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Durable keratin-based bilayered electrospun mats for wound closure
Singaravelu, Sivakumar,Ramanathan, Giriprasath,Muthukumar, Thangavelu,Raja, M. D.,Nagiah, Naveen,Thyagarajan, Sitalakshmi,Aravinthan, Adithan,P., Gunasekaran,Natarajan, T. S.,V. N. Geetha Selva, Ganga The Royal Society of Chemistry 2016 Journal of Materials Chemistry B Vol.4 No.22
<P>A bilayered nanofibrous scaffold with rapid wound healing properties is found to be suitable for tissue regeneration applications. The objective of this study is to reveal the fabrication of a poly(3-hydroxybutyric acid) (P)-gelatin (G) nanofibrous mat through electrospinning, with a horn keratin-chitosan-based biosheet (KC) as a bilayered nanofibrous scaffold. The mupirocin (D)-loaded horn KC biosheet (KCD) acts as the primary layer over which PG nanofibers were electrospun to act as the secondary layer. It is shown that this engineered bilayered nanofibrous scaffold material (KC-PG) should fulfill the functions of the extracellular matrix (ECM) by elucidating its function<I>in vitro</I>and<I>in vivo</I>. The bilayered nanofibrous scaffold was designed to exhibit improved physiochemical, biological and mechanical properties, with better swelling and porosity for enhanced oxygen permeability, and it also exhibits an acceptable antibacterial property to prevent infection at the wound site. The bilayered nanofibrous scaffold assists in better biocompatibility towards fibroblast and keratinocyte cell lines. The morphology of the nanofibrous scaffold aids increased cell adhesion and proliferation with cell material interactions. This was elucidated with the help of<I>in vitro</I>fluorescence staining against both cell lines. The bilayered KCD-PG nanofibrous scaffold material gives accelerated wound healing efficiency during<I>in vivo</I>wound healing. The results showed the regulation of growth factors with enhanced collagen synthesis, thereby helping in faster wound healing.</P>
Ahn, Do-Hwan,Singaravelu, Gunasekaran,Lee, Sooung,Ahnn, Joohong,Shim, Yhong-Hee WILEY-VCH 2006 Proteomics Vol. No.
<P>Calcineurin is a heterodimeric serine/threonine protein phosphatase, important for many cellular processes such as T-cell regulation, cardiac hypertrophy and kidney development. We previously reported the characterization of Caenorhabditis elegans calcineurin mutants as providing a simple but excellent genetic model system for studying in vivo functions of calcineurin. Calcineurin loss-of-function mutants, cnb-1(lf), and gain-of-function mutants, tax-6(gf), show certain opposite phenotypes as well as some similar phenotypes. In order to explain the phenotypic similarity observed in both loss-of-function and gain-of-function mutants, we examined the proteins that followed similar trends in both mutants relative to wild-type worms by using 2-DE. Interestingly, VHA-13, HSP-6 and phosphoenolpyruvate carboxykinase are down-regulated in both mutants. A total of 96 differentially regulated proteins were identified by MALDI-TOF/MS. Among these, 42 proteins are up-regulated and 54 proteins are down-regulated in calcineurin mutants. Furthermore, knock-down of about 30% of the genes, which are down-regulated in calcineurin mutants, showed some of the phenotypes of calcineurin-null mutants. This analysis suggests the functional relevance of these proteins to calcineurin activity in C. elegans.</P>
RNT-1 regulation in C. elegans
Ji, Yon Ju,Singaravelu, Gunasekaran,Ahnn, Joohong Wiley Subscription Services, Inc., A Wiley Company 2005 Journal of cellular biochemistry Vol.96 No.1
<P>RUNXs are important transcription factors, which are involved in animal development and human carcinogenesis. RNT-1, the only homologue of RUNXs, in Caenorhabditis elegans (C. elegans) has been identified and viable mutant animals of rnt-1 gene have been isolated and characterized recently. Genetic analyses using rnt-1 mutants have shown that RNT-1 is regulated by TGFβ- and Wnt-signaling pathways in the body size regulation and male tail development. Here, we review our current understanding of RNT-1 functions in these signaling pathways. Furthermore, future prospects of RNT-1 and BRO-1 studies in C. elegans are discussed in this review. © 2005 Wiley-Liss, Inc.</P>
Lee, Wonhae,Kim, Ki Ra,Singaravelu, Gunasekaran,Park, Byung-Jae,Kim, Do Han,Ahnn, Joohong,Yoo, Yung Joon WILEY-VCH 2006 Proteomics Vol. No.
<P>Proper folding and maintenance of the native structure are central to protein function and are assisted by a family of proteins called chaperones. Calreticulin and calnexin are ER resident chaperones well conserved from worm to human. Calreticulin/calnexin knock-out mice exhibit a severe phenotype, whereas in Caenorhabditis elegans, calreticulin [crt-1(jh101)]- and calnexin [cnx-1(nr2009)]-null mutant worms exhibit only a mild phenotype, suggesting the possible existence of alternative chaperone machinery that can compensate for the deficiency of calreticulin and/or calnexin. In order to rapidly identify the compensatory chaperone components involved in this process, we analyzed the proteome of crt-1(jh101) mutants and [crt-1(jh101);cnx-1(nr2009)] double mutants. When grown at 20°C, we found that five proteins were up-regulated and two proteins were down-regulated in crt-1(jh101) mutants; nine proteins were up-regulated and five proteins were down-regulated in [crt-1(jh101);cnx-1(nr2009)] double mutants. In addition, elevation of the cultivation temperature to 25°C, which is still permissive to growth but causes specific defects in mutants, led to the identification of several additional proteins. Interestingly, the consistent increment of heat shock protein-70 family members (hsp70) together with protein disulfide isomerase (PDI) at all the examined conditions suggests the possible compensatory function imparted by hsp70 and PDI family members in the absence of calreticulin and/or calnexin.</P>
Soo-Ung Lee,송현옥,Wonhae Lee,Gunasekaran Singaravelu,Jae-Ran Yu,박우윤 한국분자세포생물학회 2009 Molecules and cells Vol.28 No.5
Calcineurin is a Ca2+/Calmodulin activated Ser/Thr phos-phatase that is well conserved from yeast to human. It is composed of catalytic subunit A (CnA) and regulatory subunit B (CnB). C. elegans homolog of CnA and CnB has been annotated to tax-6 and cnb-1, respectively and in vivo function of both genes has been intensively studied. In C. elegans, calcineurin play roles in various signaling path-ways such as fertility, movement, body size regulation and serotonin-mediated egg laying. In order to understand additional signaling pathway(s) in which calcineurin func-tions, we screened for binding proteins of TAX-6 and found a novel binding protein, HLH-11. The HLH-11, a member of basic helix-loop-helix (bHLH) proteins, is a pu-tative counterpart of human AP4 transcription factor. Pre-viously bHLH transcription factors have been implicated to regulate many developmental processes such as cell pro-liferation and differentiation, sex determination and myo-genesis. However, the in vivo function of hlh-11 is largely unknown. Here, we show that hlh-11 is expressed in phar-ynx, intestine, nerve cords, anal depressor and vuvla mus-cles where calcineurin is also expressed. Mutant analyses reveal that hlh-11 may have role(s) in regulating body size and reproduction. More interestingly, genetic epistasis suggests that hlh-11 may function to regulate serotonin-mediated egg laying at the downstream of tax-6.
Cho, Jeong Hoon,Ko, Kyung Min,Singaravelu, Gunasekaran,Ahnn, Joohong Elsevier 2005 FEBS letters Vol.579 No.3
<P><B>Abstract</B></P><P>The <I>Caenorhabditis elegans</I> PMR1, a P-type Ca<SUP>2+</SUP>/Mn<SUP>2+</SUP> ATPase, is expressed in hypodermal seam cells, intestinal cells and spermatheca; localized in Golgi complex. Knock down of <I>pmr-1</I> as well as overexpression of truncated <I>Caenorhabditis elegans</I> PMR1, which mimics dominant mutations observed in human Hailey–Hailey disease, renders the worm highly sensitive to EGTA and Mn<SUP>2+</SUP>. Interestingly, <I>pmr-1</I> knock down not only causes animals to become resistant to oxidative stress but also suppresses high reactive oxygen species sensitivity of <I>smf-3</I> RNA-mediated interference and <I>daf-16</I> worms. These findings suggest that <I>C. elegans</I> PMR1 has important roles in Ca<SUP>2+</SUP> and Mn<SUP>2+</SUP> homeostasis and oxidative stress response.</P>
Yun Hee Kim,송현옥,Kyung Min Ko,Gunasekaran Singaravelu,Changhoon Jee,강준수,안주홍 한국분자세포생물학회 2008 Molecules and cells Vol.25 No.4
Calcineurin (Cn) is a calcium/calmodulin-dependent serine/threonine protein phosphatase that has diverse functions in different cell types and organisms. We screened proteins interacting with the C. elegans CnA homolog, TAX-6, by the yeast two-hybrid system. CNP-3 (Calcineurin interacting protein-3) is a novel protein that physically interacts with the catalytic domain of TAX-6. It is strongly expressed in the nuclei of intestine, hypodermis, dorsal uterine regions and spermatheca. Expression begins around the 60-cell stage and proceeds during all larval stages and the adult. To elucidate the biological function of cnp-3 we isolated a cnp-3 deletion mutant. Since CNP-3 binds CnA, we looked at factors associated with calcineurin loss-of-function mutants, such as brood size, body size, serotonin- and levamisole-mediated egg-laying behavior. The cnp-3(jh145) single mutant had no gross defects compared to wild-type animal. However, the phenotypes of the double mutants, tax-6(p675);cnp- 3(jh145) and cnb-1(jh103);cnp-3(jh145), were more severe in terms of brood size, body size and serotoninmediated egg-laying defects than tax-6(p675) and cnb- 1(jh103), respectively. These results suggest that dysfunction of cnp-3 enhances certain calcineurin loss-offunction phenotypes in C. elegans.