Fibronectin (FN) is a ubiquitous extracellular matrix (ECM) glycoprotein that plays vital roles during tissue repair. The plasma form of FN circulates in the blood, and upon tissue injury, is incorporated into fibrin clots to exert effects on platelet function and to mediate hemostasis. Cellular FN is then synthesized and assembled by cells as they migrate into the clot to reconstitute damaged tissue. The assembly of FN into a complex three-dimensional matrix during physiological repair plays a key role not only as a structural scaffold, but also as a regulator of cell function during this stage of tissue repair. FN fibrillogenesis is a complex, stepwise process that is strictly regulated by a multitude of factors. During fibrosis, there is excessive deposition of ECM, of which FN is one of the major components. Aberrant FN-matrix assembly is a major contributing factor to the switch from normal tissue repair to misregulated fibrosis. Understanding the mechanisms involved in FN assembly and how these interplay with cellular, fibrotic and immune responses may reveal targets for the future development of therapies to regulate aberrant tissue-repair processes.

/pdf/plasma-and-cellular-fibronectin-distinct-and-independent-59554k8buh.pdf

Plasma and cellular fibronectin: distinct and independent functions during tissue repair

Collagen and gelatin have been widely used in the food, pharmaceutical, and cosmetic industries due to their excellent biocompatibility, easy biodegradability, and weak antigenicity. Fish collagen and gelatin are of renewed interest, owing to the safety and religious concerns of their mammalian counterparts. The structure of collagen has been studied using various modern technologies, and interpretation of the raw data should be done with caution. The structure of collagen may vary with sources and seasons, which may affect its applications and optimal extraction conditions. Numerous studies have investigated the bioactivities and biological effects of collagen, gelatin, and their hydrolysis peptides, using both in vitro and in vivo assay models. In addition to their established nutritional value as a protein source, collagen and collagen-derived products may exert various potential biological activities on cells in the extracellular matrix through the corresponding food-derived peptides after ingestion, and this might justify their applications in dietary supplements and pharmaceutical preparations. Moreover, an increasing number of novel applications have been found for collagen and gelatin. Therefore, this review covers the current understanding of the structure, bioactivities, and biological effects of collagen, gelatin, and gelatin hydrolysates as well as their most recent applications.

Collagen and gelatin.

The extracellular matrix molecule tenascin-C is highly expressed during embryonic development, tissue repair and in pathological situations such as chronic inflammation and cancer. Tenascin-C interacts with several other extracellular matrix molecules and cell-surface receptors, thus affecting tissue architecture, tissue resilience and cell responses. Tenascin-C modulates cell migration, proliferation and cellular signaling through induction of pro-inflammatory cytokines and oncogenic signaling molecules amongst other mechanisms. Given the causal role of inflammation in cancer progression, common mechanisms might be controlled by tenascin-C during both events. Drugs targeting the expression or function of tenascin-C or the tenascin-C protein itself are currently being developed and some drugs have already reached advanced clinical trials. This generates hope that increased knowledge about tenascin-C will further improve management of diseases with high tenascin-C expression such as chronic inflammation, heart failure, artheriosclerosis and cancer.

/pdf/the-role-of-tenascin-c-in-tissue-injury-and-tumorigenesis-109s5qgwlz.pdf

The role of tenascin-C in tissue injury and tumorigenesis.

In the present study, we identified several food-derived collagen peptides in human blood after oral ingestion of some gelatin hydrolysates. Healthy human volunteers ingested the gelatin hydrolysates (9.4−23 g) from porcine skin, chicken feet, and cartilage after 12 h of fasting. Negligible amounts of the peptide form of hydroxyproline (Hyp) were observed in human blood before the ingestion. After the oral ingestion, the peptide form of Hyp significantly increased and reached a maximum level (20−60 nmol/mL of plasma) after 1−2 h and then decreased to half of the maximum level at 4 h after the ingestion. Major constituents of food-derived collagen peptides in human serum and plasma were identified as Pro-Hyp. In addition, small but significant amounts of Ala-Hyp, Ala-Hyp-Gly, Pro-Hyp-Gly, Leu-Hyp, Ile-Hyp, and Phe-Hyp were contained. Keywords: Collagen; gelatin hydrolysates; Pro-Hyp; fibroblast; peptide; food; gelatin; skin; osteoporosis

Identification of Food-Derived Collagen Peptides in Human Blood after Oral Ingestion of Gelatin Hydrolysates

Leukocytes must traverse inflamed tissues to effectively control local infection. Although motility in dense tissues seems to be integrin independent and based on actomyosin-mediated protrusion and contraction, during inflammation, changes to the extracellular matrix (ECM) may necessitate distinct motility requirements. Indeed, we found that the interstitial motility of T cells was critically dependent on Arg-Gly-Asp (RGD)-binding integrins in the inflamed dermis. Inflammation-induced deposition of fibronectin was functionally linked to higher expression of integrin αV on effector CD4⁺ T cells. By intravital multiphoton imaging, we found that the motility of CD4⁺ T cells was dependent on αV expression. Selective blockade or knockdown of αV arrested T helper type 1 (TH1) cells in the inflamed tissue and attenuated local effector function. Our data demonstrate context-dependent specificity of lymphocyte movement in inflamed tissues that is essential for protective immunity.

https://ir.ymlib.yonsei.ac.kr/bitstream/22282913/158500/1/T201306251.pdf

Inflammation-induced interstitial migration of effector CD4⁺ T cells is dependent on integrin αV.

In order to investigate whether the oral ingestion of collagen peptide affects the extracellular matrix of tendon, two doses (0.2 g/kg and 1.0 g/kg body weight) were orally administered daily for 56 d to a rabbit, and both the size of collagen fibrils and the amount of glycosaminoglycans in the Achilles tendon were measured in comparison with those in a rabbit fed with a control protein, lactalbumin, or water alone. Ingestion of collagen peptide or lactalbumin induced a significant increase in collagen fibril diameter and a decrease in fibril density except for a high dose of lactalbumin compared with the water control. A histogram pattern of fibril diameter in a high dose of collagen peptide showed a peak at 160-180 nm, which was not observed in other groups. However the percentage of diameters over 200 nm was the lowest in this group but highest in the low-dose group of collagen peptide. The mean fibril diameter and mass average diameter of a high dose of collagen peptide were significantly smaller than those in a low dose. The amount of dermatan sulphate increased in the high-dose groups, while the amount of hyaluronic acid decreased in rabbits fed with collagen peptide or lactalbumin at either dose. These results suggest that the ingestion of collagen peptide affects the size of collagen fibrils and composition of glycosaminoglycans in the Achilles tendon and thus may improve the mechanical properties of the Achilles tendon.

/pdf/effects-of-ingestion-of-collagen-peptide-on-collagen-fibrils-4sjk4smton.pdf

Effects of ingestion of collagen peptide on collagen fibrils and glycosaminoglycans in Achilles tendon.

https://www.jidonline.org/article/S0022-202X(15)30572-8/pdf

Collagen of chronically inflamed skin is over-modified and upregulates secretion of matrix metalloproteinase 2 and matrix-degrading enzymes by endothelial cells and fibroblasts.

Malnutrition, particularly protein undernutrition, contributes to the occurrence of osteoporotic fracture by lowering bone mass. In this study, the effects of dietary protein on bone mineral density and body weight in protein undernutrition were compared between gelatin and milk casein. When mice were fed for 10 wk with a low protein diet containing 10(%) casein or 6% casein +4% gelatin, there was no significant difference in the final body weight between the 6% casein+4% gelatin group and the 10% casein group. In contrast, bone mineral content and bone mineral density of the femur were significantly higher in the 6% casein+4% gelatin group than in the 10% casein group. Bone mineral content and bone mineral density did not differ significantly in 14% protein groups between 14% casein and 6% casein +80% gelatin. These results suggest that gelatin has differential effects on bone mineral density and body weight in protein undernutrition.

Ingestion of gelatin has differential effect on bone mineral density and body weight in protein undernutrition.

Spatiotemporal changes of fibronectin, tenascin-C, fibulin-1, and fibulin-2 in the skin during the development of chronic contact dermatitis.

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Effects of ingestion of collagen peptide on collagen fibrils and glycosaminoglycans in Achilles tendon.

Collagen of chronically inflamed skin is over-modified and upregulates secretion of matrix metalloproteinase 2 and matrix-degrading enzymes by endothelial cells and fibroblasts.

Ingestion of gelatin has differential effect on bone mineral density and body weight in protein undernutrition.

Spatiotemporal changes of fibronectin, tenascin-C, fibulin-1, and fibulin-2 in the skin during the development of chronic contact dermatitis.