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111 results on '"Pan, Te-Cheng"'

11. Extracellular matrix protein fibulin-2 is expressed in the embryonic endocardial cushion tissue and is a prominent component of valves in adult heart

Author

Zhang, Hong-Yan, Chu, Mon-Li, Pan, Te-Cheng, Sasaki, Takako, Timpl, Rupert, and Ekblom, Peter

Subjects
Proteins -- Analysis, Endocardial cushion defects -- Research, Heart valves -- Research, Gene expression -- Analysis, Biological sciences
Abstract

Immunofluoresence studies reveal that fibulin-1 and -2 are significantly codistributed throughout the development of the endocardial cushion tissue (ECT) and are expressed in the heart valve in the adult stage. A comparative study suggests that fibulin-2 is a better marker than fibulin-1 for the ECT. ECT development and the tensile strength of the cardiac values are influenced by these two fibulins.

Published
1995

17. A Mouse Model for Dominant Collagen VI Disorders

Author

Pan, Te-Cheng, Zhang, Rui-Zhu, Arita, Machiko, Bogdanovich, Sasha, Adams, Sheila M., Gara, Sudheer Kumar, Wagener, Raimund, Khurana, Tejvior S., Birk, David E., Chu, Mon-Li, Pan, Te-Cheng, Zhang, Rui-Zhu, Arita, Machiko, Bogdanovich, Sasha, Adams, Sheila M., Gara, Sudheer Kumar, Wagener, Raimund, Khurana, Tejvior S., Birk, David E., and Chu, Mon-Li

Abstract

Background: Dominant collagen VI gene mutations cause the severe Ullrich congenital muscular dystrophy (UCMD) and mild Bethlem myopathy. Results: A mutant mouse mimicking the most common molecular defect in dominant UCMD patients was generated and characterized. Conclusion: The mutant mouse displays muscle and connective tissue abnormalities. Significance: The mutant mouse provides an animal model for dominant collagen VI disorders. Dominant and recessive mutations in collagen VI genes, COL6A1, COL6A2, and COL6A3, cause a continuous spectrum of disorders characterized by muscle weakness and connective tissue abnormalities ranging from the severe Ullrich congenital muscular dystrophy to the mild Bethlem myopathy. Herein, we report the development of a mouse model for dominant collagen VI disorders by deleting exon 16 in the Col6a3 gene. The resulting heterozygous mouse, Col6a3(+/d16), produced comparable amounts of normal Col6a3 mRNA and a mutant transcript with an in-frame deletion of 54 bp of triple-helical coding sequences, thus mimicking the most common molecular defect found in dominant Ullrich congenital muscular dystrophy patients. Biosynthetic studies of mutant fibroblasts indicated that the mutant 3(VI) collagen protein was produced and exerted a dominant-negative effect on collagen VI microfibrillar assembly. The distribution of the 3(VI)-like chains of collagen VI was not altered in mutant mice during development. The Col6a3(+/d16) mice developed histopathologic signs of myopathy and showed ultrastructural alterations of mitochondria and sarcoplasmic reticulum in muscle and abnormal collagen fibrils in tendons. The Col6a3(+/d16) mice displayed compromised muscle contractile functions and thereby provide an essential preclinical platform for developing treatment strategies for dominant collagen VI disorders.

Published
2014

18. Fibulin-2 is dispensable for mouse development and elastic fiber formation

Author

Sicot, Francois-Xavier, Tsuda, Takeshi, Markova, Dessislava, Klement, John, Arita, Machiko, Zhang, Rui-Zhu, Pan, Te-Cheng, Mecham, Robert P., Birk, David E., Chu, Mon-Li, Sicot, Francois-Xavier, Tsuda, Takeshi, Markova, Dessislava, Klement, John, Arita, Machiko, Zhang, Rui-Zhu, Pan, Te-Cheng, Mecham, Robert P., Birk, David E., and Chu, Mon-Li

Abstract

Fibulin-2 is an extracellular matrix protein belonging to the five-member fibulin family, of which two members have been shown to play essential roles in elastic fiber formation during development. Fibulin-2 interacts with two major constituents of elastic fibers, tropoelastin and fibrillin-1, in vitro and localizes to elastic fibers in many tissues in vivo. The protein is prominently expressed during morphogenesis of the heart and aortic arch vessels and at early stages of cartilage development. To examine its role in vivo, we generated mice that do not express the fibulin-2 gene (Fbln2) through homologous recombination of embryonic stem cells. Unexpectedly, the fibulin-2-null mice were viable and fertile and did not display gross and anatomical abnormalities. Histological and ultrastructural analyses revealed that elastic fibers assembled normally in the absence of fibulin-2. No compensatory up-regulation of mRNAs for other fibulin members was detected in the aorta and skin tissue. However, in the fibulin-2 null aortae, fibulin-1 immunostaining was increased in the inner elastic lamina, where fibulin-2 preferentially localizes. The results demonstrate that fibulin-2 is not required for mouse development and elastic fiber formation and suggest possible functional redundancy between fibulin-1 and fibulin-2.

Published
2008

34. The large non-collagenous domain (NC-1) of type VII collagen is amino-terminal and chimeric. Homology to cartilage matrix protein, the type III domains of fibronectin and the A domains of von Willebrand factor

Author

Christiano, Angela M., primary, Rosenbaum, Louise M., additional, Chung-Honet, Linda C., additional, Parente, M. Gabriela, additional, Woodley, David T., additional, Pan, Te-Cheng, additional, Zhang, Rui Zhu, additional, Chu, Mon-Li, additional, Burgeson, Robert E., additional, and Uitto, Jouni, additional

Published
1992
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36. The Structure of Type VI Collagen

Author

CHU, MON-LI, primary, PAN, TE-CHENG, additional, CONWAY, DOROTHY, additional, SAITTA, BIAGIO, additional, STOKES, DAVID, additional, KUO, HUEY-JU, additional, GLANVILLE, ROBERT W., additional, TIMPL, RUPERT, additional, MANN, KARLHEINZ, additional, and DEUTZMANN, RAINER, additional

Published
1990
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39. Missense mutation in a von Willebrand factor type A domain of the α3(VI) collagen gene ( COL6A3) in a family with Bethlem myopathy.

Author

Pan, Te‐Cheng, Zhang, Rui‐Zhu, Pericak‐Vance, Margaret A., Tandan, Rup, Fries, Timothy, Stajich, Jeffrey M., Viles, Kristi, Vance, Jeffery M., Chu, Mon‐Li, and Speer, Marcy C.

Abstract

Identifies a G-to-A mutation in the N-terminal globular domain-coding region of the collagen gene COL6A3 in a large American pedigree, leading to the substitution of glycine by glutamic acid in the N2 motif. Characteristics of Bethlem myopathy; Existing evidence on linkage and genetic heterogeneity in Bethlem myopathy.

Published
1998
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40. Recombinant analysis of human α1(XVI) collagen.

Author

Tillet, Emmanuelle, Mann, Karlheinz, Nischt, Roswitha, Pan, Te-cheng, Chu, Mon-Li, and Timpl, Rupert

Subjects
COLLAGEN, EXTRACELLULAR matrix proteins, PROLINE hydroxylase, PROTEIN research, HYDROXYLATION, CHEMICAL reactions, MOLECULAR biology
Abstract

The N-terminal non­collagenous domain NCll of the human collagen α1(XVI) chain was obtained as a recombinant 35-kDa protein from stably transfected kidney cell clones. This form had undergone proteolytic trimming at a basic cleavage motif indicating a similar release in vivo. Domain NCll showed a globular shape after rotary shadowing and was resistant to neutral proteases. Specific antibodies could be raised against recombinant NCll and were used for the analysis of other cell clones transfected with the full-length α(XVI) chain. Immunoprecipitation of detergent extracts of metabolically labelled cells demonstrated the presence of disulfide-bonded 200-kDa polypeptides possessing NCll epitopes. This material was partially resistant to pepsin, indicating the formation of αl(XVI) chain homotrimers with a triple-helical conformation. Yet a substantial proportion of these homotrimers was degraded to fragments of variable size (35–150 kDa) when secreted into the culture medium. Several of these fragments could be obtained on a semi-preparative scale from cells grown in hollow fiber cassettes and showed substantial hydroxylation of proline, consistent with triple-helix formation. Edman degradation demonstrated the origin of some from the N-terminal and of one from a more C-terminal position of collagen XVI. This extensive degradation may be explained by the release of NCll and by further cleavages within some of the nine interruptions of the triple-helical domain of the α1(XVI) chain. Whether this process also occurs in situ remains to be shown. [ABSTRACT FROM AUTHOR]

Published
1995
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41. Recombinant expression and properties of the Kunitz-type VI collagen α2(VI) chain.

Author

Mayer, Ulrike, Pöschl, Ernst, Nischt, Roswitha, Specks, Ulrich, Pan, Te-Cheng, Chu, Mon-Li, and Timpl, Rupen

Subjects
COLLAGEN, RECOMBINANT proteins, PROTEOLYTIC enzymes, FIBROBLASTS, RECOMBINANT molecules, EXTRACELLULAR matrix proteins
Abstract

The Kunitz-type inhibator motif (domain C5) present at C-terminus of the human collagen α3(VI) chain was prepared in a recombinant from the culture medium of stably transfected protease treatment. The recombinant protein was disulfide bonded and showed a high sability against protease treatment. The recombinant protein lacked, however, any inhibitory activity for trypsin, thrombin, kallikerein and several other protease, which could be due to a few unusual substitutions of C5 epitopes in normal human serum and fibroblast medium. The C5 epitopes could not be detected on intact collagen VI purified from guanidine extracts of human placenta. Collagen VI was shown to possess several α3(VI) chain bands (approximately 200 kDa) and reacted strongly with antibodies to an N-terminal recombinant fragment. Immunofluorescence with anti-C5 antibodies failed to stain several human tissues but produced a distinct intracellular staining of cultured fibroblasts. The data indicates the rapid loss of the C5 domain after biosynthesis of collagen VI. [ABSTRACT FROM AUTHOR]

Published
1994
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42. Recombinant expression and structural and binding properties of α1(VI) and α2(VI) chains of human collagen type VI.

Author

Tillet, Emmanuelle, Wiedemann, Hanna, Golbik, Ralph, Pan, Te-Cheng, Zhang, Rui-Zhu, Mann, Karlheinz, Chu, Mon-Li, and Timpl, Rupert

Subjects
RECOMBINANT proteins, COLLAGEN, KIDNEYS, CELLS, ELECTRON microscopy, HYDROXYLATION
Abstract

Full-length alpha 1(VI) and α 2(VI) cDNAs in an eukaryotic expression vector were used to obtain stably transfected human kidney cell clones and to purify these collagen-VI chains in substantial quantities from the culture medium. Both chains appeared mainly as monomers together with some dimers that were disulfide linked through their C-terminal globular domains. Despite sufficient hydroxylation of proline and lysine residues, the chains did not form a triple-helix, as shown by electronmicroscopy, CD spectra and pepsin sensitivity. Digestion of the chains with bacterial collagenase released the N-terminal and C-terminal globular domains, which were identified by their size and partial sequences. They showed a substantial content of alpha-helical conformation and a distinct globular structure after rotary shadowing. Antibodies could be raised that distinguished between the two chains and reacted with the globular domains. The α 2(VI) but not the α 1(VI) chain showed binding to a heparan sulfate proteoglycan (perlecan), fibronectin and pepsin-solubilized collagen VI. Purified globular domains did not bind these ligands indicating the localization of binding sites within the triple-helical domain. Both chains showed a distinct affinity for heparin but failed to bind to various collagen types. [ABSTRACT FROM AUTHOR]

Published
1994
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44. COL6A1genomic deletions in Bethlem myopathy and Ullrich muscular dystrophy

Author

Pepe, Guglielmina, Lucarini, Laura, Zhang, Rui‐Zhu, Pan, Te‐Cheng, Giusti, Betti, Quijano‐Roy, Susana, Gartioux, Corine, Bushby, Katharine M. D., Guicheney, Pascale, and Chu, Mon‐Li

Abstract

We have identified highly similar heterozygous COL6A1genomic deletions, spanning from intron 8 to exon 13 or intron 13, in two patients with Ullrich congenital muscular dystrophy and the milder Bethlem myopathy. The 5′ breakpoints of both deletions are located within a minisatellite in intron 8. The mutations cause in‐frame deletions of 66 and 84 amino acids in the amino terminus of the triple‐helical domain, leading to intracellular accumulation of mutant polypeptides and reduced extracellular collagen VI microfibrils. Our studies identify a deletion‐prone region in COL6A1and suggest that similar mutations can lead to congenital muscle disorders of different clinical severity. Ann Neurol 2005

Published
2006
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45. Zinc finger protein <TOGGLE>Zac1</TOGGLE> is expressed in chondrogenic sites of the mouse

Author

Tsuda, Takeshi, Markova, Dessislava, Wang, Hui, Evangelisti, Lucia, and Pan, Te-Cheng

Abstract

Zac1 is a zinc finger transcription factor that elicits antiproliferative activity and is a potential tumor suppressor gene. Through a detailed spatiotemporal study by in situ hybridization of mouse embryos, we have found that Zac1 transcript is predominantly localized in developing chondrogenic tissue, in addition to the central nervous system as reported elsewhere. Zac1 is also expressed transiently in the myocardium, skeletal muscle, and basal aspect of the stratified embryonic epithelia. During cartilage development, the pattern of Zac1 expression is in close accordance with the distribution of type II collagen mRNA in mesenchymal condensation and prehypertrophic chondrocytes. In mouse ATDC5 cells undergoing in vitro chondrogenesis, the Zac1 mRNA is up-regulated in parallel with genes expressed in precartilage but the Zac1 expression is low when type II collagen mRNA is markedly increased in differentiated cells. Together, these results suggest that Zac1 is a potential regulatory gene involved in chondrogenic differentiation. Developmental Dynamics 229:340–348, 2004. © 2004 Wiley-Liss, Inc.

Published
2004
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46. Prominent expression of <TOGGLE>lysyl oxidase</TOGGLE> during mouse embryonic cardiovascular development

Author

Tsuda, Takeshi, Pan, Te-Cheng, and Evangelisti, Lucia

Abstract

By mRNA differential display in mouse hearts, lysyl oxidase (Lox), a key enzyme catalyzing cross-links in elastin and collagens, was found to be up-regulated between embryonic days 11 (E11) and 13 (E13). This was confirmed by semiquantitative RT-PCR. We analyzed its spatio-temporal expression pattern by in situ hybridization in regard to the development of myocardial cells, endocardial cushion tissue, aortic arch vessels, and epicardium. Anat Rec Part A 270A:93–96, 2003. © 2003 Wiley-Liss, Inc.

Published
2003
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47. Prominent expression of lysyl oxidaseduring mouse embryonic cardiovascular development

Author

Tsuda, Takeshi, Pan, Te-Cheng, Evangelisti, Lucia, and Chu, Mon-Li

Abstract

By mRNA differential display in mouse hearts, lysyl oxidase(Lox), a key enzyme catalyzing cross-links in elastin and collagens, was found to be up-regulated between embryonic days 11 (E11) and 13 (E13). This was confirmed by semiquantitative RT-PCR. We analyzed its spatio-temporal expression pattern by in situ hybridization in regard to the development of myocardial cells, endocardial cushion tissue, aortic arch vessels, and epicardium. Anat Rec Part A 270A:93–96, 2003. © 2003 Wiley-Liss, Inc.

Published
2003
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48. Effects on collagen VI mRNA stability and microfibrillar assembly of three COL6A2 mutations in two families with Ullrich congenital muscular dystrophy.

Author

Zhang, Rui-Zhu, Sabatelli, Patrizia, Pan, Te-Cheng, Squarzoni, Stefano, Mattioli, Elisabetta, Bertini, Enrico, Pepe, Guglielmina, and Chu, Mon-Li

Abstract

We recently reported a severe deficiency in collagen type VI, resulting from recessive mutations of the COL6A2 gene, in patients with Ullrich congenital muscular dystrophy. Their parents, who are all carriers of one mutant allele, are unaffected, although heterozygous mutations in collagen VI caused Bethlem myopathy. Here we investigated the consequences of three COL6A2 mutations in fibroblasts from patients and their parents in two Ullrich families. All three mutations lead to nonsense-mediated mRNA decay. However, very low levels of undegraded mutant mRNA remained in patient B with compound heterozygous mutations at the distal part of the triple-helical domain, resulting in deposition of abnormal microfibrils that cannot form extensive networks. This observation suggests that the C-terminal globular domain is not essential for triple-helix formation but is critical for microfibrillar assembly. In all parents, the COL6A2 mRNA levels are reduced to 57-73% of the control, but long term collagen VI matrix depositions are comparable with that of the control. The almost complete absence of abnormal protein and near-normal accumulation of microfibrils in the parents may account for their lack of myopathic symptoms.

Published
2002
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50. Rabbit apolipoprotein A‐I mRNA and gene

Author

PAN, Te‐cheng, primary, HAO, Qian‐lin, additional, YAMIN, Ting‐Ting, additional, DAI, Pei‐Hua, additional, CHEN, Bao‐sheng, additional, CHEN, Shiow‐ling, additional, KROON, Paulus A., additional, and CHAO, Yu‐sheng, additional

Published
1987
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