A cluster of 21 keratin-associated protein genes within introns of another gene on human chromosome 21q22.3

Shibuya, Kazunori; Obayashi, Izumi; Asakawa, Shuichi; Minoshima, Shinsei; Kudoh, Jun; Shimizu, Nobuyoshi

doi:10.1016/j.ygeno.2003.09.024

Cited by 34 publications

(21 citation statements)

References 36 publications

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“…The keratin-associated proteins, which constitute the matrix of the keratin composite of wool, are a large group of possibly up to 100 different proteins. They are divided into three main families based on their amino acid composition: ultrahigh sulfur keratin-associated proteins (Ͼ30% Cys content), high sulfur keratin-associated proteins (16 -30% Cys content) (29), and high Gly/Tyr keratin-associated proteins (35-60% Gly and Tyr content) (32). Among these three types, the high sulfur keratin-associated proteins possess Cys clusters such as Cys-Cys-Val-Pro and Cys-Cys-Gln-Pro (Fig.…”

Section: Purification Of a Tgase Substrate And Its Nucleotide Sequence-mentioning

confidence: 99%

A Cysteine-rich Protein from an Arthropod Stabilizes Clotting Mesh and Immobilizes Bacteria at Injury Sites

Matsuda¹,

Osaki²,

Hashii³

et al. 2007

Journal of Biological Chemistry

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Hemolymph coagulation in arthropods plays key roles in host defense, including sealing wounds to staunch bleeding and immobilizing invading microorganisms. We have previously reported that horseshoe crab transglutaminase (TGase) promotes cross-linking of a clotting protein (coagulin) with hemocyte-derived proteins (proxins), resulting in the formation of stable coagulin fibrils. Here we show that TGase also cross-links proxins to another hemocyte-derived protein named stablin. Stablin is a cysteine-rich protein of 131 residues. Surface plasmon resonance analysis revealed the specific interaction of stablin with proxin-1 at K d ‫؍‬ 4.0 ؋ 10 ؊9 M. Stablin was predominantly localized in the large granules of hemocytes and secreted by lipopolysaccharide-induced exocytosis. Interestingly, stablin bound to chitin at K d ‫؍‬ 1.5 ؋ 10 ؊8 M, as determined by using a quartz-crystal microbalance. Stablin also interacted with lipopolysaccharides and lipoteichoic acids and exhibited bacterial agglutinating activity against Gram-positive and -negative bacteria. Immunostaining showed that stablin is co-localized with coagulin in the clotting fibrils that effectively trap bacteria. Moreover, an anti-stablin antibody strongly inhibited the proper formation of the clotting fibrils. These data suggest that stablin promotes the formation of the clotting mesh and the immobilization of invading microbes at injury sites. In arthropods, the TGase-mediated cross-linking may play an important role in the initial stage of host defense, wound closure, and healing, as in the case of mammals.

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Section: Purification Of a Tgase Substrate And Its Nucleotide Sequence-mentioning

confidence: 99%

A Cysteine-rich Protein from an Arthropod Stabilizes Clotting Mesh and Immobilizes Bacteria at Injury Sites

Matsuda¹,

Osaki²,

Hashii³

et al. 2007

Journal of Biological Chemistry

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“…; Rogers and Powell, 1993;Powell and Rogers, 1997;Rogers et al, 2001Rogers et al, , 2002Wu et al, 2008). In humans, five clusters of KRTAP genes, which include approximately 100 individual KRTAP genes, have been characterized on chromosomes 11p15, 11q13, 17q12-21, 21q22.1, and 21q23, respectively (Rogers et al, , 2002(Rogers et al, , 2004Shibuya et al, 2004;Yahagi et al, 2004). Studies of specific KRTAP gene families have shown that the cluster harboring five high-sulfur (KRTAP1-3, 16, and 29) and three ultrahigh-sulfur (KRTAP4, 9, and 17) families are located on chromosome 17q12-21 Wu et al, 2008).…”

Section: Introductionmentioning

confidence: 99%

Characterization of the Human Hair Keratin–Associated Protein 2 (KRTAP2) Gene Family

Fujikawa

Fujimoto

Farooq

et al. 2012

Journal of Investigative Dermatology

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Hair keratin-associated proteins (KRTAPs) are one of the major structural components of the hair shaft. Approximately 100 KRTAP genes have been identified in humans to date, with each of the genes classified into a number of families based on their sequence homology and the nature of the repeat structures. The biophysical features of KRTAPs, however, have remained largely unknown. In this study, we investigated the characteristics of the human KRTAP2 family members at the DNA, RNA, and protein levels. We initially found that these genes had various size polymorphisms that were mainly due to differences in the length of the 3'-noncoding sequences. Reverse transcriptase-PCR experiments further detected the presence of KRTAP2 transcripts in plucked human hairs. Using indirect immunofluorescence with an anti-KRTAP2 antibody, we found that there was a predominant expression of the KRTAP2 proteins in the keratinizing zone of the human hair shaft cortex. In addition, we showed that the KRTAP2 proteins interacted with each other and preferentially bound to hair keratins, but not to epithelial keratins. Finally, we determined that the head domain of the hair keratins was essential for the affinity to KRTAP2 proteins. Our results further enhance the crucial roles of KRTAPs in hair shaft keratinization in humans.

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“…In the present study, we focused on the hair shaft cuticle-specific KRTAP10 family members and analyzed their biological features, especially the interactions between KRTAP10 proteins and hair keratins. In humans, a total of 12 functional KRTAP10 genes (KRTAP10-1-KRTAP10-12) have been identified on chromosome 21q22.3 (Rogers et al, 2004;Shibuya et al, 2004). The identified KRTAP10 proteins belong to the high-sulfur group.…”

mentioning

confidence: 99%

Characterization of the Human Hair Shaft Cuticle–Specific Keratin-Associated Protein 10 Family

Fujikawa

Fujimoto

Farooq

et al. 2013

Journal of Investigative Dermatology

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A cluster of 21 keratin-associated protein genes within introns of another gene on human chromosome 21q22.3

Cited by 34 publications

References 36 publications

A Cysteine-rich Protein from an Arthropod Stabilizes Clotting Mesh and Immobilizes Bacteria at Injury Sites

A Cysteine-rich Protein from an Arthropod Stabilizes Clotting Mesh and Immobilizes Bacteria at Injury Sites

Characterization of the Human Hair Keratin–Associated Protein 2 (KRTAP2) Gene Family

Characterization of the Human Hair Shaft Cuticle–Specific Keratin-Associated Protein 10 Family

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