Morphometric Analysis of Collagen: a Comparative Study in Cow and Pig Skins

Kobayashi, Ataru; Takehana, Kazushige; Eerdunchaolu,; Iwasa, Kenji; Abe, Masayuki; Yamaguchi, Mamoru

doi:10.1046/j.1439-0264.1999.00196.x

Cited by 6 publications

(6 citation statements)

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“…CFI value in the CP group was significantly higher than that in the other 2 groups, as both fibril diameter and fibril density were highest in the CP group. Biochemical analysis GAG in the dermis mainly comprised HA and DS, as reported previously ( 17 ). Although the ratio of DS was higher in the CP group, no significant differences were observed between each pair of groups.…”

Section: Morphological Analysissupporting

confidence: 79%

“…All animal experiments in this study were approved by the Ethics Com-mittee of Rakuno Gakuen University. A litter of 9 healthy 66-d-old piglets (Landrace, Large White stock crossbreeds) were divided into three groups (3 piglets/ group) such that the average body weight did not differ among the groups (group 1: 41.7 Ϯ 14.2、 group 2: 43.5 Ϯ 9.6、 group 3: 45.7 Ϯ 3.1 kg, respectively), as no sex differences were observed in collagen fibrils in our previous study ( 17 ). Pigs were selected as experimental animals because their skin is used clinically as a skin substitute and because, like humans, they are omnivorous.…”

Section: Methodsmentioning

confidence: 99%

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Effects of Ingestion of Collagen Peptide on Collagen Fibrils and Glycosaminoglycans in the Dermis

Matsuda

Koyama

Hosaka

et al. 2006

J Nutr Sci Vitaminol

101

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Summary In order to investigate the effects of collagen peptide ingestion on fibroblasts and the extracellular matrix in the dermis, collagen peptide was administered orally to pigs at 0.2 g/kg body weight/d for 62 d, and its effects were compared with those of lactalbumin and water controls. Fibroblast density, and diameter and density of collagen fibrils were significantly larger in the collagen peptide group than in the lactalbumin and water control groups. The two major components of dermal glycosaminoglycans, hyaluronic acid and dermatan sulfate, which are present in the inter-fibrillar space, did not differ significantly among the three groups. However, the ratio of dermatan sulfate, which is derived from fibrilbound decorin, was largest in the collagen peptide group. These results suggest that ingestion of collagen peptide induces increased fibroblast density and enhances formation of collagen fibrils in the dermis in a protein-specific manner. Key Words collagen peptide, dermis, collagen fibril, glycosaminoglycan, electron microscopyThe skin is the largest organ in the human body and protects the body from various external insults. Skin comprises two layers, the epidermis and the dermis, consisting of stratified squamous epithelium and connective tissues, respectively. The dermis contains large amounts of extracellular matrix (ECM) components, such as collagen and glycosaminoglycans (GAG), mainly produced by fibroblasts ( 1 ). Collagen is the most abundant protein in the vertebrate body, comprising approximately 30% of the total protein. To date, over 20 types of collagen genes have been identified, and these are divided into three groups: fibrous collagen, fibrilassociated collagen and basement membrane collagen ( 2 ). In the dermis, type I collagen forms collagen fibrils that are further organized into collagen fibers in association with other types of fibrous or fibril-associated collagen ( 3 ). The size of collagen fibrils is an important factor that determines the physical nature of tissue, as collagen fibrils/fibers form the framework of the vertebrate body ( 4 ). The size of collagen fibrils varies depending on tissue type and physiological conditions ( 5 ). Their diameters are reportedly regulated, for example, by the content of collagen types III or V or other types of non-fibrous collagen. Rates of synthesis and degradation of collagen also probably determine the size of collagen fibrils ( 6 , 7 ).GAG consists of repeating two-sugar units and, with the exception of hyarulonic acid (HA), exists in tissue as proteoglycans that form covalent bonds with core proteins ( 8 ). The dermatan sulfate (DS) proteoglycan decorin is located on the surface of collagen fibrils and regulates their size ( 9 ). On the other hand, HA is highly hydrophilic and forms a gel with large amounts of water, playing a role in resisting external mechanical stresses ( 8 , 10 ). The change in the ratio of HA affects the diameter of the collagen fibrils ( 11 ). Thus, the size of collagen fibrils and the amount of GAG, such as ...

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Section: Morphological Analysissupporting

confidence: 79%

Section: Methodsmentioning

confidence: 99%

Effects of Ingestion of Collagen Peptide on Collagen Fibrils and Glycosaminoglycans in the Dermis

Matsuda

Koyama

Hosaka

et al. 2006

J Nutr Sci Vitaminol

101

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“…However, other reports give quite different values for fibril diameters in skin and tendon: 202−204 nm in diameter (ovine tendon, measured using TEM) 30 and 142−163 nm in diameter (bovine skin, measured using TEM). 43 As mentioned in the Introduction, diameters determined by TEM can vary greatly depending on the sample preparation procedures and fixation method. 31 We find that in some parts of the cross sections (not shown) of some samples, particularly the ovine leather, there is a bimodal distribution of fibril diameter.…”

Section: ■ Resultsmentioning

confidence: 99%

“…However, other reports give quite different values for fibril diameters in skin and tendon: 202–204 nm in diameter (ovine tendon, measured using TEM) and 142–163 nm in diameter (bovine skin, measured using TEM) . As mentioned in the Introduction, diameters determined by TEM can vary greatly depending on the sample preparation procedures and fixation method …”

Section: Discussionmentioning

confidence: 99%

Collagen Fibril Diameter and Leather Strength

Wells

Edmonds

Kirby

et al. 2013

J. Agric. Food Chem.

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The main structural component of leather and skin is type I collagen in the form of strong fibrils. Strength is an important property of leather, and the way in which collagen contributes to the strength is not fully understood. Synchrotronbased small angle X-ray scattering (SAXS) is used to measure the collagen fibril diameter of leather from a range of animals, including sheep and cattle, that had a range of tear strengths. SAXS data were fit to a cylinder model. The collagen fibril diameter and tear strength were found to be correlated in bovine leather (r 2 = 0.59; P = 0.009), with stronger leather having thicker fibrils. There was no correlation between orientation index, i.e., fibril alignment, and fibril diameter for this data set. Ovine leather showed no correlation between tear strength and fibril diameter, nor was there a correlation across a selection of other animal leathers. The findings presented here suggest that there may be a different structural motif in skin compared with tendon, particularly ovine skin or leather, in which the diameter of the individual fibrils contributes less to strength than fibril alignment does.

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“…This characteristic was observed in innumerable species of mammals, as for example in the dog, rats or guinea pigs (Ferry, Argentieri, & Lochner, 1995;Kazanci, Kurus, & Atasever, 2017;Schwarz, Le Roux, Schaller, & Neurand, 1979;Thomas, 2005). However, it contrast with some species in which the skin is much thicker, such as in humans, goat, horses, cows or pigs (Ferry et al, 1995;Jørgensen, Lazzarini, Pirone, Jacobsen, & Miragliotta, 2018;Kobayashi et al, 1999;Moyo, Gomes, & Erlwanger, 2018;Razvi, Suri, & Sarma, 2014;Yabuki et al, 2007).…”

Section: Discussionmentioning

confidence: 99%

Histomorphometrical study on the skin of different regions of the Caribbean common opossum (Didelphis marsupialis Linnaeus, 1758)

Mohamed

Pérez

Veiga

2020

Anat Histol Embryol

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Common opossums (Didelphis marsupialis) are found throughout the Caribbean island of Trinidad and Tobago. The present work was conducted on the fresh normal skin of 10 common opossums and aimed to provide morphometric data and a histological description of the skin in different regions of the body. In the examined regions, the skin presented a typical thin skin morphology, with numerous folds on the surface. The dermis–epidermis junction is smooth, without the occurrence of dermal papillae. The average thickness of the opossum epidermis was 19.5 µm. The cranial region of the back showed the greatest epidermal thickness, and together with the other areas of the back presented an epidermis 2–3 times thicker compared with the other areas examined. To further confirm that the skin changes in the opossum are age‐ or diet‐related, additional studies are required.

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Morphometric Analysis of Collagen: a Comparative Study in Cow and Pig Skins

Cited by 6 publications

References 0 publications

Effects of Ingestion of Collagen Peptide on Collagen Fibrils and Glycosaminoglycans in the Dermis

Effects of Ingestion of Collagen Peptide on Collagen Fibrils and Glycosaminoglycans in the Dermis

Collagen Fibril Diameter and Leather Strength

Histomorphometrical study on the skin of different regions of the Caribbean common opossum (Didelphis marsupialis Linnaeus, 1758)

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