scholarly journals THE DISTRIBUTION OF ANTIGENIC DETERMINANTS IN RAT SKIN COLLAGEN

1971 ◽  
Vol 133 (6) ◽  
pp. 1309-1324 ◽  
Author(s):  
Herbert Lindsley ◽  
Mart Mannik ◽  
Paul Bornstein
Keyword(s):  
Terminal Region ◽  
Antigenic Determinants ◽  
Collagen Molecule ◽  
Rat Skin ◽  
Amino Terminal ◽  
Skin Collagen ◽  
Native Collagen ◽  
Carboxy Terminal Region ◽  
Carboxy Terminal ◽  
Hyperimmune Rabbit

Immunological studies of rat skin collagen were carried out with a sensitive and quantitative radioimmunoassay. Hyperimmune rabbit antisera to rat skin collagen and isolated α2 chains were used. Iodine-labeled α chains and CNBr-produced peptides served as test antigens, and native collagen, α chains, and CNBr peptides were employed as inhibitors in the assay. The α1 and α2 chains were immunologically distinct. Although the α1 chain was not immunogenic, antibodies to α1 were detected in antisera to the intact collagen molecule. The major antigenic determinant of the α1 chain was located in α1-CB6 which constitutes the carboxy-terminal region of the chain. The α2 chain contained two non-cross-reacting antigenic determinants, one in the amino-terminal region (α2-CB1) and the other in the carboxy-terminal region (α2-CB5) of the chain. The native collagen molecule was less effective than isolated α chains in inhibiting binding of labeled peptides to antisera, indicating that antigenic determinants were less accessible in the triple helical molecule. These immunologic studies are consistent with preliminary comparative biochemical data which indicate that interspecies structural differences in collagen predominate at both the amino- and carboxy-terminal ends of the chains.

scholarly journals Evidence for two antigenic determinants in the C -terminal region of rat skin collagen

FEBS Letters ◽  
1970 ◽  
Vol 9 (1) ◽  
pp. 11-14 ◽  
Author(s):  
R. Timpl ◽  
P.P. Fietzek ◽  
H. Furthmayr ◽  
W. Meigel ◽  
K. Kühn
Keyword(s):  
Terminal Region ◽  
Antigenic Determinants ◽  
Rat Skin ◽  
Skin Collagen

DEVELOPMENT OF HOMOLOGOUS IMMUNOLOGICAL ASSAYS FOR HUMAN PARATHYROID HORMONE

1980 ◽  
Vol 85 (1) ◽  
pp. 161-170 ◽  
Author(s):  
R. M. MANNING ◽  
G. N. HENDY ◽  
S. E. PAPAPOULOS ◽  
J. L. H. O'RIORDAN
Keyword(s):  
Parathyroid Hormone ◽  
Trichloroacetic Acid ◽  
Terminal Region ◽  
Human Parathyroid Hormone ◽  
Antibody Assay ◽  
Amino Terminal ◽  
High Affinity ◽  
Carboxy Terminal Region ◽  
Immunological Assays ◽  
Carboxy Terminal

SUMMARY Antisera to a trichloroacetic-acid precipitate of human parathyroid hormone (PTH) were produced in goats. Two of these antisera (G36 and G31) were of high affinity, and the bovine and porcine hormones were less reactive. Synthetic peptides containing the amino-terminal region of human PTH reacted with both antisera; the 1–34 peptide (PTH-(1–34)), with the sequence proposed by Niall, Sauer, Jacobs, Keutmann, Segre, O'Riordan, Aurbach & Potts in 1974, was more reactive than that having the sequence proposed by Brewer, Fairwell, Ronan, Sizemore & Arnaud in 1972. The antisera were further characterized with a number of other native and synthetic fragments of human PTH and reacted poorly with fragments from the carboxy-terminal region of the molecule. Since the amino-terminal fragments did not account for all the immunoreactivity, it is assumed that the antisera had some recognition sites for the central part of the molecule. Highly purified human PTH-(1–84) was labelled with 125I and radioimmunoassays were developed using this tracer and antiserum G36. To avoid the problems associated with labelling human PTH with 125I, a labelled antibody assay was developed with G36 and an immunoadsorbent consisting of human PTH-(1–34) (sequence of Niall et al.) coupled to cellulose. A sensitive homologous amino-terminal specific assay was developed in this way.

scholarly journals Structure and Function Analysis of LIN-14, a Temporal Regulator of Postembryonic Developmental Events in Caenorhabditis elegans

2000 ◽  
Vol 20 (6) ◽  
pp. 2285-2295 ◽  
Author(s):  
Yang Hong ◽  
Rosalind C. Lee ◽  
Victor Ambros
Keyword(s):  
Caenorhabditis Elegans ◽  
Function Analysis ◽  
Cell Types ◽  
Terminal Region ◽  
Gene Products ◽  
Amino Terminal ◽  
Carboxy Terminal Region ◽  
Carboxy Terminal ◽  
Terminal Domains

ABSTRACT During postembryonic development of Caenorhabditis elegans, the heterochronic gene lin-14 controls the timing of developmental events in diverse cell types. Three alternativelin-14 transcripts are predicted to encode isoforms of a novel nuclear protein that differ in their amino-terminal domains. In this paper, we report that the alternative amino-terminal domains of LIN-14 are dispensable and that a carboxy-terminal region within exons 9 to 13 is necessary and sufficient for in vivo LIN-14 function. A transgene capable of expressing only one of the three alternativelin-14 gene products rescues a lin-14 null mutation and is developmentally regulated by lin-4. This shows that the deployment of alternative lin-14 gene products is not critical for the ability of LIN-14 to regulate downstream genes in diverse cell types or for the in vivo regulation of LIN-14 level by lin-4. The carboxy-terminal region of LIN-14 contains an unusual expanded nuclear localization domain which is essential for LIN-14 function. These results support the view that LIN-14 controls developmental timing in C. elegans by regulating gene expression in the nucleus.

Regulation of fibrillin carboxy-terminal furin processing by N-glycosylation, and association of amino- and carboxy-terminal sequences

1999 ◽  
Vol 112 (22) ◽  
pp. 4163-4171
Author(s):  
J.L. Ashworth ◽  
V. Kelly ◽  
M.J. Rock ◽  
C.A. Shuttleworth ◽  
C.M. Kielty
Keyword(s):  
Extracellular Space ◽  
Molecular Mechanisms ◽  
Terminal Region ◽  
Amino Terminus ◽  
Terminal Sequence ◽  
Amino Terminal ◽  
Fibrillin 1 ◽  
Carboxy Terminal Region ◽  
Efficient Processing ◽  
Carboxy Terminal

The molecular mechanisms of fibrillin assembly into microfibrils are poorly understood. In this study, we investigated human fibrillin-1 carboxy-terminal processing and assembly using a recombinant approach. Processing of carboxy-terminal fibrillin-1 was strongly influenced by N-glycosylation at the site immediately downstream of the furin site, and by association with calreticulin. The carboxy terminus of fibrillin-2 underwent less efficient processing than carboxy-terminal fibrillin-1 under identical conditions. Size fractionation of the amino-terminal region of fibrillin-1, and of unprocessed and furin-processed carboxy-terminal region of fibrillin-1, revealed that the amino terminus formed abundant disulphide-bonded aggregates. Some association of unprocessed carboxy-terminal fibrillin-1 was also apparent, but processed carboxy-terminal sequences remained monomeric unless amino-terminal sequences encoded by exons 12–15 were present. These data indicate the presence of fibrillin-1 molecular recognition sequences within the amino terminus and the extreme carboxy-terminal sequence downstream of the furin site, and a specific amino- and carboxy-terminal association which could drive overlapping linear accretion of furin-processed fibrillin molecules in the extracellular space. Differences in processing of the two fibrillin isoforms may reflect differential abilities to assemble in the extracellular space.

scholarly journals The structure of the sarcomeric M band: localization of defined domains of myomesin, M-protein, and the 250-kD carboxy-terminal region of titin by immunoelectron microscopy.

1996 ◽  
Vol 134 (6) ◽  
pp. 1441-1453 ◽  
Author(s):  
W M Obermann ◽  
M Gautel ◽  
F Steiner ◽  
P F van der Ven ◽  
K Weber ◽  
...  
Keyword(s):  
Immunoelectron Microscopy ◽  
Three Dimensional ◽  
Kinase Domain ◽  
Terminal Region ◽  
M Protein ◽  
Amino Terminal ◽  
Thick Filaments ◽  
Carboxy Terminal Region ◽  
Oriented Parallel ◽  
Carboxy Terminal

The M band of vertebrate cross-striated myofibrils has remained an enigmatic structure. In addition to myosin thick filaments, two major structural proteins, myomesin and M-protein, have been localized to the M band. Also, titin is expected to be anchored in this structure. To begin to understand the molecular layout of these three proteins, a panel of 16 polyclonal and monoclonal antibodies directed against unique epitopes of defined sequence was assembled, and immunoelectron microscopy was used to locate the position of the epitopes at the sarcomere level. The results allow the localization and orientation of defined domains of titin, myomesin, and M-protein at high resolution. The 250-kD carboxy-terminal region of titin clearly enters the M band with the kinase domain situated approximately 52 nm from the central M1-line. The positions of three additional epitopes are compatible with the view that the titin molecule reaches approximately 60 nm into the opposite sarcomere half. Myomesin also seems to bridge the central M1-line and is oriented parallel to the long axis of the myofibril. The neighboring molecules are oriented in an antiparallel and staggered fashion. The amino-terminal portion of the protein, known to contain a myosin binding site, seems to adopt a specific three-dimensional arrangement. While myomesin is present in both slow and fast fibers, M-protein is restricted to fast fibers. It appears to be organized in a fundamentally different manner: the central portion of the polypeptide is around the M1-line, while the terminal epitopes seem to be arranged along thick filaments. This orientation fits the conspicuously stronger M1-lines in fast twitch fibers. Obvious implications of this model are discussed.

scholarly journals The Carboxy-Terminal Region of apoA-I Is Required for the ABCA1-Dependent Formation of α-HDL But Not Preβ-HDL Particles in Vivo†

Biochemistry ◽  
2007 ◽  
Vol 46 (19) ◽  
pp. 5697-5708 ◽  
Author(s):  
Angeliki Chroni ◽  
Georgios Koukos ◽  
Adelina Duka ◽  
Vassilis I. Zannis
Keyword(s):  
Terminal Region ◽  
Carboxy Terminal Region ◽  
Carboxy Terminal

The removal of the carboxy-terminal region of tubulin favors its vinblastine-induced aggregation into spiral-like structures

1986 ◽  
Vol 249 (2) ◽  
pp. 611-615 ◽  
Author(s):  
Luis Serrano ◽  
Javier De La Torre ◽  
Richard F. Luduena ◽  
Jesus Avila
Keyword(s):  
Terminal Region ◽  
Carboxy Terminal Region ◽  
Carboxy Terminal ◽  
Induced Aggregation

Structural differences between repressed and derepressed forms of p60c-src

1989 ◽  
Vol 9 (6) ◽  
pp. 2648-2656
Author(s):  
A MacAuley ◽  
J A Cooper
Keyword(s):  
Kinase Activity ◽  
Kinase Domain ◽  
Terminal Region ◽  
Phosphorylation Sites ◽  
Carboxy Terminus ◽  
Kinase Activation ◽  
Amino Terminal ◽  
Structural Differences ◽  
Carboxy Terminal ◽  
Pronase E

The kinase activity of p60c-src is derepressed by removal of phosphate from Tyr-527, mutation of this residue to Phe, or binding of a carboxy-terminal antibody. We have compared the structures of repressed and active p60c-src, using proteases. All forms of p60c-src are susceptible to proteolysis at the boundary between the amino-terminal region and the kinase domain, but there are several sites elsewhere that are more sensitive to trypsin digestion in repressed than in derepressed forms of p60c-src. The carboxy-terminal tail (containing Tyr-527) is more sensitive to digestion by pronase E and thermolysin when Tyr-527 is not phosphorylated. The kinase domain fragment released with trypsin has kinase activity. Relative to intact p60c-src, the kinase domain fragment shows altered substrate specificity, diminished regulation by the phosphorylated carboxy terminus, and novel phosphorylation sites. The results identify parts of p60c-src that change conformation upon kinase activation and suggest functions for the amino-terminal region.

Tubulin folding is altered by mutations in a putative GTP binding motif

1996 ◽  
Vol 109 (6) ◽  
pp. 1471-1478 ◽  
Author(s):  
J.C. Zabala ◽  
A. Fontalba ◽  
J. Avila
Keyword(s):  
Intramolecular Interaction ◽  
Terminal Region ◽  
Binding Motif ◽  
Beta Tubulin ◽  
Alpha Tubulin ◽  
Proposed Model ◽  
Carboxy Terminal Region ◽  
Carboxy Terminal ◽  
Hydrolysis Of

Tubulins contain a glycine-rich loop, that has been implicated in microtubule dynamics by means of an intramolecular interaction with the carboxy-terminal region. As a further extension of the analysis of the role of the carboxy-terminal region in tubulin folding we have mutated the glycine-rich loop of tubulin subunits. An alpha-tubulin point mutant with a T150-->G substitution (the corresponding residue present in beta-tubulin) was able to incorporate into dimers and microtubules. On the other hand, four beta-tubulin point mutants, including the G148-->T substitution, did not incorporate into dimers, did not release monomers, but were able to form C900 and C300 complexes (intermediates in the process of tubulin folding). Three other mutants within this region (which approximately encompasses residues 137–152) were incapable of forming dimers and C300 complexes but gave rise to the formation of C900 complexes. These results suggest that tubulin goes through two sequential folding states during the folding process, first in association with TCP1-complexes (C900) prior to the transfer to C300 complexes. It is this second step that implies binding/hydrolysis of GTP, reinforcing our previous proposed model for tubulin folding and assembly.

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