AN EXTRACELLULAR-MATRIX PROTEIN OF JELLYFISH HOMOLOGOUS TO MAMMALIAN FIBRILLINS FORMS DIFFERENT FIBRILS DEPENDING ON THE LIFE STAGE OF THE ANIMAL

被引：58

作者：

REBERMULLER, S ^{[1
]}

SPISSINGER, T ^{[1
]}

SCHUCHERT, P ^{[1
]}

SPRING, J ^{[1
]}

SCHMID, V ^{[1
]}

机构：

[1] UNIV BASEL,BIOCTR,CH-4056 BASEL,SWITZERLAND

来源：

DEVELOPMENTAL BIOLOGY | 1995年 / 169卷 / 02期

关键词：

D O I：

10.1006/dbio.1995.1177

中图分类号：

Q [生物科学];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

A monoclonal antibody generated against the isolated extracellular matrix (ECM) of the medusa Podocoryne carnea M. Sars (Coelenterata, Cnidaria, Hydrozoa) stains a fibrillar component of the Podocoryne ECMs in immunohistochemical preparations. The antigen shows a different staining pattern according to the type of ECMs from the animals life cycle. In ontogeny the epitope first appears after gastrulation in the planula larva as single widely dispersed small fibrils, which later accumulate to form a dense meshwork in the larval ECM. The distribution of the antigen strongly suggests an important role of the molecule to cover the biomechanical needs of the animal. In immunoblots one band with a size of 330 kDa is detectable in the polyp ECM, whereas in the outer ECM of the medusa a 340-kDa band is observed. Both the 330- and the 340-kDa bands appear when probed on the inner ECM of the medusa or on ECMs of the larva. The antibody was used to isolate a cDNA clone from an expression library. The deduced amino acid sequence of this cDNA fragment reveals a molecular structure composed of tandemly repeated epidermal growth factor-like repeats interrupted by a second cystein-rich motif first found in the latent transforming growth factor beta binding protein. Comparison of the sequence to the data bases indicates >40% identity to human fibrillins. The presence of fibrillin-like beaded microfibrils in the ECM of P. carnea is furthermore demonstrated by electron microscopy after rotary shadowing. Our results demonstrate for the first time the existence of this noncollagenous interstitial ECM protein in invertebrates and suggest that the structure and the function of fibrillin have been conserved during evolution. (C) 1995 Academic Press, Inc.

引用

页码：662 / 672

页数：11

共 40 条

[1]

Boelsterli U., An electron microscopic study of early developmental stages, oogenesis and cnidogenesis in the anthomedusa, Podocoryne came a M. Sars, J. Morphol., 154, pp. 259-290, (1977)

[2]

Bouillon J., Coppois G., Etude comparative de la mesoglee des cnidaires, CakiersBiol. Mar, 18, pp. 339-368, (1977)

[3]

Chapman G., The structure and functions of the mesoglea, The Cnidaria and Their Evolution, pp. 147-168, (1966)

[4]

Cleary E.G., Gibson M.A., Elastin-associated microfibrils and microfibrillar proteins, Jnt Rev. Connect. Tissue Res, 10, pp. 97-209, (1983)

[5]

Conway Morris S., The fossil record and the early evolution of the metazoa, Nature, 361, pp. 219-225, (1993)

[6]

Corson G.M., Chalberg S.C., Dietz H.C., Charbonneau N.L., Sakai L.Y., Fibrillin binds calcium and is coded by cDNAs that reveal a multidomain structure and alternatively spliced exons at the 5' end, Genomics, 17, pp. 476-484, (1993)

[7]

Devereux J., Haeberli P., Smithies O., A comprehensive set of sequence analysis programs for the VAX, Nucleic Acids Res, 12, pp. 387-396, (1984)

[8]

Dietz H.C., McIntosh I., Sakai L.Y., Corson G.M., Chalberg S.C., Pyeritz R.E., Francomano C., Four novel FBN1 mutations: Significance for mutant transcript level and EGF-like domain calcium binding in the pathogenesis of Marfan syndrome, Genomics, 17, pp. 468-475, (1993)

[9]

Doolittle R.F., Reconstructing history with amino acid sequences, Protein Sci, 1, pp. 191-200, (1992)

[10]

Engel J., Efimov V.P., Maurer P., Domain organizations of extracellular matrix proteins and their evolution, Development (Suppl), pp. 35-42, (1994)

← 1 2 3 4 →