Primary structure of the signal peptide of tropoelastin b.

Karr, Stephen R.; Foster, Jeffrey S.

doi:10.1016/s0021-9258(19)69105-2

Cited by 37 publications

(4 citation statements)

References 13 publications

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“…The sequence does not include the start codon, and the first codon specifies an alanine in a position where protein sequencing of chick pre-tropoelastin has placed the starting methionine (Karr & Foster, 1981). This difference might be due to chick strain variability.…”

Section: Resultsmentioning

confidence: 99%

Repeating structure of chick tropoelastin revealed by complementary DNA cloning

Bressan¹,

Argos²,

Stanley³

1987

Biochemistry

117

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A cDNA library was constructed from chick aorta poly(adenylic acid)-containing RNA in the expression vector pEX1. Several clones were identified by screening the library with a polyclonal antiserum raised against chick tropoelastin and confirmed by DNA sequencing. Analysis of the deduced amino acid sequence, corresponding to the mature tropoelastin and most of the signal peptide, revealed that the molecule is composed of at least 8, and possibly 13, repeating units. The common features of each unit include an N-terminal region composed largely of alanines and lysines and ending with an aromatic amino acid, followed by a GAG span and then a C-terminal region consisting mostly of valines, prolines, and glycines often present in several copies of the sequence (VPGV). This structure is discussed in terms of the functional properties of the molecule.

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Section: Resultsmentioning

confidence: 99%

Repeating structure of chick tropoelastin revealed by complementary DNA cloning

Bressan¹,

Argos²,

Stanley³

1987

Biochemistry

117

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“…Paired glutamine residues, at the site of proteolytic processing, are not unique to pro-Apo A-I. The initial translation product of tropoelastin b mRNA contains a 24 amino acid NH2-terminal peptide which, like the prosegment of Apo A-I, contains a gin-gin dipeptide at its carboxyterminus (23). Tropoelastin b, a major component of connective tissue, is an extracellular protein.…”

Section: Discussionmentioning

confidence: 99%

Biosynthesis of high density lipoprotein by chicken liver: intracellular transport and proteolytic processing of nascent apolipoprotein A-1.

Banerjee¹,

Mukherjee²,

Redman³

1985

The Journal of Cell Biology

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To study the in vivo processing and secretion of Apolipoprotein A-I (Apo A-I), young chickens were administered individual L-[3H]amino acids intravenously and the time of intracellular transport of nascent Apo A-I from rough endoplasmic reticulum (RER) to the Golgi apparatus was measured. Within 3 to 9 min there was maximal incorporation of radioactivity into Apo A-I in both the RER and the Golgi cell fractions. By contrast, the majority of radioactive albumin was also present in the RER by 3 to 9 min, but did not reach peak amounts in the Golgi fraction until 9 to 25 min. Both radioactive Apo A-I and albumin appeared in the blood at about the same time (between 20 and 30 min). NH2-terminal amino acid sequence analysis of nascent intracellular Apo A-I showed that it contains a pro-hexapeptide extension identical to that of human Apo A-I. After 30 min of administration of radioactive amino acids radioactive Apo A-I was isolated by immunoprecipitation from the liver and serum. NH2-terminal sequence analysis of 20 amino acids indicated that chicken liver contained an equal mixture of nascent pro-Apo A-I and fully processed Apo A-I, whereas the serum only contained processed Apo A-I. Further studies showed that the RER only contained pro-Apo A-I, whereas a mixture of pro-Apo A-I and processed Apo A-I was found in the Golgi complex. These results indicate that, in chicken hepatocytes, there is a more rapid transport of Apo A-I than of albumin from the RER to the Golgi cell fractions, and that Apo A-I remains in the Golgi apparatus for a longer period of time before it is secreted into the blood. In addition these studies show that the in vivo proteolytic processing of chicken pro-Apo A-I to Apo A-I occurs in the Golgi cell fractions.

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“…These fibers are an abundant component of the extracellular matrix where they provide the critical function of elasticity to tissues such as blood vessels, lung, and skin (Mecham and Davis, 1994). Apart from cleavage of a signal sequence as the completed polypeptide chain enters the ER (Karr and Foster, 1981;Saunders and Grant, 1984;Grosso and Mecham, 1988), the tropoelastin monomer remains relatively unchanged as it traverses the secretory pathway en route to the cell surface, with no glycosylation or proteolytic processing.…”

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confidence: 99%

Identification of Tropoelastin as a Ligand for the 65-kD FK506-binding Protein, FKBP65, in the Secretory Pathway

Davis

Broekelmann

Ozawa

et al. 1998

The Journal of Cell Biology

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The folding and trafficking of tropoelastin is thought to be mediated by intracellular chaperones, although the identity and role of any tropoelastin chaperone remain to be determined. To identify proteins that are associated with tropoelastin intracellularly, bifunctional chemical cross-linkers were used to covalently stabilize interactions between tropoelastin and associated proteins in the secretory pathway in intact fetal bovine auricular chondrocytes. Immunoprecipitation of tropoelastin from cell lysates after cross-linking and analysis by SDS-PAGE showed the presence of two proteins of ∼74 kD (p74) and 78 kD (p78) that coimmunoprecipitated with tropoelastin. Microsequencing of peptide fragments from a cyanogen bromide digest of p78 identified this protein as BiP and sequence analysis identified p74 as the peptidyl-prolyl cis–trans isomerase, FKPB65. The appearance of BiP and FKBP65 in the immunoprecipitations could be enhanced by the addition of brefeldin A (BFA) and N-acetyl-leu-leu-norleucinal (ALLN) to the culture medium for the final 4 h of labeling. Tropoelastin accumulates in the fused ER/Golgi compartment in the presence of BFA if its degradation is inhibited by ALLN (Davis, E.C., and R.P. Mecham. 1996. J. Biol. Chem. 271:3787–3794). The use of BFA and other secretion-disrupting agents suggests that the association of tropoelastin with FKBP65 occurs in the ER. Results from this study provide the first identification of a ligand for an FKBP in the secretory pathway and suggest that the prolyl cis–trans isomerase activity of FKBP65 may be important for the proper folding of the proline-rich tropoelastin molecule before secretion.

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Primary structure of the signal peptide of tropoelastin b.

Cited by 37 publications

References 13 publications

Repeating structure of chick tropoelastin revealed by complementary DNA cloning

Repeating structure of chick tropoelastin revealed by complementary DNA cloning

Biosynthesis of high density lipoprotein by chicken liver: intracellular transport and proteolytic processing of nascent apolipoprotein A-1.

Identification of Tropoelastin as a Ligand for the 65-kD FK506-binding Protein, FKBP65, in the Secretory Pathway

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