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Milf Ohne HeuSchen


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Balisto Choco Chips. Protein Chips, Sweet Chilli. Other unicellular organisms lend shape to their cell by means of a hard shell. In contrast, amoebas appear to be miss- ing any sort of framework.

Their shape constantly changes. Nonetheless, they do not completely dissipate and can in individual cases become very large. In- vestigations employing the electron mi- croscope have shown that a complex network of fibrillar and filament-forming proteins are responsible for this change in form.

Research in cell and molecular biology during the past 20 years has shown that this network or cytoskeleton principally consists of the same mole- cules in all eukaryotic cells, the cells of higher organisms.

The Filamentous Components of the Cytoskeleton The cytoskeleton mainly consists of three, different, independent filament systems: 1 microfilaments with a di- ameter of 7 nanometers nm , 2 mi- crotubules, tube-shaped filaments with a 25 nm external diameter, and 3 intermediate filaments that were so named, because their diameter at 10 nm lies between that of the microfila- ments and microtubules.

Every eukar- yotic cell contains microfilaments and microtubules; both are essential for life, even for simple organisms such as yeast.

In contrast, intermediate fila- ments have until now only been found in animal organisms, not in plants, pro- tozoans or simple multicellular organ- isms.

They mainly consist of pseudo-crystalline, intermedi- ate filament bundles that are intercon- nected and arranged in parallel.

In the s, research into the structure of pro- teins with x-rays began with their exam- ination In Wladimir Engelhardt clearly characterized the first cytoskeleton pro- tein, myosin, and its function.

It is seen with increasing clarity that almost every cellular movement and all intracellular transport processes depend on filaments.

Even cellular mo- tion that employs flagella and cilia, the 34 The Cytoskeleton: A Complex System of Dynamic Structural Elements transport of vesicles or the distribution of chromosomes to the daughter cells during cell division is based on the interaction between ATP adenosine tri- phosphate splitting motor proteins and filaments.

It is easy to imagine that such a state of complex mobility exter- nal movement accompanied by simul- taneously occurring diverse internal transport processes can very rapidly degenerate into a state of complete chaos.

Structure of the Intermediate Filament Proteins The histochemical analysis of many cell types in the s, especially in hu- mans, yielded the finding that the tis- sues of the more developed verte- brates contain a third filament system.

These so-called intermediate filaments are present in addition to the microfila- ments and the microtubules in almost every cell.

The intermediate filaments do not form any polar structures and cannot, therefore, be used by motor proteins for directed movements.

Using immunological methods, one recog- nized that intermediate filaments are extremely heterogeneous in their com- position although they cannot be exter- nally distinguished from one another, not even with the electron microscope.

A human being possesses approxi- mately 50 different intermediate fila- ment proteins; these are comparable in their composition and similar in biologi- cal structure.

However, their primary sequence, the genetically determined order of the amino acids in the different intermediate filament proteins, varies greatly.

Scientists conclude from this that filaments formed from such pro- teins can possess very different proper- ties and can, therefore, usually not form any mixed complexes.

This is also the reason why two different intermediate filament systems may exist indepen- dently of one another in a single cell.

All kinds of different proteins belong to the family of intermediate filament pro- teins: lamins are transported Into the cell nucleus where they stabilize the nuclear membrane and the nuclear pores; neurofilament proteins fill out the long axonal processes in nerve cells; vimentin Is found in connective tissue cells and the lens of the eye; and the cytokeratins CK that pervade the cyto- plasm of internal epithelial cells and covering tissues, ranging from the ex- ternal nuclear envelope to the plasma membrane; they are the main protein in the epidermis.

Along with Interconnect- ing proteins, the cytokeratins, after the cells that produce them have died, form scales, hair, feathers and nails.

The long quills of the porcupine are an un- usual creation of nature that consist of interconnected, quasi-crystalline, inter- mediate filament bundles arranged in parallel order.

Such a diversity of proteins may con- fuse non-specialists and may appear insignificant to them. Because of this, it Is possible to determine the histoge- netic origin of a tumor by immunologi- cally ascertaining the type of intermedi- ate filament protein.

Thanks to their intermediate filament protein profile, very small tumors and micrometastases can also be quickly identified. This pro- cedure has in the meantime become a main technique in tumor diagnosis.

Initially, standardized and uniform minifilaments above are created. These subsequently combine, one after another, to form long cords as shown in the center and below At the Deutsches Krebsforschungszen- trum more than 50 different monoclonal antibodies have been produced that are routinely used throughout the world to diagnose tumors according to the ex- pression catalog for cytokeratins com- piled by Roland Moll and Werner W.

Franke in the Division of Cell Biology. Detailed knowledge of the protein rec- ognized by the antibody with respect to its biochemical properties as well as its tissue-specific expression is a neces- sary prerequisite for using the cytokera- tins in diagnostic procedures.

This means that closely related intermediate filaments must also be distinguished from one another. Often this proves dif- ficult since several of the identified cy- tokeratins were originally viewed by many scientists as being degradation products of a frequently occurring cyto- keratin of the skin.

In our laboratory, Christine Collin was, for example, able 35 2 to demonstrate that CK2e and CK2p are indeed distinct cytokeratins.

This cytokeratin is only synthe- sized in very few cell types, but Is Inval- uable in tumor diagnostics. In combina- tion with antibodies directed against other cytokeratins, antibodies specific for CK20 are employed in the differen- tial diagnosis of adenocarcinomas.

Significant progress resulted from real- izing that intermediate filament proteins release relatively stable fragments the -helix coiled coils during the decom- position of tumor cells.

These frag- ments are in turn easily detectable with immunological methods even when present only in very small quantities.

In the early stages of certain types of lung tumors, fragments from cytokeratin 19 CK19; cloned by Bernhard Bader in our laboratory can be detected in the blood.

In this case, an early detection of cancer Is possible by simply drawing blood and employing serodiagnosis. Function of the Intermediate Filament Proteins What are the advantages for a multicel- lular organism consisting of organs and tissues in synthesizing such a large number of different proteins and regu- lating them in such a complex diversity that is specific for each cell type?

Why is this necessary? In the end, only a single system of apparently similar fila- ments is maintained In the cells. What happens when the synthesis of these 36 Fig.

The organizational structures in the cells find their counterpart in the form of a complex structure outside of the cells that is not lacking in diversity when compared to the internal structures.

This so-called extracellular matrix that is located near the cells is, for example, mainly excreted by fibroblasts in epithe- lial tissues.

Transmembrane proteins, of the inte- grin type among others, bind the extra- cellular matrix to the internal cytoskele- ton by means of specific protein com- plexes.

Other transmembrane proteins, the cadherins, assume the task of coupling the cytoskeletons between in- dividual cells. In this manner, a trans- cellular cytoskeleton pervades the en- tire tissue.

Cytoskeleton and matrix pro- teins have a unique quality that distin- Fig. Biophysical examinations of the three filament systems have shown that they are fundamentally different in one pa- rameter, namely in their viscoelasticity.

For example, under torsional stress the ability of the intermediate filaments to react elastically increases. A redistribution of the molecules in the filament is probably responsible for this.

In contrast, microfilaments and microtu- bules break under such conditions. Among the intermediate fila- The Cytoskeleton: A Complex System of Dynamic Structural Elements ment proteins there are relatively large differences with respect to their viscoe- lastic properties that are additionally in- fluenced by the proteins, with which they are associated.

These findings from experiments con- ducted on tissue cultures readily led to the assumption that intermediate fila- ments may also have something to do with stabilizing cells against tensile stress in the living organism.

Clarifying the cause of a certain genetically- based skin disease epidermolysis bul- losa simplex has confirmed this in an Impressive manner.

In patients so af- fected the basal cell layer of the epider- mis breaks away upon the slightest pressure, thereby, forming blisters.

These patients are missing an exten- sive Intermediate filament system in the basal cell layer. Intermediate filaments are instead found In aggregates near the cell nucleus.

The cause of this clumping is a mutation that leads to the exchange of an amino acid at a certain location in cytokeratin 5 or How can such an apparently slight change have such drastic effects?

Similar to the dy- namic filament systems of the microfila- ments and microtubules the actual ele- ments of the cytoskeleton, the interme- diate filaments, are not static, rigid cell components.

Already slight variations in the molecule can lead to the formation of flat or clump-like aggregates Instead of the desired filaments.

From this the question arises: what are the possible consequences of such malformations in a filament system for the cells and the tissue in a living or- ganism?

Thereafter, the nerve cells die. In contrast, the additional, quantita- tively comparable synthesis of appropri- ate mouse neurofilaments is tolerated by the mouse nerve cells without any recognizable problems.

Since the two proteins from man and mouse are very similar, it follows that even very slight differences may bring about the com- pletely opposite behavior of the respec- tive proteins in the nerve cells.

Thereby, the feedback loops in the cell can be affect- ed. This protein is deposited in band-shaped aggre- gates In the cytoplasm. In contrast, the synthesis of an epidermal cytokeratin In Fig.

Using this meth- od, it was possible for the first time to vis- ualize the spaces in the cell nucleus into which the vimentin had spread the pancreatic islet cells of a transgenic mouse proved to be fatal.

Within a few weeks after birth, the mice developed a severe case of diabetes since the islet cells died. By em- ploying techniques from genetic engi- neering a certain gene in the germ plasma of a mouse can specifically be switched off.

For example, the Inactivation of vlmen- 37 2 Fig. The image is produced with a laser scanning microscope using an immunofluores- cence technique tin apparently had no visible effect on the embryonic development of this mouse.

This proved to be puzzling, be- cause scientists had previously as- sumed that this protein plays a central role in the mesoderm development of the mouse.

In contrast, the inactivation of the gene responsible for the sister molecule of vimentin, called desmin, that is exclusively synthesized in the muscle resulted In severe damage to the heart muscle.

Thus, the desmin system plays a decisive role In the mechanical stability of this organ. The original assumption that Intermedi- ate filament proteins are found with pro- nounced complexity only in higher ver- tebrates can no longer be defended.

Even a small roundworm such as Cae- norhabditis elegans, one of the model organisms used in cell differentiation studies, contains a multitude of inter- mediate filament proteins that partially possess a high degree of sequence similarity to the corresponding mam- malian proteins.

Integration of the Filaments in the Cytoskeleton In the approximately different types of cells found in human beings, the three filament systems are always found together with a multitude of asso- ciated proteins that are usually also synthesized in a tissue-specific manner.

For example, this includes the proteins of the desmoplakin family, elongated ae-helical proteins, that form molecular chains and can bridge larger distances in the cell.

Desmoplakins may partially be extracted with nonionic detergents and, therefore, do not strictly fulfill the criteria of a cytoskeleton protein.

It does not describe the functional, dynamic entity of the inter- acting systems. One of these mole- cules is plectin.

This giant protein con- sists of approximately 5, amino acids and, depending on cell type, is capable of binding intermediate fila- ments with microtubules, microfila- ments or with fodrin a fibrillar protein of the plasma membrane skeleton.

Cell poisons such as colchicine that dis- solve microtubules and bring about a drastic reorganization of the vimentin intermediate filament system mainly leave the plectin network undisturbed.

However, a certain portion of the plectin become displaced by the intermediate filaments. From this, it follows that dif- ferent posttranslationally modified plec- tins are functionally present in a cell.

Desmoplakin, which lends Its name to this family of proteins, is almost exclu- sively found on the interior side of the cell at desmosomes, special cell-to-cell binding structures.

Either alone or with the assistance of additional compo- nents and mainly in epithelial cells, but also in the heart muscle, it recruits intermediate filaments onto the cell membrane.

In this manner, the cell-to- cell binding complexes join the interme- diate filament systems of individual cells in a single epithelium or organ into an elastic support system that pervades the entire tissue.

Only this enables cells to move out of or through orga- nized tissue. The latter fact is of decisive importance in the formation of tumors and their dis- semination throughout the body in the process of metastasis.

The mecha- nisms wich Involved in the migration of cells out of an epithelium and which re- quire, among other things, that the des- mosomes which bind the cells dissolve are still unexplained.

However, scien- tists were recently able to demonstrate that proteins located in the cell-to-cell binding structures are components of signal chains or are themselves trans- ported into the cell nucleus where they may possibly participate in the control of gene activity.

Thereby, it appears feasible to examine the direct influence of the cytoskeletal components on the regulation of gene activity.

These stud- ies may in the future permit a focused intervention in the molecular mecha- nisms that enable cells in primary tu- mors to break free and form metasta- ses in other tissues.

Harald Herrmann-Lerdon Division of Cell Biology Participating staff Monika Brettel Prof. Franke Christine Grund Dr.

Use Hofmann Cacilia Kuhn Dr. Kevin R. Rogers Dr. Herbert Spring In collaboration with Dr. Joanna Bridger Priv. Peter Lichter Division of Organization of Complex Genomes, Deutsches Krebsforschungszentrum Prof.

Jorg Langowski Division of Biophysics of Macromolecules, Deutsches Krebsforschungszentrum Prof. Ueli Aebi Biocenter, University of Basel, Switzerland Prof.

Jurgen MarkI Institute of Zoology, University of Mainz Prof. Manfred Schliwa Institute of Cell Biology, University of Munich Selected publications Moll, R.

Expressionsproflle von Epithellen und epithelialen Tumoren. Gustav Fischer Verlag, Stuttgart, Jena, New York, Herrmann, H.

Cell Biol. Cell Sci. In: Onkologie. Precisely this is the aim of molec- ular embryology, which asks which ge- netic mechanisms regulate the devel- opment of the fertilized egg into adult.

We now know that there are specific genes that control particular processes during embryogenesis. It turns out that these developmental control genes not only regulate embryonic processes but can also play important roles in cancer.

Moreover, developmental control genes have been modified very little during evolution and are used In many differ- ent processes.

For example, the ras gene regulates eye development in the fruit fly, while it is important for the de- velopment of muscle and blood in the frog.

Yet, in adult man and mouse a de- fective ras gene can lead to cancer. Thus, the medical significance of devel- opmental control genes is that they often represent potential cancer - or oncogenes.

Due to the importance of these genes one major goal of current molecular embryology Is, therefore, to Identify new developmental control genes and to study their roles.

The evolutionary conservation of devel- opmental control genes allows one to use lower species as model organisms to study them.

Our division of molecular embryology uses the South African clawed frog, Xenopus laevis, a tradi- tional subject for embryologists. These frogs are bred specifically for scientific research.

They are particularly well suited for the analysis of early em- bryonic development, since hundreds of embryos are obtained from a single frog, which develop outside the mother in the pretri dish.

Identification of devel- opmental control genes is easier in the frog than in mouse or man and their function can often be tested more di- rectly.

Therefore, the frog embryo serves as a model system for man to study developmental control genes. In contrast to Central European frogs, Xenopus can be induced to lay eggs throughout the year by hormone treat- ment.

The eggs are fertilized in vitro and develop synchronously. Embryo- genesis from the fertilized egg to the swimming tadpole takes only two days, and the larvae begin feeding after one week.

Function of Developmental Control Genes There are many developmental control genes known that function at different stages and in different tissues.

These genes encode proteins with diverse bio- chemical roles. They may be hor- mones, hormone receptors or direct regulators of gene activity.

Often a de- velopmental control gene is only active in a few regions of the embryo. The brachyury gene, for example, regulates the differentiation of mesodermal cells, which give rise to blood, connective tis- sue, and muscle.

Such selective ex- pression is probably an important factor regulating the activity of developmental control genes. In the frog, the function of a develop- mental control gene is tested by activat- ing the gene in regions of the embryo which normally do not express it.

To do this, the genetic information of the gene which has been isolated by cloning, is translated into so called messenger ri- bonucleic acid mRNA In the test tube.

A tiny amount of the gene is incubated 40 Developmental Control Genes Fig. This synthetic mRNA can be in- troduced into the embryo by microin- jecting it into a desired region with a fine glass needle.

This then leads to the artificial activation of the gene. The de- veloping embryo can subsequently be analyzed for the formation of unusual tissues at the injected site, which would give an important hint towards the func- tion of the gene in regulating cell diffe- rentiation.

Dozens of developmental control genes have been indentified in this manner. There are developmental control genes whose micoinjection leads to the forma- tion of Siamese twins, which have two heads and trunks.

These genes are way up in the hierarchy of embryonic development and serve as main switch- es, initiating and organizing embryo- genesis.

The later a gene acts during development the more restricted its regulative properties typically are. While early expressed developmental control genes can induce whole Sia- mese twins, the late genes will only be able to induce for example muscle tis- sue.

Embryogenesis is thus controlled by a series of hierarchically ordered de- velopmental control genes, which serve progressively more specialized func- tions during development.

Identification of New Developmental Control Genes Many developmental control genes were discovered in the fruit fly, where mutants were isolated, which show dis- tinct embryonic malformations.

The af- fected genes have been meanwhile cloned and homologs of most of these have been isolated in vertebrate spe- cies. To identify new developmental control genes that may not yet have been found in the fly, we have devised a novel screen in our laboratory.

In this project hundrets of genes are presently isolated In the frog embryo to discover novel genes among them. If one were to do this screen with mice, about pregnant females would have to be sacrificed.

In the frog only 60 females are needed, since every animal lays hundreds of eggs. Furthermore, the frogs need not be sacrificed since they lay the eggs into the aquarium.

To discover novel developmental con- trol genes, genes are taken randomly from a gene library and the distribution of their gene products, their mRNA, Is analyzed in the whole embryo using a special staining procedure.

Genes showing a particularly interesting stain- ing pattern are then selected and ana- lyzed more carefully. In cooperation with Dr. Hajo Delius the sequence of 41 the deoxyribonucleic acid DNA of these genes is determined and com- pared to the sequence of known genes that are compiled in databases.

Often genes are found that already have a human homolog which was identified in the worldwide efforts to sequence the human genome.

Frequently, nothing but the DNA sequence is known for the gene. The staining of the homologous frog gene yields valuable information about a potential function in human.

We have identified novel genes in this manner among which are many de- velopmental control genes. The next step will be to test the function of the developmental control genes by micro- injection and to study selected genes more closely.

This screen yields an abundance of data, photos of staining patterns of the genes as well as DNA sequences. We will make these data available to the public by releasing them on the internet in form of a gene expression database.

Hans Lehrach at the Max Planck Institute in Berlin we plan to continue this screen on an even larger basis, to systematically study embryo- nal gene expression, and to discover new developmental control genes.

Christof Niehrs Division of Molecular Embryology Participating scientists Dr. Volker Gawantka Rebecca Nitsch In collaboration with Dr.

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