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have remained unclear. Two recombinant trichocyte keratins—human type I hair keratin 37 and human type II hair keratin 81—were expressed using a bacterial expression system and subsequently forming recombinant keratin nanoparticles (RKNPs) through ultrasonic dispersion. It has been revealed that RKNPs significantly boosted cell proliferation and migration in laboratory settings. Moreover, when applied to dermal wounds in vivo, RKNPs facilitated improved wound healing, leading to enhanced epithelialization, vascularization, collagen deposition, and remodeling. Importantly, tests for in vivo biocompatibility showed no signs of systemic toxicity. RKNPs have potential as a promising approach for advancing wound healing and suggests new avenues for developing keratin-based biomaterials.
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38 s) and K81 (approximately 40 s) compared to the vehicle alone (approximately 170 s, p < .01), with notably reduced total blood loss (p < .01). Furthermore, in the femoral artery injury model, the recombinant keratin proteins significantly reduced bleeding time compared to the control group (approximately 50 s vs. 270 s). Notably, K37 and K81 exhibited stronger haemostatic effects than extracted keratins (approximately 80 s) in treating rat liver injury. Additionally, the recombinant keratin proteins demonstrated a robust capacity to promote the formation of a fibrin clot at the injury site, effectively stopping the bleeding. Consequently, recombinant human hair keratins offer potential for developing novel haemostatic products based on keratin biomaterials.
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Over the last decade, numerous KRTAP genes have been identified across mammals, including humans. They are categorized into three groups based on their amino acid composition: high sulfur (with <30 mol% cysteine), ultrahigh sulfur (>30 mol% cysteine), and high glycine/tyrosine. Hair keratins form intermediate filaments (KIFs) within trichocytes, specialized cells that contribute to hair formation. As these cells move upward in the cortex, KIFs aggregate, surrounded by a space called the matrix. KRTAPs, also known as KAPs, are a significant part of this matrix between KIFs. It's suggested that KRTAPs play a role in establishing a cross-linked network with KIFs, contributing to the creation of the rigid hair shaft.
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keratinocytes, distinct patterns of keratin gene expression are evident, indicating the presence of different hierarchical transcription processes among various cell types. Examination of keratin gene promoter regions reveals conserved sequence motifs that might govern these cell-specific traits. Moreover, through the isolation of related sheep and human cuticle keratin genes, conserved DNA motifs and expression patterns during cuticle cell differentiation have been discovered. Further, the expression of sheep wool follicle IF and high-sulfur keratin genes in transgenic mice suggests that the regulatory DNA elements and proteins associated with hair keratin genes maintain functional conservation across mammalian species.
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desmosomes (see Fig. 1b, d) and hemidesmosomes, contributing not only to cell-to-cell stability but also to the attachment to the basement membrane and the connective tissue within a particular epithelium. In non-stratified (simple) epithelia of internal organs experiencing minimal mechanical stress, only a few keratin types form sparsely distributed filaments within the cytoplasm. However, a more substantial number of keratin types participate in the intermediate filament cytoskeletal framework of squamous epithelia, which becomes more prominent in cornified stratified epithelia like the epidermis covering the body's outer surface. Here, keratins are abundant and densely packed, forming tonofilaments.
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of the full-length KRT81, encompassing its 5' region, in breast cells. Immunohistochemical and immunofluorescence examinations located KRT81 within the cytoplasm. Additionally, in KRT81-knockdown MDA-MB231 cells, zymography illustrated decreased MMP9 activity, while scratch and invasion assays demonstrated diminished cell migration and invasion capabilities. This presents the first evidence of complete KRT81 expression in both normal breast epithelial cells and breast cancer cells. Furthermore, the findings suggest that KRT81 plays a role in the migration and invasion of breast cancer cells.
82:, a prevalent secondary structure exists: a well-preserved, central alpha-helical domain made up of four coiled-coil segments along with non-helical end-terminal domains that vary in sequences and lengths . Recent findings suggest that the interaction between acidic and basic soft keratins initiates with the creation of a heterodimer. This heterodimer comprises an acidic and a basic monomeric keratin. Two of these heterodimers then combine to form a tetramer, which subsequently polymerizes, resulting in the formation of the final 10-nanometer filamentous structure.
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intermediate filament network is formed by the necessary pairing of equal amounts of type I and type II keratins. While hair keratins, such as KRT81, are typical in hard-keratinized structures like hair and nails, they are thought to serve as structural proteins specific to these organs without expression elsewhere, such as the mammary gland.
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KRT81, a type II hair keratin, is a major hair protein expressed in the hair cortex. Interestingly, despite being typically associated with hair structures, KRT81 expression has been observed in the SKBR3 human breast cancer cell line and metastatic lymph nodes of breast carcinomas, but not in normal
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Western blot analysis detected the presence of the complete 55-kDa KRT81 in various human breast cancer cell lines (MCF7, SKBR3, MDA-MB-231), normal human mammary epithelial cells (HMEC), and non-neoplastic cells (MCF10A). Reverse transcription-polymerase chain reaction confirmed the expression
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Recent attention has been drawn to the remarkable wound-healing capabilities and excellent biocompatibility of keratin derived from human hair. While recombinant keratin proteins produced via recombinant DNA technology offer higher purity compared to extracted keratin, their wound-healing properties
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Due to their role as structural stabilizers in epithelial cells, keratin filaments have garnered significant interest across biology, embryology, pathology, and dermatology. This fundamental cytoskeletal function extends beyond individual cell levels. Typically, keratin filaments are integrated into
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found in animals, constituting tough structures like hair, feathers, nails, and horns. It's classified based on tissue origin and sulfur content: soft keratins have lower sulfur, while hard keratins, found in hair and claws, contain more sulfur, creating a stronger structure. Keratins belong to two
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Keratin constitutes a large multigene family known as cytokeratins. These cytokeratins are differentially expressed across various epithelial types and have been extensively studied as markers for breast cancer. They are categorized into acidic type I and basic-to-neutral type II cytokeratins. The
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The hair shaft is majorly composed of hair keratins and their associated proteins (KRTAPs). KRTAPs are products of diverse gene families resulting from gene duplication events in their evolutionary history. These genes are typically small, comprising a single exon less than 1,000 base pairs long.
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In vivo haemostasis efficacy studies were conducted using rat models of liver puncture and femoral artery injury. For both models, K37 and K81 (10 mg) were applied to cover the wound areas. In the liver puncture model, bleeding time significantly decreased with recombinant K37 (approximately
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and the hair follicle's cyclic activity. Encircling these cells is the matrix cell region, the hair follicle's proliferative compartment, responsible for the formation of different follicle compartments (except the ORS) and the production of crucial structural elements of hair - hair keratins and
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The arrangement of hair's layers—the cortex and cuticle—forms a hierarchical structure. The cortex primarily consists of a keratin coiled-coil protein phase. These proteins assemble into intermediate filaments, progressively forming larger fibers. Enveloping the hair is the cuticle, composed of
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During hair growth, as follicle bulb cells swiftly transform into cortical or cuticle hair keratinocytes, approximately 50-100 keratin genes become activated at the transcriptional level. However, this intricate process can be simplified into a few highly preserved gene families. In cortical
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deceased cells. X-ray data from various samples consistently reveal specific signals associated with the coiled-coil keratin phase, intermediate filament development in the cortex, and the cell membrane complex. The figure demonstrates signal assignments and their respective length scales.
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breast epithelial cells. Moreover, the expressed KRT81 was found to be a 5′-truncated isoform (ΔHb1), with the full-length protein not being expressed. However, the exact function of this truncated form in breast cancer cells remains unclear.
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evolves into one of the most complex structures in the human body, comprising 7–8 distinct tissue sections. The base of the hair follicle contains the bulb, housing dermal fibroblasts known as the
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types - acidic Type I and neutral-basic Type II, further categorized into Type I a and b, and Type II a and b. The initial step in forming keratin is the alignment of type I and type II keratin
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Gao F, Li W, Deng J, Kan J, Guo T, Wang B, Hao S (May 2019). "Recombinant Human Hair
Keratin Nanoparticles Accelerate Dermal Wound Healing".
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to create a heterodimer, which then aggregates into higher-order structural units. Similar to other intermediate filament
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Powell BC, Nesci A, Rogers GE (December 1991). "Regulation of keratin gene expression in hair follicle differentiation".
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Cruz CF, Azoia NG, Matamá T, Cavaco-Paulo A (August 2017). "Peptide-protein interactions within human hair keratins".
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Yu J, Yu DW, Checkla DM, Freedberg IM, Bertolino AP (July 1993). "Human hair keratins".
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665:"Characterization of the human hair keratin-associated protein 2 (KRTAP2) gene family"
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Rogers MA, Langbein L, Praetzel-Wunder S, Winter H, Schweizer J (January 2006).
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Nanashima N, Horie K, Yamada T, Shimizu T, Tsuchida S (May 2017).
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Fujikawa H, Fujimoto A, Farooq M, Ito M, Shimomura Y (July 2012).
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Guo T, Li W, Wang J, Luo T, Lou D, Wang B, Hao S (2018).
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669:The Journal of Investigative Dermatology
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27:Type of keratin found in hair and nails
567:ACS Applied Materials & Interfaces
117:There are two types of hair keratin:
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1499:Cartilage oligomeric matrix protein
66:associated proteins known as KAPs.
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378:International Review of Cytology
519:Histochemistry and Cell Biology
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630:10.1080/21691401.2018.1459633
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1263:Cartilage associated protein
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384:. Academic Press: 209–263.
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807:Medical Subject Headings
803:Keratins,+Hair-Specific
579:10.1021/acsami.9b01725
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294:type II hair keratin 6
283:type II hair keratin 5
272:type II hair keratin 4
261:type II hair keratin 3
250:type II hair keratin 2
239:type II hair keratin 1
163:type I hair keratin 3B
152:type I hair keratin 3A
1277:Procollagen peptidase
335:Clinical significance
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218:type I hair keratin 8
207:type I hair keratin 7
196:type I hair keratin 6
185:type I hair keratin 5
174:type I hair keratin 4
141:type I hair keratin 2
130:type I hair keratin 1
69:Keratin is a crucial
778:10.3892/or.2017.5564
483:(1 Suppl): 56S–59S.
234:type II hair keratin
18:Type II hair keratin
682:10.1038/jid.2012.73
573:(20): 18681–18690.
308:Associated proteins
125:type I hair keratin
1443:Matrix gla protein
1254:Prolyl hydroxylase
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1258:Lysyl hydroxylase
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351:
347:
343:
329:
320:
297:
286:
275:
264:
253:
242:
233:
221:
210:
199:
188:
177:
166:
155:
144:
133:
124:
116:
107:
98:
89:
76:polypeptides
68:
52:
31:Hair keratin
30:
29:
1484:Cytokeratin
1413:Vitronectin
1094:multiplexin
438:: 805–814.
1115:Endostatin
1104:type XVIII
453:1822/56408
413:2023-11-28
357:References
1494:Reticulin
1187:type VIII
595:141367865
86:Stability
37:found in
1530:Keratins
1524:Category
1509:diseases
1505:See also
1448:Tectorin
1267:Leprecan
1177:type VII
1007:type XII
930:type III
883:Collagen
820:30 March
787:28405679
739:33504645
717:: 1–20.
691:22495175
639:29621887
587:31038908
549:18461349
462:28315768
408:16939781
49:Function
41:and the
1489:Gelatin
1480:Keratin
1428:Decorin
1401:Elastin
1296:Laminin
1272:ADAMTS2
1246:Enzymes
1236:COL28A1
1231:COL27A1
1224:COL11A2
1219:COL11A1
1214:type XI
1208:COL10A1
1149:type VI
1146:other:
1140:COL25A1
1135:COL23A1
1130:COL17A1
1125:COL13A1
1110:COL18A1
1098:COL15A1
1054:type IV
1042:COL22A1
1037:COL21A1
1032:COL20A1
1027:COL19A1
1022:COL16A1
1017:COL14A1
1011:COL12A1
985:type IX
965:COL26A1
960:COL24A1
918:type II
860:Protein
731:1725577
647:4620386
540:2386534
497:7686952
35:keratin
1433:FAM20C
1204:type X
1197:COL8A2
1192:COL8A1
1181:COL7A1
1170:COL6A5
1165:COL6A3
1160:COL6A2
1155:COL6A1
1085:COL4A6
1080:COL4A5
1075:COL4A4
1070:COL4A3
1065:COL4A2
1060:COL4A1
1000:COL9A3
995:COL9A2
990:COL9A1
953:COL5A3
948:COL5A2
943:COL5A1
937:type V
923:COL2A1
910:COL1A2
905:COL1A1
899:type I
874:matrix
809:(MeSH)
785:
737:
729:
689:
645:
637:
593:
585:
547:
537:
495:
460:
406:
396:
168:KRT33B
157:KRT33A
122:acidic
1473:Other
1458:TECTB
1453:TECTA
1423:FREM2
1418:FRAS1
1396:ALCAM
1389:Other
1378:LAMC3
1373:LAMC2
1368:LAMC1
1363:gamma
1356:LAMB4
1351:LAMB3
1346:LAMB2
1341:LAMB1
1329:LAMA5
1324:LAMA4
1319:LAMA3
1314:LAMA2
1309:LAMA1
1304:alpha
981:FACIT
974:Other
735:S2CID
643:S2CID
591:S2CID
299:KRT86
288:KRT85
277:KRT84
266:KRT83
255:KRT82
244:KRT81
231:basic
223:KRT38
212:KRT37
201:KRT36
190:KRT35
179:KRT34
146:KRT32
135:KRT31
113:Types
43:nails
1438:ECM1
1336:beta
822:2017
783:PMID
727:PMID
687:PMID
635:PMID
583:PMID
545:PMID
493:PMID
458:PMID
404:PMID
394:ISBN
39:hair
773:doi
719:doi
715:642
677:doi
673:132
625:doi
575:doi
535:PMC
527:doi
523:129
485:doi
481:101
448:hdl
440:doi
436:101
386:doi
382:251
1526::
1096::
1051::
983::
862::
781:.
769:37
767:.
763:.
747:^
733:.
725:.
713:.
699:^
685:.
671:.
667:.
655:^
641:.
633:.
621:46
619:.
615:.
603:^
589:.
581:.
571:11
569:.
557:^
543:.
533:.
521:.
517:.
505:^
491:.
479:.
456:.
446:.
434:.
422:^
402:.
392:.
380:.
376:.
364:^
296:,
285:,
274:,
263:,
252:,
241:,
220:,
209:,
198:,
187:,
176:,
165:,
154:,
143:,
132:,
45:.
1482:/
1265:/
1256:/
1210:)
1206:(
1183:)
1179:(
1013:)
1009:(
925:)
921:(
852:e
845:t
838:v
824:.
789:.
775::
741:.
721::
693:.
679::
649:.
627::
597:.
577::
551:.
529::
499:.
487::
464:.
450::
442::
416:.
388::
20:)
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