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  • 1
    Electronic Resource
    Electronic Resource
    Studies on reactivity of human leukocyte elastase, cathepsin G, and porcine pancreatic elastase toward peptides including sequences related to the reactive site of .alpha.1-protease inhibitor (.alpha.1-antitrypsin) (1980)
    s.l. : American Chemical Society
    Biochemistry 19 (1980), S. 3973-3978 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00558a013
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  • 2
    Electronic Resource
    Electronic Resource
    Structural optimization of pep7, a small peptide extracted from epimorphin, for effective induction of hair follicle anagen (2005)
    Oxford, UK; Malden, USA : Munksgaard International Publishers
    Experimental dermatology 14 (2005), S. 0 
    Details
    ISSN: 1600-0625
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract:  Epimorphin is representative of a unique class of stromal membrane-anchored proteins that plays distinct functions depending on its membrane topology. When exposed extracellularly, this molecule acts as a morphoregulator for various tissues including hair follicle epithelia. Previous study identified its functional domain (the pep7 domain: SIEQSCDQDE) for hair follicular morphogenesis followed by the successful generation of a chemically modified active peptide. Here, we report optimization of this peptide by the introduction of sequential mutations and subsequent structural determination. We found that three residues from the C-terminus are dispensable, and alternation of the seventh amino acid to an Alanine residue enhanced activity. To favour the biologically active conformation, ε-Acp (NH(CH2)5CO) linked to a Cysteine residue was connected at the N-terminus followed by the introduction of an intramolecular disulphide bridge, the modification process of which could be included in the peptide synthesis. The obtained modified peptide, termed ‘EPM (epimorphin-derived) peptide’, has a Mw of 950 Da and exerts an inductive effect on hair follicle regeneration at a concentration of approximately 0.00001% or even lower. The action of this EPM peptide was more apparent in mice treated with 1% minoxidil, suggesting its potential clinical benefit as a new type of hair-regenerating agent.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.0906-6705.2005.00346.x
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  • 3
    Electronic Resource
    Electronic Resource
    The [53–63] amino acid portion of the parathyroid hormone molecule is essential for the stimulatory effect of carboxyl-terminal PTH fragments on alkaline phosphatase activity in dexamethasone-treated rat osteoblastic osteosarcoma cells, ROS 17/2.8 (1994)
    Springer
    Journal of bone and mineral metabolism 12 (1994), S. S139 
    Details
    ISSN: 1435-5604
    Keywords: parathyroid hormone ; parathyroid hormone fragments ; alkaline phosphatase ; osteoblasts
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The effect of a series of truncated carboxyl-terminal parathyroid hormone (PTH) fragments on alkaline phosphatase (ALP) activity was further examined in dexamethasone-treated rat osteoblastic osteosarcoma cells, ROS 17/2.8. As we previously reported, dexamethasone-induced ALP activity was inhibited not only by hPTH(1-84) and aminoterminal PTH fragment hPTH(1-34), but also by carboxyl-terminal PTH fragment hPTH(69-84). The longer carboxyl-terminal PTH fragment hPTH(53-84) stimulated ALP activity, and the shorter carboxyl-terminal PTH fragment hPTH(71-84) did not affect ALP activity. The longest newly synthesized carboxyl-terminal PTH fragment hPTH(35-84), which is complementary to amino-terminal PTH fragment hPTH(1-34), stimulated ALP activity as potently as hPTH(53-84), but not more potently than hPTH(53-84). Another newly synthesized carboxyl-terminal PTH fragment hPTH(64-84), which has an intermediate peptide length between hPTH (53-84) and hPTH(69-84), inhibited ALP activity as potently as hPTH(69-84). These results suggest that the 35-52 amino acid portion of the PTH molecule might not be crucial for the stimulatory effect of carboxyl-terminal PTH fragments on ALP activity, and that the 53–63 portion, but not the 64–68 portion, of the PTH molecule might be essential for the stimulatory effect of carboxyl-terminal PTH fragments on ALP activity. Furthermore, the importance of the 69th and 70th amino acid of the PTH molecule for the inhibitory effect of carboxyl-terminal PTH fragments on ALP activity was confirmed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02375692
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  • 4
    Electronic Resource
    Electronic Resource
    Binding of the carboxyl-terminal fragments of human parathyroid hormone to rat osteoblastic cells ROS 17/2.8 (1994)
    Springer
    Journal of bone and mineral metabolism 12 (1994), S. S131 
    Details
    ISSN: 1435-5604
    Keywords: parathyroid hormone ; parathyroid hormone fragments ; ROS 17/2.8 cells ; binding study
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract We have recently demonstrated that the carboxyl-terminal (C-terminal) PTH fragments increase or decrease alkaline phosphatase activity in dexamethasone-treated ROS 17/2.8 cells, depending on the length of deletion of amino-terminal amino acids of the PTH molecule, and interact with amino-terminal (N-terminal) PTH fragment [Acta Endocrinol 128:367]. In the present study, we examined individual and combined inhibitory effects of N-terminal and a series of truncated C-terminal PTH fragments [PTH (1-34), (35-84), (53-84) and (71-84)] on the binding of intact PTH molecule [PTH (1-84)] to ROS 17/2.8 cells. The C-terminal PTH fragments, as well as the N-terminal PTH fragment, partially inhibited the binding of [35S]-labeled PTH (1-84) to the cells. The inhibitory effect of C-terminal PTH fragments was reduced along with the deletion of aminoterminal amino acids of the PTH molecule, but still retained in the shortest C-terminal PTH fragment, PTH (71-84). When added together, PTH (1-34) reinforced the inhibitory effect of each C-terminal PTH fragment. The combination of PTH (1-34) and the complementary C-terminal PTH fragment, PTH (35-84), resulted in inhibition of [35S] PTH (1-84) binding to the level obtained by addition of the same concentration of unlabeled PTH (1-84). These findings suggested that the region relatively close to the C-terminal end of the PTH molecule might be essential for the binding of C-terminal PTH fragment could be responsible for the modification of the binding affinity of the peptide to the receptor and the action of the peptide.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02375690
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  • 5
    Electronic Resource
    Electronic Resource
    Improvement in the oxidative folding of endothelin-1 by a lys-Arg extension at the amino terminus: Implication of a salt bridge between Arg−1 and Asp8 (1997)
    Springer
    International journal of peptide research and therapeutics 4 (1997), S. 185-192 
    Details
    ISSN: 1573-3904
    Keywords: α-Helix ; Carboxamide substitution ; Circular dichroism ; Disulfide isomer ; KR-ET-1 ; Prosequence
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary An amino-terminal extension of endothelin-l by the lys-Arg dipeptide in the prosequence (KR-ET-1) greatly increased the ratio of native-type to non-native-type disulfide isomer (96/4 versus 71/29) during the oxidative folding reaction. This improvement was completely abolished by substituting Asn for Asp at position 8 (D8N-KR-ET-1), whereas most of it was maintained with similar carboxamide analogues replaced at Glu10 or Asp18. Structure analyses by circular dichroism spectroscopy revealed that (i) in the carboxylate state, the α-helical content of the native-type isomer of KR-ET-l is higher than that of the native-type isomer of ET-1, while such a variation is not observed in the corresponding non-native-type isomer of KR-ET-l; and (ii) the enhanced α-helicity resulting from the Lys-Arg extension is largely diminished in D8N-KR-ET-l. From these results and our previous findings that the helical structure in KR-ET-l is stabilized by a particular salt bridge between the extended Arg−1 basic moiety and either the Asp8 or Glu10 acidic side chain in Et-1 [Aumelas, A. et al., Biochemistry, 34 (1995) 4546], we conclude that the formation of a specific salt bridge between the side chains of Arg−1 and Asp8 in KR-ET-1 is critical for the predominant generation of the native-type disulfide isomer, probably because it stabilizes the helical structure of parental ET-1.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02443532
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  • 6
    Electronic Resource
    Electronic Resource
    Strong immunogenicity of a multicomponent peptide vaccine developed with the branched lysine oligopeptide method for human immunodeficiency virus infection (1993)
    Chicester [u.a.] : Wiley-Blackwell
    Journal of Molecular Recognition 6 (1993), S. 101-109 
    Details
    ISSN: 0952-3499
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: We synthesized one V3 peptide each from HTLV-IIIB, Thai A and Thai B, conjugating then to the T cell epitope of the env region, and we also synthesized a p17 protein peptide of the gag region (HGP-30). These peptide were then coupled to 8-lysine copolymers using N-succinimidyl maleimido carboxylate (Mr = ca 60 000). We designated this the branched lysine oligopeptide method. The large peptide complexes constructed from these four macromolecular peptide were used with aluminium hydroxide or complete Freund's adjuvant to immunize mice and rabbits four times. ELISA assay with aluminium hydroxide or complete Freund's adjuvant to immunize mice and rabbits four times. ELISA assay showed high titres of anti-peptide antibodies to each V3loop peptide and the HGP-30 peptide. Strong inhibition of CD4+ dependent cell fusion was obtained with these antisera when IIIb, Thai A and Thai B strains of human immunodeficiency virus (HIV) were used. Strong anti-fusion inhibition was also observed with two other HIV strains. In addition, an increase of the anti-HIV effect was observed when we used sera obtained by multicomponent vaccine immunization. The same kind of inhibition was also observed in p24 assay systems using these immunized antisera. Activation of IL-2 production in lymphocytes was observed in p24 assay systems using these immunized antisera. Activation of IL-2 production in lymphocytes was observed in mice immunized with this vaccine. These results suggest that immunization with macromolecular peptide complexes can result in strong immunogenicity towards HIV-1.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jmr.300060302
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  • 7
    Electronic Resource
    Electronic Resource
    Improvement in the oxidative folding of endothelin-1 by a Lys-Arg extension at the amino terminus: Implication of a salt bridge between Arg-1 and Asp8 (1997)
    Springer
    International journal of peptide research and therapeutics 4 (1997), S. 185-192 
    Details
    ISSN: 1573-3904
    Keywords: α-Helix ; Carboxamide substitution ; Circular dichroism ; Disulfide isomer ; KR-ET-1 ; Prosequence
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract An amino-terminal extension of endothelin-1 by the Lys-Arg dipeptide in the prosequence (KR-ET-1) greatly increased the ratio of native-type to non-native-type disulfide isomer (96/4 versus 71/29) during the oxidative folding reaction. This improvement was completely abolished by substituting Asn for Asp at position 8 (D8N-KR-ET-1), whereas most of it was maintained with similar carboxamide analogues replaced at Glu10 or Asp18. Structure analyses by circular dichroism spectroscopy revealed that (i) in the carboxylate state, the α-helical content of the native-type isomer of KR-ET-1 is higher than that of the native-type isomer of ET-1, while such a variation is not observed in the corresponding non-native-type isomer of KR-ET-1; and (ii) the enhanced α-helicity resulting from the Lys-Arg extension is largely diminished in D8N-KR-ET-1. From these results and our previous findings that the helical structure in KR-ET-1 is stabilized by a particular salt bridge between the extended Arg-1 basic moiety and either the Asp8 or Glu10 acidic side chain in ET-1 [Aumelas, A. et al., Biochemistry, 34 (1995) 4546], we conclude that the formation of a specific salt bridge between the side chains of Arg-1 and Asp8 in KR-ET-1 is critical for the predominant generation of the native-type disulfide isomer, probably because it stabilizes the helical structure of parental ET-1.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1008835323518
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  • 8
    Electronic Resource
    Electronic Resource
    Conformational study of endothelins and sarafotoxins with the cystine-stabilized helical motif by means of CD spectra (1992)
    New York : Wiley-Blackwell
    Biopolymers 32 (1992), S. 353-357 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: A series of CD measurements were carried out on members of peptides in the endothelin and sarafotoxin families. The helical structures taken by these peptides containing the helical motif with the sequences of Cys-X-X-X-Cys and Cys-X-Cys [Y. Kobayashi et al. (1991) Neurochemistry International Vol. 18, pp. 525-534] are classified into three groups: a group of structures of ET-1, ET-2 and vasoactive intestinal contractor (VIC), a group of sarafotoxin, and a group of ET-3.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.360320410
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