scholarly journals Complete amino acid sequence of the N-terminal extension of calf skin type III procollagen

1984 ◽  
Vol 219 (2) ◽  
pp. 625-634 ◽  
Author(s):  
A Brandt ◽  
R W Glanville ◽  
D Hörlein ◽  
P Bruckner ◽  
R Timpl ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Type Iii Collagen ◽  
Type I ◽  
Globular Domain ◽  
Type Iii ◽  
Type I Procollagen ◽  
Type Iii Procollagen ◽  
Calf Skin

The N-terminal extension peptide of type III procollagen, isolated from foetal-calf skin, contains 130 amino acid residues. To determine its amino acid sequence, the peptide was reduced and carboxymethylated or aminoethylated and fragmented with trypsin, Staphylococcus aureus V8 proteinase and bacterial collagenase. Pyroglutamate aminopeptidase was used to deblock the N-terminal collagenase fragment to enable amino acid sequencing. The type III collagen extension peptide is homologous to that of the alpha 1 chain of type I procollagen with respect to a three-domain structure. The N-terminal 79 amino acids, which contain ten of the 12 cysteine residues, form a compact globular domain. The next 39 amino acids are in a collagenase triplet sequence (Gly- Xaa - Yaa)n with a high hydroxyproline content. Finally, another short non-collagenous domain of 12 amino acids ends at the cleavage site for procollagen aminopeptidase, which cleaves a proline-glutamine bond. In contrast with type I procollagen, the type III procollagen extension peptides contain interchain disulphide bridges located at the C-terminus of the triple-helical domain.

scholarly journals Structure of cDNA clones coding for the entire preproα1 (III) chain of human type III procollagen. Differences in protein structure from type I procollagen and conservation of codon preferences

1989 ◽  
Vol 260 (2) ◽  
pp. 509-516 ◽  
Author(s):  
L Ala-Kokko ◽  
S Kontusaari ◽  
C T Baldwin ◽  
H Kuivaniemi ◽  
D J Prockop
Keyword(s):  
Amino Acid ◽  
Type I Collagen ◽  
Type Iii Collagen ◽  
Cdna Clones ◽  
Type I ◽  
Base Pairs ◽  
Type Iii ◽  
Human Type ◽  
Type I Procollagen ◽  
Type Iii Procollagen

Two overlapping cDNA clones that cover the complete length of the mRNA for human type III procollagen were characterized. The data provided about 2500 base pairs of sequence not previously defined for human type III procollagen. Two tripeptide sequences of -Gly-Xaa-Yaa- were identified that were not detected previously by amino acid sequencing of human type III collagen. The two additional tripeptide units, together with three previously detected, establish that the alpha 1 (III) chain is 15 amino acids longer than either the alpha 1 (I) or alpha 2 (I) chains of type I collagen. The additional tripeptide units made hydropathy plots of the N-terminal and C-terminal regions of type III collagen distinctly different from those of type I collagen. The data also demonstrated that human type III procollagen has the same third base preference in codons for glycine, proline and alanine that was previously found with human and chick type I procollagen. In addition, comparison of two cDNA clones from the same individual revealed a variation in structure in that the codon for amino acid 880 of the alpha 1 (III) chain was -CTT- for leucine in one clone and -TTT- for phenylalanine in the other.

scholarly journals Metabolism of rabbit skin collagen. Differences in the apparent turnover rates of type-I- and type-III-collagen precursors determined by constant intravenous infusion of labelled amino acids

1979 ◽  
Vol 181 (1) ◽  
pp. 75-82 ◽  
Author(s):  
S P Robins
Keyword(s):  
Amino Acid ◽  
Collagen Synthesis ◽  
Specific Radioactivity ◽  
Deae Cellulose ◽  
Type Iii Collagen ◽  
Type I ◽  
Turnover Rates ◽  
Type Iii ◽  
Type I Procollagen ◽  
Skin Collagen

Growing rabbits were infused for up to 10 h with labelled proline, tyrosine and leucine to achieve plateau conditions within body free pools, for [3H]proline infusion, blood free-proline specific radioactivity remained constant after about 1 h. For individual animals, type-I- and type-III-collagen precursors were isolated by precipitation with (NH4)2SO4 and DEAE-cellulose chromatography. Experiments where 3H- and 14C-labelled proline and tyrosine were infused concurrently for different periods of time showed that type I procollagen reached plateau specific radioactivity within 3 h and 90% of the plateau value after 2 h infusion, corresponding to a calculated apparent t 1/2 of less than 26 min. Plateau values for type I procollagen were taken as precursor amino acid pool specific radioactivities. The type-III-collagen-precursor fractions consistently showed lower rates of label incorporation and, by assuming that both type I and type III collagens are synthesized from the same amino acid pools, kinetic analysis revealed an apparent t 1/2 for the isolated type-III-collagen precursors of 3.9 h. For proline, there were large variations between animals in the ratio between the precursor pool for collagen synthesis and the skin homogenate free pool (0.31 +/- 0.13, mean +/- S.D.), so that collagen-synthesis rates based solely on total tissue free-pool values for proline are subject to large and inconsistent errors.

Type I and III procollagen propeptides in growth hormone-deficient patients: effects of increasing doses of GH

1991 ◽  
Vol 124 (3) ◽  
pp. 278-282 ◽  
Author(s):  
Lars T. Jensen ◽  
Jens O.L. Jørgensen ◽  
Juha Risteli ◽  
Jens S. Christiansen ◽  
Ib Lorenzen
Keyword(s):  
Type Iii Collagen ◽  
Type I ◽  
Dose Dependency ◽  
Loose Connective Tissue ◽  
Gh Therapy ◽  
Type Iii ◽  
Type I Procollagen ◽  
Type Iii Procollagen ◽  
Procollagen Propeptides ◽  
Serum Type

Abstract. The effect of increasing doses of growth hormone on collagen synthesis in GH-treated GH-deficient patients was determined in a short-term study. The synthesis of type I and III collagen was estimated by measurements of the carboxyterminal propeptide of type I procollagen and the aminoterminal propeptide of type III procollagen. Type I collagen is mainly found in bone and type III collagen in loose connective tissue. We observed a GH dose dependency of both procollagen propeptides. Serum type I procollagen propeptide was significantly higher following GH doses of 4 and 6 IU/day for 14 days compared with 2 IU/day (normal replacement dose) (p=0.04). Withdrawal of GH therapy for 14 days resulted in wider variation, but not significantly different from the levels at 2, 4 and 6 IU/day. A dose dependency was found regarding type III procollagen propeptide, showing significantly higher serum concentrations at a GH dose of 4 IU/day compared with 2 IU/day (p=0.001), and of 6 IU/day compared with 4 IU/day (p=0.001). Withdrawal of GH therapy resulted in significantly lower type III procollagen propeptide concentrations compared with those at a GH dose of 4 and 6 IU/day (p=0.03). Serum type III procollagen propeptide increased twice as much as type I procollagen propeptide, by 47 vs 25%, at a GH dose of 6 IU/day compared with 2 IU/day. The differences between the effects on type I and type III collagen may reflect differences in secretion or turn-over rate of collagen in bone and loose connective tissue. Serum type I and type III procollagen propeptides may prove useful as monitors of GH therapy, especially regarding the GH dose levels in the individual patients.

Inhibition by Peptidic Fragments of Clq of Platelet - Collagen Interactions

1979 ◽  
Author(s):  
J.L. wautier ◽  
K.B.M. Reid ◽  
Y. Legrand ◽  
J.P. Caen
Keyword(s):  
Amino Acid ◽  
Platelet Aggregation ◽  
Amino Acid Sequence ◽  
Platelet Adhesion ◽  
Type Iii Collagen ◽  
Type I ◽  
Inhibit Platelet Aggregation ◽  
Pepsin Digestion ◽  
Type Iii ◽  
Collagen Peptides

Clq (first component of complement) has been shown to inhibit platelet aggregation induced by collagen. Platelet aggregation and adhesion to purified type I or type III collagen have been studied in the presence of various fragment of Clq.The collagen like region was obtained by digestion of Clq by pepsin and by isolation of the fragments by chromatography on sephadex G 200. The globular region was prepared by digestion of Clq by collagenase, and filtration. The collagen like region is as effective as native Clq in inhibiting platelet aggregation or adhesion in the presence of type I or type III collagen, while the globular region was without effect.Using peptides obtained from the collagen like region of Clq (reduction and alkylation, performic oxidation, CNBr treatment, extensive pepsin digestion) it could be shown that the fragment (FR II = 70 Amino Acid) was responsible for the inhibition of the platelet adhesion and aggregation induced by type I or type III collagen.The Amino Acid sequence of this fragment was compared to the known sequence of the collagen peptides involved in platelet adhesion (see Fauvel et al).

Methionine-Specific Staining of Collagen

1982 ◽  
Vol 40 ◽  
pp. 294-295
Author(s):  
E.M. Kuhn ◽  
K.D. Marenus ◽  
M. Beer
Keyword(s):  
Amino Acids ◽  
Collagen Fibers ◽  
Type Iii Collagen ◽  
Type I ◽  
Electron Microscopic ◽  
Good Correspondence ◽  
Specific Staining ◽  
Type Iii ◽  
Different Types ◽  
Sulfur Containing

Fibers composed of different types of collagen cannot be differentiated by conventional electron microscopic stains. We are developing staining procedures aimed at identifying collagen fibers of different types.Pt(Gly-L-Met)Cl binds specifically to sulfur-containing amino acids. Different collagens have methionine (met) residues at somewhat different positions. A good correspondence has been reported between known met positions and Pt(GLM) bands in rat Type I SLS (collagen aggregates in which molecules lie adjacent to each other in exact register). We have confirmed this relationship in Type III collagen SLS (Fig. 1).

scholarly journals Isolation and Characterization of a Type I Gene Encoding a Light-harvesting Chlorophyll a/b-binding Protein of Photosystem II in Peach

1998 ◽  
Vol 123 (4) ◽  
pp. 493-499 ◽  
Author(s):  
Kyu H. Chung ◽  
Dennis E. Buetow ◽  
Schuyler S. Korban
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Photosystem Ii ◽  
Amino Acid Sequence ◽  
Woody Plants ◽  
Light Harvesting ◽  
Binding Protein ◽  
Transit Peptide ◽  
Type I ◽  
Polyadenylation Sites

A nuclear gene, Lhcb1*Pp1, encoding a light-harvesting chlorophyll a/b-binding protein of photosystem II has been isolated from peach [Prunus persica (L.) Batsch. `Stark Earliglo'] leaf genomic DNA, cloned, and sequenced. This gene encodes a precursor polypeptide of 267 amino acids with a transit peptide of 34 and a type I mature protein of 233 amino acids. The amino acid sequence of the mature polypeptide is 89% to 94% and 80% to 94% similar to those encoded by type I Lhcb genes of annual and other woody plants, respectively. In contrast, the amino acid sequence of the peach transit peptide is less conserved being 47% to 69% similar to those of annual plants and only 17% to 22% similar to those of other woody plants. The peach gene was used as a probe for Lhcb gene expression. Lhcb mRNA is detected in leaves of field-grown trees during June to October. Lhcb mRNA is detected at a high level in leaves of peach shoots grown in tissue culture in the light, but only at a trace level in leaves grown in the dark. Some Lhcb genes appear to be light-modulated in stems. Lhcb1*Ppl contains four potential polyadenylation sites. S1 nuclease analysis detected transcripts of the sizes expected from each of the four polyadenylation sites. All four are found in leaves of light-grown shoots and of field-grown trees throughout the growing season. In contrast, only three are detected in stems of light-grown shoots.

Serum concentrations of aminoterminal propeptide of type III procollagen and propeptide of human type I procollagen in systemic lupus erythematosus

2005 ◽  
Vol 26 (8) ◽  
pp. 712-716
Author(s):  
A. I. Villa-Manzano ◽  
J. I. Gamez-Nava ◽  
M. Salazar-Paramo ◽  
I. C. Valera-Gonzalez ◽  
A. Garcia-Gonzalez ◽  
...  
Keyword(s):  
Systemic Lupus Erythematosus ◽  
Lupus Erythematosus ◽  
Type I ◽  
Serum Concentrations ◽  
Systemic Lupus ◽  
Type Iii ◽  
Human Type ◽  
Type I Procollagen ◽  
Type Iii Procollagen

scholarly journals Completion of the amino acid sequence of the α1 chain from type I calf skin collagen. Amino acid sequence of α1(I)B8

1983 ◽  
Vol 215 (1) ◽  
pp. 183-189 ◽  
Author(s):  
R W Glanville ◽  
D Breitkreutz ◽  
M Meitinger ◽  
P P Fietzek
Keyword(s):  
Staphylococcus Aureus ◽  
Amino Acid ◽  
Sequence Analysis ◽  
Amino Acid Sequence ◽  
Type I ◽  
Amino Acid Sequence Analysis ◽  
Complete Amino Acid Sequence ◽  
Skin Collagen ◽  
Arginine Residues ◽  
Calf Skin

The complete amino acid sequence of the 279-residue CNBr peptide CB8 from the alpha 1 chain of type I calf skin collagen is presented. It was determined by sequencing overlapping fragments of CB8 produced by Staphylococcus aureus V8 proteinase, trypsin, Endoproteinase Arg-C and hydroxylamine. Tryptic cleavages were also made specific for lysine by blocking arginine residues with cyclohexane-1,2-dione. This completes the amino acid sequence analysis of the 1054-residues-long alpha (I) chain of calf skin collagen.

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