Evotec 566480, wohin geht die Reise??? (Seite 6598)
eröffnet am 12.01.07 11:23:52 von
neuester Beitrag 02.05.24 10:56:14 von
neuester Beitrag 02.05.24 10:56:14 von
Beiträge: 82.041
ID: 1.104.790
ID: 1.104.790
Aufrufe heute: 5.694
Gesamt: 16.202.856
Gesamt: 16.202.856
Aktive User: 2
ISIN: DE0005664809 · WKN: 566480 · Symbol: EVT
9,9550
EUR
+2,68 %
+0,2600 EUR
Letzter Kurs 12:48:53 Tradegate
Neuigkeiten
| Evotec Aktien jetzt im kostenlosen Demokonto handeln!Anzeige |
13:03 Uhr · Felix Haupt Anzeige |
09:47 Uhr · inv3st.de Anzeige |
04:45 Uhr · inv3st.de Anzeige |
Werte aus der Branche Biotechnologie
| Wertpapier | Kurs | Perf. % |
|---|---|---|
| 4,0920 | +167,10 | |
| 1,2500 | +92,01 | |
| 3,0380 | +75,15 | |
| 0,8905 | +74,51 | |
| 1,7900 | +35,61 |
| Wertpapier | Kurs | Perf. % |
|---|---|---|
| 1,2029 | -14,15 | |
| 1,6100 | -15,26 | |
| 1,9600 | -16,24 | |
| 13,010 | -19,94 | |
| 3,5000 | -26,24 |
Beitrag zu dieser Diskussion schreiben
Feedback
....sieht ja irgendwie scheisse aus insges. 
GEN News Highlights : Aug 15, 2011
Scientists Find High-Fat Diet Causes Beta
Cell Dysfunction Leading to Type 2 Diabetes
Studies suggest elevated levels of fatty acids impact key enzyme that promotes
glucose sensing in pancreatic beta cells.
Scientists report new insights into the mechanisms by which a high fat diet can lead to type 2 diabetes.
Mouse and human studies by researchers in the U.S. and Japan suggest that elevated levels of free fatty
acids leads to both reduced expression of the transcription factors FOXA2 and HNF1A in pancreatic
beta cells, and their exclusion from the cell nuclei. This in turn results in a deficit of GnT-4a
glycosyltransferase expression in beta cells, leading to the characteristic signs of metabolic disease,
including hyperglycemia, impaired glucose tolerance, hyperinsulinemia, hepatic steatosis and diminished
insulin action in muscle and adipose tissues.
The scientists, from the Sanford-Burnham Medical Research Institute at the University of California
Santa Barbara, the RIKEN Advanced Science Institute in Japan, and the University of California San
Diego, further showed that protection from disease could be provided by enforced beta cell–specific
GnT-4a protein glycosylation, which supported the maintenance of glucose transporter expression and
the preservation of glucose transport.
Co-authors Kazuaki Ohtsubo, Ph.D., Mark Z. Chen, Ph.D., Jerrold M. Olefsky, Ph.D., and Jamey D.
Marth, Ph.D., report their findings in Nature Medicine, in a paper titled, “Pathway to diabetes through
attenuation of pancreatic beta cell glycosylation and glucose transport.”
Insulin resistance is a metabolic hallmark of type 2 diabetes, and pancreatic beta cell dysfunction
represents a diagnostic determinant of the disease, causing the loss of glucose-stimulated insulin
secretion (GSIS), the authors explain. Clues as to the molecular pathways involved in type 2 diabetes
development are embodied in a mouse model of the disease that lacks GnT-4a glycosyltransferase, an
enzyme encoded by the Mgat4a gene. GnT-4a is involved in positioning of the Slc2a2-encoded glucose
transporter-2 (Glut-2) glycoprotein on the cell surface.
The Sanford-Burnham-led team set out to search for factors that control GnT-4a function and glucose
transporter expression, and to see whether a deficiency in GnT-4a protein glycosylation and glucose
transport are truly causal in disease pathogenesis in the mouse model, and potentially in humans.
The researchers first showed that wild-type mice fed a high-fat diet (HFD) became deficient in Mgat4a
and Slc2a2 RNA in pancreatic islet cells, when compared with animals fed a regular diet. Through
promoter region DNA sequence analyses of the mouse Mgat4a and Slc2a2 genes, the orthologous
human genes MGAT4A and SLC2A1 (also known as GLUT1), and the human SLC2A2 gene, they
identified potential binding sites on multiple transcription factors including mouse and human FOXA2
and HNF1A.
In mice Foxa2 and Hnf1a binding to the Mgat4a and Slc2a2 genes was significantly reduced in
pancreatic islets from mice eating a HFD. This reduced binding coincided with decreased abundance of
the Foxa2 and Hnf1a proteins, a marked reduction in their nuclear localization of both, and increased
cytoplasmic localization. Decreased protein abundance and changes in localization combined to varying
degrees, resulting in an 80% drop in the levels of both Foxa2 and Hnf1a in the cell nuclei.
Studies in mouse islet cells confirmed that Foxa2 and Hnf1a normally contribute to Mgat4a and Slc2a2
transactivation in normal mice fed the standard diet, but that this transactivation was impaired in islets of
mice fed HFD. Significantly, when cultured islet cells from mice fed a normal diet were treated with
palmitic acid (a lipid used to model the diabetogenic effect of increased free fatty acids) nuclear
exclusion of Foxa2 and Hnf1a again resulted, and was associated with the downregulation of Mgat4a
and Slc2a2 gene expression.
Importantly, similar studies in human islets from healthy nondiabetic donors showed that in the absence
of exogenouse palmitic acid, FOXA2 and HNF1A proteins localized primarily in the nucleus, whereas the
addition of palmitic acid caused nuclear exclusion and increased cytoplasmic localization of both factors.
The addition of palmitic acid also diminished FOXA2 and HNF1A binding to the promotor regions of
MGAT4A, SLC2A1 and SLC2A2 genes, and attenuated mRNA expression of the three genes, which
coincided with the loss of GSIS.
“The similarities we observed in the responses of normal mouse and human islet cells to palmitic acid
suggested that islets from human type 2 diabetes donors may show defects comparable to those of mice
rendered diabetic by high-fat diet administration,” the authors note.
Further analyses showed that FOXA2 and HNF1A were excluded by more than 70% from the nuclei of
islet cells in tissue from type 2 diabetic patients. In the diabetic islet tissue expression of SLC2A1 and
SLC2A2 mRNAs encoding the human GLUT1 and GLUT2 glucose transporters was also decreased by
70–90%, and MGAT4A mRNA expression was reduced by 60%. The reduction in MGAT4A expression
translated to a 10-50-fold reduction of the GnT-4a glycan product. Importantly, islet cells from donors
with type 2 diabetes were 80-90% deficient in cell surface expression of both GLUT1 and GLUT2
glycoproteins, had very low glucose transport activity, and lacked the GSIS response.
The team moved on to evaluate the impact of diminished GnT-4a glycosylation on glucose transporter
expression and the onset of disease signs in a HFD–induced mouse model of type 2 diabetes. They
generated transgenic mice that constitutively expressed the human MGAT4A gene specifically in beta
cells, but in no other cell type or tissue. Both wild-type and transgenic mice fed a HFD became obese,
but while the HFD wild-type mice displayed hyperglycemia and hyperinsulinemia, MGAT4A transgenic
littermates maintained much lower concentrations of blood glucose and insulin.
Fasted MGAT4A transgenic animals also displayed markedly greater glucose tolerance, reduced
insulinemia and preserved GSIS. Circulating free fatty acid and triglyceride concentrations in these
animals were in addition markedly reduced in comparison with wild-type littermates, “indicating that
enforced beta cell GnT-4a protein glycosylation diminished multiple and systemic disease signs,” the
authors write.
Moreover, insulin tolerance tests in mice fed a HFD indicated greater glucose clearance in MGAT4A
transgenic mice than in wild-type animals, and glucose infusion rate studies suggested whole-body
insulin sensitivity was significantly greater in MGAT4A transgenic mice. Hepatic steatosis was evident in
wild-type mice that received the high-fat diet, whereas the livers of HFD MGAT4A transgenic mice
notably lacked signs of steatosis.
To test whether the disease protection afforded by GnT-4a involves maintenance of beta cell glucose
sensing, the researchers then generated transgenic mice bearing constitutive beta cell–specific
expression of the human SLC2A2 gene. In these animals there was greater beta cell GLUT-2
glycoprotein expression and glucose transport in comparison with beta cells from wild-type and MGAT4A
transgenic mice that received the standard diet.
In fact, the SLC2A2 transgene conferred an intermediate degree of improvement at the biochemical level
between wild-type and MGAT4A transgenic mice. For example, the SLC2A2 transgene provided an
intermediate reduction in hyperglycemia and hyperinsulinemia, whereas the development of obesity was
unaffected. Glucose transporter glycosylation by GnT-4a remained optimal in islet cells of MGAT4A
transgenic mice receiving the high-fat diet, whereas corresponding SLC2A2 transgenic beta cells
showed a decrease in GLUT-2 glycosylation among mice fed the high-fat diet, consistent with the
downmodulation of endogenous Mgat4a expression, diminished GnT-4a activity and decreased GLUT-2
abundance.
The overall results suggest a molecular and pathogenic pathway that includes a key role of pancreatic
beta cell GnT-4a glycosylation and glucose transport in the origin and severity of disease signs including
insulin resistance that are together diagnostic of type 2 diabetes, the authors conclude.
“A pathogenic tipping point in this pathway may occur when elevated free fatty acid (FFA) concentrations
impair the expression and function of FOXA2 and HNF1A transcription factors sufficiently in beta cells to
deplete GnT-4a glycosylation and glucose transporter expression. The resulting dysfunction of beta cells
leads to impaired glucose tolerance and failure of GSIS and further contributes to hyperglycemia, hepatic
steatosis and systemic insulin resistance. Preservation of beta cell GnT-4a glycosylation and glucose
transporter expression breaks this pathogenic cycle and its link to diet and obesity.”
The impact of enforced beta cell-specific expression of MGAT4A and SLC2A2 on metabolic
abnormalities including GSIS and insulin resistance was particularly notable, they add. “Constitutive beta
cell expression of GnT-4a or Glut-2 preserved considerable systemic insulin sensitivity, indicating that
beta cell function influences insulin action on these peripheral target tissues.”
The results were something of a surprise, however, Dr. Marth notes. “The observation that beta cell
malfunction significantly contributes to multiple disease signs, including insulin resistance, was
unexpected.” However, the findings do provide pointers to new potential therapeutic approaches, he
adds. “Now that we know more fully how states of over-nutrition can lead to type 2 diabetes, we can see
more clearly how to intervene. The identification of the molecular players in this pathway to diabetes
suggests new therapeutic targets and approaches towards developing an effective preventative or
perhaps curative treatment. This may be accomplished by beta cell gene therapy or by drugs that
interfere with this pathway in order to maintain normal beta cell function.”
© 2010 Genetic Engineering & Biotechnology News, All Rights Reserved
Scientists Find High-Fat Diet Causes Beta
Cell Dysfunction Leading to Type 2 Diabetes
Studies suggest elevated levels of fatty acids impact key enzyme that promotes
glucose sensing in pancreatic beta cells.
Scientists report new insights into the mechanisms by which a high fat diet can lead to type 2 diabetes.
Mouse and human studies by researchers in the U.S. and Japan suggest that elevated levels of free fatty
acids leads to both reduced expression of the transcription factors FOXA2 and HNF1A in pancreatic
beta cells, and their exclusion from the cell nuclei. This in turn results in a deficit of GnT-4a
glycosyltransferase expression in beta cells, leading to the characteristic signs of metabolic disease,
including hyperglycemia, impaired glucose tolerance, hyperinsulinemia, hepatic steatosis and diminished
insulin action in muscle and adipose tissues.
The scientists, from the Sanford-Burnham Medical Research Institute at the University of California
Santa Barbara, the RIKEN Advanced Science Institute in Japan, and the University of California San
Diego, further showed that protection from disease could be provided by enforced beta cell–specific
GnT-4a protein glycosylation, which supported the maintenance of glucose transporter expression and
the preservation of glucose transport.
Co-authors Kazuaki Ohtsubo, Ph.D., Mark Z. Chen, Ph.D., Jerrold M. Olefsky, Ph.D., and Jamey D.
Marth, Ph.D., report their findings in Nature Medicine, in a paper titled, “Pathway to diabetes through
attenuation of pancreatic beta cell glycosylation and glucose transport.”
Insulin resistance is a metabolic hallmark of type 2 diabetes, and pancreatic beta cell dysfunction
represents a diagnostic determinant of the disease, causing the loss of glucose-stimulated insulin
secretion (GSIS), the authors explain. Clues as to the molecular pathways involved in type 2 diabetes
development are embodied in a mouse model of the disease that lacks GnT-4a glycosyltransferase, an
enzyme encoded by the Mgat4a gene. GnT-4a is involved in positioning of the Slc2a2-encoded glucose
transporter-2 (Glut-2) glycoprotein on the cell surface.
The Sanford-Burnham-led team set out to search for factors that control GnT-4a function and glucose
transporter expression, and to see whether a deficiency in GnT-4a protein glycosylation and glucose
transport are truly causal in disease pathogenesis in the mouse model, and potentially in humans.
The researchers first showed that wild-type mice fed a high-fat diet (HFD) became deficient in Mgat4a
and Slc2a2 RNA in pancreatic islet cells, when compared with animals fed a regular diet. Through
promoter region DNA sequence analyses of the mouse Mgat4a and Slc2a2 genes, the orthologous
human genes MGAT4A and SLC2A1 (also known as GLUT1), and the human SLC2A2 gene, they
identified potential binding sites on multiple transcription factors including mouse and human FOXA2
and HNF1A.
In mice Foxa2 and Hnf1a binding to the Mgat4a and Slc2a2 genes was significantly reduced in
pancreatic islets from mice eating a HFD. This reduced binding coincided with decreased abundance of
the Foxa2 and Hnf1a proteins, a marked reduction in their nuclear localization of both, and increased
cytoplasmic localization. Decreased protein abundance and changes in localization combined to varying
degrees, resulting in an 80% drop in the levels of both Foxa2 and Hnf1a in the cell nuclei.
Studies in mouse islet cells confirmed that Foxa2 and Hnf1a normally contribute to Mgat4a and Slc2a2
transactivation in normal mice fed the standard diet, but that this transactivation was impaired in islets of
mice fed HFD. Significantly, when cultured islet cells from mice fed a normal diet were treated with
palmitic acid (a lipid used to model the diabetogenic effect of increased free fatty acids) nuclear
exclusion of Foxa2 and Hnf1a again resulted, and was associated with the downregulation of Mgat4a
and Slc2a2 gene expression.
Importantly, similar studies in human islets from healthy nondiabetic donors showed that in the absence
of exogenouse palmitic acid, FOXA2 and HNF1A proteins localized primarily in the nucleus, whereas the
addition of palmitic acid caused nuclear exclusion and increased cytoplasmic localization of both factors.
The addition of palmitic acid also diminished FOXA2 and HNF1A binding to the promotor regions of
MGAT4A, SLC2A1 and SLC2A2 genes, and attenuated mRNA expression of the three genes, which
coincided with the loss of GSIS.
“The similarities we observed in the responses of normal mouse and human islet cells to palmitic acid
suggested that islets from human type 2 diabetes donors may show defects comparable to those of mice
rendered diabetic by high-fat diet administration,” the authors note.
Further analyses showed that FOXA2 and HNF1A were excluded by more than 70% from the nuclei of
islet cells in tissue from type 2 diabetic patients. In the diabetic islet tissue expression of SLC2A1 and
SLC2A2 mRNAs encoding the human GLUT1 and GLUT2 glucose transporters was also decreased by
70–90%, and MGAT4A mRNA expression was reduced by 60%. The reduction in MGAT4A expression
translated to a 10-50-fold reduction of the GnT-4a glycan product. Importantly, islet cells from donors
with type 2 diabetes were 80-90% deficient in cell surface expression of both GLUT1 and GLUT2
glycoproteins, had very low glucose transport activity, and lacked the GSIS response.
The team moved on to evaluate the impact of diminished GnT-4a glycosylation on glucose transporter
expression and the onset of disease signs in a HFD–induced mouse model of type 2 diabetes. They
generated transgenic mice that constitutively expressed the human MGAT4A gene specifically in beta
cells, but in no other cell type or tissue. Both wild-type and transgenic mice fed a HFD became obese,
but while the HFD wild-type mice displayed hyperglycemia and hyperinsulinemia, MGAT4A transgenic
littermates maintained much lower concentrations of blood glucose and insulin.
Fasted MGAT4A transgenic animals also displayed markedly greater glucose tolerance, reduced
insulinemia and preserved GSIS. Circulating free fatty acid and triglyceride concentrations in these
animals were in addition markedly reduced in comparison with wild-type littermates, “indicating that
enforced beta cell GnT-4a protein glycosylation diminished multiple and systemic disease signs,” the
authors write.
Moreover, insulin tolerance tests in mice fed a HFD indicated greater glucose clearance in MGAT4A
transgenic mice than in wild-type animals, and glucose infusion rate studies suggested whole-body
insulin sensitivity was significantly greater in MGAT4A transgenic mice. Hepatic steatosis was evident in
wild-type mice that received the high-fat diet, whereas the livers of HFD MGAT4A transgenic mice
notably lacked signs of steatosis.
To test whether the disease protection afforded by GnT-4a involves maintenance of beta cell glucose
sensing, the researchers then generated transgenic mice bearing constitutive beta cell–specific
expression of the human SLC2A2 gene. In these animals there was greater beta cell GLUT-2
glycoprotein expression and glucose transport in comparison with beta cells from wild-type and MGAT4A
transgenic mice that received the standard diet.
In fact, the SLC2A2 transgene conferred an intermediate degree of improvement at the biochemical level
between wild-type and MGAT4A transgenic mice. For example, the SLC2A2 transgene provided an
intermediate reduction in hyperglycemia and hyperinsulinemia, whereas the development of obesity was
unaffected. Glucose transporter glycosylation by GnT-4a remained optimal in islet cells of MGAT4A
transgenic mice receiving the high-fat diet, whereas corresponding SLC2A2 transgenic beta cells
showed a decrease in GLUT-2 glycosylation among mice fed the high-fat diet, consistent with the
downmodulation of endogenous Mgat4a expression, diminished GnT-4a activity and decreased GLUT-2
abundance.
The overall results suggest a molecular and pathogenic pathway that includes a key role of pancreatic
beta cell GnT-4a glycosylation and glucose transport in the origin and severity of disease signs including
insulin resistance that are together diagnostic of type 2 diabetes, the authors conclude.
“A pathogenic tipping point in this pathway may occur when elevated free fatty acid (FFA) concentrations
impair the expression and function of FOXA2 and HNF1A transcription factors sufficiently in beta cells to
deplete GnT-4a glycosylation and glucose transporter expression. The resulting dysfunction of beta cells
leads to impaired glucose tolerance and failure of GSIS and further contributes to hyperglycemia, hepatic
steatosis and systemic insulin resistance. Preservation of beta cell GnT-4a glycosylation and glucose
transporter expression breaks this pathogenic cycle and its link to diet and obesity.”
The impact of enforced beta cell-specific expression of MGAT4A and SLC2A2 on metabolic
abnormalities including GSIS and insulin resistance was particularly notable, they add. “Constitutive beta
cell expression of GnT-4a or Glut-2 preserved considerable systemic insulin sensitivity, indicating that
beta cell function influences insulin action on these peripheral target tissues.”
The results were something of a surprise, however, Dr. Marth notes. “The observation that beta cell
malfunction significantly contributes to multiple disease signs, including insulin resistance, was
unexpected.” However, the findings do provide pointers to new potential therapeutic approaches, he
adds. “Now that we know more fully how states of over-nutrition can lead to type 2 diabetes, we can see
more clearly how to intervene. The identification of the molecular players in this pathway to diabetes
suggests new therapeutic targets and approaches towards developing an effective preventative or
perhaps curative treatment. This may be accomplished by beta cell gene therapy or by drugs that
interfere with this pathway in order to maintain normal beta cell function.”
© 2010 Genetic Engineering & Biotechnology News, All Rights Reserved
Antwort auf Beitrag Nr.: 41.942.485 von brooker69 am 12.08.11 10:57:57und nun????Ruckzuck über €2,50????
Ich denke schon. Jetzt gehts los....jetzt gehts los.....
LG
k-torte
Ich denke schon. Jetzt gehts los....jetzt gehts los.....
LG
k-torte
Evotec unterzeichnet Partnerschaft zur Entwicklung ihres P2X7 Antagonisten EVT 401 im Bereich Tiergesundheit
Lizenz an ein führendes Unternehmen zur Entwicklung der proprietären Substanz im Bereich Tiergesundheit exklusiv gewährt
Teilen
15.08.2011: Evotec AG gab bekannt, dass sie eine weltweite Lizenz- und Kooperationsvereinbarung mit einem führenden Unternehmen im Bereich der Tiergesundheit eingegangen ist. Ziel ist es, Evotecs proprietäre Substanz EVT 401, ein selektiver niedermolekularer P2X7 Antagonist, als Wirkstoff zur Behandlung von Entzündungskrankheiten in Haustieren, zu entwickeln.
Wie vertraglich vereinbart wird Evotec eine „Technology-Transfer-Zahlung“, Entwicklungs- und kommerzielle Meilensteinzahlungen sowie Nettoumsatzbeteiligungen bei erfolgreicher Markteinführung von Produkten erhalten. Evotec behält sämtliche Rechte auf dieses Programm zur Entwicklung von Wirkstoffkandidaten für die human- therapeutische Verwendung.
Dr. Werner Lanthaler, Chief Executive Officer von Evotec, kommentierte: “Wir sind stolz darauf, mit einem weltweit führenden Unternehmen zusammen zu arbeiten, dass die Fähigkeit besitzt, Medikamente für Tierkrankheiten zu entwickeln. Damit erreichen wir nicht nur zusätzlichen Produktmehrwert, sondern unterstreichen unsere Stärke in der Anwendung der Medizinalchemie. Wir freuen uns über eine enge Zusammenarbeit mit einem der weltweit führenden Unternehmen im Bereich Tiergesundheit, um dieses Produkt erfolgreich zu entwickeln.”
Einzelheiten zu finanziellen Details wurden nicht bekanntgegeben.
http://www.bionity.com/de/news/133942/evotec-unterzeichnet-p…
Lizenz an ein führendes Unternehmen zur Entwicklung der proprietären Substanz im Bereich Tiergesundheit exklusiv gewährt
Teilen
15.08.2011: Evotec AG gab bekannt, dass sie eine weltweite Lizenz- und Kooperationsvereinbarung mit einem führenden Unternehmen im Bereich der Tiergesundheit eingegangen ist. Ziel ist es, Evotecs proprietäre Substanz EVT 401, ein selektiver niedermolekularer P2X7 Antagonist, als Wirkstoff zur Behandlung von Entzündungskrankheiten in Haustieren, zu entwickeln.
Wie vertraglich vereinbart wird Evotec eine „Technology-Transfer-Zahlung“, Entwicklungs- und kommerzielle Meilensteinzahlungen sowie Nettoumsatzbeteiligungen bei erfolgreicher Markteinführung von Produkten erhalten. Evotec behält sämtliche Rechte auf dieses Programm zur Entwicklung von Wirkstoffkandidaten für die human- therapeutische Verwendung.
Dr. Werner Lanthaler, Chief Executive Officer von Evotec, kommentierte: “Wir sind stolz darauf, mit einem weltweit führenden Unternehmen zusammen zu arbeiten, dass die Fähigkeit besitzt, Medikamente für Tierkrankheiten zu entwickeln. Damit erreichen wir nicht nur zusätzlichen Produktmehrwert, sondern unterstreichen unsere Stärke in der Anwendung der Medizinalchemie. Wir freuen uns über eine enge Zusammenarbeit mit einem der weltweit führenden Unternehmen im Bereich Tiergesundheit, um dieses Produkt erfolgreich zu entwickeln.”
Einzelheiten zu finanziellen Details wurden nicht bekanntgegeben.
http://www.bionity.com/de/news/133942/evotec-unterzeichnet-p…
der Kurs wird unten gehalten da steigen erst noch ein paar ein! Ihr wißt schon wie das läuft und dann Rackzack übe 2,10€
Trading Spotlight
Moin auch,
denke dass Du mit Deiner Pipeline Betrachtung richtig liegst, allerdings glaube ich nach wie vor an gute Aussichten bei H3: In der Präsentation „Evotec_H1-2011“ stehen bei den R&D Ausgaben:
CureBeta initiative, EVT 501, response prediction, etc.
Für mich ist die Aussage wenn, Evotec hier noch investiert glaubt man noch an das Programm. P2X3 sollte ebenfalls gute Chancen haben einen Partner zu finden: potentiell first & best in class…
Dass 401 noch verpartnert werden konnte, ist auf jeden Fall positiv zu sehen (war für mich auf dem gleichen Nullpunkt wie EVT-302 – aber auch EVT-201), allerdings hätte ich mir trotzdem für dieses Jahr eine bessere Partnerschaftsmeldung erhofft. Ähnlich zumindest dem BI Deal mit Alt-Develogen oder Medimmune.
Aber zurück zu den Umsätzen. Ich glaube das hier noch einige am Jahresende sich umschauen werden. Ich halte meine angestrebten 72 bis 74 Mil für durchaus realistisch, sogar konservativ:
Der Umsatz im 1.H lag bei etwa 33,4 Mil, bedenkt man das kaum dicke Meilensteine im 1.H geflossen sind und das Evotec von Anfang an gesagt und damit rechnet dass die Meilensteine im Jahre 2011 ähnlich hoch wie 2010 ausfallen, ist noch mit einigen zu rechnen!
Also: würde der Umsatz im 2.H genauso hoch sein wie im ersten hätten wir 33,4 Mil. schon mal im Sack (SEHR konservativ gerechnet). Zuzüglich zwei weiteren dicken Meilensteinen nochmals 4 Mil. kommen wir dann schon auf 37,4 Mil.
Zudem wird der Umsatz von Compound Management von etwa nochmals 4 Mil. hinzukommen (Übernahme war im Juni, also noch keine wesentlichen Umsätze im 1.H). Damit komme ich auf etwa 41 Mil. Euro Umsätze für dass 2.H ohne dass ich die Umsätze vom 1.H „raufgeschraubt“ habe.
Da Compound Management äußerst profitabel arbeitet denke ich dass Evotec in diesem Jahr einen Nettoumsatz von 5-6 Mil. erzielen wird (und das obwohl R&D Ausgaben 60% erhöht werden). Und der Umsatz wird aus meiner Sicht ein bischen größer als 74 Mil.!
Grüße
denke dass Du mit Deiner Pipeline Betrachtung richtig liegst, allerdings glaube ich nach wie vor an gute Aussichten bei H3: In der Präsentation „Evotec_H1-2011“ stehen bei den R&D Ausgaben:
CureBeta initiative, EVT 501, response prediction, etc.
Für mich ist die Aussage wenn, Evotec hier noch investiert glaubt man noch an das Programm. P2X3 sollte ebenfalls gute Chancen haben einen Partner zu finden: potentiell first & best in class…
Dass 401 noch verpartnert werden konnte, ist auf jeden Fall positiv zu sehen (war für mich auf dem gleichen Nullpunkt wie EVT-302 – aber auch EVT-201), allerdings hätte ich mir trotzdem für dieses Jahr eine bessere Partnerschaftsmeldung erhofft. Ähnlich zumindest dem BI Deal mit Alt-Develogen oder Medimmune.
Aber zurück zu den Umsätzen. Ich glaube das hier noch einige am Jahresende sich umschauen werden. Ich halte meine angestrebten 72 bis 74 Mil für durchaus realistisch, sogar konservativ:
Der Umsatz im 1.H lag bei etwa 33,4 Mil, bedenkt man das kaum dicke Meilensteine im 1.H geflossen sind und das Evotec von Anfang an gesagt und damit rechnet dass die Meilensteine im Jahre 2011 ähnlich hoch wie 2010 ausfallen, ist noch mit einigen zu rechnen!
Also: würde der Umsatz im 2.H genauso hoch sein wie im ersten hätten wir 33,4 Mil. schon mal im Sack (SEHR konservativ gerechnet). Zuzüglich zwei weiteren dicken Meilensteinen nochmals 4 Mil. kommen wir dann schon auf 37,4 Mil.
Zudem wird der Umsatz von Compound Management von etwa nochmals 4 Mil. hinzukommen (Übernahme war im Juni, also noch keine wesentlichen Umsätze im 1.H). Damit komme ich auf etwa 41 Mil. Euro Umsätze für dass 2.H ohne dass ich die Umsätze vom 1.H „raufgeschraubt“ habe.
Da Compound Management äußerst profitabel arbeitet denke ich dass Evotec in diesem Jahr einen Nettoumsatz von 5-6 Mil. erzielen wird (und das obwohl R&D Ausgaben 60% erhöht werden). Und der Umsatz wird aus meiner Sicht ein bischen größer als 74 Mil.!
Grüße
ich tippe auf talfahrt. dann kann ich wieder einsteigen...
aber im ernst:die scheine hier sind weit mehr wert, aber im augenblick traue ich den kursen alle möglichen kapriolen zu. mal sehen, was so passiert.
aber im ernst:die scheine hier sind weit mehr wert, aber im augenblick traue ich den kursen alle möglichen kapriolen zu. mal sehen, was so passiert.
Das Kaufinteresse ist da unter 2€ eingestiegen! Schau mer mal was daraus wird wenn die Börsen nicht total verückt spielen!
werde mir auch wieder ein paar EVO gönnen aber erst mal sehen was heute passiert könnte ein schwarzer Freitag werden!
Antwort auf Beitrag Nr.: 41.938.976 von evotecci am 11.08.11 17:52:18Danke Evotecci für deine ausführliche und sehr informative Ausführung
Durchsuchen
Evotec 566480, wohin geht die Reise???
