagen reserves gradually decrease [12]. This results in weakened bones and joints, weakened hair and also loss of skin firmness and the appearance of wrinkles [13]. Because the skin ageing process involves the conversion of soluble collagen to an insoluble form and a lack of renewal, collagen has found applications in plastic surgery and aesthetic medicine, where it is used as a dermal filler to combat wrinkles (Figure 3). Collagen is also an ingredient in many cosmetics, advertised as anti-wrinkle products.

Zmiany zachodzące w budowie skóry podczas jej procesu starzenia.
Fig. 3 Changes in skin structure during the ageing process. Based on [14].

4.

Literature

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  1. Collagen structure and stability. M. D. Shoulders and R. T. Raines Annu Rev Biochem. (2009);78:929–958
  2. Collagens at a glance. K. E. Kadler, C. Baldock, J. Bella and R. P. Boot-Handford Journal of Cell Science (2007);120:1955–1958
  3. Collagen family of proteins. M. Van Der Rest and R. Garrone The FASEB Journal (1991);5:2814–2823
  4. http://www.ebi.ac.uk/interpro/potm/2009_1/Protein_focus_2009_01-Collagen.html
  5. Collagen as a double-edged sword in tumor progression. M. Fang, J. Yuan, C. Peng and Y. Li Tumor Biol. (2014);35:2871–2882
  6. http://sp.uconn.edu/~bi102vc/1102fall10/Images/collagen.jpg
  7. Collagens–structure, function, and biosynthesis. K. Gelse, E. Poschl and T. Aigner Advanced Drug Delivery Reviews (2003);55:1531–1546
  8. Collagen fibril morphology and organization: Implications for force transmission in ligament and tendon. P. P. Provenzano , R. Vanderby Jr. Matrix Biology (2006);25:71–84
  9. Collagen dressing versus conventional dressings in burn and chronic wounds: a retrospective study. O. Singh, S. S. Gupta, M. Soni, S. Moses, S. Shukla and R. K. Mathur Journal of Cutaneous and Aesthetic Surgery (2011);1:12–16
  10. Effects of Oral Administration of Type II Collagen on Rheumatoid Arthritis. D. Trentham, R. Dynesius-Trentham, J. Orav, D. Combitchi, C. Lorenzo, K. Sewell, D. Hafler and H. Weiner Science (1993);(5119):1727–1730.
  11. Effect of the novel low molecular weight hydrolyzed chicken sternal cartilage extract, BioCell Collagen, on improving osteoarthritis-related symptoms: A randomized, double-blind, placebo-controlled trial. A. Schauss, J. Stenehjem, J. Park, J. Endres and A. Clewell Journal of Agricultural and Food Chemistry (2012);(16):4096–101.
  12. Decreased Collagen Production in Chronologically Aged Skin. Varani J., Dame M., Rittie L. et al. Am J Pathol. (2006);168(6):1861-1868.
  13. Natural and Sun-Induced Aging of Human Skin. Rittie L., Fisher G. Cold Spring Harb Perspect Med. (2015);5(1):a015370-a015370.
  14. https://dermestetic.pl/poradnik/zmarszczki/zabiegi-anti-aging-na-kazdy-wiek

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