The structure and function of fibrillin.

D. P. Reinhardt, S. C. Chalberg, Lynn Sakai

Research output: Contribution to journalReview article

23 Citations (Scopus)

Abstract

Fibrillin is a very large molecule whose primary structure is now known from the cloning and sequencing of 10 kb of cDNA. Immunohistochemical results suggest that one of the functions of fibrillin molecules is to contribute to the structure of the microfibril. The importance of fibrillin as a structural macromolecule has been demonstrated by the identification of the gene for fibrillin (FBN1) as the disease-causing gene in Marfan's syndrome. While it is clear that fibrillin contributes to the structure of the microfibril, it is not known whether fibrillin molecules self-assemble or whether fibrillin interacts with other molecules in order to form microfibrils. In order to investigate whether particular domains of fibrillin are important to the assembly of the microfibril and to specify domains that participate in interactions with other proteins, we have produced recombinant fibrillin 1 peptides in human cells and used them in studies described here. Additionally, new information regarding the 5' end of FBN1 has been obtained from studies investigating promoter activity, and potential proteolytic cleavage sites have been identified in the N- and C-terminal domains.

Original languageEnglish (US)
JournalCiba Foundation symposium
Volume192
StatePublished - Jan 1 1995
Externally publishedYes

Fingerprint

Microfibrils
Marfan Syndrome
Fibrillins
Genes
Organism Cloning
Complementary DNA
Peptides
Proteins

ASJC Scopus subject areas

  • General

Cite this

The structure and function of fibrillin. / Reinhardt, D. P.; Chalberg, S. C.; Sakai, Lynn.

In: Ciba Foundation symposium, Vol. 192, 01.01.1995.

Research output: Contribution to journalReview article

Reinhardt, D. P. ; Chalberg, S. C. ; Sakai, Lynn. / The structure and function of fibrillin. In: Ciba Foundation symposium. 1995 ; Vol. 192.
@article{6a1d2492df5a4bcf947278eb80fa6601,
title = "The structure and function of fibrillin.",
abstract = "Fibrillin is a very large molecule whose primary structure is now known from the cloning and sequencing of 10 kb of cDNA. Immunohistochemical results suggest that one of the functions of fibrillin molecules is to contribute to the structure of the microfibril. The importance of fibrillin as a structural macromolecule has been demonstrated by the identification of the gene for fibrillin (FBN1) as the disease-causing gene in Marfan's syndrome. While it is clear that fibrillin contributes to the structure of the microfibril, it is not known whether fibrillin molecules self-assemble or whether fibrillin interacts with other molecules in order to form microfibrils. In order to investigate whether particular domains of fibrillin are important to the assembly of the microfibril and to specify domains that participate in interactions with other proteins, we have produced recombinant fibrillin 1 peptides in human cells and used them in studies described here. Additionally, new information regarding the 5' end of FBN1 has been obtained from studies investigating promoter activity, and potential proteolytic cleavage sites have been identified in the N- and C-terminal domains.",
author = "Reinhardt, {D. P.} and Chalberg, {S. C.} and Lynn Sakai",
year = "1995",
month = "1",
day = "1",
language = "English (US)",
volume = "192",
journal = "Ciba Foundation symposium",
issn = "0300-5208",
publisher = "Wiley Subscription Services",

}

TY - JOUR

T1 - The structure and function of fibrillin.

AU - Reinhardt, D. P.

AU - Chalberg, S. C.

AU - Sakai, Lynn

PY - 1995/1/1

Y1 - 1995/1/1

N2 - Fibrillin is a very large molecule whose primary structure is now known from the cloning and sequencing of 10 kb of cDNA. Immunohistochemical results suggest that one of the functions of fibrillin molecules is to contribute to the structure of the microfibril. The importance of fibrillin as a structural macromolecule has been demonstrated by the identification of the gene for fibrillin (FBN1) as the disease-causing gene in Marfan's syndrome. While it is clear that fibrillin contributes to the structure of the microfibril, it is not known whether fibrillin molecules self-assemble or whether fibrillin interacts with other molecules in order to form microfibrils. In order to investigate whether particular domains of fibrillin are important to the assembly of the microfibril and to specify domains that participate in interactions with other proteins, we have produced recombinant fibrillin 1 peptides in human cells and used them in studies described here. Additionally, new information regarding the 5' end of FBN1 has been obtained from studies investigating promoter activity, and potential proteolytic cleavage sites have been identified in the N- and C-terminal domains.

AB - Fibrillin is a very large molecule whose primary structure is now known from the cloning and sequencing of 10 kb of cDNA. Immunohistochemical results suggest that one of the functions of fibrillin molecules is to contribute to the structure of the microfibril. The importance of fibrillin as a structural macromolecule has been demonstrated by the identification of the gene for fibrillin (FBN1) as the disease-causing gene in Marfan's syndrome. While it is clear that fibrillin contributes to the structure of the microfibril, it is not known whether fibrillin molecules self-assemble or whether fibrillin interacts with other molecules in order to form microfibrils. In order to investigate whether particular domains of fibrillin are important to the assembly of the microfibril and to specify domains that participate in interactions with other proteins, we have produced recombinant fibrillin 1 peptides in human cells and used them in studies described here. Additionally, new information regarding the 5' end of FBN1 has been obtained from studies investigating promoter activity, and potential proteolytic cleavage sites have been identified in the N- and C-terminal domains.

UR - http://www.scopus.com/inward/record.url?scp=0029439126&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0029439126&partnerID=8YFLogxK

M3 - Review article

C2 - 8575254

AN - SCOPUS:0029439126

VL - 192

JO - Ciba Foundation symposium

JF - Ciba Foundation symposium

SN - 0300-5208

ER -