Human Keratin Research Articles

Keratin 36, a specific marker of tongue filiform papillae, is downregulated in squamous cell carcinoma of the mobile tongue.

Human keratin 36 (K36) is a member of the hair keratin family and is a marker of hair cortex differentiation. The human KRT36 gene is located on the long arm of chromosome 17 and belongs to the cluster of structurally unrelated acidic hair keratins. Recently, it has been reported that KRT36 mRNA is specifically expressed in normal tongue epithelium and downregulated in squamous cell carcinomas of the mobile tongue. Furthermore, KRT36 levels have been reported to be downregulated in clinically normal mobile tongue tissue that is adjacent to tumours, suggesting it could be a marker of pre-neoplastic changes. However, the exact role and the potential role of K36 in tongue tumour formation remains unclear. The aim of the present study was to investigate expression of K36 in a series of squamous cell carcinomas of the mobile tongue, normal mobile tongue and a small panel of other human tissues (normal tissue from the appendix, cervix, hair, lip, mamilla, nail, oesophagus, skin, thymus and vagina) and selected cancer tissue (cervical cancer, melanoma and basal cell carcinoma). Affinity purified polyclonal antibodies against K36 were generated and used for immunohistochemical analysis. The results revealed that in the normal tongue, K36 was detected specifically in the filiform papillae of the dorsal surface of the tongue. Additionally, none of the tongue cancer tissue samples were K36-positive. Immunostaining also revealed that K36 was expressed in nail beds, Hassal's corpuscles in the thymus and the hair cortex. However, K36 was not expressed in the squamous epithelia of the skin, cervix and oesophagus, and the squamous cells of cervical carcinomas, basal cell carcinoma or melanoma. The present data indicated that K36 may be inactivated in tumours of the tongue. However, whether this is part of the tumoural process or if it is an effect of the tumour itself remains to be elucidated.

Potential use of human hair shaft keratin peptide signatures to distinguish gender and ethnicity.

BackgroundMost human hairs collected at old crime scenes do not contain nuclear DNA and are therefore of less value for forensic investigations. In the present study, hair shaft proteins were extracted from 40 healthy subjects between the ages of 21 to 40 years and profiled using gel electrophoresis-based proteomics to determine if they can be used to distinguish gender and ethnicity.MethodsExtraction of the human hair shaft proteins was performed using a newly developed alkaline solubilisation method. The extracts were profiled by 2-dimensional electrophoresis and resolved protein spots were identified by mass spectrometry and queried against the human hair database. The study was then followed-up by immunoblotting of the identified hair shaft keratin of interest using commercially available antibodies.ResultsSeparation of the human hair shaft proteins by 2-dimensional electrophoresis generated improved and highly resolved profiles. Comparing the hair shaft protein profiles of 10 female with 10 male subjects and their identification by mass spectrometry and query of the human hair database showed significant altered abundance of truncated/processed type-II keratin peptides K81 (two spots), K83 (one spot) and K86 (three spots). The 2-dimensional electrophoresis profiling of 30 hair shaft samples taken from women of similar age range but from three distinctive ethnic subpopulations in Malaysia further showed significant altered abundance of one type-I and four type-II truncated/processed keratin peptides including K33b, K81, K83 and K86 (2 spots) between at least two of the ethnic groups. When a followed-up immunoblotting experiment was performed to detect the relative expression of the K86 peptides using commercialised antibodies, similar trends of expression were obtained. The present data, when taken together, demonstrated the potential use of keratin peptide signatures of the human hair shaft to distinguish gender and ethnicity although this needs to be further substantiated in a larger scale study.

Keratin nanoparticles obtained from human hair for removal of crystal violet from aqueous solution: Optimized by Taguchi method

Developing the cheap but superior adsorbents is of importance for environmental applications. In this paper, the Taguchi experimental design was applied to establish the optimum condition for the removal of crystal violet (CV) dye using keratin nanoparticles obtained from human hair waste. The average diameter of keratin particles was found about 63.7 nm, using DLS. Effective factors on the removal of CV dye including pH, adsorbent dose, temperature and contact time were considered using an L16 orthogonal array. The optimum condition was found to be pH = 9, adsorbent dose = 0.004 g, temperature = 25 °C and contact time = 10 h in the studied range for different parameters. ANOVA results indicated that the pH has the highest contribution percentage (75.97%) on the adsorption process. Moreover, the equilibrium data were well described by Freundlich Isotherm, indicating a multilayer adsorption process with a maximum adsorption capacity of 555.56 mg/g through an endothermic and spontaneous adsorption process that could be used for up to 5 cycles of adsorption process. The kinetic adsorption data were evaluated by different kinetic models, where the data followed a pseudo-second-order model with three steps of diffusion indicated by the intra-particle diffusion model. The obtained results clearly show the high potential of human hair-obtained keratin nanoparticles for removal of cationic dyes from wastewater.

Carboxymethyl cellulose-human hair keratin hydrogel with controlled clindamycin release as antibacterial wound dressing

This study offers a new antibacterial wound dressing from carboxymethyl cellulose (CMC)-human hair keratin with topical clindamycin delivery. Keratin was successfully extracted from human hair. Different sponges fabricated by changing CMC to keratin ratio were characterized and compared. Halloysite nanotubes were used as carriers to control the clindamycin release. Various characterization techniques were used to determine the effects of keratin addition on the structure, morphology, physical properties, drug release, antibacterial activity, and cellular behavior of CMC hydrogels. As proved by SEM and EDS, porous structure with interconnected pores was successfully formed and clindamycin-loaded HNTs were uniformly dispersed within the porous structures. Increasing the keratin in CMC hydrogel not only lowered its water vapor transmission rate to a suitable range for wound healing but also improved the water stability of CMC hydrogel. The in vitro release study indicated that clindamycin was released slower in samples containing higher keratin and the Fickian diffusion mechanism controlled their release profile. The fabricated dressing effectively inhibits S. aureus bacterial colonies growth after 24 h. Fibroblast culturing on the fabricated sponges indicated that cellular attachment, proliferation, and spreading were significantly enhanced with increasing the keratin amount.

Stable Isotope Studies of North American Arctic Populations: A Review

We review the major stable carbon and nitrogen isotope studies conducted on human remains in the North American Arctic (NAA) and discuss the findings with respect to two major research themes: diachronic subsistence, and the development of food cultures across the NAA. The interpretation of stable isotope data from human bone collagen and hair keratin is complicated by issues of equifinality in addition to uncertainty arising from the high fat/high protein diets of Arctic hunter gatherers. We suggest future lines of inquiry which may help to alleviate some of these challenges. Our review of Arctic stable isotope studies shows the ongoing potential of stable isotope analysis of Arctic hunter-gatherers and faunal populations, but we include the caveat that regardless of how cutting-edge or refined the analytical method, future stable isotope studies must be contextualized with other lines of evidence from well-excavated sites, and would profoundly benefit from the incorporation of indigenous perspectives and research priorities.

Sensitive Method for the Confident Identification of Genetically Variant Peptides in Human Hair Keratin.

Recent reports have demonstrated that genetically variant peptides derived from human hair shaft proteins can be used to differentiate individuals of different biogeographic origins. We report a method involving direct extraction of hair shaft proteins more sensitive than previously published methods regarding GVP detection. It involves one step for protein extraction and was found to provide reproducible results. A detailed proteomic analysis of this data is presented that led to the following four results: (i) A peptide spectral library was created and made available for download. It contains all identified peptides from this work, including GVPs that, when appropriately expanded with diverse hair‐derived peptides, can provide a routine, reliable, and sensitive means of analyzing hair digests; (ii) an analysis of artifact peptides arising from side reactions is also made using a new method for finding unexpected modifications; (iii) detailed analysis of the gel‐based method employed clearly shows the high degree of cross‐linking or protein association involved in hair digestion, with major GVPs eluting over a wide range of high molecular weights while others apparently arise from distinct non‐cross‐linked proteins; and (v) finally, we show that some of the specific GVP identifications depend on the sample preparation method.

IL-1β-Activated Schwann Cells and Human Hair Keratin Compound Culture to Construct Artificial Nerve Bridging for Repair of Sciatic Nerve Defects in Sprague-Dawley Rats

Human hair keratin (HHK) and interleukin (IL)-1β-Activated Schwann Cells and Human Hair Keratin Compound Culture to Construct Artificial Nerve Bridging for Repair of Sciatic Nerve Defects in Sprague-Dawley Rats-activated Schwann cells were combined to construct artificial nerves. End-to-end anastomosis of nerve defects could repair the sciatic nerve defect in Sprague-Dawley (SD) rats. In this study, a neural injury animal model was used to simulate the repair process of artificial nerves to repair peripheral nerve injury. We found that HHK can act as a biodegradable scaffold to induce Schwann cells to dedifferentiate and then activate macrophages through proliferation and secretion of macrophage migration inhibitory factor and other active substances. A large number of macrophages appeared in the nerve terminal after peripheral nerve injury, such as phagocytic and scavenging degeneration of axons and the myelin sheath. Peripheral nerve damage was also caused by secreting related factors of neurons and other non-neuronal cells, which are involved in a complex relationship. Among them, IL-1β-Activated Schwann Cells and Human Hair Keratin Compound Culture to Construct Artificial Nerve Bridging for Repair of Sciatic Nerve Defects in Sprague-Dawley Rats and other active substances can induce Schwann cells to divide, proliferate, and differentiate, showing high expression of nerve growth factor (NGF) and other active substances, which can further activate macrophages and Schwann cells and promote nerve regeneration. This study describes HHK preparation and advantages, morphological changes of Schwann cells and macrophages in the process of nerve repair, expression of main active substances, and the effect of HHK artificial nerve implantation on animal nerve defect repair. We reveal a related mechanism of nerve repair. Funding Statement: The study was supported by the Medical Technique and Research of Guangdong Province, China (grant number A2017463); China Postdoctoral Science Foundation, China (grant number 2017M613432); Military medical science and technology youth training program (grant number 19QNP005) and Guangdong medical science and technology research foundation (grant number 2016102511210492). Declaration of Interests: The authors have declared that no competing interests exists. Ethical Approval Statement: The experimental protocols were reviewed and approved by the Institutional Animal Care and Use Committee of the Southern Medical University, Guangzhou, China.

Biallelic KRT5 mutations in autosomal recessive epidermolysis bullosa simplex, including a complete human keratin 5 “knock-out”

Epidermolysis bullosa simplex (EBS) is usually inherited as an autosomal dominant disease due to monoallelic gain-of-function mutations in KRT5 or KRT14. Although autosomal recessive forms of EBS have been associated with mutations in at least 10 genes, recessive EBS due to homozygous biallelic KRT5 mutations has not been reported previously; it has been hypothesized that it would result in prenatal lethality. We sought the genetic causes of EB in a cohort of 512 distinct EB families by performing whole exome sequencing (WES) and using an EB-targeting next-generation sequencing (NGS) panel of 21 genes. The pathogenicity and consequences of the mutations were determined by expression profiling and at tissue and ultrastructural levels. Two pathogenic, homozygous missense variants of KRT5 in two patients with generalized EBS and a homozygous null mutation in a patient who died as a neonate from complications of EB were found. The two missense mutations disrupted keratin 5 expression on immunofluorescence microscopy, and the human “knock-out” of KRT5 showed no RNA and protein expression. Collectively, these findings identify biallelic KRT5 mutations with a phenotypic spectrum varying from mild, localized and generalized to perinatal lethal, expanding the genotypic profile of autosomal recessive EBS.

Development and characterization of a biomimetic coating for percutaneous devices

Percutaneous osseointegrated prosthetics (POP), which consist of a metallic post attached to the bone that extends outward through the skin to connect to an external prosthesis, have become a clinically relevant option to replace the typical socket-residual limb connection. POP devices offer several advantages such as mechanical off-loading of soft tissues, direct force transfer to the musculoskeletal system, greater proprioception, and overall improvement in limb kinesis compared to a socket system. However, POP devices create several challenges including epidermal downgrowth, increased infection risk, and mechanical tearing at the skin-implant interface. To address these issues, biomimetic surfaces and coatings have been developed in an attempt to create an infection-free and cohesive interface between POP devices and skin. The fingernail is a prime example of a natural system with a skin interface that is both mechanically and biologically stable. Exploiting keratins’ previously demonstrated tissue compatibility and creating a biomimetic coating for POP devices that can imitate the human fingernail, and demonstrating its ability to promote a stable interface with skin tissue is the goal of this work. Silane coupling aided in producing a coating on titanium substrates consisting of human keratin proteins. Several combinations of silane and keratin derivatives were investigated, and in general showed a nano-scale coating thickness that supported skin cell (i.e. fibroblast and keratinocyte) adhesion. Initial enzyme-mediated degradation resistance was also demonstrated, but the coatings appeared to degrade at long time periods. Importantly, keratinocytes showed a stable phenotype with no indication of wound healing-like activity. These data provide justification to further explore keratin biomaterials for POP coatings that may stabilize the implant-skin interface.

Human hair keratins promote the regeneration of peripheral nerves in a rat sciatic nerve crush model

Axon regeneration and functional recovery after peripheral nerve injury remains a clinical challenge. Injury leads to axonal disintegration after which Schwann cells (SCs) and macrophages re-engage in the process of regeneration. At present, biomaterials are regarded as the most promising way to repair peripheral nerve damage. As a natural material, keratin has a wide range of sources and has good biocompatibility and biodegradability. Here, a keratin was extracted from human hair by reducing method and a keratin sponge with porous structure was obtained by further processing. The results suggested that keratin can promote cell adhesion, proliferation, migration as well as the secretion of neurotrophic factors by SCs and the regulation of the expression of macrophage inflammatory cytokines in vitro. We report for the first time that human hair keratin can promote the extension of axon in DRG neurons. The motor deficits caused by a sciatic nerve crush injury were alleviated by keratin sponge dressing in vivo. Thus, keratin has been identified as a valuable biomaterial that can enhance peripheral nerve regeneration.

Conformation changes in human hair keratin observed using confocal Raman spectroscopy after active ingredient application.

ObjectiveIn hair care cosmetic products’ evaluation, one commonly used method is to evaluate the hair appearance as a gold standard in order to determine the effect of an active ingredient on the final state of the hair via visual appreciation. Although other techniques have been proposed for a direct analysis of the hair fibres, they give only surface or structural information, without any accurate molecular information. A different approach based on confocal Raman spectroscopy has been proposed for tracking in situ the molecular change in the keratin directly in the human hair fibres. It presents a high molecular specificity to detect chemical interactions between molecules and can provide molecular information at various depths at the cortex and cuticle levels.MethodsTo evaluate the potential of confocal Raman spectroscopy in testing the efficiency of cosmetic ingredients on keratin structure, we undertook a pilot study on the effectiveness of a smoothing shampoo on natural human hair, by analysing α‐helix and β‐sheet spectral markers in the Amide I band and spectral markers specific to the cystin sulfur content.ResultsWe confirmed that an active proved to be effective on a gold standard decreases α‐helix keratin conformation and promotes β‐sheet keratin conformation in the hair fibres. We also showed that treatment with the effective active decreases the intensity of covalent disulfide (S–S at 510 cm‐1) cross‐linking bands of cysteine. These data confirm that the effective active also acts on the tertiary structure of keratin.ConclusionFrom these experiments, we concluded that the effective active has a smoothing effect on the human hair fibres by acting on α‐helix and β‐sheet keratin conformation and on the tertiary structure of keratin. Based on these results, confocal Raman spectroscopy can be considered a powerful technique for investigating the influence of hair cosmetic ingredients on keratin structure in human hair fibres. Moreover, this analytical technique has the advantage of being non‐destructive and label free; in addition, it does not require sample extraction or purification and it can be applied routinely in cosmetic laboratories.

Human keratin 1/10-1B tetramer structures reveal a knob-pocket mechanism in intermediate filament assembly.

To characterize keratin intermediate filament assembly mechanisms at atomic resolution, we determined the crystal structure of wild-type human keratin-1/keratin-10 helix 1B heterotetramer at 3.0Å resolution. It revealed biochemical determinants for the A11 mode of axial alignment in keratin filaments. Four regions on a hydrophobic face of the K1/K10-1B heterodimer dictated tetramer assembly: the N-terminal hydrophobic pocket (defined by L227K1, Y230K1, F231K1, and F234K1), the K10 hydrophobic stripe, K1 interaction residues, and the C-terminal anchoring knob (formed by F314K1 and L318K1). Mutation of both knob residues to alanine disrupted keratin 1B tetramer and full-length filament assembly. Individual knob residue mutant F314AK1, but not L318AK1, abolished 1B tetramer formation. The K1-1B knob/pocket mechanism is conserved across keratins and many non-keratin intermediate filaments. To demonstrate how pathogenic mutations cause skin disease by altering filament assembly, we additionally determined the 2.39Å structure of K1/10-1B containing a S233LK1 mutation linked to epidermolytic palmoplantar keratoderma. Light scattering and circular dichroism measurements demonstrated enhanced aggregation of K1S233L/K10-1B in solution without affecting secondary structure. The K1S233L/K10-1B octamer structure revealed S233LK1 causes aberrant hydrophobic interactions between 1B tetramers.

Cysteinyl-tRNA Synthetase Mutations Cause a Multi-System, Recessive Disease That Includes Microcephaly, Developmental Delay, and Brittle Hair and Nails

Aminoacyl-tRNA synthetases (ARSs) are essential enzymes responsible for charging tRNA molecules with cognate amino acids. Consistent with the essential function and ubiquitous expression of ARSs, mutations in 32 of the 37 ARS-encoding loci cause severe, early-onset recessive phenotypes. Previous genetic and functional data suggest a loss-of-function mechanism; however, our understanding of the allelic and locus heterogeneity of ARS-related disease is incomplete. Cysteinyl-tRNA synthetase (CARS) encodes the enzyme that charges tRNACys with cysteine in the cytoplasm. To date, CARS variants have not been implicated in any human disease phenotype. Here, we report on four subjects from three families with complex syndromes that include microcephaly, developmental delay, and brittle hair and nails. Each affected person carries bi-allelic CARS variants: one individual is compound heterozygous for c.1138C>T (p.Gln380∗) and c.1022G>A (p.Arg341His), two related individuals are compound heterozygous for c.1076C>T (p.Ser359Leu) and c.1199T>A (p.Leu400Gln), and one individual is homozygous for c.2061dup (p.Ser688Glnfs∗2). Measurement of protein abundance, yeast complementation assays, and assessments of tRNA charging indicate that each CARS variant causes a loss-of-function effect. Compared to subjects with previously reported ARS-related diseases, individuals with bi-allelic CARS variants are unique in presenting with a brittle-hair-and-nail phenotype, which most likely reflects the high cysteine content in human keratins. In sum, our efforts implicate CARS variants in human inherited disease, expand the locus and clinical heterogeneity of ARS-related clinical phenotypes, and further support impaired tRNA charging as the primary mechanism of recessive ARS-related disease.

Human hair keratin-based hydrogels as dynamic matrices for facilitating wound healing

Recently, human hair-derived keratin protein has been recognized as biomaterial with high potential due to its excellent bioactivity and biocompatibility. Here, we designed human hair-derived keratin-based in situ cross-linkable hydrogels that can serve as a dynamic matrix for the enhanced wound healing. We demonstrated that our developed the keratin-based hydrogels accelerated re-epithelization and wound healing process in a full-thickness animal. Also, we investigated the molecular mechanism underlying the enhanced wound healing. In conclusion, our study proposes that human hair-derived keratin-based hydrogels with excellent bioactivity have great potential for use as a wound healing material, along with its other biomedical applications.

Transcriptome Analysis of Improved Wool Production in Skin-Specific Transgenic Sheep Overexpressing Ovine β-Catenin.

β-Catenin is an evolutionarily conserved molecule in the canonical Wnt signaling pathway, which controls decisive steps in embryogenesis and functions as a crucial effector in the development of hair follicles. However, the molecular mechanisms underlying wool production have not been fully elucidated. In this study, we investigated the effects of ovine β-catenin on wool follicles of transgenic sheep produced by pronuclear microinjection with a skin-specific promoter of human keratin14 (k14). Both polymerase chain reaction and Southern blot analysis showed that the sheep carried the ovine β-catenin gene and that the β-catenin gene could be stably inherited. To study the molecular responses to high expression of β-catenin, high-throughput RNA-seq technology was employed using three transgenic sheep and their wild-type siblings. These findings suggest that β-catenin normally plays an important role in wool follicle development by activating the downstream genes of the Wnt pathway and enhancing the expression of keratin protein genes and keratin-associated protein genes.

Human hair keratin for physically transient resistive switching memory devices

A physically transient non-volatile memory device made of keratin exhibits great resistive switching performance.

Synergistic influence of keratin and TPU: An approach towards bioinspired artificial skin

Abstract Inspired from the keratin-elastin composition of the human skin, here we have developed a robust, flexible and biocompatible composite film of thermoplastic polyurethane (TPU) and bio-waste human hair keratin using extrusion-based melt-mixing method for artificial skin applications. During the melt-mixing, the molecules of TPU and keratin forms H-bonding among their polar functionalities. The H-bonding interaction between TPU and keratin molecules was studied and verified by FTIR and 1H NMR results. Because of both the H-bonding interaction (between TPU and keratin) and lubricating behavior of cysteine-rich keratin, TPK exhibits unique mechanical and tribological performances. Hygroscopic keratin enhances the hydrophilicity and the porous morphology allows the moisture permeability of TPK. TPK containing 1 wt% keratin (i.e., 1% TPK) shows elastic modulus of 31.44 MPa, ultimate tensile strength (UTS) of 18.52 MPa, coefficient of friction (COF) of 0.18 and water contact angle of 85° which are closer to that of the human skin of different body parts. Also, the 1% TPK shows very high toughness value of 77.5 J*m−3*106, which is similar to that of the mammalian collagen fibrils.

Health improvement of human hair and their reshaping using recombinant keratin K31

Hair, being one of the most important components of the beauty care processes, attracts the use of a variety of hair treating cosmetics. Conventional hair treating cosmetics are not satisfactory for one reason or the other. Commercially used keratins are isolated from wool or chicken feathers. As these lack complete sequence identity with human hair keratin, are likely to be less efficient than the human hair keratin. K31, a type I acidic keratin, is a major protein of human hair keratin complex and it is essential for maintaining the hair tensile strength. In this study keratin K31 (46 kDa) gene was expressed in Escherichia coli at a level of approximately 35% of the total cell proteins. The protein, however, was expressed as insoluble inclusion bodies. The expressed protein was refolded and purified by FPLC using an anion-exchange column. The CD analysis results showed that the K31 was properly refolded. MALDI-TOF mass spectroscopy showed the characteristics expected for human K31 keratin. The refolded and partially purified K31 protein, when applied on chemically damaged hairs, increased the diameter of the hair up to 49%. The mechanical strength of the bleached hair increased by almost 2 fold after a single treatment of K31. The protein also straightened curly hair efficiently on a single treatment for one hour. Application of K31 resulted in marked improvements in smoothness, diameter and mechanical strength of the damaged hair.

Freeze-thaw cycles for biocompatible, mechanically robust scaffolds of human hair keratins.

The keratin-based scaffolds are getting more and more attention in the application of tissue engineering. Though various approaches have been considered to improve the physical properties of these scaffolds, few succeeded in achieving the enhanced properties of the pure keratin scaffolds. Due to the presence of -OH, -NH2 , >CO, and -SH on the extracted human hair keratin (HHK), the formation of hydrogen bonds and disulfide bridges could be triggered under certain conditions, leading to the self-cross-linking of HHK materials. Herein, a simple and green strategy was introduced, via freeze-thaw cycles of keratin solutions without addition of extraneous reagents, to obtain the mechanically robust HHK scaffolds. The comparative quantitation of residual -SH among the samples treated with 1, 5, and 9 cycles confirmed the oxidation in the thaw process for forming disulfide bonds. So, the equivalent thaw time was applied in this study, and three groups of the treated samples after 1, 5, and 9 cycles with an appropriate extension thaw time were prepared to solely investigate the effects of physical cross-linking networks, primarily by formation of hydrogen bonds, on the properties of the obtained scaffolds. The systematic assessments including swelling behavior, porosity, thermal analysis, compressive measurement, and microstructural observation confirmed that the repetitive freeze-thaw treatment contributed to mechanically robust scaffolds with good porous interconnectivity. The cell culturing experiments further verified that these HHK scaffolds had desirable cytocompatibility, permitting the proper proliferation, attachment, and infiltration. Accordingly, this study provided a simple and efficient method to obtain biocompatible, mechanically robust keratin scaffolds. © 2018 Wiley Periodicals, Inc. J Biomed Mater Res Part B: Appl Biomater 107B: 1452-1461, 2019.

Strontium isotope ratios (87 Sr/86 Sr) of human fingernail clippings reveal multiple location signals.

Strontium isotope ratios (87 Sr/86 Sr) in human fingernail keratin tissues have been underexplored for region of origin and travel history reconstruction studies. Here we investigated 87 Sr/86 Sr ratios in fingernail keratin to establish baseline measurements in a resident group and to examine how 87 Sr/86 Sr ratios changed with relocation. Fingernail clippings were collected from resident (n = 10) and non-resident/traveler groups (n = 4 and n = 4) that were part of a larger study in Salt Lake City (UT, USA) from 2015 to 2016. Strontium abundance and 87 Sr/86 Sr ratios were determined via multicollector inductively coupled plasma mass spectrometry (MC-ICP-MS). 87 Sr/86 Sr and oxygen (δ18 O) isotope ratios from the traveler participants were compared to examine temporal patterns. Strontium abundance and 87 Sr/86 Sr ratios in fingernails from the resident group established a baseline against which we could evaluate potential differences in non-resident/traveler groups. Resident 87 Sr/86 Sr ratios remained constant over the study period and were consistent with previously measured tap waters for the area. 87 Sr/86 Sr ratio changes in non-resident/traveler groups were rapid and reflected the current location of the individual within 4-5 weeks of arrival. Lastly, δ18 O and 87 Sr/86 Sr ratios of the same fingernail clippings did not exhibit similar temporal patterns, since fingernail δ18 O ratios required more time to attain values characteristic of the new environment. Our findings suggest that strontium is incorporated into fingernail tissues differently from hair and this could be advantageous to forensic investigations. We found that 87 Sr/86 Sr and δ18 O ratios of the same fingernail clippings revealed two different time points reflecting an individual's residence over short- (4-5 weeks, 87 Sr/86 Sr ratios) and long-term (3-5 months, δ18 O values) time scales. It is likely that the 87 Sr/86 Sr ratios of fingernail clippings reflect exogenous signals that are incorporated through bathing waters and that these signals change rapidly with movement to a new location. Our results may aid future forensic studies in the determination of region of origin in unidentified remains.