Mechanisms of hepatocyte attachment to keratin biomaterials

Richter, Jillian R.; Guzman, Roche C. de; Dyke, Mark Van

doi:10.1016/j.biomaterials.2011.06.061

Cited by 52 publications

(31 citation statements)

References 39 publications

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“…Keratins have been reported as stand-alone materials or with controlled release of therapeutic agents for TERM applications including those in nerve, 15, 21, 22, 23 muscle, 24 skin, 25, 26, 27 and bone. 28, 29, 30 Keratins are known to promote attachment of various cell types including osteoblasts, 31, 32, 33 fibroblasts, 34 hepatocytes, 35 and neural cells, 15 though the mechanisms of attachment are not fully known in all cases. The inflammatory response to keratins is minimal.…”

Section: Introductionmentioning

confidence: 99%

Tunable Keratin Hydrogels for Controlled Erosion and Growth Factor Delivery

et al. 2015

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Tunable erosion of polymeric materials is an important aspect of tissue engineering for reasons that include cell infiltration, controlled release of therapeutic agents, and ultimately to tissue healing. In general, the biological response to proteinaceous polymeric hydrogels is favorable (e.g., minimal inflammatory response). However, unlike synthetic polymers, achieving tunable erosion with natural materials is a challenge. Keratins are a class of intermediate filament proteins that can be obtained from several sources including human hair and have gained increasing levels of use in tissue engineering applications. An important characteristic of keratin proteins is the presence of a large number of cysteine residues. Two classes of keratins with different chemical properties can be obtained by varying the extraction techniques: (1) keratose by oxidative extraction and (2) kerateine by reductive extraction. Cysteine residues of keratose are “capped” by sulfonic acid and are unable to form covalent crosslinks upon hydration, whereas cysteine residues of kerateine remain as sulfhydryl groups and spontaneously form covalent disulfide crosslinks. Here, we describe a straightforward approach to fabricate keratin hydrogels with tunable rates of erosion by mixing keratose and kerateine. SEM imaging and mechanical testing of freeze-dried materials showed similar pore diameters and compressive moduli, respectively, for each keratose-kerateine mixture formulation (~1200 kPa for freeze-dried materials and ~1.5 kPa for hydrogels). However, the elastic modulus (G’) determined by rheology varied in proportion with the keratose-kerateine ratios, as did the rate of hydrogel erosion and the release rate of thiol from the hydrogels. The variation in keratose-kerateine ratios also led to tunable control over release rates of recombinant human insulin-like growth factor 1.

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Section: Introductionmentioning

confidence: 99%

Tunable Keratin Hydrogels for Controlled Erosion and Growth Factor Delivery

et al. 2015

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“…Keratin proteins have some advantages of both natural and synthetic polymer systems that make their use for TERM applications potentially advantageous. As a natural, protein-derived polymer, keratins have cell binding motifs in their primary protein structure 33 and promote attachment and growth of cells through mechanisms that are only beginning to be elucidated 34 . Keratins are characterized by a relatively high cysteine residue content, providing the potential for flexible chemistry reminiscent of synthetic polymers when appropriate types of extraction are used (see below).…”

Section: Introductionmentioning

confidence: 99%

Keratin hydrogel carrier system for simultaneous delivery of exogenous growth factors and muscle progenitor cells

et al. 2015

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Ideal material characteristics for tissue engineering or regenerative medicine approaches to volumetric muscle loss (VML) include the ability to deliver cells, growth factors and molecules that support tissue formation from a system with a tunable degradation profile. Two different types of human hair-derived keratins were tested as options to fulfill these VML design requirements: (1) oxidatively extracted keratin (keratose) characterized by a lack of covalent crosslinking between cysteine residues, and (2) reductively extracted keratin (kerateine) characterized by disulfide crosslinks. Human skeletal muscle myoblasts cultured on coatings of both types of keratin had increased numbers of multinucleated cells compared to collagen or Matrigel™ and adhesion levels greater than collagen. Rheology showed elastic moduli from 102 – 105 Pa and viscous moduli from 101 – 104 Pa depending on gel concentration and keratin type. Kerateine and keratose showed differing rates of degradation due to the presence or absence of disulfide crosslinks, which likely contributed to observed differences in release profiles of several growth factors. In vivo testing in a subcutaneous mouse model showed that keratose hydrogels can be used to deliver mouse muscle progenitor cells and growth factors. Histological assessment showed minimal inflammatory responses and an increase in markers of muscle formation.

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“…Preparations of keratin, in order to make keratin‐based scaffolds in various sizes and geometries (for example, porous or fibrous scaffold) with its intrinsic ability, have been investigated in the relevant fields such as biomaterials, tissue engineering, and regenerative medicine . Keratin‐based materials are suitable for biomedical applications for two reasons: (1) keratin derived from different sources (for example, wool or human hair) has been shown to preserve cell binding motifs including leucine‐aspartic acid‐valine (LDV) and glutamic acid‐aspartic acid‐serine (EDS) binding sites, enabling mammalian cells to attach onto keratin‐treated surfaces or keratin‐based scaffolds via protein–ligand interactions; and, (2) keratin is one of the intermediate filaments involved in regulating cellular behaviors (for example, migration, adhesion, and proliferation) . Several characteristics have been identified using keratin extracted from human hair: (1) serine, glutamic acid, and cysteine are three main amino acids existing in keratin; and, (2) alpha‐ and gamma‐keratin extracted from human hair have been well‐identified …”

Section: Introductionmentioning

confidence: 99%

“…1,2 Keratin-based materials are suitable for biomedical applications for two reasons: (1) keratin derived from different sources (for example, wool or human hair) has been shown to preserve cell binding motifs including leucine-aspartic acid-valine (LDV) and glutamic acidaspartic acid-serine (EDS) binding sites, enabling mammalian cells to attach onto keratin-treated surfaces or keratin-based scaffolds via protein-ligand interactions 3,4 ; and, (2) keratin is one of the intermediate filaments involved in regulating cellular behaviors (for example, migration, adhesion, and proliferation). [5][6][7][8][9][10] Several characteristics have been identified using keratin extracted from human hair: (1) serine, glutamic acid, and cysteine are three main amino acids existing in keratin; and, (2) alpha-and gamma-keratin extracted from human hair have been well-identified. 11,12 Yamauchi et al have examined the cell compatibility of keratin films using mouse fibroblast cultures.…”

Section: Introductionmentioning

confidence: 99%

Modulation of keratin in adhesion, proliferation, adipogenic, and osteogenic differentiation of porcine adipose‐derived stem cells

Lin

Cheng

et al. 2015

J Biomed Mater Res

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Recently, keratin attracts tremendous interest because of its intrinsic ability to interact with different cells. It has the potential to serve as a controllable extracellular matrix protein that can be used to demonstrate cell mechanism and cell-matrix interaction. However, there have been relatively few studies on the effects of keratin on stem cells. In the present work, we study the effects of human keratin on porcine adipose-derived stem cells (pASCs) and a series of selective cell lines: 3T3 fibroblasts, Madin-Darby canine kidney (MDCK) cells, and MG63 osteoblasts. Relative to un-treated culture plate, our results showed that keratin coating substrates promote cell adhesion and proliferation to above cell lines. Keratin also improved pASCs adhesion, proliferation, and enhanced cell viability. Evaluation of genetic markers showed that adipogenic and osteogenic differentiations of pASCs can be successfully induced, thus demonstrating that keratin did not influence the stemness of pASCs. Furthermore, keratin improved adipogenic differentiations of pASCs in terms of up-regulations in lipoprotein lipase, peroxisome proliferator-activated receptor gamma, and CCAAT-enhancer-binding protein alpha. The osteogenic markers type I collagen, runt-related transcription factor 2, and vitamin D receptor were also upregulated when pASCs cultured on keratin substrates. Therefore, keratin can serve as a biological derived material for surface modification and scaffold fabrication for biomedical purpose. The combination of keratin with stem cells may be a potential candidate for tissue repair in the field of regenerative medicine. © 2015 Wiley Periodicals, Inc. J Biomed Mater Res Part B: Appl Biomater, 105B: 180-192, 2017.

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Mechanisms of hepatocyte attachment to keratin biomaterials

Cited by 52 publications

References 39 publications

Tunable Keratin Hydrogels for Controlled Erosion and Growth Factor Delivery

Tunable Keratin Hydrogels for Controlled Erosion and Growth Factor Delivery

Keratin hydrogel carrier system for simultaneous delivery of exogenous growth factors and muscle progenitor cells

Modulation of keratin in adhesion, proliferation, adipogenic, and osteogenic differentiation of porcine adipose‐derived stem cells

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