Hydroxyproline content determines the denaturation temperature of chick tendon collagen

Rosenbloom, Joel; Harsch, Margaret; Jimenez, Sergio A.

doi:10.1016/0003-9861(73)90539-0

Cited by 215 publications

(97 citation statements)

References 21 publications

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“…It is known that the presence of high hydroxyproline residues is related to higher denaturation temperatures [43] and an increase of the stability of the triple helix of collagen due to the hydrogen bonds between the polypeptides [44]. We observed a higher content of hydroxyproline in codfish them in salmon.…”

Section: Amino Acid Content Of Collagen Extractssupporting

confidence: 44%

Cosmetic Potential of Marine Fish Skin Collagen

et al. 2017

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Many cosmetic formulations have collagen as a major component because of its significant benefits as a natural humectant and moisturizer. This industry is constantly looking for innovative, sustainable, and truly efficacious products, so marine collagen based formulations are arising as promising alternatives. A solid description and characterization of this protein is fundamental to guarantee the highest quality of each batch. In the present study, we present an extensive characterization of marine-derived collagen extracted from salmon and codfish skins, targeting its inclusion as component in cosmetic formulations. Chemical and physical characterizations were performed using several techniques such as sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE), Fourier Transformation Infrared (FTIR) spectroscopy rheology, circular dichroism, X-ray diffraction, humidity uptake, and a biological assessment of the extracts regarding their irritant potential. The results showed an isolation of type I collagen with high purity but with some structural and chemical differences between sources. Collagen demonstrated a good capacity to retain water, thus being suitable for dermal applications as a moisturizer. A topical exposure of collagen in a human reconstructed dermis, as well as the analysis of molecular markers for irritation and inflammation, exhibited no irritant potential. Thus, the isolation of collagen from fish skins for inclusion in dermocosmetic applications may constitute a sustainable and low-cost platform for the biotechnological valorization of fish by-products.

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Section: Amino Acid Content Of Collagen Extractssupporting

confidence: 44%

Cosmetic Potential of Marine Fish Skin Collagen

et al. 2017

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“…With Lapiere and Nusgens, we demonstrated a lack of proline hydroxylation in hydroxyproline, probably due to a defect of the prolyl-hydroxylase activity producing an abundant proportion of underhydroxylated collagen (Chantraine et al, 1976b). On the other hand, we know that thermic stability of underhydroxylated collagen is less than normal hydroxylated collagen (Rosenbloom et at., 1973). In these patients, the urinary hydroxyproline excretion is also largely increased and might represent the cata bolism of such hydroxylated collagen.…”

Section: Discussionmentioning

confidence: 99%

Actual concept of osteoporosis in paraplegia

Chantraine

1978

Spinal Cord

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Abstract.The osteoporosis which appears in paraplegics below the neurological lesion has been studied in 100 patients with the following parameters: quantitative X-rays, urinary hydroxyproline excretion, kinetic study of calcium metabolism by 45Ca, serum phosphorus and calcium, parathormone and calcitonin radio-immunoassay, quantitative histology, density fractionation of bone and amino-acid composition of fractionated bone analysis.All our results show that the important bone resorption occurring very early in the paraplegia is immediately followed by an increase of the bone repair. This osteoporosis below the neurological lesion in paraplegia represents an unbalance between the synthesis and the resorption of bone which possesses a large degree of activity. Furthermore, we demonstrated that the collagen of this bone is underhydroxylated. Following the quanti tative X-rays and intraosseous phlebography results we have considered the aetiopatho genesis of this osteoporosis. It seems that vascular modifications due to the lesion of the autonomic nervous system play an important role and furthermore we believe that immobilisation represents only a minor factor in the aetiology of this osteoporosis.IN paraplegia an osteoporosis appears very early after the spinal cord lesion and is located below this lesion.The aetiopathogenesis of this osteoporosis is not known although the disuse factor has been advanced. On the other hand, the angiographic investigations made by Galibert (1959) and Rossier et al. (1973) have shown that modifications existed below the spinal lesion since the beginning of the paraplegia. Benassy et al. (1963) reported changes in the arterial and venous blood gases (02 saturation, pH, pC02, pOz) consisting in a marked arterialisation of lower limb venous blood. Thus, these modifications evolve in the same direction as the angiographic ones. These blood flow modifications could play a role in the pathogenesis of this porosis. Vasomotor paralysis, a consequence of the orthosympathic system damage, provokes a slowdown of the intraosseous circulation. Arterio-venous shunts also give an increase of the venous pressure. This situation leads to an increase of the intraosseous medullary pressure. Trueta (I964, 1968) and Dhem (1973) have shown the consequence of intraosseous circulation decrease on the cellular differentiation.Stimulated by these data and the fact that the autonomic nervous system CANS) might play a role in this osteoporosis, we have reviewed the problem and investigated the following parameters: X-rays; intramedullary pressure of bone; urinary hydroxyproline excretion; kinetic study of calcium metabolism by 45Ca; urine calcium; serum calcium and phosphorus; serum calcitonin and parathormone; quantitative histological study; density fractionation of bone and amino-acid composition of fractionated bone analysis.We will briefly summarise the methods and the results of those investigations which have been reported elsewhere.

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“…AsA is essential for hydroxylation of the proline residues of procollagen molecule in rER (Kivirikko and Myllyla, 1985;Schwarz et al, 1987), and stimulates collagen secretion through its effect on proline hydroxylation (Blanck and Peterkofsky, 1975). The hydroxylation appears to increase the thermal stability of collagen (Berg and Prockop, 1973), and to be required for the formation of the triple helix of procollagen molecules Ramaley et al, 1973;Rosenbloom and Harsch, 1973), which may be necessary for normal secretion of procollagen (Uitto et al, 1972;Jimenez et al, 1973;Ramaley et al, 1973;Rosenbloom and Harsch, 1973). In osteoblasts, as in fibroblasts, type I collagen precursors are processed along the rough endoplasmic reticulum-Golgi-secretory granule pathway (Leblond, 1989).…”

Section: Osteoblasts and Osteoclastsmentioning

confidence: 99%

Morphological influence of ascorbic acid deficiency on endochondral ossification in osteogenic disorder Shionogi rat

Sakamoto

Takano

2002

Anat. Rec.

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The influences of chronic deficiency of L-ascorbic acid (AsA) on the differentiation of osteo-chondrogenic cells and the process of endochondral ossification were examined in the mandibular condyle and the tibial epiphysis and metaphysis by using Osteogenic Disorder Shionogi (ODS) rats that bear an inborn deficiency of L-gulonolactone oxidase. Weanling male rats were kept on an AsA-free diet for up to 4 weeks, until the symptoms of scurvy became evident. The tibiae and condylar processes of scorbutic rats displayed undersized and distorted profiles with thin cortical and scanty cancellous bones. In these scorbutic bones, the osteoblasts showed characteristic expanded round profiles of rough endoplasmic reticulum, and lay on the bone surface where the osteoid layer was missing. Trabeculae formation was deadlocked, although calcification of the cartilage matrix proceeded in both types of bone. Scorbutic condylar cartilage showed severe disorganization of cell zones, such as unusual thickening of the calcification zone, whereas the tibial cartilage showed no particular alterations (except for a moderately decreased population of chondrocytes). In condylar cartilage, hypertrophic chondrocytes were encased in a thickened calcification zone, and groups of nonhypertrophic chondrocytes occasionally formed cell nests surrounded by a metachromatic matrix in the hypertrophic cell zone. These results indicate that during endochondral ossification, chronic AsA deficiency depresses osteoblast function and disturbs the differentiation pathway of chondrocytes. The influence of scurvy on mandibular condyle cartilage is different from that on articular and epiphyseal cartilage of the tibia, suggesting that AsA plays different roles in endochondral ossification in the mandibular condyle and long bones. Anat Rec 268: 93-104, 2002.

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Hydroxyproline content determines the denaturation temperature of chick tendon collagen

Cited by 215 publications

References 21 publications

Cosmetic Potential of Marine Fish Skin Collagen

Cosmetic Potential of Marine Fish Skin Collagen

Actual concept of osteoporosis in paraplegia

Morphological influence of ascorbic acid deficiency on endochondral ossification in osteogenic disorder Shionogi rat

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